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Q6NRM8

MEFPEHSRHLLQCLSEQRHQGFLCDCTVLVGDAHFRAHRAVLASCSMYFHLFYKDQLDKKNIVYLNSDIVTAPAFALLLEFMYEGKLQFKDLPIEDVLAAASYLHMYDIVKVCKKKLKEKATTEADSTKKEEDTLSCSDKIECLSDGSSHMAGDLPSDEDDVEEEKINSKTDLATESGNMWIRLSSDSASIPQTGGEVDTHTTAAGKTADSPCSSTGSLSHRSATSMGDSTDVDCVLDLSVKSSLSGTETLNNSYLSSQEILRNSLVQVKIEREASCEDNDIHTSEYDIERNTVKENVSSNIRAPYEPVHLAPIREDSVLRELDHDDKAINDDMITPENERVQMEANIDNSLLPYVQNILSPAGQIFMCPLCNKVFPSPHILQIHLSTHFREQEGIRSKPTNDVHVPTCSLCGKTFSCMYTLKRHERTHSGEKPFTCTQCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCELVNSLSVKSETLGLPAVRDWTLEDSSQELWK

Transcriptional repressor that plays a role in various developmental processes. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes (By similarity). Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily.

Q0IH98

MEFSSHHIRLLQQLDEQRQKDLFCDCHIIVEGQMFKAHRNVLFASSGYFKMLLSQSCRDMGEPITATFDVFSADTFTAILDFVYSGKLPLSGQNVIEVMSAASYLQMTDVIGVCKMFIKSSLDINEKDRDGFFSLSDKDAGSNGSGLYAAGWRTESSPTHTHDTAEHGSFIAGYNYPPPITSRLQRPFSKHPRKPELVRKHRRRLLPEPLTPAPLSHIPLGDLVGGSAECMLHDEETVESVSQEEERTQTQESIISIKDEDEDAASHSWPESPQQESLDQGPALHITKAEELYKAMPTMLGGVSGWGEDELSSGRFKCPFCTHTVKRKADLKRHLRCHTGERPYPCEACGKRFTRLEHLRNHFQTIHEAGKLICRRCKLPVTKVTGRVIQDGTRRYRLCHACLAEAGLDNVNFDYGEDQPLVLPPENEREHCWNFKEEGRKENGSERAESDLAIQEVVDSEDDELKEKQD

May be involved in transcriptional regulation.

A1L2U9

MEFSSHHIRLLQQLDEQRRRDLFCDCHIIVEGQMFKAHRNVLFASSGYFKMLLSQSCRDMGEPITATFDVFSADTFTAILDFVYSGKLPLSGQNVIEVMSAASYLQMTDVIGVCKMFIKSSLDINEKDRDGFFSLSDKDTDSNGSGLYAAGWRTESSPTHTHKTTEHGSFIAGYNYPPPISSRLQHPFSKSPRKPELVRKHRRRLLPEALTPALSHIPLGDLVGGSTECMLHDEETVESVSQEEERTQTQVSIISIKVEDLDATSNSWPESPPQESLDQGSALHITKAEELYKAMPTILGGVSGWGEDELSSGRFKCPFCTHTVKRKADLKRHLRCHTGERPYPCEACGKRFTRLEHLRNHFQTIHEAGKLICRRCKLPVTKVTGRVIQDGTRRYRLCQACLAEAGLDNVNFDYGEDQPLVLPPENEREHCWNFKEEGRQENGSEAAESDLVIQEVVDSEEDELKQKQD

May be involved in transcriptional regulation.

Q6P882

MDLPSHHSRLLRQLDEQRRRNLFCDCHIMIDGHTFRAHRNVLYASSGYFKMLLSQSSGNVGQPTTATFDVFSADTFTAILDFMYSGKLNLSGQNVIEIMSAASYLQMTEVIGVCKMFIKSSLDINEKDRDGFLDISDKETGQQTGQCGLYSTGWGMGRYHCNQPEGDIAAYLETSSCTPYGFCSRTDEHPSSQNSISTATMKMLDRHNRIPQIPSSTCSPEEHLRECRILESDDTGCHIEVELPQGEETEAFLNCQTVVQPRSRRRHSLNRATKADEVYAKIMGIKGCLGEDNLPSLHFKCPFCTHTVKRKADLKRHLLCHTGERPYPCQACGKRFTRLEHVRSHYRTIHEAGKPICRWCKRHVTEDSGQVVQEGTRRFRLCNKCVAEVGVGSFPNEVDDDEPTIILSGDEDKEPTWNFHDGIQTSDPEIIEDVSSDVVIHKVDDSDDEIKPIIC

May be involved in transcriptional regulation.

Q96BY4

MENKSLESSQTDLKLVAHPRAKSKVWKYFGFDTNAEGCILQWKKIYCRICMAQIAYSGNTSNLSYHLEKNHPEEFCEFVKSNTEQMREAFATAFSKLKPESSQQPGQDALAVKAGHGYDSKKQQELTAAVLGLICEGLYPASIVDEPTFKVLLKTADPRYELPSRKYISTKAIPEKYGAVREVILKELAEATWCGISTDMWRSENQNRAYVTLAAHFLGLGAPNCLSMGSRCLKTFEVPEENTAETITRVLYEVFIEWGISAKVFGATTNYGKDIVKACSLLDVAVHMPCLGHTFNAGIQQAFQLPKLGALLSRCRKLVEYFQQSAVAMYMLYEKQKQQNVAHCMLVSNRVSWWGSTLAMLQRLKEQQFVIAGVLVEDSNNHHLMLEASEWATIEGLVELLQPFKQVAEMLSASRYPTISMVKPLLHMLLNTTLNIKETDSKELSMAKEVIAKELSKTYQETPEIDMFLNVATFLDPRYKRLPFLSAFERQQVENRVVEEAKGLLDKVKDGGYRPAEDKIFPVPEEPPVKKLMRTSTPPPASVINNMLAEIFCQTGGVEDQEEWHAQVVEELSNFKSQKVLGLNEDPLKWWSDRLALFPLLPKVLQKYWCVTATRVAPERLFGSAANVVSAKRNRLAPAHVDEQVFLYENARSGAEAEPEDQDEGEWGLDQEQVFSLGDGVSGGFFGIRDSSFL

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha transcription repression, increased recruitment of RNA polymerase II to gene promoters and positive regulation of transcription including H1-5 and ribosomal proteins such as: RPS6, RPL10A, and RPL12 (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). The resulting increased transcriptional activity drives cell proliferation (PubMed:12663651, PubMed:17220279). Binds to 5'-TGTCG[CT]GA[CT]A-3' consensus sequences in gene promoters of ribosomal proteins (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). (Microbial infection) Binds to human adenovirus gene promoters and contributes to transcriptional repression and virus growth inhibition during early stages of infection. Protein modification; protein sumoylation. Homodimer and homomultimer (PubMed:17209048). Homodimerization is necessary for protein nuclear localization and DNA binding (PubMed:17209048). Interacts with KPNB1; required for nuclear import of ZBED1/hDREF (PubMed:17209048). Interacts with CHD3/Mi2-alpha (PubMed:27068747). Interacts with SUMO1 (PubMed:27068747). Interacts with UBE2I/UBC9 (PubMed:27068747). (Microbial infection) Interacts (via C-terminus) with human adenovirus early E1A protein (via C-terminus); the interaction is direct. In granular structures. (Microbial infection) Upon interaction with human adenovirus early E1A protein, the protein is redistributed to the peripheral areas of PML bodies. Ubiquitously expressed at low levels (PubMed:9887332). Expression is highest in skeletal muscle, heart, spleen and placenta (PubMed:9887332). Expression is linked to the cell cycle: low in serum-starved fibroblasts, increasing during the G1/S phase, highest during the S/G2 phase and then decreasing again. Autosumoylated with SUMO1, SUMO2, and SUMO3. The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes. Was first identified as gene weakly similar to Ac transposable elements, but does not code for any transposase activity.

D3DN62

MMRREDEEEEGTMMKAKGDLEMKEEEEISETGELVGPFVSAMPTPMPHNKGTRFSEAWEYFHLAPARAGHHPNQYATCRLCGRQVSRGPGVNVGTTALWKHLKSMHREELEKSGHGQAGQRQDPRPHGPQLPTGIEGNWGRLLEQVGTMALWASQREKEVLRRERAVEWRERAVEKRERALEEVERAILEMKWKVRAEKEACQREKELPAAVHPFHFV

Transcriptional regulator which has intrinsic repressor activity and which competes with the transcriptional activator IRF1 for binding to the 5'-[CA]GAA[AC]C[CT]-3' consensus sequence in gene promoters (PubMed:32385160). May thereby play a role in keratinocyte differentiation (PubMed:31552090). Expressed in keratinocytes. Induced by TGF-beta.

Q96IU2

MRSGEPACTMDQARGLDDAAARGGQCPGLGPAPTPTPPGRLGAPYSEAWGYFHLAPGRPGHPSGHWATCRLCGEQVGRGPGFHAGTSALWRHLRSAHRRELESSGAGSSPPAAPCPPPPGPAAAPEGDWARLLEQMGALAVRGSRRERELERRELAVEQGERALERRRRALQEEERAAAQARRELQAEREALQARLRDVSRREGALGWAPAAPPPLKDDPEGDRDGCVITKVLL

Acts as a positive regulator in the activation of the canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic beta-catenin (By similarity). Involved in transcription activation of Wnt target gene expression (By similarity). Plays a role in symmetric division of blastomeres in the early stages of embryogenesis via regulation of mitotic spindle central positioning and organization of the F-actin filament network (By similarity). Plays a role in regulating the distribution of cellular organelles, via modulation of cytoskeletal dynamics and cytoplasmic lattice formation (By similarity). Associates with the subcortical maternal complex (SCMC) composed of at least NLRP5, KHDC3L, OOEP, and TLE6 via interaction with NLRP5 and TLE6 (By similarity). Interacts with AXIN1; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations (By similarity). Secreted in blood plasma, and expressed in skeletal muscle and adipose tissue (at protein level). Induced in blood plasma by hyperglycemia (PubMed:24283382). Decreased in blood plasma by hyperinsulinemia (PubMed:24283382).

Q9D0L1

MKSKKPLKITMEDSRRLNDPAEQGGLCPAPVGPSYSEAWGYFHLDPAQPRHRMMSAWATCRLCGLQVGGLPNFQMWTRALCQHLSDVHLPELKKSAAPSSPTTMPCPPPPSPTMAAEGDWARLLEQMGELAMRGSQRELELERREAALMQAELELERKRQALKQEAQSVEQERHQLQVEREALSKWIKKQSPGAQVPEPPSPLPLLPKEDPDIHDNNSDNDMVTKVLL

Acts as a positive regulator in the activation of the canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic beta-catenin (PubMed:19141611). Involved in transcription activation of Wnt target gene expression (PubMed:19141611). Plays a role in symmetric division of blastomeres in the early stages of embryogenesis via regulation of mitotic spindle central positioning and organization of the F-actin filament network (PubMed:28992324). Plays a role in regulating the distribution of cellular organelles, via modulation of cytoskeletal dynamics and cytoplasmic lattice formation (PubMed:28992324). Associates with the subcortical maternal complex (SCMC) composed of at least NLRP5, KHDC3, OOEP, and TLE6 via interaction with NLRP5 and TLE6 (PubMed:28992324, PubMed:31575650). Interacts (via PPPSP motif) with AXIN1; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations (PubMed:19141611). Colocalizes with AXIN1 in the cytoplasm (PubMed:19141611). Colocalizes with NLRP5 in the oocyte subcortex (PubMed:28992324). Expressed in the liver (at protein level) (PubMed:24283382). Abundantly expressed in muscle, with lower expression in brain, fat, and heart (PubMed:24283382). Expressed in the spleen, lungs and kidney (PubMed:24283382, PubMed:28992324). Abundantly expressed in ovaries and testis, with lower expression in the uterus (PubMed:28992324). Expressed in the cytoplasm of germinal vesicle oocytes before becoming concentrated in the subcortex of metaphase 2 oocytes (PubMed:28992324). Expressed in ovaries at birth, expression peaks at postnatal day 10 (P10), expression is then decreased at P17 and further decreased at P21 (PubMed:31575650). Dual phosphorylation on serine and tyrosine residues of the cytoplasmic PPPSP motif by GSK3 and CK1 may be required for AXIN1-binding. Males show normal fertility however females produce smaller litters (PubMed:28992324). Increase in the number of 2-cell embryos with asymmetric blastomeres as a result of impaired central mitotic spindle position and therefore an increase in the distance between the cellular center and the chromosomes (PubMed:28992324). Disorganization of the F-actin filament network around the mitotic spindle and loss of FMN2-expressing endoplasmic reticulum localization to the mitotic spindle periphery in zygotes and oocytes (PubMed:28992324). Mitochondria are mislocalized to the plus-ends of elongated microtubules in the subcortical cytoplasm in oocytes prior to nuclear envelope breakdown (PubMed:28992324). Loss of cytoplasmic lattices and extension of the alpha-tubulin pool into the subcortical region following microtubule-organizing center congression in oocytes (PubMed:28992324).

Q9UGG8

MENNLKTCPKEDGDFVSDKIKFKIEEEDDDGIPPDSLERMDFKSEQEDMKQTDSGGERAGLGGTGCSCKPPGKYLSAESEDDYGALFSQYSSTLYDVAMEAVTQSLLSSRNMSSRKKSPAWKHFFISPRDSTKAICMYCVKEFSRGKNEKDLSTSCLMRHVRRAHPTVLIQENGSVSAVSSFPSPSLLLPPQPADAGDLSTILSPIKLVQKVASKIPSPDRITEESVSVVSSEEISSDMSVSEKCGREEALVGSSPHLPALHYDEPAENLAEKSLPLPKSTSGSRRRSAVWKHFYLSPLDNSKAVCIHCMNEFSRGKNGKDLGTSCLIRHMWRAHRAIVLQENGGTGIPPLYSTPPTLLPSLLPPEGELSSVSSSPVKPVRESPSASSSPDRLTEDLQSHLNPGDGLMEDVAAFSSSDDIGEASASSPEKQQADGLSPRLFESGAIFQQNKKVMKRLKSEVWHHFSLAPMDSLKAECRYCGCAISRGKKGDVGTSCLMRHLYRRHPEVVGSQKGFLGASLANSPYATLASAESSSSKLTDLPTVVTKNNQVMFPVNSKKTSKLWNHFSICSADSTKVVCLHCGRTISRGKKPTNLGTSCLLRHLQRFHSNVLKTEVSETARPSSPDTRVPRGTELSGASSFDDTNEKFYDSHPVAKKITSLIAEMIALDLQPYSFVDNVGFNRLLEYLKPQYSLPAPSYFSRTAIPGMYDNVKQIIMSHLKEAESGVIHFTSGIWMSNQTREYLTLTAHWVSFESPARPRCDDHHCSALLDVSQVDCDYSGNSIQKQLECWWEAWVTSTGLQVGITVTDNASIGKTLNEGEHSSVQCFSHTVNLIVSEAIKSQRMVQNLLSLARKICERVHRSPKAKEKLAELQREYALPQHHLIQDVPSKWSTSFHMLERLIEQKRAINEMSVECNFRELISCDQWEVMQSVCRALKPFEAASREMSTQMSTLSQVIPMVHILNRKVEMLFEETMGIDTMLRSLKEAMVSRLSATLHDPRYVFATLLDPRYKASLFTEEEAEQYKQDLIRELELMNSTSEDVAASHRCDAGSPSKDSAAEENLWSLVAKVKKKDPREKLPEAMVLAYLEEEVLEHSCDPLTYWNLKKASWPGLSALAVRFLGCPPSIVPSEKLFNTPTENGSLGQSRLMMEHFEKLIFLKVNLPLIYFQY

Transcriptional regulator that binds to poly-guanine tracts in gene promoters and activates transcription (By similarity). Able to bind single- and double-stranded DNA and RNA (By similarity). Homodimer; via C-terminus (PubMed:17209048). Interacts with MYH9 (PubMed:22693546). Interacts with SAFB/SAFB1 (PubMed:22693546). Expressed in testis, heart, lung, and weakly expressed in brain, liver, muscle, placenta and small intestine (PubMed:19369242). Expressed in the retina, found in the cone photoreceptors, Mueller cells, cone pedicles and in the innermost retinal layer (PubMed:19369242). Extended N-terminus.

Q8R329

MEDKQETCPKGDSDFVSDKVNFKTEEDDDQTPCHSLEQVDFKSESEDMRQTDSGDEQADIRAASCACQPSGKFLAAESEDDYGSLFSQYSSTLYSVAMEAVTQSLLSSRHISSRKKSPAWKHFFISPRDSTKAICTYCMKEFSRGKNEKDLSTSCLMRHVRRAHPTKLIQENGSLSAGSSFSPPSLLLPPQPADVGDLSTVLSPVRLVQKMAPKIPSPDQIMEESVTVVSSEELSSDVSVTEKYSREEALAGSSPNLSMLHYDDASETMADRNLSLPKSTSGSRRRSAVWKHFYLSPLDSSKAVCVHCMNEFSRGKNGKDLGTSCLIRHMWRAHRSIVLQENGGNTGIPPLYPMPPTLLPALLPPEGDLNSASLSPGKQVKESPSASSSPERLPEDLSSHTNPGDVSREDVSMLSSSDDLGEASVVSSPEKQPADTVNPRFESGTVFQQNKKVMRRLKSEVWHHFSLAPMDSLKAVCRYCSCVISRGKKGDVGTSCLMRHLYRRHPEVVGNQKDFLGASLANSPYATLASAESSSKLTDLPAVVRKNHQGVFPTNSKKTSKLWNHFSICSADSTKVVCLHCGRTISRGKKPTNLGTSCLLRHLQRFHGHVLKNDVSEATLSRSPGIRRPLGIELSGPSSFRDSTEKFYDSHPVAKKITSLIAEMIALDLQPYSLVDNVGFNRLLEYLKPQYSLPSPSYFSRTAIPGMYDNVKQIIMSHLKEAESGVVHFTSGIWMSSQTREYLTLTAHWVTFASAVRPHCEDHHCSALLDVSQIDCDYSGNSIQKQLECWWEAWVTSIGLQIGITVTDNPSIGKMLSEGEHSSVQCFSHTVNLIVSEAIKSQRMVQNLLSIARKLCERVHRSPRAREKLAELQKEYELPQHQLIQDVPSKWSTSFHMLERLIEQKRAVNEVSIECNFRELISCDQWEVMQSVCHVLRPFDAASREMSAHMSTLSQVIPMIHILSRKVEMLFGETMGIDTMLKSLKEAMASRLSATLHDPRYIFATLLDPRYKASLFTEEEAEQYRQDLIRELEILNSTSEDTATSNGCDSGSPLKDTGTEESLWSLAPIKRDQREKLPEDMVLAYLEEEVLEHSCDPLTYWNLKRSSWPGLSTLAVRFLGCPPSTVPSEKLFSTPMDAGSFGQPRLMMEHFEKLIFLKVNLPLICFQY

Transcriptional regulator that binds to poly-guanine tracts in gene promoters and activates transcription (By similarity). Able to bind single- and double-stranded DNA and RNA (PubMed:22693546). Homodimer; via C-terminus (By similarity). Interacts with MYH9 (By similarity). Interacts with SAFB/SAFB1 (By similarity). Expressed in the thymus (PubMed:19369242). In the retina, expressed in the cone photoreceptors (PubMed:19369242, PubMed:22693546). The sequence differs from that shown because it seems to be derived from a pre-mRNA.

A4Z943

MIAHFLCILSYNVNTFVILNVYTKLTMFCTTNSLPMDLLLKQGSLKQEVESFCYQIVSESHDQKVGILQSEDEHLQPSVSKNSEGELSRVKFISNSNKITTFSKKPKRRKYDESYLSFGFTYFGNRDAPHAQCVLCKKILSNSSLAPSKLRRHLETKHAAYKDKDISFFKQHLDSPENNKPPTPKIVNTDNESATEASYNVSYHIALSGEAHTIGELLIKPCAKDVVMRMFDEQYSKKIDAVQLSNSTVARRIKDLAADIEEELVCRLKICDGFSLQLDESADVSGLAVLLVFVRYRFNKSIEEDLLLCESLQSNATGEEIFNCINSFMQKHEIEWEKCVDVCSDASRAMDGKIAEAVTLIKYVAPESTSSHCLLYRHALAVKTMPTSLKNVLDQAVQIINYIKARPHQSRLLKILCEEMGAQHTALLLNTEVRWLSRGKVLVRLFELRRELLVFMDSAFRLSDCLTNSSWLLRLAYLADIFTKLNEVNLSMQGKNVTVFTVFDKMSSLLRKLEFWASSVEEENFDCFPTLSDFLTEINSTVDKNICSAIVQHLRGLRSTLLKYFPVTNDIHAWVRNPFTVTVKPASLVARDYESLIDLTSDSQVKQSFSELSLNDFWSSLIQEYPSVARRAVRVLLPFATMHLCETGFSYYAATKTKYRKRLDAAPHMRIRLSNITPNIKRICDKKTQKHCSH

May be derived from an ancient transposon that has lost its ability to translocate.

A4Z944

MIAHLLCILSYNFNTSVILNVYSKLTMFCTTNTLPMDLLLKQGSLKQEVESFCYQIVSESNDQKVGILQSENEQLQPSVSKKSEGELSRVKFMSSSNKITTFSKKPKRRKYDESYLSFGFTYFGNRDAPHAQCVLCKKILSNSSLAPSKLRRHLETKHAAYKDKDISFFKQHLDSPENNKPPTPKIVNTDNESATEASYNVSYHIALSGEAHTIGELLIKPCAKDVVMRMFDEQYSKKIDAVQLSNSTVARRIKDLAADIEEELVCRLKICDGFSLQLDESADVSGLAVLLVFVRYRFNKSIEEDLLLCESLQSNATGEEIFNCINSFMQKHEIEWEKCVDVCSDASRAMDGKIAEAVTLIKYVAPESTSSHCLLYRHALAVKIMPTSLKNVLDQAVQIINYIKARPHQSRLLKILCEEMGAQHTALLLNTEVRWLSRGKVLVRLFELRRELLVFMDSAFRLSDCLTNSSWLLRLAYLADIFTKLNEVNLSMQGKNVTVFTVFDKMSSLLRKLEFWASSVEEENFDCFPTLSDFLTEINSTVDKDICSAIVQHLRGLRSTLLKYFPVTNDNNTWVRNPFTVTVKPASLVARDYESLIDLTSDSQVKQNFSELSLNDFWSSLIQEYPSIARRAVRVLLPFATMHLCETGFSYYAATKTKYRKRLDAAPHMRIRLSNITPNIKRICDKKTQKHCSH

May be derived from an ancient transposon that has lost its ability to translocate.

Q9UBJ4

MIAPLLCILSYNFNTFAILNVYSKLTMFCTTNSLPMDLLLKQGSLKQEVESFCYQIVSESNDQKVGILQSEDKQLQPSVSKKSEGELSRVKFISNSNKITFSKKPKRRKYDESYLSFGFTYFGNRDAPHAQCVLCKKILSNSSLAPSKLRRHLETKHAAYKDKDISFFKQHLDSPENNKPPTPKIVNTDNESATEASYNVSYHIALSGEAHTIGELLIKPCAKDVVMRMFDEQYSKKIDAVQLSNSTVARRIKDLAADIEEELVCRLKICDGFSLQLDESADVSGLAVLLVFVRYRFNKSIEEDLLLCESLQSNATGEEIFNCINSFMQKHEIEWEKCVDVCSDASRAVDGKIAEAVTLIKYVAPESTSSHCLLYRHALAVKIMPTSLKNVLDQAVQIINYIKARPHQSRLLKILCEEMGAQHTALLLNTEVRWLSRGKVLVRLFELRRELLVFMDSAFRLSDCLTNSSWLLRLAYLADIFTKLNEVNLSMQGKNVTVFTVFDKMSSLLRKLEFWASSVEEENFDCFPTLSDFLTEINSTVDKDICSAIVQHLRGLRATLLKYFPVTNDNNAWVRNPFTVTVKPASLVARDYESLIDLTSDSQVKQNFSELSLNDFWSSLIQEYPSIARRAVRVLLPFATMHLCETGFSYYAATKTKYRKRLDAAPHMRIRLSNITPNIKRICDKKTQKHCSH

May be derived from an ancient transposon that has lost its ability to translocate. Contaminating sequence. Potential poly-A sequence.

A8WMM4

MPPKQAPSKKAENKRKEKVIEDKTFGLKNKKGNKNQKFVAQIENQVRNNNTRMDLVRQQEAAKKKEKDELLDIQNLLKPVEQKVAKDVDPKSLLCVFFKQGLCGKGAKCKFSHDLAVAQKTAKKNLYADSREVEKDETNENWDKEKLDEVVNKKNKGGHVIDIVCKYFLEAVENNKYGWFWECPNGGDKCQYRHCLPEGYVLKKDRKAMEAQKEDEISIEELVEKERAALNSKDLTKLTLQTFVAWKKKKLKERKEKEEADLKAKKEKIKSGKHNGMSGRDLFLFDANLINNDDDEAGDIEMEKEEVDENEKVFEIDANFFKFDGMDDELTNQMSNSTAAVSSVAGAVAKMDINEDLFDIDEDVGDLDSDSDED

Belongs to the ZC3H15/TMA46 family.

Q93618

MPPKQQGPSKKSEQKRKEKVIEDKTFGLKNKKGNKNQKFVAQVENQVRNNNTRMDLVRQQEAAKKKEKDELLDIANLLKPVEQKVAKDVDPKSLLCVFFKQGLCGKGAKCKFSHDLAVAQKTAKKNLYADSREVEKDEETNENWDSDKLNEVVNKKNKNKHMIDIVCKYFLEAVENNKYGWFWECPNGGEKCQYRHCLPEGYVLKKERKAMEQQKEDEISIEELVEKERAALSSKNLTKLTLQTFIAWKKKKLRERKEKEEADLKEKKEKIKSGKHNGMSGRDLFLYDANLVNNDDDEAGDIEMEKEEVDENEKVFEIDANFFKFDGMDDELTDQMSKSSTAVESTAKGMAKMDINEDLFDIDEDVENLDSDED

Belongs to the ZC3H15/TMA46 family.

Q5ZKM8

MPPKKQQQPAGSSKKADQKKKEKIIEDKTFGLKNKKGAKQQKFFKAVTHLVKFGQQYPRQAAQTESEKKLKKEDKKKELQELNELFKPVVAAQKISKGADPKSVVCAFFKQGQCTKGDKCKFSHDLSLERKCEKRSVYIDARDEDLEKDTMDNWDEKKLEEVVNKKHGEAEKKKPKTQIVCKYFLDAIENNKYGWFWVCPGGGDNCMYRHALPPGFVLKKDKKKEEKQDEISLEDLIEKERAALGPNVTKITLECFIAWKRRKRQEKIDKAEQDMERRKADFKAGKALVISGREVFEFRPELVDADDEEADDTRYTQGTGEDDEVEDPVCVNDVDLSLYVPKAVDETGITVASPERFSTYASIEKDDNKLSEASGGEINSSEQNDLEDRDGDEELENGVMDAVPVDENLFTGEDLDELEEELNTLDLEE

Protects DRG1 from proteolytic degradation. Interacts with DRG1. Belongs to the ZC3H15/TMA46 family.

Q803J8

MPPKKPAPAAANKKTQEKKKEKIIEDKTFGLKNKKGAKQQKFIKAVTQQVKFGQQNARQIAAAESEKTKKKDDKKKELSELNELFKPVVAAQKVSKGVDPKSVLCAFFKQGQCTKGDKCKFSHDLSLERKCEKRSLYVDGRDDELLEKDTMENWDEKKLEEVVNKKHGEAEKKKAKTQIVCKYFLDAIENNKYGWFWVCPGGGDNCMYRHALPVGFVLKKDKKNEEKNEEEISLEDLIETERSLLGANVTRITLETFLAWKKRKRQEKLAKAEQDMERKKADFKAGRALGVSGREVFEFRPELVDDDDEEADDTKYAEEDYNYGMSNQVEDTEEVQDIDIARFIPKEVDNAGITVASADRFTAKAPPTNDIDDNKLSEASGGTMENGEHSEDQTLEDGETNEESEAVPVDENLFTGEDLDELEEELNTLDLDE

Protects drg1 from proteolytic degradation. Interacts with drg1. Belongs to the ZC3H15/TMA46 family.

Q54DA5

MPPKQAQSKKTVEKEKKKKVEDKTFGLKNKNKSKKVAAYVSQVEAQVKHSGLQNKEAALKEKAKRDKELAEKAKKEAESILVNTIVQSKVPLGVDPKSIVCEYFKQGVTCPKGNRCKFAHDLAAGRKSEKIDIYTDRRKDEDTMENWDEAKLKSVVEKKRTTENKAKPTAIICKFFLDAIESKKYGWFWECPNGGEKCAYQHCLPEGYQLKKKKSREEDEVEEIPIEELIEEERAKLTKSTPVTLETFLRWKEEKRLQKEKAAKDAQDKRLADIKAGKTSMSGREMFVFNPDLFVDDESAIDTKSKEYEKSEEEIAALANQINTSLFTDGGVLPSDDDDDDDDDDDDDEDGDDEEEDDDEEEGEYEEEEASDE

Belongs to the ZC3H15/TMA46 family.

Q7JWR9

MPPKKAPPGPSKKTEQKKKEKVIEDKTFGLKNKKGNKQQKFIQQVQKQVQSGGQHPRQDGDKRKEEKEKKLAEQREMALIFKPVQTQKVEKGTDPKSVVCAFFKQGTCTKGDKCKFSHDLSQENKVEKRSIYVDMRDEDDPMTNWDDAKLKEVVEKKSSGEKQRPTTDIICKFFLEAVEKSKYGWFWECPNGGKCIYRHALPAGYVLKRDKKKEEKPTEISLVDLIEKERAALGPNQTRVTLESFLAWKKRKIAEKKAKLAAEEERKKSDFSKGKQFGISGREMFSFNPDLVDDGPMEEGDAAFDVYNREDDDDNAVEFKELDLAALSLAAKEVDGSGTIASTNRLLDQATEAAKTAAAEDAAADEDGPSSSAPANDAAPINKDLFVDLAGELDDLDLDDEDDD

Belongs to the ZC3H15/TMA46 family.

Q28Y69

MPPKKAPAGPSKKTEQKKKEKVIEDKTFGLKNKKGNKQQKFIQQVQKQVQAGGHHPRQDGDKKKDEKEKKLADLREMASIFKPVQTQKVDKGTDPKSVVCAFFKQGLCTKGDKCKFSHDLSLENKVEKRSMYVDMRDNEDDLMTNWDDAKLKEVVDKKHSEEKRRPTTEIICKFFLEAVEKSKYGWFWECPNGEKCIYRHALPPGYVLKRDKKKEDKPTEISLVDLIEKERAALGSNQTRVTLETFLAWKKRKLQEKKAKMVAEEERKKSDFSKGKQFGISGREMFSFNPDLVDDGPIEEGDAAFDVYKREDDDDDNAFEFKELDLAALSLAAKEVDGSGTIASSTRLLDQATEAAKTAAAEDGAASDDENPSSSAPANDAAPFNKDLFVDLAGELDDLDLDDEDD

Belongs to the ZC3H15/TMA46 family.

Q9P079

MPPKKQAQAGGSKKAEQKKKEKIIEDKTFGLKNKKGAKQQKFIKAVTHQVKFGQQNPRQVAQSEAEKKLKKDDKKKELQELNELFKPVVAAQKISKGADPKSVVCAFFKQGQCTKGDKCKFSHDLTLERKCEKRSVYIDARDEELEKDTMDNWDEKKLEEVVNKKHGEAEKKKPKTQIVCKHFLEAIENNKYGWFWVCPGGGDICMYRHALPPGFVLKKDKKKEEKEDEISLEDLIERERSALGPNVTKITLESFLAWKKRKRQEKIDKLEQDMERRKADFKAGKALVISGREVFEFRPELVNDDDEEADDTRYTQGTGGDEVDDSVSVNDIDLSLYIPRDVDETGITVASLERFSTYTSDKDENKLSEASGGRAENGERSDLEEDNEREGTENGAIDAVPVDENLFTGEDLDELEEELNTLDLEE

Protects DRG1 from proteolytic degradation (PubMed:19819225). Stimulates DRG1 GTPase activity likely by increasing the affinity for the potassium ions (PubMed:23711155). Interacts with DRG1; this interaction prevents DRG1 poly-ubiquitination and degradation by proteasome. DRG1-ZC3H15/DFRP1 complex co-sediments with polysomes. Associates with microtubules. The DRG1-DFRP2/ZC3H15 complex associates with polysomes. Belongs to the ZC3H15/TMA46 family.

Q9DAP2

MPPKKQAQAGGSKKAEQKKKEKIIEDKTFGLKNKKGAKQQKFIKAVTHQVKFGQQNPRQVAQSEAEKKLKKDDKKKELQELNELFKPVVAAQKISKGADPKSVVCAFFKQGQCTKGDKCKFSHDLTLERKCEKRSVYIDARDEELEKDTMDNWDEKKLEEVVNKKHGEAEKKKPKTQIVCRHFLEAIENNKYGWFWVCPGGGDNCMYRHALPPGFVLKKDKKKEEKEDEISLEDLIERERSALGPNVTKITLESFLAWKKRKRQEKIDKLEQDMERRKADFKAGKALVISGREVFEFRPELVNDDDEEADDTRYIQGTGGDEVDDSMGVNDIDISLYVPRDVEETGITVASVERFSTYAPDKDENKLSEASGGLAENGERSDLDEDSGGGGQENGSIDAVPVDENLFTGEDLDELEEELNTLDLEE

Protects DRG1 from proteolytic degradation (PubMed:15676025). Stimulates DRG1 GTPase activity likely by increasing the affinity for the potassium ions (By similarity). Interacts with DRG1; the interaction forms a polysomal DRG1-DFRP1/ZC3H15 complex which provides protein stability to DRG1 possibly by blocking poly-ubiquitination (PubMed:15676025). Associates with microtubules (By similarity). The DRG1-DFRP2/ZC3H15 complex associates with polysomes. By erythropoietin. Belongs to the ZC3H15/TMA46 family.

Q6U6G5

MPPKKQAQAGGSKKAEQKKKEKIIEDKTFGLKNKKGAKQQKFIKAVTHQVKFGQQNPRQVAQSEAEKKLKKDDKKKELQELNELFKPVVAAQKISKGADPKSVVCAFFKQGQCTKGDKCKFSHDLTLERKCEKRSVYIDARDEELEKDTMDNWDEKKLEEVVNKKHGEAEKKKPKTQIVCRHFLEAIENNKYGWFWVCPGGGDNCMYRHALPPGFVLKKDKKKEEKEDEISLEDLIERERSALGPNVTKITLESFLAWKKRKRQEKIDKLEQDMERRKADFKAGKALVISGREVFEFRPELVNDDDEEADDTRYIQGTGGDEVDDSVGVNDIDLSLYVPRDVEETGITVASLERFSTYASDKDENKLSEASGGLAENGERSDLDEDSGGGGQENGSIDAVPVDENLFTGEDLDELEEELNTLDLEE

Protects DRG1 from proteolytic degradation. Stimulates DRG1 GTPase activity likely by increasing the affinity for the potassium ions. Interacts with DRG1; the interaction forms a polysomal DRG1-DFRP1/ZC3H15 complex which provides protein stability to DRG1 possibly by blocking poly-ubiquitination. Associates with microtubules. The DRG1-DFRP2/ZC3H15 complex associates with polysomes. Ubiquitously expressed. By NGF in neuronal cells. Belongs to the ZC3H15/TMA46 family.

Q6DD06

MPPKKAPAAPQASKKTEQKKKEKIIEDKTFGLKNKKGAKQQKFIKNVTHQVKSGQQNPRLVAQAEGDKKNKKDDKMKELQELNDLFKPVVVAQKVSKGADPKSVVCAFFKQGQCTKGDKCKFSHDLSLERKCEKRSVYVDGRDDELEKDTMENWDEKKLEEVVNKKHGEAEKIKAKTQIVCKFFLEAIENNKYGWFWVCPGGGDTCMYRHALPPGFVLKKEKVKEDKDEDISLEDLIEKERAALGPNVTRITLESFLQWKKRKRADRILKLEEEMEKRKEDFKSGKSLGVSGREVFEFRPELINDDDEEADDASYTFELEDSEAEEIDDVQDIDLSRYVLKDVDETGITVASCERFSSYVASTEKDENKLCVASGGVMENENQSEEEQEGDLENGFVDAVPVDENLFTGEDMDELEEELYTLDLEK

Protects drg1 from proteolytic degradation. Interacts with drg1. Strongly expressed in ovary. Moderately expressed in brain, kidney, spleen, testis, intestine and colon. Weakly expressed in late gastrula. Strongly expressed from late neurula (stages 20-22) to tadpole (stages 40-41). At stage 22, expressed in blood islands, somites, eyes, trunk neural crest, mandibular crest segment, hyoid crest segment and branchial crest segment. At stage 32, expressed in otic vesicle, pronephros, forebraiin, midbrain, hindbrain, branchial arch, eyes, lens, spinal cord and notochord. Belongs to the ZC3H15/TMA46 family.

Q28F75

MPPKKAPAAPQSGKKTEQKKKEKIIEDKTFGLKNKKGAKQQKFIKNVIHQVKFGQQNPRLVAQAEGEKKTKKDDKKKELLELNDLFKPVVAAQKVSKGADPKSVVCAFYKQGQCTKGDKCKFSHDLSLERKCEKRSVYVDGRDEELEKDTMENWDEKKLEEVVNKKHGEAEKIKPKTQIVCKFFLEAIENNKYGWFWVCPGGGDMCMYRHALPPGFVLKKDKKKEEKDEEISLEDLIERERAGLGLNVTRITLESFLEWKKRKRQDRIVKLEEEMEKRKADFKAGKSLGISGREVFEFRPELINDDDEEADDTDYIFDKEDSDSETADDIKDIDLSRFVLKDVDETGITVASCERFSSYVISTEKDEEKLCVASGGEMENEDQSEEQQENDLENGFVDAVPVDENLFTGEDMDELEEELYTLDLEK

Protects drg1 from proteolytic degradation. Interacts with drg1. Belongs to the ZC3H15/TMA46 family.

Q7T3I0

MADEQEIMCKLENIKEIRNKTIQMEKIKSRLRTEFEALESEEKHLREYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSESDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLSQEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQAARKQDARQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKPDE

Plays a role in GABAergic and V2 interneurons differentiation (PubMed:26056227). Involved in motoneuron development and in neuromuscular junction formation (PubMed:23623388). Expressed throughout the developing central nervous system, but excluded from the most medial ventricular zone (PubMed:26056227). Larva with TALEN-induced zc4h2 null mutations show abnormally pectoral flexed fins, outward positioning of eyes, continuous swimming movements and balance problems at 5 days post-fertilization (dpf) (PubMed:26056227). Also exhibited an open mouth as well as continuous jaw movements (PubMed:26056227). Display a reduction in the number of V2 interneuron precursors in the hindbrain and spinal cord at 24 hours post-fertilization (hpf). Display a reduction in the number of GABAergic interneurons in the midbrain tegmentum at 35 hpf (PubMed:26056227).

Q9ULQ4

MADEQEIMCKLESIKEIRNKTLQMEKIKARLKAEFEALESEERHLKEYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSENDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLCEEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQVARKQDTRQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKQDE

Plays a role in interneurons differentiation (PubMed:26056227). Involved in neuronal development and in neuromuscular junction formation. Upon transfection into mouse primary hippocampal neurons, localizes at excitatory, but not inhibitory, postsynaptic sites. Expressed in fetal tissues, including in brain, intestine, lung, kidney and muscle (PubMed:23623388). Isoform 1 is expressed in numerous fetal brain regions. Isoform 3 is highly expressed in numerous fetal brain regions and spinal cord (PubMed:26056227). The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Extended N-terminus.

Q6ZPW6

MADEQEIMCKLESIKEIRNKTLQMEKIKARLKAEFEALESEERHLKEYKQEMDLLLQEKMAHVEELRLIHADINVMENTIKQSENDLNKLLESTRRLHDEYKPLKEHVDALRMTLGLQRLPDLCEEEEKLSLDYFEKQKAEWQTEPQEPPIPESLAAAAAAAQQLQVARKQDTRQTATFRQQPPPMKACLSCHQQIHRNAPICPLCKAKSRSRNPKKPKRKQDE

Plays a role in interneurons differentiation. Involved in neuronal development and in neuromuscular junction formation. Expressed in embryonic and adult brain and spinal cord. In all brain areas, expression levels are high during embryonic development and decrease postanatally.

Q9P0M8

MNSGRPETMENLPALYTIFQGEVAMVTDYGAFIKIPGCRKQGLVHRTHMSSCRVDKPSEIVDVGDKVWVKLIGREMKNDRIKVSLSMKVVNQGTGKDLDPNNVIIEQEERRRRSFQDYTGQKITLEAVLNTTCKKCGCKGHFAKDCFMQPGGTKYSLIPDEEEEKEEAKSAEFEKPDPTRNPSRKRKKEKKKKKHRDRKSSDSDSSDSESDTGKRARHTSKDSKAAKKKKKKKKHKKKHKE

Interacts with PNN. Associates with the 60S ribosomal subunit (By similarity).

Q95KF9

MSSCRVDKPSEIVDVGDKVWVKLIGREMKNDRIKVSLSMKVVNQGTGKDLDPNNVIIEQEERRRRSFQDYTGQKITLEAVLNTTCKKCGCKGHFAKDCFMQPGGTKYSLIPDEEEEKEEAKSAEFEKPVPTRNPSRKRKKEKKKKKHRDRKSSDSDSSDSESDTGKRARHTSKDSKAAKKKKKKKKHKKKHKE

May interact with PNN. May associate with the 60 S ribosomal subunit (By similarity).

Q9ESX4

MNSGRPETMENLPALYTIFQGEVAMVTDYGAFIKIPGCRKQGLVHRTHMSSCRVDKPSEIVDVGDKVWVKLIGREMKNDRIKVSLSMKVVNQGTGKDLDPNNVVIEQEERRRRSFQDYTGQKITLEAVLNTTCKKCGCKGHFAKDCFMQPGGTKYSLIPEEEEEKEEAKAEGLEKPDPTKNSSRKRKKEKKKKKHRDRKSSDCDSSDSESDTGKKARHSSKDSKATKKKKKKKKHKKKHKE

Interacts with PNN (By similarity). Associates with the 60S ribosomal subunit. Expressed in liver, brain, heart, kidney testis, stomach, small intestine, skin, thymus, uterus, placenta, spleen, lung and skeletal muscle. Less abundant than isoform 1.

P0CG32

MASITACVGNSRQQNAPLPPWAHSMLRSLGRSLCPLVVKMAERNMKLFSGRVVPAQGKETFENWLIQVNEVLPDWSMSEEEKLKRLMKTLRGPAREVMRLLQAANPNLSVADFLRAMKLVFGESESSVTAHGKFFNTLQAQGEKASLYVIRLEVQLQNAIQAGILAEKDANQTRLQQLLLGAELNRDLRFRLKHLLRMYANKQERLPNFLELIKMIREEEDWDDAFIKRKRPKRSEPIMERAASPVAFQGAQPIAISSADCNCNVIEIDDTLDDSDEDVILVVSLYPSLTPTGAPPFRGRARPLDQVLVIDSPNNSGAQSLSTSGGSGYKNDGPGNIRRARKRKYTTRCSYCGEEGHSKETCDNESNKAQVFENLIITLQELTHTEERSKEVPGEHSDASEPQ

Belongs to the ZCCHC12 family.

Q9DB17

MASLLARMGNSRRQNAAFMPFAHSMLRALGRSLGPLIANIAERNIQSFSGRAELGPGEETFENWLSQVHEVLPDWPMSEEEKIKRLMRTLRGPAREAMRLFQADNPNLNVAEFLRAMKLLFGASESSITAHGKFLSTLQAQGEKPSLYVIRLEVQLQNAIQAGVLPQSEANRTRLHQLLVGAELSRELRTKLKGLLQMHAHNEQENLPDFLELIRMIREEEDWDETFLRNKRPRRSETVMERAASPVVFQGSLPIVIGSADCNVIEIDDSQDDSDEDVILVEPEDPPLSSPGASSLRGTASTQEEMLIIESPDDFDEESPSTSSGSGQRNNGPGDLGRTRKRKYPIRCPHCGEEGHAKETCDNTSNKGQVFENLIVTLQELTHMERPKPSVPY

Belongs to the ZCCHC12 family.

Q9FYD4

MGFVYYVTLFVFIDDWVGLQSSAGKLNALLFSLLASLCLFSLSICVLVDPGRVPASYAPDVEDSGWSNSNVTETRKCDKCFAYKPLRTHHCRVCRRCVLKMDHHCLWINNCVGYANYKAFFILVFYATVASIYSTVLLVCCAFKNGDSYAGNVPLKTFIVSCGIFMIGLSITLGTLLCWHIYLITHNMTTIEHYDSKRASWLARKSGQSYRHQFDVGFYKNLTSVLGPNMIKWLCPTFTRNPEDGISFSASRDS

Palmitoyl acyltransferase. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q0VC89

MAPCTLWRCCQRTVGWVPVLFITFVVVWSYYAYVVELCVFTLSGNGENGKAVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFCLSNSEKERYEKEFSQERQQEILRRAARDLPIYTTSASKTVRYCERCQLIKPDRAHHCSACDMCILKMDHHCPWVNNCVGFSNYKFFLLFLFYSLLYCLFVATTVLQYFIKFWTNELTDTRAKFHVLFLFFVSTMFFISVLSLLSYHCWLVGKNRTTIESFRAPMFSYGTDGNGFSLGCSKNWRQVFGDEKKYWLLPVFSSQGDGCSFPTRLVGTDPEQASVSNQSESARSIGSNQPFPIKPLSESKNRLLDSDPQWLESGSEEGVGGSGTNNHVTVAIEN

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein] The DHHC domain is required for palmitoyltransferase activity. Autopalmitoylated (in vitro). Belongs to the DHHC palmitoyltransferase family.

Q6NVU8

MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVFTIFGNEENGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQEILRRAARALPIYTTSASKTIRYCEKCQLIKPDRAHHCSACDSCILKMDHHCPWVNNCVGFSNYKFFLLFLLYSLLYCLFVAATVLEYFIKFWTNELTDTRAKFHVLFLFFVSAMFFISVLSLFSYHCWLVGKNRTTIESFRAPTFSYGPDGNGFSLGCSKNWRQVFGDEKKYWLLPIFSSLGDGCSFPTRLVGMDPEQASVTNQNEYARSSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (PubMed:27153536, PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation (PubMed:27153536). Has a preference for acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245). (Microbial infection) Dominant palmitoyltransferase responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike protein. Through a sequential action with ZDHHC9, rapidly and efficiently palmitoylates spike protein following its synthesis in the endoplasmic reticulum (ER). In the infected cell, promotes spike biogenesis by protecting it from premature ER degradation, increases half-life and controls the lipid organization of its immediate membrane environment. Once the virus has formed, spike palmitoylation controls fusion with the target cell. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein] The DHHC domain is required for palmitoyltransferase activity. Autopalmitoylated (in vitro). Belongs to the DHHC palmitoyltransferase family.

Q9D3Q8

MAPWTLWRCCQRVVGWVPVLFITFVVVWSYYAYVVELCVSTISRTGEKGKTVVYLVAFHLFFVMFVWSYWMTIFTSPASPSKEFYLSNSEKERYEKEFSQERQQDILRRAARDLPIYTTSASKAIRYCEKCQLIKPDRAHHCSACDRCVLKMDHHCPWVNNCVGFTNYKFFMLFLLYSLLYCLFVAATVLEYFIKFWTLCRRKSTENCPKNEPTVLNFPSAKFHVLFLFFVSAMFFVSVLSLFSYHCWLVGKNRTTIESFRAPMFSYGIDGNGFSLGCSKNWRQVFGDEKKYWLVPIFSSLGDGCSFPARLVGMDPEQASVANQSDYVRSIGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGVTKSGTNNHVTVEIEN

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (PubMed:15603741). Catalyzes palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR, and modulates the duration of EGFR signaling by modulating palmitoylation-dependent EGFR internalization and degradation. Has a preference for acyl-CoA with C16 fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty acid chains (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-tetradecanoyl-L-cysteinyl-[protein] L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-octadecanoyl-L-cysteinyl-[protein] Highest levels in lung. The DHHC domain is required for palmitoyltransferase activity. Autopalmitoylated (in vitro). Belongs to the DHHC palmitoyltransferase family.

Q9FF67

MQRERMSKKKISQVHCIPSGDHILMTASSSKHIPHIRFYKAWKGNNRFCCGGRLIFGPDVSSLYLTSFLIGAPALTFCIRMLVWIKRGDPFFNYTVLASGFILTLLDFTFLMLTSARDPGIIPRNKTSMILEDDSDSSLTQSMEWVNNKTPNLKIPRTKDVFVNGYTIKVKFCDTCLLYRPPRASHCSICNNCVQRFDHHCPWVGQCIARRNYPFFICFISSSTLLCIYVFVFSWINLIRQPGKLWRTMSDDIVSVILIVYTFVAVWFVGGLTIFHFYLMSTNQTTYENFRYRYDKKENPYKRGLLKNVKEVLFAKIPPSQLDLRAMVPEEDDMTIASNDSEYESEYTSSVRYDTEMGGKLIKRDSPRKLPLPTRNLDDIKDISDNYDRSTTTREDASDRDPSFFSSQLDLPK

Palmitoyl acyltransferase. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Expressed in flowers and pollen. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

A2VDT6

MGLRIHFVVDPHGWCCMGLIVFVWLYNFFLIPKIVLFPHYEEGHIPGILIIIFYGIAMFCLVALVRASITDPGRLPENPKIPHGEREFWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVVRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEEISRPRKPWQQTFSEVFGTRWKILWFIPFRRRQPLRVPYHFANHV

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

A0A2R8RMA6

MKMRLHFVVDPMGWFCMSMVFFVWIYNSFLIPKLVLLPHYAEGHITAEPVICYYLASLLCFSALFRASTTDPGKLAQDPKIPLAERDNWELCNKCNMMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTQVLSFYTLVLDFCQYYYFLPLSSVDQADFAVHHELALLRVSCFMGLIMFGGISSLFYTQVKGILTDTTTIEKMSHLTEEVPRRPWQQAMAEVFGTRWKVLWFLPFRSRHPLKLNLTIRSHV

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Probably maternally supplied, the zygotic expression becomes significative at 4.0 hpf and remains constant until 24 hpf. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q5VWG1

MGLRIHFVVDPHGWCCMGLIVFVWLYNIVLIPKIVLFPHYEEGHIPGILIIIFYGISIFCLVALVRASITDPGRLPENPKIPHGEREFWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVFRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEDISRPRKPWQQTFSEVFGTRWKILWFIPFRQRQPLRVPYHFANHV

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:22031296). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane (PubMed:22031296). This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (PubMed:22031296). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Widely expressed. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q80XQ3

MGLRIHFVVDPHGWCCMGLIVFVWLYNIVIIPKIVLFPHYEEGHIPGILIIIFYGISIFCLVALVRASLTDPGRLPENPKIPHAERELWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVVRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEEISRPRKPWQQTFSEVFGTRWKILWFIPFRQRQPLRVPYHFANHV

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (PubMed:19956733, PubMed:26715683, PubMed:27653213). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation (PubMed:19956733). Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium (PubMed:27653213). Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction (PubMed:26715683). May also palmitoylate eNOS and LCK (PubMed:19956733). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Widely expressed (PubMed:26715683). Expressed in Henle's layer within the hair bulb and the hair shaft cuticle (at protein level) (PubMed:19956733). Expression is limited to the post-mitotic lineages of inner root sheath (IRS) and cuticle (PubMed:19956733). In the developing skin, expression is not be detected prior to hair follicle induction (13 dpc). Expression is initially detected in the inner root sheath (IRS) of developing vibrissae follicles at 16 dpc and later in the developing IRS of 18.5 dpc pelage follicles. The DHHC domain is required for palmitoyltransferase activity. Defects in zdhhc21 are the cause of the depilated (dep) phenotype. It is a recessive phenotype characterized by variable hair loss, with thinner and shorter hairs remaining in a greasy coat which is due to a defect in the epidermis, rather than the dermis (PubMed:19956733). Depilated (dep) mutant mice are protected against endothelial dysfunction in systemic inflammatory response syndrome (PubMed:27653213). They are also tachycardic and hypotensive (PubMed:26715683). Belongs to the DHHC palmitoyltransferase family.

Q5RB84

MGLRIHFVVDPHGWCCMGLIVFVWLYNIVLIPKIVLFPHYEEGHIPGILIIIFYGISIFCLVALVRASITDPGRLPENPKIPHGEREFWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVFRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEDISRPRKPWQQTFSEVFGTRWKILWFIPFRQRQPLRVPYHFANHV

Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates (By similarity). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q0WQT8

MSSEIEVVEEIQSNPKENGESSSKGIEEESLKNDVYTAAAYGDLEKLHRLVECEGSSVSEPDALGYYALQWSALNNRVAVAQYLIEHGGDVNATDHTGQTALHWSAVRGAIQVAELLLQEGARVDATDMYGYQATHVAAQYGQTAFLCHVVSKWNADPDVPDNDGRSPLHWAAYKGFADSIRLLLFLDAYRGRQDKEGCTPLHWAAIRGNLEACTVLVQAGKKEDLMITDKTGLTPAQLAAEKNHRQVSFFLGNARSLLEKRCDGSSPLGRLSKLGLAPVLWIMILLLLLVYTNSVVLASNLPKLTTGIGALAWLGFILATAGLFLFYRCSRKDPGYIRMNIHDPQTMKDDEPLLKIELNNPALLAGNWTQLCATCKIIRPLRAKHCSTCDRCVEQFDHHCPWVSNCVGKKNKWEFFLFLLLEVLAMLITGGVTLARVLSDPSAPSSFGAWMSHVASNHVGALSFLLVEFCLFFSVAVLTVIQASQISRNITTNEMANALRYSYLRGPGGRFRNPYDLGCRRNCSDFLVKGYNEDIECHEEDATQRPEGISMMQMQRNPNLQNGNGHVAIDVNPTHNSQSAHVHSANCSHSHNSKSKSDNVPLGLGLGLSRNPTRPVVSP

Palmitoyltransferase involved in cell growth regulation. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Expressed in root, leaf, inflorescence stem, pollen and floral tissue. The DHHC domain is required for palmitoyltransferase activity. Plants have defects in root hair growth and pollen tube germination. Belongs to the DHHC palmitoyltransferase family.

X1WBB5

MGKLKLLNTIAPAYFYAATVVTFALHFLLFTPTIFQSSDVTINPAMLAHISIFLFLMGNALGNYIMTIRNPSESANETVIPVCSPDCPDRIDAHYLLNGRHFCKVCKKVILKRDHHCFFTGNCIGNRNMRYFIMFSIYTSSSCLYSLVIGVAYLTIEYSISFENPLTFLTLLPLSTGYFFLGLISGLQFFLVIMLYIWLGIGLVSVGFCCQQLLLVARGQTWCELQKGQLSECRGTWRANLTDVFGSHWVLGLFVPVPTVETVPGNWQVYHDHKHD

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Probably maternally supplied, the zygotic expression becomes significative at 4.0 hpf and remains constant until 24 hpf. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q149P4

MLALRLLNVVAPAYFLCISLVTFVLQLFLFLPSMREDPAAARLFSPALLHGALFLFLSANALGNYVLVIQNSPDDLGACQGASARKTPCPSPSTHFCRVCARVTLRHDHHCFFTGNCIGSRNMRNFVLFCLYTSLACLYSMVAGVAYISAVLSISFAHPLAFLTLLPTSISQFFSGAVLGSEMFVILMLYLWFAIGLACAGFCCHQLLLILRGQTRHQVRKGVAVRARPWRKNLQEVFGKRWLLGLLVPMFNVGSESSKQQDK

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (PubMed:22399288). Catalyzes the palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (PubMed:22399288). Might also mediate palmitoylation of CNN3 (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with CNN3. Widely expressed. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

A0PK84

MLALRLLNVVAPAYFLCISLVTFVLQLFLFLPSMREDPTATPLFSPAVLHGALFLFLSANALGNYVLVIQNSPDDLGTCQGTMSQRPQCPPPSTHFCRVCSRVTLRHDHHCFFTGNCIGSRNMRNFILFCLYTSLACLYSMVAGVAYISAVLSISFAHPLAFLTLLPTSISQFFSGAVLGSDMFVILMLYLWFAVGLACAGFCCHQLLLILRGQTRYQVRKGMAVRARPWRKNLQEVFGKRWLLGLLVPMFNVGTESSKQQDK

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (By similarity). Catalyzes the palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By similarity). Might also mediate palmitoylation of CNN3 (Probable). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with CNN3. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q2TGI8

MLALRLLNVVAPAYFLCISLVTFVLQLFLFLPSMREDPTATPLFSPAVLHGALFLFLSANALGNYILVVQNSPDDLGACQGTSSQRPQRPPPSTHFCRVCARVTLRHDHHCFFTGNCIGSRNMRNFILFCLYTSLACLYSMVAGVAYISAVLSISFAHPLAFLTLLPTSISQFFSGAVLGSDMFVILMLYLWFAVGLACAGFCCHQLLLILRGQTRYQVRKGVAVRARPWRKNLQEVFGKRWLLGLLVPMFNVGTESSKQQDK

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (By similarity). Catalyzes the palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By similarity). Might also mediate palmitoylation of CNN3 (By similarity). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with CNN3. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q9FLM3

MYVVTPPQRSGFGSDCDLRVYQTWKGSNIFCLQGRFIFGPDVRSLGLTISLIVAPVTIFCIFVASKLMDDFSDSWGVSIILVAVVFTIYDLILLMLTSGRDPGIIPRNSHPPEPEVVDGNTGSGTSQTPRLPRVKEVEVNGKVFKVKYCDTCMLYRPPRCSHCSICNNCVERFDHHCPWVGQCIAQRNYRFFFMFVFSTTLLCVYVFAFCCVYIKKIKESEDISILKAMLKTPASIALILYTFISTFFVGGLTCFHLYLISTNQTTYENFRYSYDRHSNPHNKGVVDNFKEIFFSPIPPSKNNFRAMVPRENPMPSRSVVGGFMSPNMGKANDDIEMGRKGVWAMAEHGDGKDGNNNERFHVNDNELNELSPDMGNIVNGDEQINRPNNHPRNANWEMSPEVMALSARRA

Palmitoyl acyltransferase. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] A number of isoforms are produced. According to EST sequences. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

D3DN76

MTQKGSMKPVKKKKTEEPELEPLCCCEYIDRNGEKNHVATCLCDCQDLDEGCDRWITCKSLQPETCERIMDTISDRLRIPWLRGAKKVNISIIPPLVLLPVFLHVASWHFLLGVVVLTSLPVLALWYYYLTHRRKEQTLFFLSLGLFSLGYMYYVFLQEVVPKGRVGPVQLAVLTCGLFLILLALHRAKKNPGYLSNPASGDRSLSSSQLECLSRKGQEKTKGFPGADMSGSLNNRTTKDDPKGSSKMPAGSPTKAKEDWCAKCQLVRPARAWHCRICGICVRRMDHHCVWINSCVGESNHQAFILALLIFLLTSVYGITLTLDTICRDRSVFTALFYCPGVYANYSSALSFTCVWYSVIITAGMAYIFLIQLINISYNVTEREVQQALRQKTGRRLLCGLIVDTGLLG

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (Probable). Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with NOS1. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q3UVA2

MKPVKKKKTEEPELEPLCCCEYIDRNGEKNHVAACLCDCQDLDEGCDRWLTCQSLRPETCERITDTISDRLRIPWLRGAKKVNISIVPPLVLLPVFLHVASWHFLLGVVVLTSLPMLALWYYYLTHRRKEQTLFFLSLGLFSLGYMYYVFLREVVPQGRVGPTQLALLTCGLLLILLALYRAKKNPGYLSNDKSPSNSQIECPVKKGQEKTKGFPGTDASGSLNNRTLKDDVRGSSRVGLDSPAKVKEDWCAKCQLVRPARAWHCRICGICVRRMDHHCVWINSCVGESNHQAFILALSIFLLTSVYGISLTLNTICRDRSLFTALFYCPGVYANYSSALSFTCVWYSVIITAGMAYIFLIQLINISYNVTEREVQQALRQKTGRRLLCGLIVDTGQYNRGFLRNWLQFSTLGTHTVHTPAEDIV

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with NOS1. Neuronal soma and dendrites. Expressed in the brain. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q2TGI7

MKPVKKKKTEEPELEPLCCCEYIDRNGEKNHVAACLCDCQDLDEGCDRWLTCKSLRPETCERITDTISDRLRIPWLRGAKKVNISILPPLVLLPVLLRVASWHFLLGVVVLTSLPMLALWYYYLTHRRKEQTLFFLSLGLFSLGYMYYVFLQEVVPQGHVGPAQLALLTCGLFLILVALYRAKKNPGYLSNPACNDKSPSNSQIECPIKKGQEKTKGFPGTDTSGSLNNRTLKDDAKGSSRVGLDSPAKSKEDWCAKCQLVRPARAWHCRICGICVRRMDHHCVWINSCVGESNHQAFILALSIFLLTSVYGISLTLNTICRDRSLFTALFYCPGVYANYSSALSFTCVWYSVIITAGMAYIFLIQLINISYNVTEREVQQALRQKTGRRLLCGLIVDTGQYNRGFLRNWLQFSTLGTRTVHTPAEDIV

Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (Probable). Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By similarity). May be involved in NOS1 regulation and targeting to the synaptic membrane (PubMed:15105416). hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with NOS1. Neuronal soma and dendrites. Expressed in the brain (at protein level), with highest levels in olfactory bulb, piriform cortex and hippocampus. Highly expressed during the first week after birth. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q9FGA9

MAGRVFEAWKGSNKFLFGGRLIFGPDAWSIPFTFLLIITPVCFFSVFVATHLRRELLPNNAGHVFLVAGVLFTVFVLILLFLTSARDPGIVPRNSHPPEEELCYDTTVSSDGRQTPTVQIPRTKEVMVYGVSVRVKYCDTCMLYRPPRCSHCSICNNCVERFDHHCPWRNYRYFFMFVSSATILCIYIFSMSALYIKVLMDNHQGTVWRAMRESPWAVMLMIYCFISLWFVGGLTGFHLYLISTNQTTYENFRYRSDNRINVYNRGCSNNFFETFCSKVKPSRNDFRAFIKEEPPRNITLATTWERPEEADEENREERRQKVEDDLDIDEDVMKLQQRLNDEEGSDTAHHKIDIDQMRIGSNERAPTIRSEARHGNWGARSNAQEEDVIAGSSVRESRSYAAAEEGR

Palmitoyl acyltransferase. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Mainly expressed in seeds. The DHHC domain is required for palmitoyltransferase activity. Belongs to the DHHC palmitoyltransferase family.

Q9V3F1

MSAQGEGGGAGGSGGGGAGSDGGGNAGQSSTGSGTVAVTNGGNSSAKNQLPLTPRFTAEEKEVLYTLFHLHEEVIDIKHRKKQRNKYSVRETWDKIVKDFNSHPHVSAMRNIKQIQKFWLNSRLRKQYPYRDGSSSNLSSGSAKISSVSVSVASAVPQQQQQQHHQQHDSVKVEPEYQISPDASEHNPQADTFDEIEMDANDVSEIDEDPMEQQQQQQQEAQAQAQAQAQAQAQVQSAAAEMQKMQQVNAVAAAAAANATMINTHQINVDQISAEKLTLNDLLHFKTARPREEIILIKHPEATATQIHTIPTQAQQHPMATITAGGYNQQIISEIKPQQITLAQYQAQQQQQAQAQAQAQAQAQAQAQAQAQAQAQAQQLAQQQLAAAQHQQLAAAVQVHHQQQQQQQAAVAVQQQQAAAAAAVKMQLTAATPTFTFSALPTVTAATTVPAAVPVPVATASSGSANSVAVNTSTASSVSINNTSLGGGGGNGATNSSATAADSFEERMNYFKIREAELRCKEQQLATEAKRIELNKAQDELKYMKEVHRLRVEELTMKIRILQKEEEQLRKCSTS

Involved in transvection phenomena (= synapsis-dependent gene expression), where the synaptic pairing of chromosomes carrying genes with which zeste interacts influences the expression of these genes. Zeste binds to DNA and stimulates transcription from a nearby promoter. Self-associates forming complexes of several hundred monomers.

Q24762

MSAAGDAGAGAANGSNNVAVVQATVSVSGNISVGDGSPNNNNNNNANGNTNGNSNNNGSTAGSSKGQLPLTPRFTAEEKDVLYTLFHLHEEVIDIKHRKKQRNKYSVRDTWDKIVRDFNSHPHVSAMRNIKQIQKFWLNSRLRKQYPYRDGSASGGSAGLGKVGTVSASAQQQQQQQQQQQQQQQQQHHDSVKVEPEYQISPEASEHNPQGEPFDEIEMDGNDVSEMEDDPLEAQQQQQQQQQQQQQAAAQAQAEAQQQQQQQSAVAEMQKLQVSAAVAAANASMLNTHRINVDSISAEKLTLNDLLHFKPARHDEIILQIKHPTDATATQIHTIPAQPQQHTMATITAGGYNQQIISEIKPQQITLAQYQAQQHQQAQARLRPGQAQQLAQQQLAAQQQQLAVAAAAAHQQQNSSSAAAVVVQQHQQQQQQQQHQQQQQQQQVQQQQQQQQQAAAAAAAVKMQLTGGTPTFTFSALPTVTAATSVPVTVPVPVTVPVTAAPAAVSNVSVSGAGTLPTGAQQQLQLQQQQQQQQQQQQQQQQAGDSYEERINYFKVKEAELRCKEQQLATEAKKIELNKAQDELKYMREVHRLRVEELKMKIRILQKEEEQLQKCSST

Involved in transvection phenomena (= synapsis-dependent gene expression), where the synaptic pairing of chromosomes carrying genes with which zeste interacts influences the expression of these genes. Zeste binds to DNA and stimulates transcription from a nearby promoter (By similarity). Self-associates forming complexes of several hundred monomers.

Q93ZP0

MKRICSVSSVQLFSRSFRALASPRSLNYPLQCIKRSSVRMESSNFSSGVRTESSVKPRGALIVLEGLDRSGKSTQCAKLLSFLNGLGHPTELWRFPDRETSVGQMISAYLSNKSQLDDHTIHLLFSANRWEKRSLMEEKLKTGTTLIVDRYSYSGVAFSSAKGLDIEWCKAPEIGLLAPDSVLYLDISPERAAERGGYGDERYERVEFQKKVADFYQTLGDSSWKIINASDAMEEVEKKIQQVVLDQVKECTEGKPLSLLWSS

Catalyzes the conversion of dTMP to dTDP (Probable). Involved in the regulation of DNA replication. Is essential to promote the first division of the zygote (PubMed:18036198). ATP + dTMP = ADP + dTDP Pyrimidine metabolism; dTTP biosynthesis. Expressed in root, rosette leaves, flower buds, flowers and siliques. Cell cycle regulated. Up-regulated at the G1/S phase transition and then decreases rapidly as cells progress into S-phase. Not up-regulated during the male and female gametophytic mitoses. Embryonic lethality when homozygous, due to arrest of the embryo sac development soon after fertilization. Belongs to the thymidylate kinase family.

Q6PGE4

MAALQSAPDSPATQLEPAEDGSECDADPEEEEEEEQQEEEDEEEEEEVVVEEVATPVQEVAEVEVEANSADNGGGDDDDDGGGGDDDVEEVLAEEQTLSLGTQERHSNGGHAKAPVLQGKALQTSRVSPTTQDEDVEEEEEEEDEEHFLTQGLVTFEDVAVYFSLEEWERLGVDQRDLYREVMQENYGILVSLGYPIPKPDLIFHLEQGEEPWVEDGPHPEEGDVVTGVYTGAWFWNDDIEDHEEEDDEDFLAEVAEEENEPPGLWSAAYGVGDVPGTWGPDDSDSVQTPEGWGPNPGSLGILAEEVEAKHFLSGREPGENFLVPWAFPAVAVPIGCPETTCDVCGKVFPHRSRLAKHQRYHAAVKPFGCDECGKGFVYRSHLAIHQRTHTGEKPFPCPDCGKRFVYKSHLVTHRRIHTGERPYRCVFCGAGFGRRSYLVTHQRTHTGERPYPCLHCGRSFSQSSALARHQAVHTADRPHCCPDCGQAFRLRADFQRHRRSGGCTEPSSGDGARMAPHEVGMAPNEVEMAVAAVATVEPEELEAAPAETEEPEAGVADGDTEAEARQDEQVVVAPAAEATVPDSKKDPEPDRRFREMGNGLAEGEGPSSHPFGFHFPMHPKSWLHPDGFPILGFPEFSERLQADGRHLPGPLGSPLSLQGMGLACDPFRSVGPGAGVDGGLRAFPPAVRSLLSEPAPAALAEEESPWICSDCGKTFGRRAALAKHQRYHAGERPHRCADCGKSFVYGSHLARHRRTHTGERPFPCPECGARFARGSHLAAHVRGHTGEKPFVCGVCGAGFSRRAHLTAHGRAHTGERPYACAECGRRFGQSAALTRHQWAHAEEKPHRCPDCGKGFGHSSDFKRHRRTHTGEKPFRCADCGRGFAQRSNLAKHRRGHTGERPFPCPECGKRFSQRSVLVTHQRTHTGERPYLCSNCGRRFSQSSHLLTHMKTHRGPGSAPAHTSSTKAQAPAKATPPLPPPGSGSGTLLEFAGGTSFGSDPAAFAGPSGSYEESIL

May be involved in transcriptional regulation. Belongs to the krueppel C2H2-type zinc-finger protein family.

Q9NVH4

MNASSEGESFAGSVQIPGGTTVLVELTPDIHICGICKQQFNNLDAFVAHKQSGCQLTGTSAAAPSTVQFVSEETVPATQTQTTTRTITSETQTITVSAPEFVFEHGYQTYLPTESNENQTATVISLPAKSRTKKPTTPPAQKRLNCCYPGCQFKTAYGMKDMERHLKIHTGDKPHKCEVCGKCFSRKDKLKTHMRCHTGVKPYKCKTCDYAAADSSSLNKHLRIHSDERPFKCQICPYASRNSSQLTVHLRSHTASELDDDVPKANCLSTESTDTPKAPVITLPSEAREQMATLGERTFNCCYPGCHFKTVHGMKDLDRHLRIHTGDKPHKCEFCDKCFSRKDNLTMHMRCHTSVKPHKCHLCDYAAVDSSSLKKHLRIHSDERPYKCQLCPYASRNSSQLTVHLRSHTGDTPFQCWLCSAKFKISSDLKRHMIVHSGEKPFKCEFCDVRCTMKANLKSHIRIKHTFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSSAAALRVHSRVHCKDRPFKCDFCSFDTKRPSSLAKHVDKVHRDEAKTENRAPLGKEGLREGSSQHVAKIVTQRAFRCETCGASFVRDDSLRCHKKQHSDQSENKNSDLVTFPPESGASGQLSTLVSVGQLEAPLEPSQDL

May be involved in the regulation of mesenchymal cell differentiation through transactivation of NOTCH1 target genes. Interacts with ZNF70; this interaction promote the transactivation of the HES1 gene (PubMed:27353377). Interacts with NOTCH1 (PubMed:27353377). Belongs to the krueppel C2H2-type zinc-finger protein family. Translation C-terminally extended.

Q5QPL4

MLQQLLITLPTEASTWVKLRHPKAATERVALWEDVTKMFKAEALLSQDADETQGESLESRVTLGSLTAESQELLTFKDVSVDFTQEEWGQLAPAHRNLYREVMLENYGNLVSVGCQLSKPGVISQLEKGEEPWLMERDISGVPSSDLKSKTKTKESALQNDISWEELHCGLMMERFTKGSSMYSTLGRISKCNKLESQQENQRMGKGQIPLMCKKTFTQERGQESNRFEKRINVKSEVMPGPIGLPRKRDRKYDTPGKRSRYNIDLVNHSRSYTKMKTFECNICEKIFKQLIHLTEHMRIHTGEKPFRCKECGKAFSQSSSLIPHQRIHTGEKPYECKECGKTFRHPSSLTQHVRIHTGEKPYECRVCEKAFSQSIGLIQHLRTHVREKPFTCKDCGKAFFQIRHLRQHEIIHTGVKPYICNVCSKTFSHSTYLTQHQRTHTGERPYKCKECGKAFSQRIHLSIHQRVHTGVKPYECSHCGKAFRHDSSFAKHQRIHTGEKPYDCNECGKAFSCSSSLIRHCKTHLRNTFSNVV

May be involved in transcriptional regulation. Essential for Golgi structural integrity (PubMed:29851555). Up-regulated by Golgi stress-inducing agent nigericin. Belongs to the krueppel C2H2-type zinc-finger protein family. Truncated N-terminus.

Q9H810

MAELDIGQHCQVEHCRQRDFLPFVCDDCSGIFCLEHRSRESHGCPEVTVINERLKTDQHTSYPCSFKDCAERELVAVICPYCEKNFCLRHRHQSDHECEKLEIPKPRMAATQKLVKDIIDSKTGETASKRWKGAKNSETAAKVALMKLKMHADGDKSLPQTERIYFQVFLPKGSKEKSKPMFFCHRWSIGKAIDFAASLARLKNDNNKFTAKKLRLCHITSGEALPLDHTLETWIAKEDCPLYNGGNIILEYLNDEEQFCKNVESYLE

Plays a role in the regulation of cytoplasmic stress granules (SGs) turnover. SGs are dynamic and transient cytoplasmic ribonucleoprotein assemblies important for cellular protein homeostasis when protein production is suspended after acute exogenous stress (PubMed:29804830). Associates with SGs and is involved in the efficient and specific arsenite-induced clearance process of SGs through the recruitment of the ubiquitin-selective ATPase VCP and the 26S proteasome (PubMed:29804830). This process requires both complexes for efficient degradation of damaged ubiquitinated SG proteins during recovery from arsenite stress, and hence avoiding aberrant cytoplasmic SGs degradation via autophagy (PubMed:29804830). Associates with the 26S proteasome; this association occurs upon exposure to arsenite and is reduced in the presence of ATP (PubMed:29804830). Interacts (via AN1-type 1 and 2 zinc fingers) with PSMD1; this interaction is increased upon arsenite treatment and occurs in an ATP-independent manner (PubMed:29804830). Interacts with PSMC4 (PubMed:29804830). Interacts with PSMA1 (PubMed:29804830). Interacts (via its ubiquitin-like region) with VCP; this interaction occurs in an arsenite-dependent manner and is necessary for the recruitment of the ubiquitin-selective ATPase VCP to stress granules (SGs) (PubMed:29804830). Colocalizes with TIA1, G3BP1, VCP and 26S proteasome in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment in a VCP-independent manner (PubMed:29804830). Not localized in SGs in response to other heat- oxidative- or osmotic-induced stress treatments. Colocalizes with VCP in cytoplasmic speckles (PubMed:29804830). The ubiquitin-like region is necessary for its localization to stress granules (SGs) in a VCP-independent manner (PubMed:29804830). The AN1-type 1 and 2 zinc finger domains are necessary for the recruitment of the 26S proteasome to SGs (PubMed:29804830). Both the AN1-type 1 and 2 zinc finger domains and the ubiquitin-like region are necessary for efficient SGs clearance upon specific arsenite-induced responses (PubMed:29804830).

Q9D7H5

MAELDIGQHCQVQHCRQRDFLPFVCDGCSGIFCLEHRSKDSHGCSEVNVVKERPKTDEHKSYSCSFKGCTDVELVAVICPYCEKNFCLRHRHQSDHDCEKLEVAKPRMAATQKLVRDIVDAKTGGAASKGRKGAKSSGTAAKVALMKLKMHADGDKSLPQTERTYFQVYLPKGSKEKSKAMFFCLRWSIGKVVDFAASLANLRNENNKLTAKKLRLCHVPSGEALPLDHTLERWITKEECPLYNGGNVILEYLNDEEQFLKNVDSYLE

Plays a role in the regulation of cytoplasmic stress granules (SGs) turnover. SGs are dynamic and transient cytoplasmic ribonucleoprotein assemblies important for cellular protein homeostasis when protein production is suspended after acute exogenous stress. Associates with SGs and is involved in the efficient and specific arsenite-induced clearance process of SGs through the recruitment of the ubiquitin-selective ATPase VCP and the 26S proteasome. This process requires both complexes for efficient degradation of damaged ubiquitinated SG proteins during recovery from arsenite stress, and hence avoiding aberrant cytoplasmic SGs degradation via autophagy. Associates with the 26S proteasome; this association occurs upon exposure to arsenite and is reduced in the presence of ATP. Interacts (via AN1-type 1 and 2 zinc fingers) with PSMD1; this interaction is increased upon arsenite treatment and occurs in an ATP-independent manner. Interacts with PSMC4. Interacts with PSMA1. Interacts (via its ubiquitin-like region) with VCP; this interaction occurs in an arsenite-dependent manner and is necessary for the recruitment of the ubiquitin-selective ATPase VCP to stress granules (SGs). Colocalizes with TIA1, G3BP1, VCP and 26S proteasome in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment in a VCP-independent manner. Not localized in SGs in response to other heat- oxidative- or osmotic-induced stress treatments. Colocalizes with VCP in cytoplasmic speckles. The ubiquitin-like region is necessary for its localization to stress granules (SGs) in a VCP-independent manner. The AN1-type 1 and 2 zinc finger domains are necessary for the recruitment of the 26S proteasome to SGs. Both the AN1-type 1 and 2 zinc finger domains and the ubiquitin-like region are necessary for efficient SGs clearance upon specific arsenite-induced responses.

Q8R3V1

MGDAGSERSKAPSLPPRCPCGFWGSSKTMNLCSKCFADFQKKQPDDDSTPSTSNSQSDLFSEETTSDNNNTSVTTPTLSPSQQSLPTELNVTSPSTEECGPCTDTAHVSLITPTKRSCGADSQSENEASPVKRPRLVENPERPEESGRSKQKSRRRCFQCQTKLELVQQELGSCRCGYVFCMLHRLPEQHDCTFDHMGRGREEAIMKMVKLDRKVGRSCQRIGEGCS

Expressed in testis. Preferentially expressed during the haploid stages of spermatogenesis.

Q5VVY5

MDNRKEPPFFNDDNMGPFYYRLHFCDTMELFIETLTGTCFELRVSPFETVISVKAKIRRLEGIPICRQHLIWNNMELENDYCLNDYNISEGCTLKLVLAMRGGPINTRRVPTDDPLRKMAEYLDSSRVEVWEKTSCSKQVTFLVYQEGDQLNFFPAVDRGDGTLTPLSDSSKKIDFHLHVLRRKGEHRMSGGSMYNSDTDEDEETEPSSSGQQIIENSITMNKMKLLKAKMKNMNLSKKPKKAVKIKPHPPVAPRPSSGSTAPSRHRLLRVLPNIGQSCSPAFGNAYPPEISRNGISSLATQLSAERYISSITGEFLKEDNSWENNTLSHFSSNVKLPPQIPHLELGNDQELADSVLHLGSSLPRQTKHFLGNLPSSNGNIVLPSEECVTEQSLLPKVGSLASFAEGNADEQSSGLEGACKVNLELLLTNADKGLKAPEQHLKHVAGVLNGESVETSVLNYRELSPHKNRLLSPLRCSAPMSLHNSLVKPERQSKCFEFGKLQPSSSQSLDVQNITDSSFSRTTCFQGVKVDSLGKRSDVISKVEARDITEMTNKASKEPVGCVNNISFLASLAGSTSRNRLQSTRGAGRLQNSGTGLSTNLQHFQEENFRKSSPQLEHTGVFLSTHGVGMNGNNAAAGKSVGECTTHHLPPVKAPLQTKKKTTNHCFLCGKKTGLASSYECRCGNNFCASHRYAETHGCTYDYKSAGRRYLHEANPVVNAPKLPKI

A report observed N-glycosylation at Asn-235 (PubMed:19139490). However, as the protein is not predicted to localize in an extracellular compartment of the cell, additional evidence is required to confirm this result.

A8K484

MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI

Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. Interacts with ubiquitin and polyubiquitinated proteins. Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity). Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain). Highly expressed in skeletal muscle. Expressed in fetal cochlea. Also expressed in infant brain, fetal heart, pancreatic islet, melanocyte, pineal gland, placenta, corneal stroma, and parathyroid tumor. Weakly expressed or undetectable in adult brain, heart, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocytes. Expressed in rhabdomyosarcoma RD cells (at protein level). The A20-type zinc finger directly binds polyubiquitin chains and associates with the 26S proteasome. The zinc-finger A20-type domain is essential for inhibition of NF-kappa-B activation (By similarity).

Q3B7K8

MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADAGLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI

Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation. Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain) (By similarity). Interacts with ubiquitin and polyubiquitinated proteins. Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity). Expressed in brain, muscle, eye, and heart, lower expression in lung, kidney, and spleen, and very low expression in liver. Expressed in myoblast C2C12 cells (at protein level). Up-regulated after TNFSF11 stimulation. Expression also induced by other cytokines such as TNF and IL1B. No significant inhibitory effect on the NF-kappa-B pathway is observed. Expression is increased in both denervation- and fasting-induced muscle atrophy. The A20-type zinc finger directly binds polyubiquitin chains and associates with the 26S proteasome. The zinc-finger A20-type domain is essential for inhibition of NF-kappa-B activation. Resistance to muscle atrophy accompanied by abnormal accumulation of polyubiquitinated proteins in skeletal muscle.

B5DF11

MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADATLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITSPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI

Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation (By similarity). Homooligomer and/or heterooligomer. Interacts (via A20-type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain) (By similarity). Interacts with ubiquitin and polyubiquitinated proteins. Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule. The A20-type zinc finger directly binds polyubiquitin chains and associates with the 26S proteasome. The zinc-finger A20-type domain is essential for inhibition of NF-kappa-B activation (By similarity).

Q3SZY7

MAQETNHSQVPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQNSSNGRISPPAPSVTSLSESLPVQCTDGSVPEAQSALDSTASSVQPSPVSNQSLLSESVASSQVDSTSVDKAIPETEDLQASVSETAQQASEEQSKSLEKPKQKKNRCFMCRKKVGLTGFECRCGNVYCGVHRYSDVHNCSYNYKADAAEKIRKENPVVVGEKIQKI

Interacts with PKN1.

Q923B4

MSYPFGKEETATEEELFEFFCECLRRGDWELAQACVPQLHRGQGEIPQKVEDILQALVQCPILLRCGPDINPQRLAWLWLLVLEKWLAPEKKLLSTAIRRKLEFLFLSEDLQGDIPETILKELFETLAQGPAGSIPDRRTPQLSPEAVSVLWNLLKQAPRPAQALLELLLEDHHSASLCPSPLQKSLLDLIREALQTLRDPASQPPGVADAVCGALQALCCKAELPESEWRVLCEELLETCRTEDSPLQEERLLGCLLHKAGRNLLSLYGHTYAEKVAERPPKATLSGKDHPDPERAMLALFSTPDPAHAWKMAFFYCLSNNKHFLEQILVTALTLLKEEDFPSLGYLLDREFRPLSHLLVLLGWTHCQSLESAKRLLQTLYRTQDQGHDELLRDACEGLWAHLEVLEWCVQQSSNLIPKRELLCHLHGGDSHSVLYSLHHLTNLPALNEEEVLKLLQKEPTKDLQGEHETHDASVPEHLSQCQSLTLYQGFCAMKYAVYALCVNSHQHSQCQDCRDSASEDLALVEPGSDSLPSPGASHLFPTYLARCRQYLHSIPASLCLEILENIFSLLLITSADLHPEPHLPEDYAEDEDIEGKGPLGLRSPSESPQHIAATERRSERASMGPRNPAHTVPGCPKAEPKDSSPGPHKHSFLDLKHFTSGVNGFLADEFAMGAFLSLLQEQLTEISSHRTPEETKLPEDQSCSAARDGLQSRLHRFSKVLSEAQWRYKVVTSNQGSEEQPSRRYRPIATRHSSLRRGRRTRRTRADGRERGSNPSLEGTSSELSTSTSEGSLSAVSGQVESDSRFQTQPQSSIIPMMFSTPESLLASCILRGNFAEAHQVVLMFNLKSSPIAGELMFVERYQEVIQELARVEHKIENQNSDGGNNTIRRTGSGRSTLQAIGSAAAAGMVFYSISDVTEKLLSPSEDPIPTLQEDFWINATPMETTTPLREVLEDLSPPAMAAFDLACCQCQLWKTCKQLLETAERRLSSSLESRGRRLDQVVLNPDGMRGFPFVLQQISKILSYPLMQTGLAKSETLEERGGGAPRSSISELLQMCWPSLTEDCVASHTSLSQQLEQALQSLREALALPESKSTPLSCLVEQAAQKAPEAEAHPVHIQSQLLQKTLGRQTPAGHRQTDYVGAFFSYCSSLAAVLLRSLSSDPDHVEVRVGNPFVLLQQSSSQLVSHLLLERQVPPDRLAALLAQEHLNLSVPQVIVSCCCEPLTLCLSRQSQQASSLLTHLGMLAREHASHLLDGLPLSTLGSPRPSENPSAERKSHSSPKDSLPAFTASALAFLKSRSKILAMVACLRTSRGTKVSKPGLSWKELRGRREAPLTAEKVAQECEHLLEQFPVFEAALLANWEPLQQASEPKQSLAASLCGQANLSTVLLGLHSSLALDILTEAFEGALVARDWPRALQLIDVYGQDLDDLSIVQDSVLTCAAVCDKEGWQYLFPVKDASLRSQLALRFVDKWPLESCLEILAYCVSDMAVQEELKSELQRKLMELRVYQKILGLQDPPVWCDWQTLRSCCAEDPSAVMDMMLDSQEYELCEEWGRLYPIPREHLVSLHHKHLLHLLERSEHDKALQLLQRIPDPTMCLEVTERSLDQHPSLATSHFLANYLTSHFYGELTTDRHREIQALYMGSKVLLTLPEQHRASYARLSSSPLLMLEQLLMNMKVDWATTAVQTLHQLLAGQDIGFTLDEVDSLLSRYAGKALDLPYPLREKRSDSMIHLQEPVHQASDSETLSRSSSAEFSAAAAPGSALVRSPSPKERAFPQTQPPVEFVPPETPPARDQWVPDETESVCMVCCREHFTMFNRRHHCRRCGRLVCGSCSTKKMVVEGFRENPTRVCDQCYSYYNKDTPEESPCQSEVPDSAKNESPPYSAVVRVPKATEVEWILSLSEEENELVRSEFYYEQAPSASLCIAILNLHRDSIACGHQLIEHCCRLSRGLTNPEVDAGLLIDIMKQLLFSAKMMFVKAGQSQDLALCDSYISKVDVLHLLVAAAYRHVPSLDQILQPAAVTRLRNQLLEAEYYQLGVEVSTKTGLDSTGAWHAWGMACLKAGNLTVAREKFTRCLKPPLDLNQLSHGSRLVQDVVEYLESTVRPLVSLQDDDYFATLRELEATLRTQSLLLEAIPEGKIMNNTYYQECLFYLHNYSTNLAIISFYMRHNCLREALLHLLNKESPPEVFIEGIFQPSYKSGKLHTLENLLESIDPTLESWGAHLIAACQHLQKNSYYHILYELQQFMKDQVRAAMTCIRFFSHKAKSYTELGEKLSWLLKAKDHLKIYLQETSRSSGRKKATFFRKKMTAADVSRHMNTLQLQMEVTRFLHRCESAGTSQVTTLPLPTLFGNNHMKMEVACKVMLGGKNVEDGFGIAFRVLQDFQLDAAATYCRAARQLVEREKYGEIRQLLKCVSESGMAAKSDGDTILLNCLEAFKRIPPQELEGLIQAIHSDDNKVRAYLTCCKLRSAYLIAVKQEHSQAAALVQQVQQAAKSSGDSVVQDICAQWLLTSHSRGAHGSGSRK

Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair (By similarity). Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with TTC19 and KIF13A (By similarity). Localizes to the centrosome during all stages of the cell cycle. Recruited to the midbody during cytokinesis by KIF13A (By similarity). The FYVE-type zinc finger mediates binding to phosphatidylinositol 3-phosphate and recruitment to the midbody during cytokinesis. Belongs to the ZFYVE26 family.

D3ZBA4

MSYPFGKEETTTEKQLFEFFCECLRRGDWELAQACVPQLQRGQGEIPQKVEDILQALVQCPILLRCGPDINPQRLAWLWLLVLEKWLPPEKKLLSTVFRRKLEFLFLSEDLQGGIPETILKELFETLAQGPAGCTSDRSQRWESGAPQLSPEAVSMLWNLLKQAPGPAQALLELLLEERHSASLCHSSLQKSLLDLIRKALQTLRDPASQPAGVTDAVCGALQALCCTAELPEGEWHVLCEELLETCRTEGSPLKEERLLGCLLHKAGRSLLSLYGHTYAEKVAERPPKASLSGKDHPDPERAMLALFSTPDPAHAWKMAFFYCLSNNKHFLEQILVTALTLLKEEDFPSLGYLLDREFRPLSHLLVLLGWTHCQSLESAKRLLQTLYRNQDQGHDELLRDACEGLWAHLEVLEWCVQQSSSLIPKRELLCHLHGGDSHSVLYSLHHLTNLPALREEEVLKLLQKVPTKDLQGEHDTHDASVPEHLSQCQSLTLYQGFCAMKYAVYALCVNSHQHSQCPDCRDSASSEELALVEPGRDSLPSPGASHLFPTYLARCRQYLQRIPDSLCLEILENIFSLLLITSADLHPEPHLPEDYAEDDDIEGKGPWGLWSPSESPQHIAATERRSERASMGPRDLAPTGPGCPKGEPKDNSPGPHTHSFLDLKHFTSSLSGFLADEFAIGAFLSLIQEQLNELSSHRTPEETELLEDQSCWAARDGLQGRLHRFSKVLSEAQWRYKVVTSNQSSEEQPSRRYRPTAKRHSSLRRGRRTRRTRADGRERGSNPSLEGTSSELSTSTSEGSLSAVSGQVEADNRFQPQPQSSIIPMMFSPPESLLASCILRGNFAEAHQVVLMFNLKSSPSAGELMFVERYQEVIQELARVEHKIENQNSDGGNNTVRRTGSGRSTLQAIGSAAAAGMVFYSISDVTDKLLSPSEDPIPTLQEDFWINAALTETNTPLRGVLEDLSPPAMAAFDLACCQCQLWKTCKQLLETAERRLSSSLEGRGRRLDQVVLNPDGMRGFPFVLQQISKILSYPLTVTGLTKSETLEERGGGAPRCSISELLQMCWPSLTEDCIASHTSLSQQLDQALQSLREALTLSEPKSTPLTCLVEQAAQKAPEAEAHPVHIQSQLLQKTLGKQTLAGPRQTDYVGAFFSYCSSLAKVLLRSLSSDPDNVEVKVGNPFVLLQQSSSQLVSHLLLERQVPPDRLAALLAQEHLNLSVPQVIVSCCCEPLTLCLSRQSQQASSLTAHLGMLAQGHASHLLDGLPLSVLGSPRPSENPSAERKSDSSPKDSLPAFTASALAFLKSRSKILAMVACLRASRGTKVSRPSLSWKELRGRREAPLTAEKVAQECEHLLEQFPVFEAALLANWEPLQQASESRPSLAASLCGQARLSTVLLGLHSTLAQDVVTEAFEEALVARDWPRALQLIDVYGQDSDDLSSVRDSVLTCATVCDKEGWQYLFPVKDASLRSQLALRFVDKWPLESCLEILAYCVSDMAVPEELKSELQRKLTELRVYQKILGLQDPPVWCDWQTLRSCCAEDPSTVMDMMLGSQEYELCEEWGCLYPIPREHLVSLHHKHLLYLLERREYEKALQLLQRIPDPTMCLEVTERSLDQHPSLATSHFLANYLTSHFYGELTTDRHHEIQALYMGSKVLLTLPEQHRASYAHLSSSPLLMLEQLLMNMKVDWATTAVQTLQQLLAGQDIGFTLDEVDSLLSRYAGKALDLPYPLREKRSDSMIHLQEPVHQASDPETLSRSSSAEFSAAAAAPAPAAPGSALVCSPSPKERAFPQTQPPLEFVPPETPPARDQWVPDETESMCMVCCREHFTMFNRRHHCRRCGRLVCGSCSTKKMVVEGCRENPTRVCDQCYSYYNKDAPEESPCQSEVPDSAKNESPSYSAVVRIPKATEVEWILSLNEEENELVRSEFYYEQAPSASLCIAILNLHRDSIACGHQLIEHCCRLSRGLTNPEVDAGLLIDIMKQLLFSAKMMFVKAGQSQDLALCDSYISKVDVLHILVAAAYRHMPSLDQILQPASVTRLRNQLLEAEYYQLGVEVSTKTGLDSTGAWHAWGMACLKAGNLTAAREKFSRCLKPPLDLNQLSHGSRLVQDVVEYLESTVRPLVSLQDDDYFATLRELEATLRTQSLFLEAIPDGKIMNNTYYQECLFYLHNYSTNLAIISFYMRHNCLREALLHLLNKESPAEVFIEGIFQPSYKSGKLHTLENLLESIDPTLESWGAYLIAACQHLQKKNYYHILYELQQFMKDQVRAAMTCIRFFSHKAKSYTELGEKLSWLLKAKDHLKIYLQENSRSSGRKKTTFFRKKMAAADVSRHMNTLQLQMEVTRFLHRCESARTSQITTLPLPTLFGNNHMKMEVACQVMLGGKNVEDGFGIAFRVLQDFQLDAAVTYCRAARQLVEKEKYGEIRQLLKCVSESGMAAKSDGDTILLNCLEAFKRIPPQELEGLIQAIHSDDNKVRAYLTCCKLRSAYLIAVKQEHTQAAALVQQVQQAAKSSGDSVVQDICAQWLLTSHSRGAHGSGSRK

Phosphatidylinositol 3-phosphate-binding protein required for the abcission step in cytokinesis: recruited to the midbody during cytokinesis and acts as a regulator of abcission. May also be required for efficient homologous recombination DNA double-strand break repair (By similarity). Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with TTC19 and KIF13A (By similarity). Localizes to the centrosome during all stages of the cell cycle. Recruited to the midbody during cytokinesis by KIF13A (By similarity). The FYVE-type zinc finger mediates binding to phosphatidylinositol 3-phosphate and recruitment to the midbody during cytokinesis. Belongs to the ZFYVE26 family.

A4IFC7

MQTSEREGCGPEVSPSTVPEATLESLPVPTKLPAFDLFNLVLSYKRLEVYLEPLKDAGDGVRYLLRWQTPLCSLLTCLGLNVLFLTLNEGAWYSVGALMISVPALLGYLQEGCQARLSESELMRRKYHSVRQEDLQRVRLSRPEAVAEVKSFLIQLEALLSRLCGTCEAAYRVLHWENPAVSSQFYGALLGTVCMLYLLPLCWVLALLNSTLFLGNVEFFRVVSEYRASLQRRMNPKQEESAFESPPPSDAGGKGALVDCTPAPTPTEDLTPGSVEEAEEAEPDEEFKDAIEEDDEGAPCPAEDELVLQDNGFLSKNEVLRSKVSRLTERLRKRYPTNNYGSCTGCSATFSVLKKRRNCSNCGNIFCSRCCSFKVPRSSMGATAPEAQRETVFVCASCNQTLSK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport. Promotes axonal elongation and contributes to the establishment of neuronal cell polarity. Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner. Can form homooligomers (monomers, dimers and tetramers). Interacts with RAB11A (GDP-bound form); regulates RAB11A. Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with VAPB (via MSP domain). Interacts with RAB11B (GDP-bound form), REEP1, REEP5, ATL1, ATL2, ATL3, SPAST, SURF4, KIF5A, KIF5B, KIF5C and RTN3. Localizes at both dendrites and axons. Localizes to endoplasmic reticulum tubular network. Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A (By similarity).

Q5ZL36

MQAAERDGVAGGLEATAAVAATGGGEASSEPPSPPKAASFDLLDLVRSYRRLELYLEPLRDAAEGVRALLRWQRPLCSLLVCLGLNFLLLTLDQAAWYSVLALLVLLPALLGYLQETYRVRPSERELLRRKYHSVRREDLRRVQLSRQEALAQVKCFLIQLEGFLSGLCYNCEAVYRVLYWENPTVSSQFYGALLGSVCILYLLPLCWVMAILNSTLFLGNSQFYQVIKELKASVEQSLGTKPLESAPEPAKPLPTDAPPDRTPTPTSTEDLTPGSVEEAEEAEPDEEFKDAIEEDDEGSQCSADFDLSLPDNGFMSKNDVIRSKVSRLTERLRKRYPSNNFGTCTGCGATFSVLKKRRSCSNCGNSFCSRCCSFKVPKAVMGATAPEAQRETVFVCAQCNQMLIK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport. Promotes axonal elongation and contributes to the establishment of neuronal cell polarity. Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Can form homooligomers (monomers, dimers and tetramers). Localizes to endoplasmic reticulum tubular network.

Q96M08

MQTSEREGSGPELSPSVMPEAPLESPPFPTKSPAFDLFNLVLSYKRLEIYLEPLKDAGDGVRYLLRWQMPLCSLLTCLGLNVLFLTLNEGAWYSVGALMISVPALLGYLQEVCRARLPDSELMRRKYHSVRQEDLQRGRLSRPEAVAEVKSFLIQLEAFLSRLCCTCEAAYRVLHWENPVVSSQFYGALLGTVCMLYLLPLCWVLTLLNSTLFLGNVEFFRVVSEYRASLQQRMNPKQEEHAFESPPPPDVGGKDGLMDSTPALTPTEDLTPGSVEEAEEAEPDEEFKDAIEETHLVVLEDDEGAPCPAEDELALQDNGFLSKNEVLRSKVSRLTERLRKRYPTNNFGNCTGCSATFSVLKKRRSCSNCGNSFCSRCCSFKVPKSSMGATAPEAQRETVFVCASCNQTLSK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (PubMed:17082457). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity (By similarity). Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner (PubMed:19289470). Contributes to both the formation and stabilization of the tubular ER network (PubMed:24668814). Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections (PubMed:23969831). Acts as an adapter protein and facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (PubMed:21976701). Can form homooligomers (monomers, dimers and tetramers) (PubMed:23969831). Interacts with RAB11A (GDP-bound form); regulates RAB11A (PubMed:17082457). Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation (PubMed:17082457, PubMed:18459960). Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation (PubMed:19289470, PubMed:21976701). Interacts with VAPB (via MSP domain) (PubMed:19289470, PubMed:21976701). Interacts with REEP1, REEP5 and ATL1 (PubMed:24668814, PubMed:23969831). Interacts with ATL2, ATL3 and SPAST (PubMed:23969831). Interacts with KIF5A and RTN3 (PubMed:21976701). Interacts with RAB11B (GDP-bound form), SURF4, KIF5B and KIF5C (By similarity). Localizes at both dendrites and axons (By similarity). Localizes to endoplasmic reticulum tubular network. Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A. The disease is caused by variants affecting the gene represented in this entry. According to PubMed:18606302, the properties of the variant Val-191 and its frequency in some populations raise doubts on the implication of that gene in the disease. Truncated N-terminus.

Q8CFP8

MQTSDRDLSGPEASPSGMPEVLSECPPAPTKSAAFDLFNLVLSYKRLEIYLEPLKDAGDGVRYLLRWQMPLCSLLTCLGLNILFLTLNEGAWYSMGALMISVPALLGYLQEVCRGQLPESELMRRKYHSIRQEDLQRVRLSRVHLSRPEAVAEVKSFLIQLEAFLARLCYTCESAYRVLHWENPVVSSQFYGALLGMVCMLYLLPLCWVLALLNSTLFLGNGDFFRVVCEYRACLQRRMNPRQEECACESSALQGAGGRGLLDSSPAPTPTEDLTPGSVEEAEEAEPDEEFKDAIEETHLVVLEDEEGTPCPAEDELTLQDNGFLSKNEVLRSKVSRLTERLRKRYPTNNFGNCAGCAATFSVLKKRRSCSNCGNSFCSRCCSFKVPRSSMGATAPEAQRETVCVCASCNQTLSK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (By similarity). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity (PubMed:24251978). Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections (By similarity). Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (PubMed:21976701). Can form homooligomers (monomers, dimers and tetramers) (By similarity). Interacts with RAB11A (GDP-bound form); regulates RAB11A (PubMed:21976701). Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation (By similarity). Isoform 1 interacts to a greater extent than isoform 2 with VAPB (via MSP domain). Isoform 1 interacts to a greater extent than isoform 2 with VAPA (via MSP domain) (PubMed:24251978). Interaction with VAPA may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with ATL2, ATL3, SPAST and RTN3 (By similarity). Interacts with REEP1, REEP5 and ATL1 (PubMed:24668814). Interacts with RAB11B (GDP-bound form), SURF4, KIF5B and KIF5C (PubMed:21976701). Isoform 1 and 2 interact with KIFA (PubMed:21976701, PubMed:24251978). Localizes at both dendrites and axons (PubMed:17082457). Localizes to endoplasmic reticulum tubular network. Astrocytes express both isoform 1 and isoform 2 and oligodendrocytes express only isoform 2 (at protein level). Isoform 1 is expressed specifically in the central nervous system and selectively in neuronal cells. Isoform 2 is expressed in cerebrum, cerebellum, spinal cord, heart, thymus, spleen, intestine and lung. Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A (Probable). Truncated N-terminus.

Q5R7K2

MQTSEREGSGPELSPSVMPEAPLESPPFPTKSPAFDLFNLVLSYKRLEIYLEPLKDAGDGVRYLLRWQMPLCSLLTCLGLNVLFLTLNEGAWYSVGALMISVPALLGYLQEVCRARLPESELMRRKYHSVRQEDLQRVRLSRPEAVAEVKSFLIQLEAFLSRLCCTCEAAYRVLHWENPVVSSQFYGALLGTICMLYLLPLCWVLTLLNSTLFLGNVEFFRVVSEYRASLQQRMNPKQEEHAFESPPPPDVGGKGGLMDSTPALTPTEDLTPGSVEEAEEAEPDEEFKDAIEETHLVVLEDDEGAPCPAEDELALQDNGFLSKNEVLRSKVSRLTERLRKRYPTNNFGNCTGCSATFSVLKKRRSCSNCGNSFCSRCCSFKVPKSSMGATAPEAQRETVFVCASCNQTLSK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport. Promotes axonal elongation and contributes to the establishment of neuronal cell polarity. Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner. Can form homooligomers (monomers, dimers and tetramers). Interacts with RAB11A (GDP-bound form); regulates RAB11A. Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with VAPB (via MSP domain). Interacts with RAB11B (GDP-bound form), REEP1, REEP5, ATL1, ATL2, ATL3, SPAST, SURF4, KIF5A, KIF5B, KIF5C and RTN3. Localizes at both dendrites and axons. Localizes to endoplasmic reticulum tubular network. Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A (By similarity).

Q6P7B7

MQSSDRDLSGPEASPSVMPEVLSECSPAPTKSTAFDLFNLVLSYKRLEIYLEPLKDAGDGVRYLLRWQMPLCSLLTCLGLNILFLTLNEGAWYSVGALIISVPALLGYLQEVCRAQLPESELMRRKYHSVRQEDLQRVRLSRPEAVAEVKSFLIRLEAFLARLCYTCESAYRVLHWENPVVSSQFYGALLGMVCMLYLLPLCWVLALLNSTLFLGNGEFFRVVSEYRACLQRRMSPKQEECVCEGSALQDAGGRAVVLDSTPAPTPTEDLTPGSVEEAEEAEPDEEFKDAIEEDDEGTPCPAEDELTMQDNGFLSKNEVLRSKVSKLTERLRKRYPTNNFGNCAGCAATFSVLKKRRSCSNCGNSFCSRCCSFKVPKSSMGATAPEAQRETVFVCASCNQTLSK

Key regulator of RAB11-dependent vesicular trafficking during neurite extension through polarized membrane transport (PubMed:17082457). Promotes axonal elongation and contributes to the establishment of neuronal cell polarity. Involved in nerve growth factor-induced neurite formation in VAPA-dependent manner. Contributes to both the formation and stabilization of the tubular ER network. Involved in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Acts as an adapter protein that facilitates the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of these proteins in neurons. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a KIF5A/B-dependent manner (By similarity). Can form homooligomers (monomers, dimers and tetramers). Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with VAPB (via MSP domain) (By similarity). Interacts with RAB11A (GDP-bound form); regulates RAB11A (PubMed:17082457). Interacts with RAB11B (GDP-bound form), REEP1, REEP5, ATL1, ATL2, ATL3, SPAST, SURF4, KIF5A, KIF5B, KIF5C and RTN3 (By similarity). Localizes at both dendrites and axons. Localizes to endoplasmic reticulum tubular network. Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A (By similarity). Truncated N-terminus.

Q3V0D8

MDEDEIELTPEEEKSLFDGIGADAVHMDSDQISVEVQETVFLSNSDVTVHNFVPDDPDSVIIQDVIENVLIEDVHCSHILEETDISDNVIIPEQVLDLDTAEEVSLAQFLIPDILTSSITSTSLTMPEHVLMSEAIHVSNVGHFEQVIHDSLVEREIITDPLTADISDILVADWASEAVLDSSGMPLEQQDDARINCEDYLMMSLDEPSKTDHEGSSEVTMNAESETDSSKLDEASPEVIKVCILKADSEVDDVGETIQAVESETDNGNEAEVTDQRTSIHVPRVNIYMLASDSQKEEEDTKVIVGDEDAGGTAADTPEHEQQMDVSEIKAAFLPIAWTAAYDNNSDEIEVQNATASAMLHHDESGGLDRVPKQKSKKKKRPESKQYQSAIFVAPDGQTLRVYPCMFCGKKFKTKRFLKRHIKNHPEYLANKKYHCTECDYSTNKKISLHNHMESHKLTIKTEKTTECDDCRKNLSHAGTMHTEKGVNKTCKCKFCDYETAEQTLLNHHLLVVHRKKFPHICGECGKGFRHPSALKKHIRVHTGEKPYECQYCEYKSADSSNLKTHIKSKHSKEIPLKCGICLLTFSDTKEAQQHAVLHQESRTHQCSHCNHKSSNSSDLKRHIISVHTKAYPHKCDMCSKGFHRPSELKKHVATHKSKKMHQCRHCDFKSPDPFLLSHHILSAHTKNVPFKCKRCKKEFQQQCELQTHMKTHSSRKVYQCEYCEYSTKDASGFKRHVISIHTKDYPHRCDFCKKGFRRPSEKNQHIMRHHKEVGLA

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily.

Q9HCI3

MSAQTSPAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKPGHVPYCDLCKGLSGHLPGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYNVSNLQESLEAEEMDEETKRKKMTEKVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPTQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEVPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGVGCKKSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGEEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDGFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNKCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDNCYEARNVQLAVTEAQVDDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSIKLSKHHCRACGQGFCDECSHDRRAVPSRGWDHPVRVCFNCNKKPGDL

Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (PubMed:30970241). Regulates the morphology, size and distribution of LDs (PubMed:31293035, PubMed:30970241). Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contacts by forming a complex with RAB18 and ZW10 (PubMed:30970241). Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger (PubMed:11739631, PubMed:11256955). Interacts with RAB18 (in GTP-bound form) (PubMed:31293035, PubMed:30970241). Interacts with BSCL2 in a RAB18-dependent manner (PubMed:30970241). Interacts with ZW10 (PubMed:30970241). Resides predominantly in the cisternal stacks of the Golgi (PubMed:11256955). Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum (PubMed:22178386). During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures (PubMed:31293035, PubMed:25876663). Localizes to lipid droplets in the presence of oleic acid (PubMed:31293035, PubMed:30970241). Highly expressed in heart. Also detected in the testis. Expressed in all tissues examined, including, brain, placenta, lung, liver, skeletal muscle, pancreas and kidney. Highly expressed in heart. Extended N-terminus. Truncated C-terminus.

Q3TC20

MSAQTSLAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKAGHVPYCDPCKGPNGHSPGVRQRAAVRCQTCKINLCLECQKRTHSGGNKRRHPITVYLVSKVQESLEGEEMDEETKRKKMTERVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPAQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEAPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGAGCKNSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGKEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDAFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNQCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDSCYDARNVQLDVTEAQADDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSVKLSKHHCRACGQGFCDECSHDCRAVPSRGWDHPVRVCFNCNKKPGDL

Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (PubMed:30970241). Regulates the morphology, size and distribution of LDs (PubMed:31293035, PubMed:30970241). Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contact sites by forming a complex with RAB18 and ZW10 (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger (By similarity). Interacts with RAB18 (in GTP-bound form) (By similarity). Interacts with BSCL2 in a RAB18-dependent manner (By similarity). Interacts with ZW10 (By similarity). Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum. During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localizes to lipid droplets in the presence of oleic acid (By similarity). Ubiquitous.

Q5RFL4

MSAQTSPAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKPGHVPYCDLCKGLSGHLPGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYNVSNLQESLEAEEMDEETKRKKMTEKVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVASIFGNTGDGKSHTLNHTFFYGREVFKTSPTQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHYTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEVPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGVGCKNSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYEGGEEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDGFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNKCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDNCYEARNVQLAVTEAQVDDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSIKLSKHHCRACGQGFCDECSHDRRAVPSRGWDHPVRVCFNCNKKPAWTSLSVMTGKGPLC

Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis (By similarity). Regulates the morphology, size and distribution of LDs (By similarity). Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contact sites by forming a complex with RAB18 and ZW10 (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger (By similarity). Interacts with RAB18 (in GTP-bound form) (By similarity). Interacts with BSCL2 in a RAB18-dependent manner (By similarity). Interacts with ZW10 (By similarity). Resides predominantly in the cisternal stacks of the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum. During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localizes to lipid droplets in the presence of oleic acid (By similarity).

Q9Y5R7

MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV

Early endosomal protein that functions to recruit SMAD2/SMAD3 to intracellular membranes and to the TGF-beta receptor. Plays a significant role in TGF-mediated signaling by regulating the subcellular location of SMAD2 and SMAD3 and modulating the transcriptional activity of the SMAD3/SMAD4 complex. Possibly associated with TGF-beta receptor internalization. Interacts (via the SBD region) with SMAD2; the interaction recruits SMAD2 to the TGF-beta receptor and is disrupted by phosphorylation of SMAD2 upon TGF-beta receptor activation. Interacts with SMAD3. Interacts with TGFBR1 and TGFBR2; the interaction recruits SMAD2 to the TGF-beta receptor. Interacts with PML. Ubiquitous. In the brain found primarily in the cerebrovascular smooth muscle cells and reactive astrocytes. The SMAD binding domain (SBD) interacts with the MH2 domains of SMAD2 or SMAD3. The FYVE-type zinc finger is necessary and sufficient for its localization into early endosomes and mediates the association with PI3P. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Truncated N-terminus.

Q95LI3

MDEDEFELQPQEPNSCFDGIGTDATHMDGDQIVVEVQETVFVSDVVDSDITVHNFVPDDPDSVVIQDVIENVVIEDVQCSDILEEADVSENVIIPEQMLSSDVTEEVSLAHCTVPDDVLASDITSASMSMPEHVLTSESVHVSDVGHVEHIVHGSVVEAEIVTDPLTADVVSEEVLVADCASEAVIDANGIPVDQQDDDKGNCEDYLMISLDDDGKMEHDCSSGMTMDAESEIDPCKVDGTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNNSIRMPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAATTVHEQEMDDSEIKTFMPIAWAAAYGNNSDGIENRSGTASALLHIDESAGLGRLTKHKPKKRRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLTKKKYRCTDCDYTTNKKISLHNHLESHKLTSKSEKAIECDDCGKHFSHAGALFTHKMVHKEKGASKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHVKTKHSKEMSFKCDICLLTFSDTKEVQQHALIHQESKTHQCVHCDHKSSNSSDLKRHIISVHTKDYPHKCDMCDKGFHRPSELKKHVAAHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCKKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHITRHHKEVGLP

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily.

Q52V16

MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDITVHNFVPDDPDSVVIQDVIEDVVIEEDVQCSDILEEADVSENVIIPEQVLESDVTEEVSLPHCTVPDDVLASDITSTSTSMPEHVLTSESMHVCDIGHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAIIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAAAVHEQQIDEDEMKTFVPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKKRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYHCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHIKTKHSKEMPFKCDICLLTFSDTKEVQQHTLVHQESKTHQCLHCDHKSSNSSDLKRHVISVHTKDYPHKCEMCEKGFHRPSELKKHVAVHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily.

Q96TF3

MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDITVHNFVPDDPDSVVIQDVVEDVVIEEDVQCSDILEEADVSENVIIPEQVLDSDVTEEVSLPHCTVPDDVLASDITSTSMSMPEHVLTSESMHVCDIGHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAVIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAAAVHEQQIDEDEMKTFVPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKKRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYHCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELRKHMRIHTGEKPYQCQYCEYRSADSSNLKTHIKTKHSKEMPFKCDICLLTFSDTKEVQQHTLVHQESKTHQCLHCDHKSSNSSDLKRHVISVHTKDYPHKCEMCEKGFHRPSELKKHVAVHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily. Was originally thought to be the testis determining factor (TDF).

Q52V17

MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDIAVHNFVPDDPDSVVIQDVIEDVVIEEDVQCSDILEEADVSENVIIPEQVLDSDVTEEVSLPHCTVPDDVLASDITSTSMSMPEHVLTSESMHVCDIEHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAIIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAAAVHEQQIDEDEMKTFVPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKKRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYHCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHIKTKHSKEMPLKCDICLLTFSDTKEVQQHTLVHQESKTHQCLHCDHKSSNSSDLKRHVISVHTKDYPHKCEMCEKGFHRPSELKKHVAVHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily.

Q29419

NHMESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHVKTKHSKEMPFKCDICLLTFSDTKEV

Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3' (By similarity). The binding of ZFY to DNA is mediated by the interaction of the GGCC core base pairs with zinc fingers 12 and 13. Belongs to the krueppel C2H2-type zinc-finger protein family. ZFX/ZFY subfamily.

Q6UW28

MGAQGAQESIKAMWRVPGTTRRPVTGESPGMHRPEAMLLLLTLALLGGPTWAGKMYGPGGGKYFSTTEDYDHEITGLRVSVGLLLVKSVQVKLGDSWDVKLGALGGNTQEVTLQPGEYITKVFVAFQAFLRGMVMYTSKDRYFYFGKLDGQISSAYPSQEGQVLVGIYGQYQLLGIKSIGFEWNYPLEEPTTEPPVNLTYSANSPVGR

Belongs to the jacalin lectin family. It is uncertain whether Met-1, Met-13 or Met-31 is the initiator.

B9EK72

MLTVALLALLCASASGNAIQARSSSYSGEYGGGGGKRFSHSGNQLDGPITALRVRVNTYYIVGLQVRYGKVWSDYVGGRNGDLEEIFLHPGESVIQVSGKYKWYLKKLVFVTDKGRYLSFGKDSGTSFNAVPLHPNTVLRFISGRSGSLIDAIGLHWDVYPSSCSRC

May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN. Highly expressed in liver. Detected at lower levels in colon, ileum and jejunum. Belongs to the jacalin lectin family.

O82106

MTATTTTAAGGGKVQPRGLPVALSLLLLLVLAAGLGGGAEAQQTCAGQLRGLAPCLRYSVPPLPGQVPPAPGPECCSALGAVSRDCACGTFSIINSLPAKCALPPVSCQ

Tapetum of anthers. Belongs to the A9/FIL1 family.

Q7BQ71

MSTCIQKLFEEQVVRTPDEVAVIFKKETLTYKELNEKSNQLARLLREGGVGPDTVVGIMVERSIEMVVGIFGILKAGGAYLPLSPNHPSSRLQFIIEDSGAKLILTQKQILHRFQDSLKADMLALDSISYEGKGENLECINKPSDLVYVIYTSGSTGKPKGVMIEHSALINRIEWMQEAYPISSKDTILQKTPYTFDVSVWEMFWWAIVGAKVCILAPGMEKFPQAIIETTESNDVTIMHFVPSMLSAFLHYLDVTGETNRIKSLKQVFVSGEALLSQHINRFNKLLNFSNGTLLTNLYGPTEATIDVTAYDCPTHEITEGSVPIGRPIKNIEMFVVDKYGNKLPEGHIGELCISGIGLARGYVNRPQLTAEKFVQYSLDTRIYKTGDLALIRSDGNIEFHGRIDFQVKVNGLRIELGEIESCLMSCEGVLQCAVIVRQESEMVVKLIAFYESENDIELERLKKYLRLFLPDYMIPNSFVRVNEMPLTDSGKIDRKVLALLGSDKYSHHTTLVGGSVNEESSKDS

Involved in the biosynthesis of the linear aminopolyol antibiotic zwittermicin A (ZmA) (PubMed:14711631). Specifically adenylates L-serine and loads it onto the holo form of ZmaH via a thioester linkage to the phosphopanthetheine moiety (PubMed:16983083). ATP + holo-[peptidyl-carrier protein] + L-serine = AMP + diphosphate + L-seryl-[peptidyl-carrier protein] kcat is 42 min(-1). Antibiotic biosynthesis. Disruption of the gene abolishes ZmA production. Belongs to the ATP-dependent AMP-binding enzyme family.

Q96NC0

MASGSGTKNLDFRRKWDKDEYEKLAEKRLTEEREKKDGKPVQPVKRELLRHRDYKVDLESKLGKTIVITKTTPQSEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSTLDQVKKRFEVNKKKMEEKQKDYDFEERMKELREEEEKAKAYKKEKQKEKKRRAEEDLTFEEDDEMAAVMGFSGFGSTKKSY

Involved in pre-mRNA splicing as a component of the spliceosome. Component of the spliceosome B complex.

Q5EBK0

MASGSGTKNLDFRRKWDKDEYEKLAEKRLTEEREKKDGKPVQPVKRELLRHRDYKVDLESKLGKTIVITKTTPQSEMGGYYCNVCDCVVKDSINFLDHINGKKHQRNLGMSMRVERSTLDQVKKRFEVNKKKMEEKQKDYDFEERMKELREEEEKAKAYKKEKQKEKKRRAEEDLTFEEDDEMAAVMGFSGFGSTKKSY

Involved in pre-mRNA splicing as a component of the spliceosome. Component of the spliceosome B complex.

Q0IIC4

MILLQHAGLPPPKRPSSSPPMSVAARSTGALQLPPQKPFGQEASLPLAGEEEPPKGGEQDTALEELCKPLYCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARMSNAVEAVAAPAVSVPPQMGSFKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSNSFSDSSEVGQRRTRKEGNEYKMMPNRRNMYAVQNNSAGPYFNPRSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEVEFRQHLESKQHKSKVSEQRYRNEMENLGYV

Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus (By similarity). Interacts with dsRNA.

Q96A21

MILLQHAVLPPPKQPSPSPPMSVATRSTGTLQLPPQKPFGQEASLPLAGEEELSKGGEQDCALEELCKPLYCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARMSNVVEPAATPVVPVPPQMGSFKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSNSFSESSELGQRRARKEGNEFKMMPNRRNMYTVQNNSAGPYFNPRSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEMEFRQHLESKQHKSKVSEQRYRNEMENLGYV

Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. Interacts with dsRNA. Highly expressed in adult brain, and moderately in adult kidney and testis. Not detected in fetal brain, heart, pancreas, adrenal gland, liver or small intestine. By DNA damage in a p53/TP53-dependent manner. Up-regulated following ionizing radiation in primary squamous cell carcinoma of the lung and in various colon cancer cell lines.

O54836

MILLQQVWLPLPNRPSTSPPMSVAARSTRTLQLPPQKAFGQEASLPLAGEEDLAKRGEPDSALEELCKPLFCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARVSSVVAEPVATPLVPVPPQVGSCKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSHSFSDSAEAGQRRTRKEGSEFKMVATRRNMNPVQSNSGPYFNARSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEVEFRQHLESKQHKSKVSEQRYRSEMENLGYVQ

Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. Interacts with dsRNA. Constitutively expressed in brain and testis. Also expressed in lung, kidney and spleen after whole body gamma irradiation. By DNA damage in a p53-dependent manner, and by methamphetamine (METH) in a catecholaminergic cell line.

O08781

MILLQQVWLPLPNRPSTSPPMSVAARSTGTLQLPPQKAFGQEASLPLAGEEDLAKRGEPDSALEELCKPLFCKLCNVTLNSAQQAQAHYQGKNHGKKLRNYYAANSCPPPARMSSVAEPVATPLVPVPPQVGSCKPGGRVILATENDYCKLCDASFSSPAVAQAHYQGKNHAKRLRLAEAQSHSFSDSAEAGQRRTRKEGSEFKMVTTRRNMYTVQSNSGPYFNARSRQRIPRDLAMCVTPSGQFYCSMCNVGAGEEVEFRQHLESKQHKSKVSEQRYRSEMENLGYVQ

Acts as a bona fide target gene of p53/TP53. May play a role in the TP53-dependent growth regulatory pathway. May contribute to TP53-mediated apoptosis by regulation of TP53 expression and translocation to the nucleus and nucleolus. Interacts with dsRNA. Highly expressed in brain, gut, lung, and testis. By DNA damage in a p53-dependent manner, and by 6-hydroxydopamine (6-OHDA) in PC12 cells.

Q2TA39

MGKRYFCDYCDRSFQDNLHNRKKHLNGLQHLKAKKLWYDMFRDAAAILLDEQNKRPCRKFLLTGQCDFGSNCRFSHMSERDLQELSVQVEEERRAREWPLDVAELPEVCLEDWLEKRAKRLSSAPSSRAEPVRATVFQYPVGWPPVQELPPSLRAPPPGGWPLQPSVQWG

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome.

Q6AXL8

MGKRYYCDYCDRSFQDNLHNRKKHLNGVQHHRAKKAWFDNFRDAATLLNDERSKEVCRKFVQTGQCVFGTSCRFSHMSEKQMKMLEQKIDDEKRQKEDPDQDGSSERSVDEWLSRREKKLAALTSGRVLRMEEEECTENIEIPPYLLSIPDLPPSLHPPPAGGWRVTVHNEWG

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome.

A8K9F6

MGKRYFCDYCDRSFQDNLHNRKKHLNGLQHLKAKKVWYDMFRDAAAILLDEQNKRPCRKFLLTGQCDFGSNCRFSHMSERDLQELSIQVEEERRAREWLLDAPELPEGHLEDWLEKRAKRLSSAPSSRAEPIRTTVFQYPVGWPPVQELPPSLRAPPPGGWPLQPRVQWG

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Not found in the major spliceosome.

Q9CQR5

MGKRYFCDYCDRSFQDNLHNRKKHLNGLQHLKAKKVWYDMFRDAAAILLDEQNKRPCRKFLLTGQCDFGSNCRFSHMSEQDLQELSVQVEEERRAREWPLETAELPEGHLEDWLEKRAKRLSSAPSSRAEPIRTTVFQYPVGWPPMQELPPSLRAPPPGGWSVLSKVQWG

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Not found in the major spliceosome (By similarity).

Q7Z7E6

MNSMDRHIQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDKFTPKSAALLSSWCEELGRLLLLRHQKSRQSDPPGKLPMQPPLSSMSSMKPTLSHSDGSFPYDSVPWQQNTNQPPGSLSVVTTVWGVTNTSQSQVLGNPMANANNPMNPGGNPMASGMTTSNPGLNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGFGASYPGGPNAPAGMGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPMGPTQAYNSQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPPPANHNDELRLTFPVRDGVVLEPFRLEHNLAVSNHVFHLRPTVHQTLMWRSDLELQFKCYHHEDRQMNTNWPASVQVSVNATPLTIERGDNKTSHKPLHLKHVCQPGRNTIQITVTACCCSHLFVLQLVHRPSVRSVLQGLLKKRLLPAEHCITKIKRNFSSVAASSGNTTLNGEDGVEQTAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMWGILNAIQHSEFEEVTIDPTCSWRPVPIKSDLHIKDDPDGIPSKRFKTMSPSQMIMPNVMEMIAALGPGPSPYPLPPPPGGTNSNDYSSQGNNYQGHGNFDFPHGNPGGTSMNDFMHGPPQLSHPPDMPNNMAALEKPLSHPMQETMPHAGSSDQPHPSIQQGLHVPHPSSQSGPPLHHSGAPPPPPSQPPRQPPQAAPSSHPHSDLTFNPSSALEGQAGAQGASDMPEPSLDLLPELTNPDELLSYLDPPDLPSNSNDDLLSLFENN

Acts as transcriptional coactivator. Increases ligand-dependent transcriptional activity of AR and promotes AR sumoylation. The stimulation of AR activity is dependent upon sumoylation (PubMed:14609956, PubMed:26522984). Also functions as a transcriptional coactivator in the TGF-beta signaling pathway by increasing the activity of the SMAD3/SMAD4 transcriptional complex (PubMed:16777850). Involved in transcriptional activation of a subset of NOTCH1 target genes including MYC. Involved in thymocyte and T cell development (By similarity). Involved in the regulation of postmitotic positioning of pyramidal neurons in the developing cerebral cortex (PubMed:30639322). Interacts with AR, but not with ESR1, NR3C1, PGR, THRB nor VDR. Interacts with NOTCH1 and RBPJ (PubMed:14609956, PubMed:26522984). Interacts with SMARCA4 (By similarity). Interacts (via SP-RING-type domain) with SMAD3 and SMAD4 (via MH2 domain) (PubMed:16777850). Enriched at replication foci throughout S phase. Expressed most abundantly in ovary and, at lower levels, in prostate, spleen and testis. Weak expression, if any, in thymus, small intestine, colon and peripheral blood leukocytes. The SP-RING-type domain mediates interaction with SMAD3 and SMAD4. The C-terminal proline-rich domain possesses a significant intrinsic transcriptional activity. This activity is inhibited by the N-terminus in the full-length protein. The disease is caused by variants affecting the gene represented in this entry. Extended N-terminus.