wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (EC 3.1.4.35) (EC 3.1.4.53) (Cyclic GMP-binding protein B) (Phosphodiesterase 6) (DdPDE6) (Phosphodiesterase E) (PdeE) (Q8MM62)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Dual specificity cAMP and cGMP phosphodiesterase with marked preference for cyclic AMP, which is activated by cAMP and cGMP. Likely functions as a cAMP-stimulated cAMP-phosphodiesterase which may play a role in regulating the cAMP relay response.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:12198158, ECO:0000305|PubMed:17040207}.
Interaction partners:
- Developmentally-regulated protein kinase 1
- cAMP-dependent protein kinase catalytic subunit
- 3',5'-cyclic-nucleotide phosphodiesterase regA
- cGMP-specific 3',5'-cGMP phosphodiesterase 3
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Bifunctional protein argC
- cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7
- Protein Dr1 homolog
- Cyclic GMP-binding protein D
Sequence:
MNSKYGDNIIDFLRYLEKFVKSLTKDNKIEEFKTFDIKSLLYPRNKDYFGNLSKFLLAVISARIGSNFINEDDIFEISELLKEFLGQELEHLPYLSYEELYVEIVEQVGEINGTVSEIIEAITVTIDFLDTFEKVSQTIDRSNEKQKLLAYLSAPVNQLDNSVSGVFNENDYTDIQRFFTELTNENNQSPDSNISILINDFQSLLNILESQQASSSSSKMIINDSPRTQQRNGTTEQQKKQQQQQYLQKNKEPFYSKDKIMQVSGPSYVFTPSDCNVSIQVGIPPDTLKRDQSICHFIVPHFLISKDVSLSEVEFPIFYNKFVQKGKTKVVIICTVEQKQRIETILCESIFGPAPEHIYTDEEITIPDYKIDLLTERLAIDPRANDEKLDSYVIFKTFDTFGVVDIDLPSASDPTKLINLRIRNTKGLISFHEDYHVVQKQLHLKLQEQQQDQQDKSSSSTTDKQMINTSGNRIILKNNTVSVIDSTIESQYVPVLPFGNDHEQVKKFKAPILGVTFLGVSHGLDFTHCSHTTGFIIWINGSGVVVDPPVGNTTYLQTNGIYGKTVEHIILTHCHADHDSGILQKIIERNKVTLYTTKTINESYMRKLKALTGLPEQSLKNYYTWVPVTIGNKIKILGAEFEFDYSFHVIPTIRFKLEIYNKKISYSADTFYDLQKFKQLKDQGVLSKKRIERLKSFVFDADMIIHESGVAPIHTPMANLLELPSEIRKKIRVVHCSSSVDTKGEIIRPKEGLENTEIIKVDRKYKGVAECIQIQTALNHCSVFSKLSPAEVQRVFFLCKKIWVKRNDVIIKKGSPSDMFYIILSGKVLVYENEYEPIKSTTSVGTVVTDTTTITTTVKTDAIKIPTIKLCAGETLGESALQLDKNIDASATVIAETDVCLLVWKTMDLRTEFHSNLNTFISKVHMDLSHINSCRDAIIRAFQHNITQHINKEEVDSIANGSKDVSFAHHQVIFNEGDTSDSMYIIKQGRVRIHSKKNKNIIRYLNVGDFFGETAYRRSNEDSNFLPTRSFTATAIDPTILLKLDIESIVNPRIQNIIEQKAKKNAEDNIRYHAYSPKIRTPRTPRKVYPIEGLSI
Protein: PNUTSDm protein (Q70HU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
Sequence:
MPRIVPLQLLRCLRVLLDNNGGILSAVEVKRISGLMAKYSKKLVSKCVYVQILKSTKTELLGDFMAVGGWSLVYTWLNDAIRAMNWPLVQEILELLLLSPVDVNRLKINSAPILVKGLCKDGGNEGVRILAKRLVEQWLKIVTENTSMTIQGAAPHIAATTASQVPASVSGAGSASVPDSASSSDSTDSAGAPVTYTITSAANSSNSNSITIKWKPLLDNPDGGDETDSGTQSKDNEVEHLEKGSSATHLLADASLGKKSGLDDSSSAAEVKSGEDVDNKKHKSSKSDKSKRSEKEREKDRKKESSSHRSSSSSHKSSSSSSSSSSKSSSSKSSSSSSSSHRSSSDKYRDKDKARSSSGSSSSSKDRERSSGSSSSSSNKHKSSKSSSSSSSSSSSSSGSSSSKDRKSSSSTSSSSSSSRQDKDKDNKLMPPPAVAASNAAGTSPTASAKESDAQKPRSIPIMSRKASISIEIRRDTEKTATVKTYQSKFRSHGLTEEAPPPPSRKGLKKPTSSAVAASPALMAVPSSLKRPSPPPRDLSTDKKAKIDINNVAGHVERPGAAKLIAPKKSKQQMLESLLMLFSILFHSPRTLVAFAFVFDRSRMSNSAVLFVDLHSILKVFNFAWAGLKL
Protein: Tektin-4 (Q8WW24)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules (By similarity). Contributes to normal sperm motility (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q149S1}. Note=Found in the abaxial (convex) surface of outer dense fibers in sperm flagella. {ECO:0000250|UniProtKB:Q149S1}.
Interaction partners:
- Tektin-1
- Tektin-2
- Cilia- and flagella-associated protein 144
- Cilia- and flagella-associated protein 52
- EF-hand domain-containing family member C2
- EF-hand domain-containing protein 1
- Protein Flattop
- Piercer of microtubule wall 1 protein
- Tektin-3
- Tubulin beta-4B chain
Sequence:
MAQTVPPCELPCKEYDVARNTGAYTSSGLATASFRTSKYLLEEWFQNCYARYHQAFADRDQSERQRHESQQLATETQALAQRTQQDSTRTVGERLQDTHSWKSELQREMEALAAETNLLLAQKQRLERALDATEVPFSITTDNLQCRERREHPNLVRDHVETELLKEAELIRNIQELLKRTIMQAVSQIRLNREHKETCEMDWSDKMEAYNIDETCGRHHSQSTEVQAHPYSTTFQESASTPETRAKFTQDNLCRAQRERLASANLRVLVDCILRDTSEDLRLQCDAVNLAFGRRCEELEDARYKLHHHLHKTLREITDQEHNVAALKQAIKDKEAPLHVAQTRLYLRSHRPNMELCRDAAQFRLLSEVEELNMSLTALREKLLEAEQSLRNLEDIHMSLEKDIAAMTNSLFIDRQKCMAHRTRYPTILQLAGYQ
Protein: Perilipin (R9WDQ0)
Organism: Sus scrofa (Pig)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MASVAVESQPSVVTRVANLPLVSSTYDLVSSAYISTKDQYPYLKSLCEMAEKGVKTITSVAMSGALPIIQKLEPQIAIANTYACKGLDRIEEKLPILNQPTNQVVANAKGAVTGAKDAMTTTVTGAKDCVASTITEVVDKTKEAVTGSVEKTKSVVNGSINTVLGSRMMQLVSSGVEKAFTKSELLVDQYLPLTEEELEKEAKKVEGFDMVQKPSYYIRLGSLSTKLRSRAYQQALTRVKEVKQKSQETISQLHSTVNLIEFARKNVHNANQKIQGTQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLVSNIQGLPQNIHDQANHLGVMAGDIYSVFHNASSFKEMSDGLLSSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQDAQSRGAENTTSPETQQPETKHIKPASASSAWGSQSGDTSCTVAAC
Protein: Complement factor D (EC 3.4.21.46) (Adipsin) (C3 convertase activator) (Endogenous vascular elastase) (Properdin factor D) (P32038)
Organism: Rattus norvegicus (Rat)
Function: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
Subcellular location: Secreted.
Interaction partners:
- Complement factor B
- 30 kDa adipocyte complement-related protein
- Complement C3
- Complement C2
- Resistin
- Properdin factor, complement
- Complement C4
- Complement C4A.
- Leptin
- Fatty acid-binding protein, adipocyte
Sequence:
MHSSVYLVALVVLEAAVCVAQPRGRILGGQEAMAHARPYMASVQVNGTHVCGGTLVDEQWVLSAAHCMDGVTKDEVVQVLLGAHSLSSPEPYKHLYDVQSVVLHPGSRPDSVEDDLMLFKLSHNASLGPHVRPLPLQREDREVKPGTLCDVAGWGVVTHAGRRPDVLQQLTVSIMDRNTCNLRTYHDGAITKNMMCAESNRRDTCRGDSGGPLVCGDAVEAVVTWGSRVCGNRRKPGVFTRVATYVPWIENVLSGNVSVNVTA
Protein: UDP-rhamnose/UDP-galactose transporter 1 (UDP-Rha/UDP-Gal transporter 1) (UDP-galactose transporter 2) (At-UDP-GalT2) (Q9SRE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleotide-sugar transporter that transports UDP-rhamnose or UDP-galactose and UMP in a strict counter-exchange mode.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16831428, ECO:0000269|PubMed:25053812}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Galactan beta-1,4-galactosyltransferase GALS1
- DNAJ heat shock N-terminal domain-containing protein
- UDP-glucose 4-epimerase 2
- Organic cation/carnitine transporter 3
- UDP-galactose/UDP-glucose transporter 2
Sequence:
MEKPESEKKSAVSDVGAWAMNVISSVGIIMANKQLMSSSGFGFGFATTLTGFHFAFTALVGMVSNATGLSASKHVPLWELLWFSIVANISIAAMNFSLMLNSVGFYQISKLSMIPVVCVLEWILHSKHYCKEVKASVMVVVIGVGICTVTDVKVNAKGFICACTAVFSTSLQQISIGSLQKKYSVGSFELLSKTAPIQAISLLICGPFVDYLLSGKFISTYQMTYGAIFCILLSCALAVFCNISQYLCIGRFSATSFQVLGHMKTVCVLTLGWLLFDSEMTFKNIAGMAIAIVGMVIYSWAVDIEKQRNAKSTPHGKHSMTEDEIKLLKEGVEHIDLKDVELGDTKP
Protein: Lon protease homolog 4, chloroplastic/mitochondrial (AtLon4) (EC 3.4.21.53) (Q9M9L7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:17478548}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:17478548}; Peripheral membrane protein {ECO:0000269|PubMed:17478548}; Stromal side {ECO:0000269|PubMed:17478548}.
Interaction partners:
- B3 domain-containing protein At3g06220
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Protease Do-like 7
- ATP-dependent zinc metalloprotease FTSH 1, chloroplastic
- CLP protease regulatory subunit CLPX1
- ATP-dependent zinc metalloprotease FTSH 10, mitochondrial
- ATP-dependent zinc metalloprotease FTSH 3, mitochondrial
- Protease Do-like 8, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- Cell differentiation, Rcd1-like protein
Sequence:
MLKFLTPTAYASHHVTPATRFRSTPVKNLLFKQLTLLTGWNRSSYELGRRSFSSDLDSDTKSSTTTVSAKPHLDDCLTVIALPLPHKPLIPGFYMPIYVKDPKVLAALQESRRQQAPYAGAFLLKDDASSDSSSSSETENILEKLKGKELINRIHEVGTLAQISSIQGEQVILIGHRQLRITEMVSESEDPLTVKVDHLKDKPYDKDDDVIKATYFQVMSTLRDVLKTTSLWRDHVRTYTQACSLHIWHCLRHIGEFNYPKLADFGAGISGANKHQNQGVLEELDVHKRLELTLELVKKEVEINKIQESIAKAVEEKFSGDRRRIILKEQINAIKKELGGETDSKSALSEKFRGRIDPIKDKIPGHVLKVIEEELKKLQLLETSSSEFDVTCNYLDWLTVLPWGNFSDENFNVLRAEKILDEDHYGLSDVKERILEFIAVGGLRGTSQGKIICLSGPTGVGKTSIGRSIARALDRKFFRFSVGGLSDVAEIKGHRRTYIGAMPGKMVQCLKNVGTENPLVLIDEIDKLGVRGHHGDPASAMLELLDPEQNANFLDHYLDVPIDLSKVLFVCTANVTDTIPGPLLDRMEVITLSGYITDEKMHIARDYLEKTARRDCGIKPEQVDVSDAAFLSLIEHYCREAGVRNLQKQIEKIFRKIALKLVRKAASTEVPRISDDVTTDTEETKSLAKTDLESPETSAEGSTVLTDELATGDPTESTTEQSGEVAETVEKYMIDESNLSDYVGKPVFQEEKIYEQTPVGVVMGLAWTSMGGSTLYIETTFVEEGEGKGGLHITGRLGDVMKESAEIAHTVARRIMLEKEPENKLFANSKLHLHVPAGATPKDGPSAGCTMITSLLSLALKKPVRKDLAMTGEVTLTGRILAIGGVKEKTIAARRSQVKVIIFPEANRRDFDELARNVKEGLEVHFVDEYEQIFELAFGYDH
Protein: HTH-type transcriptional activator AmpR (P24734)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: This protein is a positive regulator of gene expression of beta-lactamase (AmpC).
Subcellular location: Cytoplasm {ECO:0000305}. Membrane {ECO:0000303|PubMed:25182487}.
Interaction partners:
- Beta-lactamase
- Beta-hexosaminidase
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- AmpG
- N-acetylmuramoyl-L-alanine amidase
- N-acetylmuramoyl-L-alanine amidase
- Porin D
- NalD
- Multidrug resistance operon repressor
- Transcriptional regulator MexT
Sequence:
MVRPHLPLNALRAFEASARHLSFTRAAIELCVTQAAVSHQVKSLEERLGVALFKRLPRGLMLTHEGESLLPVLCDSFDRIAGLLERFEGGHYRDVLTVGAVGTFTVGWLLPRLEDFQARHPFIDLRLSTHNNRVDIAAEGLDYAIRFGGGAWHGTEALALFEAPLTVLCCPEVAAQLHSPADLLQHTLLRSYRADEWPLWFQAAGLPAHAPLTRSIVFDTSLAMLEAARQGVGVALAPAAMFARQLASESIRRPFATEVSTGSYWLTRLQSRGETSAMLAFRGWLLEMAAVEARGR
Protein: Mediator of RNA polymerase II transcription subunit 6 (CeMED6) (Mediator complex subunit 6) (c-MED6) (MED-6) (Q9N337)
Organism: Caenorhabditis elegans
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Acts to repress beta-catenin target genes. Required for asymmetric division of T-cells and for gonad and germ cell development.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 22
- TFIIS N-terminal domain-containing protein
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 11
Sequence:
MMPRMGPPAAARQDNPLHVSFRNPQWPPNFINKDNVLDYFCNQANAFYEMNSCNQQIRMQNIVNRTVEECLRTMPGIQYVLWYSQPPLFIICKQRRNNVTNVSPIAYYYVINGSVHQAPDMYSLVQSRLLGALEPLRNAFGEVTNYSRYNTAKGYYWEFKNKPNVKKREEEKKEDEEEKLEDRSTNFQKTRTMMLLNQLFSEMPAEDALEREEKEEVEEEEEETLKTEEPTTSTDEPKFAEPTARTTSKQ
Protein: Syntaxin-3 (Q08849)
Organism: Rattus norvegicus (Rat)
Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. Apical receptor involved in membrane fusion of apical vesicles. Essential for survival of retinal photoreceetors.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Localized to the inner and outer plexiform layers, the cell body and the inner segments of photoreceptors. {ECO:0000250|UniProtKB:Q64704}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 8
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 4
- Vesicle-associated membrane protein 1
- Syntaxin-binding protein 2
- Vesicle-trafficking protein SEC22b
- Synaptosomal-associated protein 29
Sequence:
MKDRLEQLKAKQLTQDDDTDEVEIAIDNTAFMDEFFSEIEETRLNIDKISEHVEEAKKLYSIILSAPIPEPKTKDDLEQLTTEIKKRANNVRNKLKSMEKHIEEDEVRSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEITGKKTTDEELEEMLESGNPAIFTSGIIDSQISKQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKKLIIIIVIVVVLLGILALIIGLSVGLK
Protein: Acetolactate synthase small subunit (AHAS) (ALS) (EC 2.2.1.6) (Acetohydroxy-acid synthase small subunit) (Q72EF2)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Acetolactate synthase
- Acetolactate synthase
- Thiamine pyrophosphate-requiring enzyme
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydrogenase
- acetolactate synthase
- Pyruvate:ferredoxin oxidoreductase
- Citramalate synthase
- Acetolactate synthase small subunit
- 2-isopropylmalate synthase
Sequence:
MKNTLSVLVRNQVGVVAQATEVFRQHNVNLNSISCAETEAFDVSRLMLTVEGQEHLFDAVKADLASKDFVLEVEDLSARDLVDRELALVKVAVTRETTTQVMQVCEVFRATVVGMGQETMTLEITGDMRKVDGFIRLLRPFGIRSLARTGSVALARGDD
Protein: Alpha-lactalbumin (Lactose synthase B protein) (allergen Bos d 4) (P00711)
Organism: Bos taurus (Bovine)
Function: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
Subcellular location: Secreted.
Interaction partners:
- Beta-lactoglobulin
- Lactotransferrin
- Beta-1,4-galactosyltransferase 1
- Albumin
- Alpha-S1-casein
- Beta-casein
- Lactoperoxidase
- Kappa-casein
- Alpha-S2-casein
- UDP-glucose 4-epimerase
Sequence:
MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL
Protein: Exocyst complex component EXO70B2 (AtExo70b2) (Exocyst subunit Exo70 family protein B2) (Q9LMJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi-independent import into the vacuole (By similarity). Positive regulator of defense responses to pathogenic bacteria (e.g. P.syringae pv. maculicola), to the biotrophic oomycete H.arabidopsidis and to fungi (e.g. B.graminis hordei), especially in cell wall apposition formation related to plant defense. Required for both immediate and later responses triggered by pathogen-associated molecular patterns (PAMPs). Positive regulator of abscisic acid (ABA)-independent mannitol (drought)-promoted stomatal closure.
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9FGH9}. Cytoplasm {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21193573, ECO:0000269|PubMed:21199889}. Nucleus {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21199889}. Note=In the cytoplasm, localized in a peri-nuclear pattern. {ECO:0000269|PubMed:21199889}.
Interaction partners:
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component SEC8
- Exocyst complex component SEC3A
- E3 ubiquitin-protein ligase PUB22
- SNAP25 homologous protein SNAP33
- Exocyst complex component SEC15B
- Exocyst complex component SEC10a
- Exocyst complex component EXO84B
- Exocyst complex component SEC5B
Sequence:
MAEAGDENLYAAARDIARALGKDPSAAGDILQILSGYGASGNRGGDPRPTPSRGGSNVNFDRALTSLERQISSYIVEDRPIWSDPVDSRTFLDSVDELLAIAGDLRSMAGDKSVAVCQSRADELIQQVMFRLQEEFGFVMDRAPDSFDSDDEFPGEEDNDTSDGVIVARPITDYKIVIEALQSSVIGDLNAIAVRMVAGGFAKECSRVYSSRRREFLEESLSRLHLRGLSMEEVQESPWQDLEDEIDRWIKAVTLIFHVFFPSERLLCDRVFSDLPVSSVTDLSFMEVCRGTTTQLLNFADAIALGSRLPERLFKVVDLYEAMQDLIPKMETLFSDRYCSPLRHEALAIHKRLGEAIRGIFMELENLIRRDPPKTAFPGGGIHPITRYVMNYLRAACKSRQSLEQILDQTGNETGSDTRPLSVQIIWVLELLESNLEGKKRTYRDPSLCFLFMMNNDKYILDKAKDNELGLVLGEDWIVKHAAKLRQYHSNYRRSSWNQVVGLLRTDGPYPKLVENLRLFKSQFDEVCKVQSQWVVSDGQLREELRSSVAGIVSPAYSNFIRRLKESPEINGRRGEPFIPYTVEDVEFIIKRLFKESSS
Protein: Protein BCAP (Basal body centriole-associated protein) (Outer dense fiber protein 2-like) (ODF2-like protein) (Q9ULJ1)
Organism: Homo sapiens (Human)
Function: Acts as a suppressor of ciliogenesis, specifically, the initiation of ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17485331}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:17485331}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:28775150}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17485331}. Note=Localizes to centrioles in proliferative cells and basal bodies in ciliated cells (PubMed:17485331). Disappears during ciliogenesis but reappears, albeit at a lower levels once ciliogenesis has completed (PubMed:28775150). {ECO:0000269|PubMed:17485331, ECO:0000269|PubMed:28775150}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:28775150}. Note=Not present in the centrioles in cycling cells. Disappears during ciliogenesis. {ECO:0000269|PubMed:28775150}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:28775150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28775150}. Note=Disappears during ciliogenesis but reappears, albeit at a lower levels once ciliogenesis has completed. {ECO:0000269|PubMed:28775150}.
Interaction partners:
Sequence:
MEKAVNDGSHSEELFCHLKTISEKEDLPRCTSESHLSCLKQDILNEKTELEATLKEAELVTHSVELLLPLFKDTIEKINFENANLSALNLKISEQKEILIKELDTFKSVKLALEHLLRKRDYKQTGDNLSSMLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKANTLKANRFSQSVKVVHERLQIQIHKREAENDKLKEYVKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKASKVYKQRLDHFTGAIEKLTSQIRDQEAKLSETISASNAWKSHYEKIVIEKTELEVQIETMKKQIINLLEDLKKMEDHGKNSCEEILRKVHSIEYENETLNLENTKLKLRFPCRITESKNMNILIVLDMLCYISSEKTTLAALKDEVVSVENELSELQEVEKKQKTLIEMYKTQVQKLQEAAEIVKSRCENLLHKNNQITKTKNKNVEKMRGQMESHLKELERVCDSLTAAERRLHECQESLQCCKGKCADQEHTIRELQGQVDGNHNLLTKLSLEEENCLIQLKCENLQQKLEQMDAENKELEKKLANQEECLKHSNLKFKEKSAEYTALARQLEAALEEGRQKVAEEIEKMSSRESALQIKILDLETELRKKNEEQNQLVCKMNSDPETP
Protein: Ribosomal RNA small subunit methyltransferase H (EC 2.1.1.199) (16S rRNA m(4)C1402 methyltransferase) (rRNA (cytosine-N(4)-)-methyltransferase RsmH) (P60390)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10572301}.
Interaction partners:
- Transcriptional regulator MraZ
- Cell division protein FtsL
- Peptidoglycan D,D-transpeptidase FtsI
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- Ribosomal RNA small subunit methyltransferase I
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Probable peptidoglycan glycosyltransferase FtsW
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
Sequence:
MMENYKHTTVLLDEAVNGLNIRPDGIYIDGTFGRGGHSRLILSQLGEEGRLLAIDRDPQAIAVAKTIDDPRFSIIHGPFSALGEYVAERDLIGKIDGILLDLGVSSPQLDDAERGFSFMRDGPLDMRMDPTRGQSAAEWLQTAEEADIAWVLKTYGEERFAKRIARAIVERNREQPMTRTKELAEVVAAATPVKDKFKHPATRTFQAVRIWVNSELEEIEQALKSSLNVLAPGGRLSIISFHSLEDRIVKRFMRENSRGPQVPAGLPMTEEQLKKLGGRQLRALGKLMPGEEEVAENPRARSSVLRIAERTNA
Protein: RE09305p (Uncharacterized protein, isoform A) (Q9VAE4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Echinoderm microtubule-associated protein-like CG42247
- Dynein axonemal assembly factor 1 homolog
- ATP-citrate synthase
Sequence:
MKANPAILLISFSLLAFQSNCVATQKSQLGQPLIQLSHDNNDDDYPEVKDEIHLEDFFWTGSGDGPPDFLKKVHTGITKGKETVFKTETVVATIYVDGNNEIDIPICLDCKPDDGGGTWDMGGPGMPPLNYSATDRRYWLLTVMSGFYTAKDNPTLEEKLARLYRLAFTRQQTRHLGINGAQQIEGVNLPAPRERRKSLTLPTRVETTTGSPADDVEILDMQDEDEQHYIKSVRRLGEDTEWASHSQEEQEQEQSEEQLPLGVTPSTSTESIDYGAYVTLIPWELIQQNGKSEKLREMHETLLTKQPPVQQQQEQQQGAQPPPQTHPQSLPHSQSQSQPLYRDEHVRVVIHNLTQISEADVQKWSTNTNGFGTMEEHNYVNLKFSNDRPIANQTELIYTVLVNGRPVLATTAAKDMELVSESEAVKTFGQAVYMKSEPYIREPTATALAPVPRSGQAGFFNSVKNNVALVVISSLAILLLMLLLVAVLLLGRTRSRQRELSAVNRNSSRNELLSDGQSMRPTTSERTEGEPSPGHSQSREAGVRNFSYEREPRISFPAPPQETRSRRESISSSTDNTSDSSVYCPINPPSADVQRILDDKAARLFDAHKRRHQYDRAEGHEETVYTSVVSEKKSDKMRHKSRRRYLNENRVGSLETSPVQGSLAGHSSAEESPEVMRRSYENFQRSEAFNPHNNYHRNKLLTQKTGRGASAEAINSEMIRNIQPSDKSDTASVGSFLSMASVRAFPKSTLPEPLNRVLDPVFVTYYDNVNAVAPHNSTRSLRSHKSQGSKDNTIATIASFPSPKAPPSVRNVRSASHSDNPDPGVVGPVVWERHKKKQTQEAQTYADYNPSPLHNPSAIRNHYEGLLEGALQMYSSQDDIPMPLPTQNFTNNRRATKREHRGSSAGLPSFHPSAEPKSLAERPATAQPEKTSKSAHSTQPPSPTYSAWGGGSMYSSHSTLNRPVSAGPFQRMEARLDATAPSGSRTGTAPLIEAIQSELRKFKQQQE
Protein: Thioredoxin reductase-like selenoprotein T (SelT) (EC 1.8.1.9) (Q1H5H1)
Organism: Rattus norvegicus (Rat)
Function: Selenoprotein with thioredoxin reductase-like oxidoreductase activity. Protects dopaminergic neurons against oxidative stress and cell death (By similarity). Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion. Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation. In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18198219}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Selenoprotein F
- Selenoprotein K
- Selenoprotein O
- Selenoprotein S
- Selenoprotein M
- Selenoprotein H
- Selenoprotein N
- Selenoprotein V
- Selenoprotein I
- thioredoxin-disulfide reductase
Sequence:
MRLLLLLLVAASAVVRSEASANLGGVPSKRLKMQYATGPLLKFQICVSUGYRRVFEEYMRVISQRYPDIRIEGENYLPQPIYRHIASFLSVFKLVLIGLIIVGKDPFAFFGMQAPSIWQWGQENKVYACMMVFFLSNMIENQCMSTGAFEITLNDVPVWSKLESGHLPSMQQLVQILDNEMKLNVHMDSIPHHRS
Protein: NAD-dependent malic enzyme (NAD-ME) (EC 1.1.1.38) (P40375)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Fumarate hydratase, mitochondrial
- Pyruvate carboxylase
- Pyruvate kinase
- Probable L-lactate dehydrogenase
- Malate dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Probable citrate synthase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- Malic acid transport protein
Sequence:
MPAGTKEQIECPLKGVTLLNSPRYNKDTAFTPEERQKFEISSRLPPIVETLQQQVDRCYDQYKAIGDEPLQKNLYLSQLSVTNQTLFYALISQHLIEMIPIIYTPTEGDAIKQFSDIYRYPEGCYLDIDHNDLSYIKQQLSEFGKSDSVEYIIITDSEGILGIGDQGVGGVLISVAKGHLMTLCAGLDPNRFLPIVLDVGTNNETHRKNHQYMGLRKDRVRGEQYDSFLDNVIKAIREVFPEAFIHFEDFGLANAKRILDHYRPDIACFNDDIQGTGAVALAAIIGALHVTKSPLTEQRIMIFGAGTAGVGIANQIVAGMVTDGLSLDKARGNLFMIDRCGLLLERHAKIATDGQKPFLKKDSDFKEVPSGDINLESAIALVKPTILLGCSGQPGKFTEKAIREMSKHVERPIIFPISNPTTLMEAKPDQIDKWSDGKALIATGSPLPPLNRNGKKYVISQCNNALLYPALGVACVLSRCKLLSDGMLKAASDALATVPRSLFAADEALLPDLNNAREISRHIVFAVLKQAVSEGMSTVDLPKDDAKLKEWIIEREWNPEYKPFV