wanglab/gogpt-training-data huggingface dataset:
Protein: Immunoglobulin heavy constant epsilon (Ig epsilon chain C region) (P06336)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01854}. Cell membrane {ECO:0000250|UniProtKB:P01854}.
Interaction partners:
Sequence:
SIRNPQLYPLKPCKGTASMTLGCLVKDYFPNPVTVTWYSDSLNMSTVNFPALGSELKVTTSQVTSWGKSAKNFTCHVTHPPSFNESRTILVRPVNITEPTLELLHSSCDPNAFHSTIQLYCFIYGHILNDVSVSWLMDDREITDTLAQTVLIKEEGKLASTCSKLNITEQQWMSESTFTCKVTSQGVDYLAHTRRCPDHEPRGVITYLIPPSPLDLYQNGAPKLTCLVVDLESEKNVNVTWNQEKKTSVSASQWYTKHHNNATTSITSILPVVAKDWIEGYGYQCIVDHPDFPKPIVRSITKTPGQRSAPEVYVFPPPEEESEDKRTLTCLIQNFFPEDISVQWLGDGKLISNSQHSTTTPLKSNGSNQGFFIFSRLEVAKTLWTQRKQFTCQVIHEALQKPRKLEKTISTSLGNTSLRPS
Protein: Probable epoxide hydrolase EphC (Epoxide hydratase) (O06576)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- O-acyltransferase WSD1 C-terminal domain-containing protein
- Probable oxidoreductase EphD
- Epoxide hydrolase EphG
Sequence:
MRAGRGERESTWRTTMAEPHWIDVKGPNGDLKALTWGPAGAPVALCLHGFPDTAYGWRKVAPRLAESGWHVVAPFMRGYAPSSIPADGSYHVGALMHDALRVRSAAGGTERDVIIGHDWGAIAATGLAAMPDSPFAKAVIMSVPPSAAFRPLGRVPERGRLLRELPHQLLRSWYILYFQLPWLPERSASWVVPLLWRRWSPGYHAEEDLRHVDAAIGTPEGRRAALGPYRATMRNTRAPADYADLNRLWTEAPKLPVLYLHGHDDGCATSAFTHWTARVLPAGSEVAVVEHAGHFLQLEQPDKIAELIVAFIGSPG
Protein: Homeobox protein Dlx1a (DLX-1) (Distal-less homeobox gene 1a) (Q98875)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Dlx2b
- Homeobox protein Dlx2a
- LIM homeobox 6
Sequence:
MTMSTIPESLNSPVSGKSVFMEFGPPSQQMSPSSMTHGHYSMHCLHSSGHPQHDSAYSPAPSFPRSLPYPYVNSVGSHSSSPYLSTVQTYPNNSALAQTRLEDPAPESEKNTVVEGGEVRFNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLMKQGGGTIDTNALANGRGLSTGSPSVAPVWNTTATVKTSTPTSYIPSYTSWYPTAHQDTMQQPQLM
Protein: cGMP-dependent protein kinase 2 (cGK 2) (cGK2) (EC 2.7.11.12) (cGMP-dependent protein kinase II) (cGKII) (Q61410)
Organism: Mus musculus (Mouse)
Function: Crucial regulator of intestinal secretion and bone growth. Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (By similarity). Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By similarity). Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q13237}; Lipid-anchor {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:19282289}; Lipid-anchor {ECO:0000255}.
Interaction partners:
- Guanylate cyclase soluble subunit alpha-2
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit alpha-1
- Inositol 1,4,5-triphosphate receptor associated 1
- guanylate cyclase
- Vasodilator-stimulated phosphoprotein
- Protein phosphatase 1 regulatory subunit 17
- Regulator of G-protein signaling 2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Potassium channel subfamily U member 1 current)
Sequence:
MGNGSVKPKHAKHPDGHSGNLSNEALRSKVLELERELRRKDAELQEREYHLKELREQLAKQTVAIAELTEELQSKCIQLNKLQDVIHVQGGSPLQASPDKVPLDVHRKTSGLVSLHSRRGAKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGEKLSTGSYVIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEEYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFDELQKYLEGYVATLNRDDEKRHAKRSMSSWKLSKALSLEMIQLKEKVARFSSTSPFQNLEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHLLGIIYRDLKPENLILDADGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGIDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLRRELSGPIDHSYFDKYPPEKGVPPDEMSGWDKDF
Protein: Myosin heavy chain type IIx (Q0GC39)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVDAKESFVKATVQSREGGKVTAKTEGGATVTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFC
Protein: Vacuolar protein sorting 45 homolog (Vacuolar protein sorting-associated protein 45) (A8E7N5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Syntaxin 16
- Rabenosyn, RAB effector.
- Vesicle transport through interaction with t-SNAREs 1A
- Vacuolar protein sorting-associated protein 16 homolog
- small monomeric GTPase
- Vacuolar protein sorting-associated protein 18 homolog
- Vesicle transport through interaction with t-SNAREs 1B
- Mitochondrial tRNA translation optimization 1
- Endoplasmic reticulum-Golgi intermediate compartment protein 3
- Vacuolar protein sorting-associated protein 11 homolog
Sequence:
MNVTLAVKQYISKMIESSGPGMKVLLMDKETTSIVSVVYTQSEILQKEVYLFERIDSQNRDNMKHLKAICFLRPTKENVEHLIQELRRPKYSVYFIYFSNVISKSEVKALAEADEQEVVAEVQEFYGDFIAVNPHLFSLNLQGVSRGRSWEPSVLPRVTQGLTSVLLSLKKCPMIRYQLSSDMSKRLAESVKQIITKEYELFDFRKTEVPPLLLILDRSDDAITPLLNQWTYQAMVHELLGLNNNRIDLSRVPGISKDLREVVLSAENDEFYANNLYLNFGEIGTNIKNLMEDFQKKKPKDQQKLESISDMKAFVENYPQFKKMSGTVSKHVTVVGELSRLVSERQLMEVSEVEQELACQNDHSNAQQMLRRLLQSPRLSEIDAVRLVMLYALRYEKHSSSILPSLMEELNRKGVSERHRKMVHAVVEYGGKRIRGSDLITPTDAVSITKQFFKGLKGVENVYTQHQPLLHDTLDQLIKGRLKDSQFPYLGPSSLRDRPQDIIVFIIGGATYEEALTVYNLNRTMPGVRIVLGGTHIHNTKSFLEEVMLSVGSGGDRSQIGGRQMSRR
Protein: Microtubule-associated tumor suppressor 1 (AT2 receptor-binding protein) (Angiotensin-II type 2 receptor-interacting protein) (Mitochondrial tumor suppressor 1) (Q9ULD2)
Organism: Homo sapiens (Human)
Function: Cooperates with AGTR2 to inhibit ERK2 activation and cell proliferation. May be required for AGTR2 cell surface expression. Together with PTPN6, induces UBE2V2 expression upon angiotensin-II stimulation. Isoform 1 inhibits breast cancer cell proliferation, delays the progression of mitosis by prolonging metaphase and reduces tumor growth.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10697957, ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=In neurons, translocates into the nucleus after treatment with angiotensin-II. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Note=Localizes with the mitotic spindle during mitosis and with the intercellular bridge during cytokinesis.
Interaction partners:
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 1
- Programmed cell death protein 1
- Type-2 angiotensin II receptor
- Hepatitis A virus cellular receptor 2
- T-cell surface glycoprotein CD4
- T-cell immunoreceptor with Ig and ITIM domains
- Aurora kinase B
- T-cell surface glycoprotein CD8 alpha chain
- Kinesin-like protein KIF2C
Sequence:
MTDDNSDDKIEDELQTFFTSDKDGNTHAYNPKSPPTQNSSASSVNWNSANPDDMVVDYETDPAVVTGENISLSLQGVEVFGHEKSSSDFISKQVLDMHKDSICQCPALVGTEKPKYLQHSCHSLEAVEGQSVEPSLPFVWKPNDNLNCAGYCDALELNQTFDMTVDKVNCTFISHHAIGKSQSFHTAGSLPPTGRRSGSTSSLSYSTWTSSHSDKTHARETTYDRESFENPQVTPSEAQDMTYTAFSDVVMQSEVFVSDIGNQCACSSGKVTSEYTDGSQQRLVGEKETQALTPVSDGMEVPNDSALQEFFCLSHDESNSEPHSQSSYRHKEMGQNLRETVSYCLIDDECPLMVPAFDKSEAQVLNPEHKVTETEDTQMVSKGKDLGTQNHTSELILSSPPGQKVGSSFGLTWDANDMVISTDKTMCMSTPVLEPTKVTFSVSPIEATEKCKKVEKGNRGLKNIPDSKEAPVNLCKPSLGKSTIKTNTPIGCKVRKTEIISYPRPNFKNVKAKVMSRAVLQPKDAALSKVTPRPQQTSASSPSSVNSRQQTVLSRTPRSDLNADKKAEILINKTHKQQFNKLITSQAVHVTTHSKNASHRVPRTTSAVKSNQEDVDKASSSNSACETGSVSALFQKIKGILPVKMESAECLEMTYVPNIDRISPEKKGEKENGTSMEKQELKQEIMNETFEYGSLFLGSASKTTTTSGRNISKPDSCGLRQIAAPKAKVGPPVSCLRRNSDNRNPSADRAVSPQRIRRVSSSGKPTSLKTAQSSWVNLPRPLPKSKASLKSPALRRTGSTPSIASTHSELSTYSNNSGNAAVIKYEEKPPKPAFQNGSSGSFYLKPLVSRAHVHLMKTPPKGPSRKNLFTALNAVEKSRQKNPRSLCIQPQTAPDALPPEKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHNGDLCSPKRSPTSSAIPLQSPRNSGSFPSPSISPR
Protein: Interleukin-1 (A3DTN4)
Organism: Columba livia (Rock dove)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAFVPDLDTLESSSLNEETFYGPNCLCLQKKPRLDLEATSPGVGIQVMATKGHPTRTFRRAAVLMVAISKLLKRPAHKDFADSDLGDFLDDIFEPVSFRRIESSYAGAPVYRYTRSQSFDILDIAQKCFVLESPTQLVALHLQGPSAGQKVKLNIALYRPRSPQDGLGSGRVPVALGIKGYQLYMSCVLSGAEPMLQLEEADIRRDIESVELTRFIFYRLDSPTEGTTRFESAAFPGWFICTSLQPRQPVGITDKPDQVNIATYALSGH
Protein: Uncharacterized protein (Q9XUJ2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDVTATPRPHSNTQRPTQAYYVPRKLLECGRGPQSKPTTIDKNEKPIQTSAQQKQKPRPLMDTVISAPPSSLKEKSPQSNRQTKSNKKSSPPPRKSPVMTSSYQVQYPNSPRDLHLVSSTPSSRSSSSMSSNNGIVSPTLTVSSPRIVKGGPQKYSMSRPNAFAPMIAQSDEKECICDRKNTHVVCKRCGYECVGRVQVTCGKHPLILALNDLRECPNPVCHSVQLLECDELDDQDVHDDGVEQLLAEPIEKIDLLS
Protein: RE33721p (Q8SYU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFIWALILVLGSIAANAERDNYCERNETIRATVPVTKQRIIVKQPSKWKIWKKTEKITEIYDSEEEQVTHRLVRECCPGYLQVESGLCEPICSRGCPAHASCAAPDRCECISGYVSARNHQDGSHYCEPICETPCPAGAQCVTPNTCACRDGYTQLQPTDDGVSGGCAPVCRVGDGCANGKCIDVDRCACNSGYRWDKAEERCIELSAESISEELETTEDNTDSPSTSSTAVFTATHCPDDFVLFRGECREKQFDSNDVGCLKSGCGPHQTCLDSGVCQCSDGYVPEESGEATGVLSCRRTLLDQNSRAERSYRR
Protein: Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) (P00962)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}.
Interaction partners:
- Arginine--tRNA ligase
- Methionine--tRNA ligase
- Isoleucine--tRNA ligase
- Leucine--tRNA ligase
- Proline--tRNA ligase
- Lysine--tRNA ligase
- Lysine--tRNA ligase, heat inducible
- Asparagine--tRNA ligase
- Tyrosine--tRNA ligase
- Serine--tRNA ligase
Sequence:
MSEAEARPTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDYKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLHAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALFEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCIYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYEFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIREFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVIHWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTWAKVGE
Protein: Late embryogenesis abundant protein 46 (Late embryogenesis abundant protein 4-5) (AtLEA4-5) (Q9FG31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved dehydration tolerance. Involved in the adaptive response of vascular plants to withstand water deficit. May possess chaperone-like activity under water deficit.
Interaction partners:
- Late embryogenesis abundant protein 18
- Late embryogenesis abundant protein 7
- Late embryogenesis abundant protein 29
- Late embryogenesis abundant protein 6
- AT3g02480/F16B3_11
- Low-temperature-induced 65 kDa protein
- Late embryogenesis abundant
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Em-like protein GEA6
- Late embryogenesis abundant
Sequence:
MQSMKETASNIAASAKSGMDKTKATLEEKAEKMKTRDPVQKQMATQVKEDKINQAEMQKRETRQHNAAMKEAAGAGTGLGLGTATHSTTGQVGHGTGTHQMSALPGHGTGQLTDRVVEGTAVTDPIGRNTGTGRTTAHNTHVGGGGATGYGTGGGYTG
Protein: TRAP-like protein (C6KT06)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MNAPYPLVCLALWLLFLLDVRKCEKLISKLTKNGDLDLVLLYDIGFVDDSENDHMNSLENIAELGKNLLVRDNKNINLSYITYDDINVDLRIESRNNIGVDNENNYDKDNNSSYKFGSDKNIEEFRNVVLDTKLKSSYKNSAHLKALNYVGLKHFYNSEKESVKMVVMFMNTDGDYNNNNNNNMNNISSSYSAELNLVHYLFDRKNIILNIITRVAFKNYCHYIQQIGSNTNELLKCVLKNSFYNISALTYEIIKYYDDISINAICHGWSEWSPCSVTCNMGYHFSKRDSLGYIKNSKSGLYKRKGRSCLEQRNLIIQECFNTSCDHSLDICDNIYMDISILLDDSSNITLESWNKYIIPFVRKFITHFNINNNQINFSLTTYSSHTYNWFNFSNVLSKDKDKLLTYLEFFKFNFGSSTKNIKQAIQYMNDHVLNTNYRRNDAKKIMLIINSGEIDNKTVTSVPDIIQRLKDTHNVQVYSICINNQNVKNCRKLSTHSMEKYGSNFAFSLPNASDLRYNVLGIQKSICRNVSGAFRRKLRSGNKDDEDKKDDEYKEEDEYKEEDEYKEEDEYKEEDEYKEEDEYKEEDEYKEEDEDMKKDEDMKKDEDMKKDEYKKGYKDYKKDQSKNDNKTEERKDEGNISTSNEHHASEKTDDEDIITQYNEEDRHDNSNDNIIIDDEPVGQDNSIFKNENFFWGRGKHDSKYTSKLSINSLGDINEYNDDYNNYDYYDDDPTNRNKGFLKKNSIILKSLYNLNEDYVNNNINNDAGSTSSHCRNNNSGHNDIPHFKNMRKYNSETNIPCSSKSNKSTNKKLLNRLYNMLFRKKKKYRIKNMDAHSKKKVEKFIENIKFSKENNDDNRKIDEQNIEIQFDTLLDGIFDFLQDYDNSSLNAFNNSTPDDDFVYFSNTTPCGVSLMDFPIYDMENMEADVGGKRNDGDNNDDDDNNDDGDNNDDGDNNDDDDNDDKSNNNNNNNNNGDPSSNNNNNNNNNNGDPSSNNNNNNNGDPSSNNNDDGDADEKRNDYISQYNLVLKDKSHNNNYYMTNEHDERKIKKQENIDILSKEEDNISSNYNNELQRTKRSLDFPEIIIKENYENPKDIIHISKKEEANESNNSKGHINLKNKKEHNNVVDNVNPCNKQNINEEDNNINNSIKTARIGIFNKNKINCRNKKASKFDKIKRFNDKINKDNHPLITNVENKNEEIDVLQNNEDKKQKILPIIKNENAKETGQKYENNDVYEEHNKTNINNNVEKLYKDKNSHHIKNQYDKGNLTENNEVTPIYSKDYDADDEEYEHWHGHQRDNKSTPVYKYAASFTLAAILFLGLSLYFINNRKGNKIVDAKESNDFAVSTNVKETSSKEQNIEIMNDTQWK
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (SSAT) (SSAT-1) (P21673)
Organism: Homo sapiens (Human)
Function: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Also acts on 1,3-diaminopropane and 1,5-diaminopentane.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:1985966, ECO:0000305|PubMed:2241897}.
Interaction partners:
- Peroxisomal N
- Ornithine decarboxylase
- Thialysine N-epsilon-acetyltransferase
- Spermidine synthase
- Guanidino acid hydrolase, mitochondrial
- Diamine oxidase [copper-containing]
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Polyamine-modulated factor 1
- PMF1-BGLAP readthrough
Sequence:
MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (Q21812)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Probable glycerol-3-phosphate acyltransferase, mitochondrial
- Probable glycerol-3-phosphate dehydrogenase 2
- Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-2
- Glycerol-3-phosphate dehydrogenase [NAD
- Probable glycerol kinase
- Probable glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipid/glycerol acyltransferase domain-containing protein
- Uncharacterized protein F52C9.3
- Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1
- Lysophosphatidylinositol acyltransferase 10
Sequence:
MIFLVFWFLILLLIFLAVTGKTLGLREYYVNTLVYIFEWGATLNEQYEEEEGSVEEDMPEDFQHKKPRRSSSASDLGIINREKSDIIDAKLHETNVPEAKQTTVSVLVDDTLDFITAGMEAVIEDQVTNRFSAAQLPSWNLLSRTKYSFHFFNWQLTLLWIAGFMFRYYVLVPCRIALFGIAIVLMIVSTSIIGLVPNAKVRKFLNRRCMLMCMRIYSRAFSSVIRFHDKENRANKGGICVANHTSPIDVMVLSCDNCYAMIGQKQAGFLGFLQTTLSRSEHHIWFERGEAGDRAKVMDRMREHVNDENKLPIIIFPEGTCINNTSVMMFKKGSFEIGSTIYPIAVKYDTRLTDAFWNSSAQSYGRYLWSMMTSWAIICDVWYLPAMTRGENEDSISFAKRVKRAIAKKGGLIDLEWDGALKRERVSSKLVTLQQKLYFERLARTTTLNAMLEEKSSDILNIMQGISEEERDELLKQIDEQDDEEEMIRKISSLKPKFKIGDHDADEHIKSD
Protein: Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (Q9I9K6)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- IRF tryptophan pentad repeat domain-containing protein.
- Interferon regulatory factor 3
- Peptidyl-prolyl cis-trans isomerase
- Cellular tumor antigen p53
- Wee1-like protein kinase.
- P53 domain-containing protein.
- Protein kinase domain-containing protein.
- Wee1-like protein kinase.
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MADEEKLPPGWEKRMSRSSGRVYYFNHMTNASQWERPIAGGKNGQGEPGKVRCSHLLVKHNQSRRPSSWRQDKITRSKDEALELINGYIQKMKSGDEDFESLASQFSDCSSAKAGGDLGSFGKGAMQKPFEDASFALRPGEMSGPVFTDSGIHIILRTE
Protein: All-trans-retinol dehydrogenase [NAD(+)] ADH1B (D6RHZ6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVAVGICHTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF
Protein: Periviscerokinin-3 (Lem-PVK-3) (RhyMa-PVK-3) (P83931)
Organism: Rhyparobia maderae (Madeira cockroach) (Leucophaea maderae)
Function: Mediates visceral muscle contractile activity (myotropic activity).
Subcellular location: Secreted.
Interaction partners:
Sequence:
GSSGMIPFPRV
Protein: Aflatoxin B1 aldehyde reductase member 2 (EC 1.1.1.n11) (Succinic semialdehyde reductase) (SSA reductase) (Q8CG76)
Organism: Mus musculus (Mouse)
Function: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity).
Subcellular location: Mitochondrion {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q8CG45}. Cytoplasm {ECO:0000250|UniProtKB:O43488}.
Interaction partners:
- Aldo-keto reductase family 1 member A1
- Succinate-semialdehyde dehydrogenase, mitochondrial
Sequence:
MLRAASRAVGRAAVRSAQRSGTSVGRPLAMSRPPPPRAASGAPLRPATVLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANPWEGKSLKPDSIRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNNWAETYRNRFWKEHHFEAIALVEKALQTTYGTNAPRMTSAALRWMYHHSQLQGTRGDAVILGMSSLEQLEQNLAATEEGPLEPAVVEAFDQAWNMVAHECPNYFR
Protein: p46 (Q9WQX5)
Organism: Rice tungro bacilliform virus
Interaction partners:
Sequence:
MNIEYPYSIHIIDKNKVPIYDQGNLFHTEKSARLSHVSRGLLDHLFTFSSDNTERVRKLHILADYLYLLESERESYRNEWISLSDQVSLLQKQNSELRARIATNKEIIEGLREPVKKPIYTTQDKERLRVFFCEERSMEYIYYHIKRLAQQSYYSHLNKLQKDCEPFRGVYMSFLTNVKFLVLCEAGYWTVPDIETNTTESLLSLSQKKGKDLLQKGVVIFNELEGGYQLSPRFIGDLYAHGFIKQINFTTKVPEGLPPIIAEKLQDYKFPGSNTVLIEREIPRWNFNEMKRETQMRTNLYIFKNYRCFYGYSPLRPYEPITPEEFGFDYYSWENMVDEDEGEVVYISKNTKIIKVTREHVWAWPEHDGDTMSCTTSIEDEWIHRMENA
Protein: Alpha-centractin (Centractin) (ARP1) (Actin-RPV) (Centrosome-associated actin homolog) (P61164)
Organism: Mus musculus (Mouse)
Function: Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85515}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P61163}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P61163}.
Interaction partners:
- Dynactin subunit 2
- Actin-related protein 10
- Dynactin subunit 4
- Dynactin subunit 6
- Dynactin subunit 1
- Dynactin subunit 5
- Dynactin subunit 3
- Beta-centractin
- Cytoplasmic dynein 1 heavy chain 1
- Actin, cytoplasmic 1
Sequence:
MESYDVIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGPKAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPRKNRERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQYYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGARSIHRKTF
Protein: Iron-sulfur protein (P31894)
Organism: Rhodospirillum rubrum
Function: The carbon monoxide dehydrogenase (CODH) oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (probably CooH). CooF is required in stoichiometric amounts in vitro for anchoring CODH to the membrane as well as for conveying the electrons to the hydrogenase.
Interaction partners:
Sequence:
MPPIKENVIIYANPDHCLSCHSCELACAVAHSGGHDMIEAIAANLPLHARNKVVSVDGTAMPMQCRQCEDAPCTFACPTGACRQADGQVQIVEQHCIGCKLCVMVCPFGAITVRSETVVEQGACTNRGVAKKCDLCVDWRASTGKTAPACVEACPTKAIRMVDLDAYRIALREARAREIAKSHRHMRVQF
Protein: Actin-related protein 2/3 complex subunit 5-like protein (Arp2/3 complex 16 kDa subunit 2) (ARC16-2) (Q9BPX5)
Organism: Homo sapiens (Human)
Function: May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3
- Actin-related protein 3B
- Actin, cytoplasmic 2
- Actin nucleation-promoting factor WASL
Sequence:
MARNTLSSRFRRVDIDEFDENKFVDEQEEAAAAAAEPGPDPSEVDGLLRQGDMLRAFHAALRNSPVNTKNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGVDLLMKYIYKGFEKPTENSSAVLLQWHEKALAVGGLGSIIRVLTARKTV
Protein: PHD finger protein 12 (PHD factor 1) (Pf1) (Q96QT6)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional TLE5 complexes to DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11390640}.
Interaction partners:
- Mortality factor 4-like protein 1
- Paired amphipathic helix protein Sin3a
- Paired amphipathic helix protein Sin3b
- Histone deacetylase 1
- Histone deacetylase 2
- AT-rich interactive domain-containing protein 4B
- Mortality factor 4-like protein 2
- Histone-binding protein RBBP7
- AT-rich interactive domain-containing protein 4A
- GATA zinc finger domain-containing protein 1
Sequence:
MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCDSCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNGLVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQNDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGSSKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDCLEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHKKHPPNRRVLQSVKRRSLKVPDAIKSQYQFPPPLIAPAAIRDGELICNGIPEESQMHLLNSEHLATQAEQQEWLCSVVALQCSILKHLSAKQMPSHWDSEQTEKADIKPVIVTDSSVTTSLQTADKTPTPSHYPLSCPSGISTQNSLSCSPPHQSPALEDIGCSSCAEKSKKTPCGTANGPVNTEVKANGPHLYSSPTDSTDPRRLPGANTPLPGLSHRQGWPRPLTPPAAGGLQNHTVGIIVKTENATGPSSCPQRSLVPVPSLPPSIPSSCASIENTSTLQRKTVQSQIGPPLTDSRPLGSPPNATRVLTPPQAAGDGILATTANQRFSSPAPSSDGKVSPGTLSIGSALTVPSFPANSTAMVDLTNSLRAFMDVNGEIEINMLDEKLIKFLALQRIHQLFPSRVQPSPGSVGTHQLASGGHHIEVQRKEVQARAVFYPLLGLGGAVNMCYRTLYIGTGADMDVCLTNYGHCNYVSGKHACIFYDENTKHYELLNYSEHGTTVDNVLYSCDFSEKTPPTPPSSIVAKVQSVIRRRRHQKQDEEPSEEAAMMSSQAQGPQRRPCNCKASSSSLIGGSGAGWEGTALLHHGSYIKLGCLQFVFSITEFATKQPKGDASLLQDGVLAEKLSLKPHQGPVLRSNSVP