wanglab/gogpt-training-data huggingface dataset:
Protein: Inhibin beta E chain (Activin beta-E chain) (P58166)
Organism: Homo sapiens (Human)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Follistatin
- Activin receptor type-1C
- Activin receptor type-2B
- Activin receptor type-2A
- Nodal homolog
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-1 proprotein
- Very low-density lipoprotein receptor
Sequence:
MRLPDVQLWLVLLWALVRAQGTGSVCPSCGGSKLAPQAERALVLELAKQQILDGLHLTSRPRITHPPPQAALTRALRRLQPGSVAPGNGEEVISFATVTDSTSAYSSLLTFHLSTPRSHHLYHARLWLHVLPTLPGTLCLRIFRWGPRRRRQGSRTLLAEHHITNLGWHTLTLPSSGLRGEKSGVLKLQLDCRPLEGNSTVTGQPRRLLDTAGHQQPFLELKIRANEPGAGRARRRTPTCEPATPLCCRRDHYVDFQELGWRDWILQPEGYQLNYCSGQCPPHLAGSPGIAASFHSAVFSLLKANNPWPASTSCCVPTARRPLSLLYLDHNGNVVKTDVPDMVVEACGCS
Protein: Ras-related protein Rab-6A (Rab-6) (EC 3.6.5.2) (Q9WVB1)
Organism: Rattus norvegicus (Rat)
Function: Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. Involved in COPI-independent retrograde transport from the Golgi to the ER. Recruits VPS13B isoform 2 to the Golgi membrane. Plays a role in neuron projection development.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:P20340}; Lipid-anchor {ECO:0000250|UniProtKB:P20340}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:P35279}; Peripheral membrane protein {ECO:0000305}. Note=BICD2 facilitates its targeting to Golgi apparatus membrane.
Interaction partners:
- Kinesin-like protein
- DENN domain-containing protein 5A
- GRIP and coiled-coil domain-containing protein 2
- BICD cargo adaptor 2)
- Rab GDP dissociation inhibitor beta
- BICD cargo adaptor 1
- Guanine nucleotide exchange factor subunit RIC1
- Syntaxin-16
- Rab GDP dissociation inhibitor alpha
- ADP-ribosylation factor-like protein 1
Sequence:
MSAGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVNEGGCSC
Protein: Transcription factor GATA-4 (GATA-binding factor 4) (Q09JY7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYQGVTMAANHGAASYESGFLHNSTSPVYVTPTRVTPMIQALPYLQAPQQSSPASGHSGWAQPGVETTSYNSSTGHHHSPVSRFTFSTSPPLTSGRDTATYTSREHFGSRALSGSYHSGYPAYVSPNIGASWTASHFDSSVLHSLQTGGAAAARHPNLEFFDDLGEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLVKPQRRLSASRRVGLSCTNCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNISKTKPGSSEGQSAISAVNSSPTEETRPIKTEPDTTPLYTHHNIHTQVSAFPAYMGSPSGSSSSKSEVWNSLILA
Protein: Transcription factor ces-2 (Cell death specification protein 2) (Q94126)
Organism: Caenorhabditis elegans
Function: Transcription factor. Required to activate programmed cell death in the sister cells of the serotoninergic neurosecretory motor (NSM) neurons. Negatively regulates the activity of ces-1 which in turn negatively regulates the activities of cell-killing genes. Binds to the DNA sequence 5'-RTTACGTAAY-3'. Involved in the development of the excretory duct cell, by positively modulating embryonic transcription of putative transcription factor lin-48, acting in concert with NFIL3 transcription factor homolog atf-2. Positively modulates expression of neuropeptide pigment dispersing factor homologs pdf-1 and pdf-2.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor atf-2
- Nuclear receptor domain-containing protein
- Nuclear hormone receptor family member nhr-169
- Nuclear hormone receptor family member nhr-174
- Cytochrome c oxidase subunit 5A, mitochondrial
- Helix-loop-helix protein hlh-2
- COX5B-domain-containing protein
- Nuclear receptor domain-containing protein
- Nuclear hormone receptor family member nhr-217
Sequence:
MDFHRALSALFTNQAAVQPLLGSLGFPFNDGTSILTTALAAQSGGKKLDTPLGILPFDSLPTTNLLTPTKKIKLEDELCASPVSSRSSTVSSSHFSSPQRSPSRKMSVPIPEEKKDSAYFERRRKNNDAAKRSRDARRQKEEQIASKAHALERENMQLRGKVSSLEQEAAQLRFLLFSKISPANSEVSCESNDSTETNDSNDSKSDSTIEV
Protein: E3 ubiquitin-protein ligase DMA2 (EC 2.3.2.27) (Checkpoint forkhead associated with RING domains-containing protein 1) (Defective in mitotic arrest protein 2) (RING-type E3 ubiquitin transferase DMA2) (P53924)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- E3 ubiquitin-protein ligase DMA1
- 2-oxoglutarate dehydrogenase, mitochondrial
- Seventh homolog of septin 1
- Mitotic check point protein BUB2
- Protein TEM1
- Protein BNI1
- Serine/threonine-protein kinase CLA4
- Translation initiation factor eIF2 assembly protein
- Ubiquitin-conjugating enzyme E2 13
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
Sequence:
MYTPIPANTPAPTAPTSSMTSNSSSASNANTTSSSGINPRNRASGTPSNERARPASGISSFLNTFGIRQNSQTASSSAAPDQRLFGTTPSNSHMSVAMESIDTAPQQQEPRLHHPIQMPLSAQFHVHRNYQLPISISLTAPTTTDHQQSSAHNFEGNNVGNVQESLNQRQPNGTNNTTTSIISMAPAATTRNIVGGADGSTIVNNSQEMYKNLRHLIYAANQPNGTEILHLDLPATSAEESNNMFNVDEVTLKQRKDKHGLFSIRLTPFIDSSSTTNQGLFFEPIIRKAGPGSQLVIGRYTERVRDAISKIPEQYHPVVFKSKVVSRTHGCFKVDSQGNWYIKDVKSSSGTFLNHQRLSPASSLSKDTPLRDGDILQLGMDFRGGTEEIYRCVRMRIELNRSWKLKANSFNKEALQRLQNLQKLTTGIEEEDCSICLCKIKPCQAIFISPCAHSWHFRCVRRLVMLSYPQFVCPNCRSSCDLEASFESSDEEDESDVESEGDQLVDQLSVLMETSKDVDSHP
Protein: Forkhead box protein P2 (P58463)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor that may play a role in the specification and differentiation of lung epithelium. May also play a role in developing neural, gastrointestinal and cardiovascular tissues. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays a role in synapse formation by regulating SRPX2 levels.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Forkhead box protein P4
- Contactin-associated protein-like 2
- T-box brain protein 1
- C-terminal-binding protein 1
- Roundabout homolog 1
- Nuclear factor of activated T-cells, cytoplasmic 2
- Homeobox protein cut-like 1
- Homeobox protein Nkx-2.1
Sequence:
MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSSEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKSSEKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLSLQRQGLISIPPGQAALPVQSLPQAGLSPAEIQQLWKEVTGVHSMEDNGIKHGGLDLTTNNSSSTTSSTTSKASPPITHHSIVNGQSSVLNARRDSSSHEETGASHTLYGHGVCKWPGCESICEDFGQFLKHLNNEHALDDRSTAQCRVQMQVVQQLEIQLSKERERLQAMMTHLHMRPSEPKPSPKPLNLVSSVTMSKNMLETSPQSLPQTPTTPTAPVTPITQGPSVITPASVPNVGAIRRRHSDKYNIPMSSEIAPNYEFYKNADVRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEYQKRRSQKITGSPTLVKNIPTSLGYGAALNASLQAALAESSLPLLSNPGLINNASSGLLQAVHEDLNGSLDHIDSNGNSSPGCSPQPHIHSIHVKEEPVIAEDEDCPMSLVTTANHSPELEDDREIEEEPLSEDLE
Protein: EG:EG0002.3 protein (Q7K7E6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIKFRYKRKEPTNVVGVAAPTAGAAALGSGASSTPGTSPTSPVSVPVPVQAHHPHPQLGHLISNNGGTLPRSSPRKLILDGADKSATLTRQQSKQKSVSALAKVASSVELAVMGYNSTGNGNSNGHINSAGNSERDRCINAVIQLQTSSEPALCPEPLRRALASGPLAGRRFPLGCLGDAAECFELLLHRVHSHISPDDGDSCESSACIAHRRFAMRVIEQSVCKCGANSEQLPFTQMVHYVSASALTSQKSLALQSHQQLSFGQLLRAAGNMGDIRDCPNTCGAKIGICRALLNRPEVVSIGIVWDSERPAADQVHAVLKAVGTSLRLGDVFHQVSEPRWAQQTQHELVGIVSYYGKHYTTFFFHTKLKVWVYFDDANVKEVGPSWEGVVDKCSRGRYQPLLLLYAVPQQPTVGNGVGIGHVDVAMPASAPSIAGSVVRRAVTPSPEKPSLGNTRRAITPTPLRTPPNDYQNLSVIQKNIFPSNLAMGTDETDAYISRKTVEHVLSAQYQNLSVIQDKIGGGNGVGVGQQSVDKDGGFLSRKPIEAVLSAQLARRQHLQLQRSHSAESSSGHASSNGSSPPSDGLTMPEHLNQPRRRDSGNWSGDRNSASSASSTTLDNPYLYMVAKRGVAAVPQSPTRHGLPYDPGYDSFSLSSTDSYPPKHALNPQLAKIPEAAMGVVPNGGAMPHGHGNGQLALSGDCEKLCHEADQLLEKSRLVEESHDLETALVLCNAAAGRARAAMDAPYSNPHTMTFARMKHNTCVMRARSLHRRILVEKGAETEAMPELKHMREGSTSSVKHVRQNSKDRTLEKEQQQLQFQQIQQIQQIHQIQQQIPASIEIYATLPKRKSPLKALASASACDDNAIEYEQEKQLATSPGKPERESRSLFGRKDKEKEKRSRSEDRNKLTREFSLTETLLVNAKDTLKKHKEDKDEKKEKDKSGKKQHKIRRKLLMGGLIRRKNRSMPDLTEAVDDSTANAGITHHPHYPAQGVTTAGTLLGTSVDDSAVGLGKHGHGMSGYISEGHFDYSGSGSASNSGAGSNPNPNLERSKLMRKSFHGSGRQLTMVPKVAPPPPMRTSSTLTPQQQQQQQQQFHHEANLSNLSAMSSNTSISEDSCQTIITTCAQVHSEQSPLKDLQMLVAQDELPLPPPMELPPYPSPPHSSCHSRQASEDFPPPPPPELDLEPLNQQLSQLQALEAASKQQRQQLESLEGTTSILAQLQQRQHLLKLRKEQANHPGAATTDATWLKELQAKQANDLRAMQRKLEASSPSSVRDLTHRFEQTSIRSYASQELLSQPGQSQQLGQLRTQMNGLPNGNAKMDVDEVDAMPAVRNSLPAALSAHQLLPKPKYEMTQSQIAEEIREVELLNTMVQQTLNQNGAAALPKRVKKKSVSFCDQVILVATAGNEEDDDFIPNPILERVLRTAQHPNEKVTAQMIQQQQQNMMRLQTEAQPRQQQVQQLQQPSPMLGRPAGATADMQRYVQRMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHQELYRQQQLHRTSMSGIASQQHLQQLDAQYTTMPRPLHHSQLGSYSVTLQKHQQLQQQQQQQQQQQAPQQLSLGYFSNGSVATSEQVPLPSPYQRVPLPHGYQPAAAGPYYPLPNAQQHLQQQQLMAKPVQKKVSFEPGTKGEADCLPPPPPPPQKNGLPETGSAGSGHPGAAPGASGAGGTTSAGITAIPTRVYNNAIVKASAKAVECNLCRKRHVIAPAVYCTNCEYYLQMLNQRR
Protein: L-seryl-tRNA(Sec) selenium transferase (EC 2.9.1.1) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase) (P0A821)
Organism: Escherichia coli (strain K12)
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule.
Subcellular location: Cytoplasm.
Interaction partners:
- Selenide, water dikinase
- Selenocysteine-specific elongation factor
- Serine--tRNA ligase
- Formate dehydrogenase H
- Formate dehydrogenase-O major subunit
- tRNA 2-selenouridine synthase
- Protein FdhE
- Formate dehydrogenase, nitrate-inducible, major subunit
- Uncharacterized GST-like protein YibF
- Uncharacterized protein YqeB
Sequence:
MTTETRSLYSQLPAIDRLLRDSSFLSLRDTYGHTRVVELLRQMLDEAREVIRGSQTLPAWCENWAQEVDARLTKEAQSALRPVINLTGTVLHTNLGRALQAEAAVEAVAQAMRSPVTLEYDLDDAGRGHRDRALAQLLCRITGAEDACIVNNNAAAVLLMLAATASGKEVVVSRGELVEIGGAFRIPDVMRQAGCTLHEVGTTNRTHANDYRQAVNENTALLMKVHTSNYSIQGFTKAIDEAELVALGKELDVPVVTDLGSGSLVDLSQYGLPKEPMPQELIAAGVSLVSFSGDKLLGGPQAGIIVGKKEMIARLQSHPLKRALRADKMTLAALEATLRLYLHPEALSEKLPTLRLLTRSAEVIQIQAQRLQAPLAAHYGAEFAVQVMPCLSQIGSGSLPVDRLPSAALTFTPHDGRGSHLESLAARWRELPVPVIGRIYDGRLWLDLRCLEDEQRFLEMLLK
Protein: Dynein regulatory complex protein 11 (Flagellar-associated protein 82) (A8IHT2)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
Interaction partners:
Sequence:
MWREAMMELLDQLEAENPEDPALAPKDLSEWACIYIKYLQIMRKLETAYDQMVHPQKRQDMRKALEACIGRMLEIRHWMVKLNRGLDFINLDDILVDLKLGPEVLEVPVPKYFIEDRAKELDDRDKFLEALIEKYNVKGPAASPIIRIGAPLGEDEAILMIQKNERGRQARERARLAAITKRQRQIEDRRVRLGVTLSHEEAARKIQAAIRGFLWRRRIKKEADKELMFIGMKPKPRDPKRDPQMGEAKNLMRRKRVQLEHGREYDEAIVNLKGKVRELEGQDMRETIQDKVNAWFVEKRNPDTGEYPDFPDPDDGGSRAILNPPPPSLASLLEDAAGDGKGKGKDGKGDAKKDAKKDPKKDKKGGGDEPQAEEQKIGAVFIPAIEAAVQEFVAKWQDRDEADNFHQKYDAELVKDELRPIVFEEIRLQVDGEMRVLLQNLKDLVEAERAAKLGKKGKKKKGKKKEPFSRIKKELLKEAKTLAPGERVLVLGNSREPYLCAKKDEKDAAGDGKGKGKDGKGGGKPGTAGSKPGTADKKKKGGKKKSLCSDWSCGA
Protein: G-protein coupled receptor (Q86RK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLPQIPSYIRTTAMFFCIVIMLLGVVGNVMVPIVIVKTKDMRNSTNIFLTNLSIADLLVLLVCTPTVLVEVNTRPETWVLGHEMCKAVPFVELTVAHASVLTILAISFERYYAICEPLKAGYVCTKGRAILICVLAWGIAALFTSPIIAISSYSVEPYGDGTDAPVCTTAADGFWSIFYFVGCITVFFFLPFGILVLLYAAIAYKLLRPNNAFHRPTSPQPQQPSGGATSGSSQVPSTKGNSHQQSNGMRKHRKQVIFMLVAVVSSFFVCLLPFRAFTLWVILASAEDVEGLGIAGYYNLLYFSRFMLYLNSAMNPILYNLMSSKFRSGFWRLLLTCLGQRPHHHHRHHYHQRQHPTAGGSGRNASTRQEQDAEEGAALAGTTSARHPRRTLRREATFLINSISTSSGTDRTTSSSAWRSNSLSISGLSERERGILGAAIIGTTAATVTTACLQERRASKI
Protein: RNA-binding protein 8A (A0A023T787)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324, ECO:0000256|RuleBase:RU361239}. Nucleus {ECO:0000256|RuleBase:RU361239}. Cytoplasm {ECO:0000256|RuleBase:RU361239}.
Interaction partners:
Sequence:
MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR
Protein: BTB/POZ and MATH domain-containing protein 3 (Protein BTB-POZ AND MATH DOMAIN 3) (AtBPM3) (O22286)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:19843165}. Cytoplasm {ECO:0000269|PubMed:19843165}.
Interaction partners:
- Cullin-3A
- Cullin-3B
- AT-rich interactive domain-containing protein 4
- E3 ubiquitin-protein ligase RGLG1
- Homeobox-leucine zipper protein ATHB-6
Sequence:
MSTVGGIEQLIPDSVSTSFIETVNGSHQFTIQGYSLAKGMSPGKFIQSDIFSVGGYDWAIYFYPDGKNPEDQSSYISLFIALASDSNDIRALFELTLMDQSGKGKHKVHSHFDRALEGGPYTLKYKGSMWGYKRFFKRSALETSDYLKDDCLVINCTVGVVRARLEGPKQYGIVLPLSNMGQGLKDLLDSEVGCDIAFQVGDETYKAHKLILAARSPVFRAQFFGPIGNNNVDRIVIDDIEPSIFKAMLSFIYTDVLPNVHEITGSTSASSFTNMIQHLLAAADLYDLARLKILCEVLLCEKLDVDNVATTLALAEQHQFLQLKAFCLEFVASPANLGAVMKSEGFKHLKQSCPTLLSELLNTVAAADKSSTSGQSNKKRSASSVLGCDTTNVRQLRRRTRKEVRAVS
Protein: Dicarboxylate transporter 1, chloroplastic (SODIT1) (2-oxoglutarate/malate translocator) (Q41364)
Organism: Spinacia oleracea (Spinach)
Function: 2-oxoglutarate/malate translocator that transports carbon skeletons into chloroplasts for net glutamate synthesis. This translocator exchanges malate for internal succinate, fumarate and 2-oxoglutarate but not for aspartate and glutamate. Involved with DIT2 in primary ammonia assimilation and in the re-assimilation of ammonia generated by the photorespiratory pathway. Imports 2-oxoglutarate into plastids as precursor for ammonia assimilation. 2-oxoglutarate is converted to glutamate, the end product of ammonia assimilation, which is exported to the cytosol by DIT2.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305|PubMed:7873543}; Multi-pass membrane protein {ECO:0000305|PubMed:7873543}.
Interaction partners:
Sequence:
MASMALSLTSSPTYSLSFRSLPSLKPLSKSQPSISLPSLRSNASKSPSLSHKHFLSPPSLLLPHKLKPISASSPTNPPPPPAPVPSPAPVSAPAQVQPWQGASIKPLLASILTGVIIWFIPTPEGVSRNAWQLLAIFLSTIVGIITQPLPLGAVALMGLGASVLTKTLTFSAAFSAFGDPIPWLIALAFFFARGFIKTGLGNRIAYQFVKLFGSSSLGLGYSLVFSEALLAPAIPSVSARAGGIFLPLVKSLCIACGSNVGDGTERKLGAWLMLTCFQTSVISSSMFLTAMAANPLSATLTFNTIGKAIGWMDWAKAAFVPGLVSLIVVPLLLYVVYPPEIKSSPDAPRLAKEKLDKMGPMTKNESIMAVTLLLTVGLWVFGGKLGVDAVTAAILGLSVLLITGVVTWKECLAESVAWDTLTWFAALIAMAGYLNKYGLITWFSENVVKVVGGLGLSWQMSFGVLVLLYFYSHYFFASGAAHIGAMFTAFLSVASALGTPPFLAAIVLSFLSNLMGGLTHYGIGSAPVFYGANYVPLPQWWGYGFLISIVNLIIWLGVGGLWWKAIGLW
Protein: BTB/POZ domain-containing protein KCTD7 (Q96MP8)
Organism: Homo sapiens (Human)
Function: May be involved in the control of excitability of cortical neurons.
Subcellular location: Cell membrane. Cytoplasm, cytosol.
Interaction partners:
- Palmitoyl-protein thioesterase 1
- Cullin-3
- Rab5 GDP/GTP exchange factor
- Prickle-like protein 1
- Ceroid-lipofuscinosis neuronal protein 6
- Protein CLN8
- Bis
- Major facilitator superfamily domain-containing protein 8
- Battenin
- E3 ubiquitin-protein ligase NHLRC1
Sequence:
MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQEFPEVVPLNIGGAHFTTRLSTLRCYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPRERVRAVYKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW
Protein: Protein atp12, mitochondrial (Q9UT16)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for the assembly of the mitochondrial F1-F0 complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein atp11
- Oxysterol-binding protein homolog C2F12.05c
- Cytochrome B pre-mRNA-processing protein 6
- Mitochondrial zinc maintenance protein 1
- ATP synthase subunit a
- ATP synthase subunit 4
Sequence:
MLRSLQFYRLSSKNLLSFKTCYSFYSTKASSPLPQPSFRRFWKNTATKIQNGEVLIQLDGRNLKSPSGKIVKVPKEMELLAHLIALEWDRLPSTSVRQHNLPITSLVSRAIDISQFKKEEKELLSTQLIRFLDTDTILIYSPETEYEGKLLEEQKENWWPLKETFENKLGVQLSYLDGDAGIIAHKQTQETHERIRNWLSSLNSWQLAAFERSVSCCKSFIVSFMILKGYLNSEKAAALTNLELQYQTNRWGSLEDAHEIDNEDLKNKLASSAILSRCIEDMHDKSNEHAH
Protein: Insulin-like peptide 7 (dILP7) (Insulin-related peptide 7) [Cleaved into: Insulin-like peptide 7 A chain; Insulin-like peptide 7 B chain] (Q9W4Q9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Insulin-like peptide 1
- Insulin-like peptide 4
- Insulin-like peptide 6
- Insulin-like peptide 3
- Insulin-like peptide 5
- Insulin-like peptide 2
- Insulin-like receptor
- GEO10744p1
- Death-associated inhibitor of apoptosis 2
- FI21465p1
Sequence:
MTRMIIQNSGSWTLCGAVLLFVLPLIPTPEALQHTEEGLEMLFRERSQSDWENVWHQETHSRCRDKLVRQLYWACEKDIYRLTRRNKKRTGNDEAWIKKTTTEPDGSTWLHVNYANMFLRSRRSDGNTPSISNECCTKAGCTWEEYAEYCPSNKRRNHY
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q9VBM4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein, isoform A
- AT13609p
- CCDC113/CCDC96 coiled-coil domain-containing protein
Sequence:
MLRFRVLLRSTCGWSRRMCFRAEEGFHRHFQLHRIKVMGLLHPFCAIFLLCLIGLLFVYELCYVLPQITDPHGIWHKLCWFMGIYTVINILGNWWLGCMTNTSVDSLVLERQYPVAGEAHLWHYCSTCQKLVPPRSWHCSLCNICILKRDHHCTFFASCIGHKNQRYFLAFLFHLSFGSGQALVYNGILNWTNKAFLVVDPLLLMFQDTTQDADFKWKYTIANLFKLNLFLFGVPLFMFVFQMIMVYRNSTCYKMLDRSYDVGWRRNFDMVLGKRRFWIFFSPTISSPLPTDGTQWFQKQTV
Protein: Palmitoyltransferase (EC 2.3.1.225) (A0A0B4KH44)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MCIVNDWCREYANLYPKKAVFYVAPDVHDGFMYKFFVISAIFTTYNILGNLLACYRTSSAVKSLPQERQIPKPGTEHLWHYCDICQKLMPPRSWHCALCKCCILKRDHHCIFAATCIGHNNHRYFFWLTFYLAFGIFMSMATLFVDVGRSFYLLHRMKAGFGNTVKSLSYFRYVCLILNIFALGFPALMLRFQVQILKLNSTYYQISSRHHDLGFRNNCQLIMGQRGLWTFISPSLRSPLPHDGTHWKIKQCF
Protein: DNA-3-methyladenine glycosylase II (EC 3.2.2.21) (3-methyladenine DNA glycosidase) (A2IDA3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAG
Protein: Insulin-like growth factor I (Q91476)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
TLSLLLCVLTLTSAATGAGPETLCGAELVDTLQFVCGERGFYFSKPTGYGPSSRRSHNRGIVDECCFQSCELRRLEMYCAPVKSGKAARSVRAQRHTDMPRTPKNLYLGIVTHLARR
Protein: Insulin-like peptide 1 (dILP1) (Insulin-related peptide 1) [Cleaved into: Insulin-like peptide 1 A chain; Insulin-like peptide 1 B chain] (Q9VT50)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Insulin-like peptide 2
- Insulin-like receptor
- Insulin-like peptide 3
- Insulin-like peptide 7
- Insulin-like peptide 5
- Insulin-like peptide 6
- Insulin receptor substrate 1
- Insulin-like peptide 4
- Death-associated inhibitor of apoptosis 2
- Bent, isoform F
Sequence:
MFSQHNGAAVHGLRLQSLLIAAMLTAAMAMVTPTGSGHQLLPPGNHKLCGPALSDAMDVVCPHGFNTLPRKRESLLGNSDDDEDTEQEVQDDSSMWQTLDGAGYSFSPLLTNLYGSEVLIKMRRHRRHLTGGVYDECCVKTCSYLELAIYCLPK
Protein: Ubiquitin-conjugating enzyme E2 W (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme W) (N-terminal E2 ubiquitin-conjugating enzyme) (EC 2.3.2.25) (N-terminus-conjugating E2) (Ubiquitin carrier protein W) (Ubiquitin-conjugating enzyme 16) (UBC-16) (Ubiquitin-protein ligase W) (Q96B02)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate.
Subcellular location: Nucleus {ECO:0000269|PubMed:16368532, ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with FANCL. {ECO:0000269|PubMed:21229326}.
Interaction partners:
- E3 ubiquitin-protein ligase FANCL
- Ubiquitin-like modifier-activating enzyme 1
- E3 ubiquitin-protein ligase CHIP
- Breast cancer type 1 susceptibility protein
- Ubiquitin-conjugating enzyme E2 variant 2
- Ataxin-3
- E3 ubiquitin-protein ligase RNF4
- Ataxin-3-like protein
- Ubiquitin-like modifier-activating enzyme 7
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC
Protein: Tyrosine-protein phosphatase vhp-1 (EC 3.1.3.48) (Vh1 dual specificity phosphatase family protein 1) (Q10038)
Organism: Caenorhabditis elegans
Function: Acts preferentially on the c-Jun N-terminal kinase (JNK) and p38 MAPKs. Plays an important role in the heavy metal stress response and in axon regeneration by negatively regulating the kgb-1 (JNK-like) and the pmk-1 (p38-type) MAPK signaling pathways.
Interaction partners:
- GLH-binding kinase 1
- Mitogen-activated protein kinase pmk-1
- Mitogen-activated protein kinase pmk-3
- Stress-activated protein kinase jnk-1
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase pmk-2
- Mitogen-activated protein kinase mpk-1
- Dual specificity protein phosphatase lip-1
- Dual specificity mitogen-activated protein kinase kinase mek-1
- Mitogen-activated protein kinase kinase kinase mlk-1
Sequence:
MTVLDTVTISTCGLAALIREAPDTTLVVDCRGFTEYNESHVRHSMNAFFSKLIRRRLFENKLDDNCLIHQLMSCSSGCTKMDEKLDLVLYAEEDKPRGNKRRIASCNAPESTAKIMRVLRERLEDTDKFRSVMVLEGGFKQFAQQYPQLCESSEGMTRLPQSLSQPCLSQPTGDGITLITPNIYLGSQIDSLDETMLDALDISVVINLSMTCPKSVCIKEDKNFMRIPVNDSYQEKLSPYFPMAYEFLEKCRRAGKKCLIHCLAGISRSPTLAISYIMRYMKMGSDDAYRYVKERRPSISPNFNFMGQLLEYENVLIKDHVLDYNQASRPHRHMDYYGPSDLCPPKVPKSASSNCVFPGSTHDESSPSSPSVSEGSAASEPETSSSAASSSSTASAPPSMPSTSEQGTSSGTVNVNGKRNMTMDLGLPHRPKALGLPSRIGTSVAELPSPSTELSRLSFNGPEAIAPSTPILNFTNPCFNSPIIPVASSSREVILTLPTPAASSSSSTSSEPSFDFSSFESSSSSSIVVENPFFASTEVPAGSSSISTPSGSQSTPASASSSAASRCRMKGFFKVFSKKAPASTSTPASSTPGTSRAARPECLRSSGIIISAPVLAITEEEDAESPESGFNEPEVGEEDDDSVSICSTSSLEIPCHQ