wanglab/gogpt-training-data huggingface dataset:
Protein: Lamin-B receptor (dLBR) (Q8MLV1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Anchors the lamina and the heterochromatin to the inner nuclear membrane.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:15054108}; Multi-pass membrane protein {ECO:0000269|PubMed:15054108}; Nucleoplasmic side {ECO:0000269|PubMed:15054108}.
Interaction partners:
- Lamin-C
- Heterochromatin protein 1
- GH25466p
- Lamin Dm0
- Barrier-to-autointegration factor
- Inner nuclear membrane protein Man1
- GM10285p
- RE26969p)
- Fatty acid hydroxylase domain-containing protein
- LD23561p
Sequence:
MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPATRTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTTNTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTEEGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLLLPTAVYYLTWSCTARNACQFKHLNLGILLDVNYLTRQVFQPRVVGAFAAYQVVVFLLVALLPGRRVHLTRETYKFNCLAVSLTLLIASGVAEYLKYPVVTFVLRHYLRFCIFGLVGAFVAAAWSYWLVDTAKYNVLRQTLTNDYGRTGSFVVDFALGRQLNPKWLGRVDWKQFQYRLSLVTTLIYATCYIYQTLVWPQKPQLGEQEGYLYQAKYYWNNVNYDPATLFSASCLLFYVLDAIIFEHHLSSSFELQHEGYGCLLLLRYAATPYLLTAVTKYFYEQRVPISCWYAPLAVAALLSLGLLVKRFSCAYKYKYRLNSQSPIFANIETIHTYQGSRLLLSGMWGWVRQPNYLGDIVALLALAAPMALRPAWPPVLGLSLIILLLLHRATRANARNQARYHSSWQRYSTQVRSYILPRVY
Protein: [Methyl coenzyme M reductase]-L-arginine C-5-methyltransferase (EC 2.1.1.379) ([Methyl-coenzyme M reductase subunit alpha]-arginine C-methyltransferase) (Q8THG6)
Organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Function: Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.
Interaction partners:
- Methyl-coenzyme M reductase subunit alpha
- TfuA-like core domain-containing protein
- YcaO domain-containing protein
- Methyltransferase
- Tetrahydromethanopterin S-methyltransferase subunit C
- Methyl coenzyme M reductase, subunit D
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit G
- Tetrahydromethanopterin S-methyltransferase subunit D
- Tetrahydromethanopterin S-methyltransferase subunit A
Sequence:
MEVVVDVGGNPGVDCKGFCKYCYFKKVKDIQPLGCKYCLPFKKGCDYCTRSVKESYSGFKSLQMVLEETANKLYFTSGEVKKFTVSGGGDLSCYPELKSLITFLSQFNTPIHLGYTSGKGFSKPDDALFYIDNGVTEVSFTVFATDPALRAEYMKDPEPEASIQVLRDFCTHCEVYGAIVLLPGINDGEVLEKTLCDLENMGAKGAILMRFANFQENGLILNNSPIIPGITPHTVSEFTEIVRSSAEKHPSIRITGTPLEDPLIGSPFAIRNVPEALLKLPRVSKKATIITGQVAASRLTEIFEALGGTVNVIPVKKDIGCLITIDDFKALDLSEVTETVFIPGRAFVHDMEIKEALRRDGVDRIVRRGPERLSVDGEMSIGMTREEVLELEVENFTELIGQINSLGLPLE
Protein: Histone deacetylase 11 (B2GUW3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Polyamine deacetylase HDAC10
- NAD-dependent protein deacetylase sirtuin-1
- Nuclear receptor corepressor 2
- Protein deacetylase HDAC6
- Protein deacetylase HDAC6
- NAD-dependent protein deacetylase sirtuin-7
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- Core histone macro-H2A
- Sirtuin 6 6
- Histone acetyltransferase
Sequence:
MPHATQLYQHVPEKRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDGMLVEAREASEEDLLVVHTRRYLNELKWSFVVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMGDKRVYIMDVYNRHIYPGDRFAKEAIRRKVELEWGTEDEEYLEKVERNVRRSLQEHLPDVVVYNAGTDVLEGDRLGGLSISPAGIVKRDEVVFRVVRAHDIPILMVTSGGYQKRTARIIADSILNLHDLGLIGPEFPYVPARNSSIPLLSRAVP
Protein: 5-hydroxytryptamine (Serotonin) receptor 2A, isoform F (E1JJ46)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEMQSYSGRGPSTGTSETATATAAVASASASDTAATFTLRHFNCRLEEADWPGPRQPFIDCEGSHTNSTSYTPSSLPTSKNLIEGPNNTFQCARQAIDEAEHNAFYSCDGESPLSENCTLRLKARLLRWPYEAYEHIRLAINGALSDYASDKLSDSSSCDEGGMVLQCKLGQAHELLLCHLQQLEREPLREVGSAEESFSNDSLLQAFQIELGAERDGLWSFLNLSELMEPDHGFLGIMNVTNTSLDMFLPNLTALNTTSTASTADMATEFAVTKSFLDYSPHGYDFLFLFVVFFIFAGGLGNILVCLAVALDRKLQNVTNYFLFSLAIADLLVSLFVMPMGAIPAFLGYWPLGFTWCNIYVTCDVLACSSSILHMCFISLGRYMGIRNPLGSRHRSTKRLTGIKIAIVWVMAMMVSSSITVLGLVNEKNIMPEPNICVINNRAFFVFGSLVAFYIPMLMMVTTYALTIPLLRKKARFAAEHPESELFRRLGGRFTLRPQHSQQQLQMFSSFSGSNNKFLSMGDGNRNFNTEGEMEEGGAPSRRSGVEPAERPLMQQRTASSRSMGTVSFRNVVNGTSGAAGSGRRTTGTAHSSFRFSGAGIFRHSSSSPASSCHSTSTSRSSSFWRKHGGYPNLMDSHPNRRASVRVTISQPQLGYPTNVGGNGGRTVGATEVGAGGNGSSAGRTSNSSLGGTSLMKIATIQGPILNQSQAAGGNHMVQKVKPTALKPEEPQRNKVRPFKFAFNRVATPTLNLRFLNNRSKRNSLSANAVATEQKATKVLGLVFFTFVLCWSPFFILNIIFAACPECQVPEHVVNTCLWLGYVSSTINPIIYTIFNRTFRAAFIRLLKCNCKRSGRPLRYRSVTEGRGALSLCAPSALPLAISFQGAPLMTPSTANATPMSEFRASCRTVTDDEC
Protein: Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein) (P60766)
Organism: Mus musculus (Mouse)
Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In its active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Regulates cell migration (By similarity). In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:30185885}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Midbody {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P60953}. Cytoplasm {ECO:0000269|PubMed:22461490}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:22461490}; Peripheral membrane protein {ECO:0000305|PubMed:22461490}; Cytoplasmic side {ECO:0000305|PubMed:22461490}. Cell projection, dendrite {ECO:0000269|PubMed:24352656}. Note=Localizes to spindle during prometaphase cells (By similarity). Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells (By similarity). Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome (By similarity). In its active GTP-bound form localizes to the leading edge membrane of migrating dendritic cells (PubMed:22461490). {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:22461490}.
Interaction partners:
- Ras GTPase-activating-like protein IQGAP1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Partitioning defective 6 homolog alpha
- Rho guanine nucleotide exchange factor 7
- BAR/IMD domain-containing adapter protein 2
- Actin nucleation-promoting factor WAS
- Serine/threonine-protein kinase PAK 1
- Partitioning defective 6 homolog beta
- Actin nucleation-promoting factor WASL
- Rho GTPase-activating protein 1
Sequence:
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL
Protein: HP1-HOAP-interacting protein (Q7JWP6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:27835648}. Chromosome {ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:27835648}. Chromosome, telomere {ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:27835648}. Note=Colocalizes with cav/HOAP at polytene and mitotic chromosome telomeres (PubMed:20057353). Telomere localization is enhanced by the activity of tefu/ATM and the MRN complex (PubMed:20057353). Telomere localization is not dependent on the MTV complex components moi/modigliani, tea or ver/verrocchio (PubMed:27835648). {ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:27835648}.
Interaction partners:
- Telomere-binding protein cav
- Heterochromatin protein 1
Sequence:
MASIDEGSRVERRFCAVGNHTLRKPYRQLNNKYLVRFACLLNSEIRAGNLICCKCYTDLVRLYRKKNDNAKRHKMARETAASITDVSGSQSSSHQSAPSLHVSGQSSEFGASYSEGGIVTPDEELCSHRSLSQDSDNVPTTSAAAIQKRQLARANLMVKPSQRLSLAQTTPDCDDYDPNSNLSLNAVNGTRLPHIQPIPKRRPTVLDKQSMDIYLMGTTGG
Protein: H(+)-transporting two-sector ATPase (EC 7.1.2.2) (Mitochondrial protein YMF19) (O47951)
Organism: Oryza sativa (Rice)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004304}.
Interaction partners:
Sequence:
MPQLDKLTYFSQFFWLCLFFFSFYILLLNNNNGILGISRILKLRNQLLSHRGNKIRFKDPKNLEDILRKGFSTGLSYMYSSLSEVSQWCKTVDYLGKRRKITLISDFGEISGSRGMERQILYLISKSSYNTSSSRITCWKKIMLTHVLHGQGSII
Protein: Neuron navigator 2 (V9GXT3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MESISESSQQQRRKPVTHGLEDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQQQQQPEKQPLSSSPLPPAGSQVAGAPSQCQAGTPQHQGLATPQAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMSENVPAPLENSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDLKEETKADLSGVAVTEMPKKSSKIASFIPKGGKLNSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLPPQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRSQTDTEGNVTAESSSAGVSMEPSHYTKSGQPALEELTEDPEARRLRTVKNIADLRQNLEETMSSLRGTQVTHSTLETTFDTNVTTEISGRSILSLTGRPTPLSWRLGQSSPRLQAGDAPSMGNGYPPRANASRFISAEAGRYVYSAPLRRQLASRGSSICHVDVSDKADDDVDLEGISMDAPGYMSDGDVLSKNIRSDDITSGYMTDGGLGLYTRRLNRLPDGMAVVRETLQRNTSLGLGDADSWDDSSSVSSGISDTIDNLSTDDINTSSSISSYANTPASSRRNLDVQTDAEKHSQVERNSLWSGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSGKKNPVLSQTGSWRRGMTAEVGITMPRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTVNANSFGFKKQSGSAAGLAMITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGLPVPKLREPSKASLGSSLPGLVNQTDKEKGISSDSESVASCNSVKVNPATQPVSSSAQATLQPGTKYADVASPTLRRLFGGKPTKPIATAETMKSAVVISNPHATLTQQGNLESPSGSGVLSSGSSSPLYSKNVDLNQSPLASSPSSAHSGPSNSLTWGTSSSAVSKDGLGFQSVSSLHTSCESIDISLGSGGGLSHNSSPGPVASTKEDSLMPFVRTSSVKTTLSESPLSSPAASPKFCRSTLPRKQDSDPHLDRNTLPKKGLRYTPTSQLRTQEDAKEWFRSHSAGGLQDTATNSPFSSGSSVTSPSGTRFNFSQLASPTAVTQMSLSNPTMLRTHSLSNADGQYDPYTDSRFRNSSMSLDEKSRTMSRSGSFRDGFEEVHGSSLSLVSSTSSIYSTPEEKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAAQAAINGVINTPELNCKGNGSAQATDLRIRRQHSSDSVSSINSATSHSSVGSNIESDSKKKKRKNWVNELRSSFKQAFGKKKSPKSASSHSDIEEMTDSSLPSSPKLPHNGSTGSTPLLRNAHSNSLISECMDSEAETVMQLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQGSGCSRAPSQVSISASPRQSLGLSQHSLNLTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEAMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIVHVDPVSQLGLSSDSVLGYSIGEIKRSNASETPELLPCGYLVGENTTILVTVKGLTENSLDSLVFESLIPKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVLREGRELTDGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILDNLHHVSSLGEIFNGLLNCKYHKCPYIIGTMNQATSSTPNLQLHHNFRWVLCANHTEPVKGFLGRFLRRKLMETEISGRVRNAELVKIINWIPKVWHHLNRFLEAHSSSDVTIGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEAVREGLQLYGRRAPWEDPAKWVMDTYPWAASPQQHEWPPLLQLRPEDVGFDGYSLPREGSTSKQVPPSDTEGDPLMNMLMRLQEAANYSSPQSYDSDSNSNSHHDDILDSSLESTL
Protein: IMP-specific 5'-nucleotidase 1 (EC 3.1.3.99) (O14349)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Interaction partners:
- Putative purine nucleoside phosphorylase
- AMP deaminase
- Putative glutamine-dependent NAD
- Uncharacterized protein C24B11.05
- Inosine-5'-monophosphate dehydrogenase
- Nicotinamide riboside kinase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Putative nicotinamide mononucleotide adenylyltransferase
- Adenine deaminase
- Uncharacterized deaminase C1683.02
Sequence:
MASRYRVEYALKQHRKDDFIEWIKGLLSVPFVLQAGTPSQKLVTREKEQETLERYAVILRDVEKLIEAHIQIVSEGGSYSQLKMLVPSITIFWTPLPLVKAMYALEPKLCLAKRSFVAPSFNDVRAILGGAQLNYLADNGLDMVSFDGDVTLYEDGQPLLPDNPVISRLIQLLSRGIYVIILTAAGYPSRTGQEYTDRFSGLLQAIEDSDLKDGQKRKLHVLGGESNYLFAYDPLHGLQWVDADSWMLPVMKTWPHDEILEILDTAEETLRSCIQGLNIDAKIVRKERSVGFVPSLGQKLRREQLEEAVLETQATLQIRNFSVPFTAFNGGNDIWCDIGDKKLGVLCLQHFFNISHPSRCLHVGDQFLSAGNNDYKARAAATTVWVSSPHETIEFLDYYFSFLKK
Protein: Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 (EC 3.1.3.16) (RNA polymerase II-associated protein 2) (Q8IXW5)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22137580}. Nucleus {ECO:0000269|PubMed:22137580}. Note=Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner.
Interaction partners:
- Protein hinderin
- Mirror-image polydactyly gene 1 protein
- GPN-loop GTPase 1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MADFAGPSSAGRKAGAPRCSRKAAGTKQTSTLKQEDASKRKAELEAAVRKKIEFERKALHIVEQLLEENITEEFLMECGRFITPAHYSDVVDERSIVKLCGYPLCQKKLGIVPKQKYKISTKTNKVYDITERKSFCSNFCYQASKFFEAQIPKTPVWVREEERHPDFQLLKEEQSGHSGEEVQLCSKAIKTSDIDNPSHFEKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLHQKSIMKKKAGHKANSKHKDKEQTVVDVTEQLGDCKLDSQEKDATCELPLQKVNTQSSSNSTLPERLKASENSESEYSRSEITLVGISKKSAEHFKRKFAKSNQVSRSVSSSVQVCPEVGKRNLLKVLKETLIEWKTEETLRFLYGQNYASVCLKPEASLVKEELDEDDIISDPDSHFPAWRESQNSLDESLPFRGSGTAIKPLPSYENLKKETEKLNLRIREFYRGRYVLGEETTKSQDSEEHDSTFPLIDSSSQNQIRKRIVLEKLSKVLPGLLVPLQITLGDIYTQLKNLVRTFRLTNRNIIHKPAEWTLIAMVLLSLLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNEDLESLTIIFRTSCLPE
Protein: Cilia- and flagella-associated protein 36 (Coiled-coil domain-containing protein 104) (Q96G28)
Organism: Homo sapiens (Human)
Function: May act as an effector for ARL3.
Subcellular location: Nucleus {ECO:0000303|PubMed:19680650}. Cytoplasm {ECO:0000303|PubMed:19680650}. Cell projection, cilium, flagellum {ECO:0000305}.
Interaction partners:
- ADP-ribosylation factor-like protein 3
Sequence:
MAAEEEDEVEWVVESIAGFLRGPDWSIPILDFVEQKCEVFDDEEESKLTYTEIHQEYKELVEKLLEGYLKEIGINEDQFQEACTSPLAKTHTSQAILQPVLAAEDFTIFKAMMVQKNIEMQLQAIRIIQERNGVLPDCLTDGSDVVSDLEHEEMKILREVLRKSKEEYDQEEERKRKKQLSEAKTEEPTVHSSEAAIMNNSQGDGEHFAHPPSEVKMHFANQSIEPLGRKVERSETSSLPQKDLKIPGLEHASIEGPIANLSVLGTEELRQREHYLKQKRDKLMSMRKDMRTKQIQNMEQKGKPTGEVEEMTEKPEMTAEEKQTLLKRRLLAEKLKEEVINK
Protein: Sodium/hydrogen exchanger 3 (Na(+)/H(+) exchanger 3) (NHE-3) (Solute carrier family 9 member 3) (P48764)
Organism: Homo sapiens (Human)
Function: Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:19088451, ECO:0000269|PubMed:26358773}; Multi-pass membrane protein {ECO:0000269|PubMed:35613257}. Cell membrane {ECO:0000269|PubMed:25851603, ECO:0000269|PubMed:35613257}; Multi-pass membrane protein {ECO:0000269|PubMed:35613257}. Recycling endosome membrane {ECO:0000269|PubMed:35613257}; Multi-pass membrane protein {ECO:0000269|PubMed:35613257}. Early endosome membrane {ECO:0000269|PubMed:25851603}; Multi-pass membrane protein {ECO:0000269|PubMed:35613257}. Note=In intestinal epithelial cells, localizes to the ileal brush border. Phosphorylation at Ser-663 by SGK1 is associated with increased abundance at the cell membrane. Angiotensin-2 enhances apical expression (By similarity). {ECO:0000250|UniProtKB:Q28362}.
Interaction partners:
- Na
- Na
- Calcineurin B homologous protein 1
- Na
- Chloride anion exchanger
- Solute carrier family 26 member 6
- Ezrin
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Cubilin
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MWGLGARGPDRGLLLALALGGLARAGGVEVEPGGAHGESGGFQVVTFEWAHVQDPYVIALWILVASLAKIGFHLSHKVTSVVPESALLIVLGLVLGGIVWAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVVGTVWNAATTGLSLYGVFLSGLMGDLQIGLLDFLLFGSLMAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVALGGDNVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRIIEPGFVFIISYLSYLTSEMLSLSAILAITFCGICCQKYVKANISEQSATTVRYTMKMLASSAETIIFMFLGISAVNPFIWTWNTAFVLLTLVFISVYRAIGVVLQTWLLNRYRMVQLEPIDQVVLSYGGLRGAVAFALVVLLDGDKVKEKNLFVSTTIIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPRLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWSHFDRKFLSRVLMRRSAQKSRDRILNVFHELNLKDAISYVAEGERRGSLAFIRSPSTDNVVNVDFTPRSSTVEASVSYLLRENVSAVCLDMQSLEQRRRSIRDAEDMVTHHTLQQYLYKPRQEYKHLYSRHELTPTEDEKQDREIFHRTMRKRLESFKSTKLGLNQNKKAAKLYKRERAQKRRNSSIPNGKLPMESPAQNFTIKEKDLELSDTEEPPNYDEEMSGGIEFLASVTKDTASDSPAGIDNPVFSPDEALDRSLLARLPPWLSPGETVVPSQRARTQIPYSPGTFCRLMPFRLSSKSVDSFLQADGPEERPPAALPESTHM
Protein: Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25) (Q9CQI9)
Organism: Mus musculus (Mouse)
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).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 11
Sequence:
MSTPPLAPTGMASGPFGGPQAQQAAREVNTATLCRIGQETVQDIVYRTMEIFQLLRNMQLPNGVTYHTGTYQDRLTKLQDHLRQLSILFRKLRLVYDKCNENCGGMDPIPVEQLIPYVDEDGSKNDDRAGPPRFASEERREIVEVNKKLKQKNQQLKQIMDQLRNLIWDINAMLAMRN
Protein: Prohibitin-5, mitochondrial (Atphb5) (Q9LY99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}; Single-pass type II membrane protein {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Prohibitin-7, mitochondrial
- Prohibitin-2, mitochondrial
- Prohibitin-1, mitochondrial
- Prohibitin-6, mitochondrial
- At5g54100
- At5g40700
- Hypersensitive-induced response protein 4
- Invertase inhibitor-like protein
- Protein Iojap-related
- Protein Iojap
Sequence:
MPWSKFTKVALGLGAAIAAVRSTMFTVDGGQRAVMFHRFEGILEEPVGEGTHRKIPWVQKPYIFDIRTKPYKINTDSGTKDLQMVNLTLRVMFRPDVVKAVVAQFNADELLTERPQVSALIRETLIKRAKEFNIVLDDVSITGLSYGKEFSLAVERKQVAQQEAERSKFVVAKADQERRAAVIRAEGESEAARVISKATAGAGMGLIKLRRVEAAREVAITLSNSPNVVYLPSGGNMLFAMNGPSKVVA
Protein: ATP synthase subunit g, mitochondrial (ATPase subunit g) (Q12233)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion membrane {ECO:0000250}.
Interaction partners:
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit e, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 4
- ATP synthase subunit d
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit a
Sequence:
MLSRIQNYTSGLVSKANLLSSKALYYGKVGAEISKQIYLKEGLQPPTVAQFKSVYSNLYKQSLNFALKPTEVLSCLKNIQKNELLKYGAYGIQLIGFYSVGEIIGRRKLVGYKHH
Protein: E3 ubiquitin-protein ligase synoviolin (EC 2.3.2.27) (RING-type E3 ubiquitin transferase synoviolin) (Synovial apoptosis inhibitor 1) (Q9DBY1)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Required for embryogenesis. Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1. During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:29907570}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.
Interaction partners:
- Protein sel-1 homolog 1
- Derlin-1
- Transitional endoplasmic reticulum ATPase
- Protein OS-9
- Derlin-2
- Derlin-3
- Endoplasmic reticulum lectin 1
- Family with sequence similarity 8, member A1
- Selenoprotein S
- Lipid droplet-regulating VLDL assembly factor AUP1
Sequence:
MFRTAVMMAASLALTGAVVAHAYYLKHQFYPTVVYLTKSSPSMAVLYIQAFVLVFLLGKVMGKVFFGQLRAAEMEHLLERSWYAVTETCLAFTVFRDDFSPRFVALFTLLLFLKCFHWLAEDRVDFMERSPNISWLFHCRIVSLMFLLGILDFLFVSHAYHSILTRGASVQLVFGFEYAILMTMVLTIFIKYVLHSVDLQSENPWDNKAVYMLYTELFTGFIKVLLYMAFMTIMIKVHTFPLFAIRPMYLAMRQFKKAVTDAIMSRRAIRNMNTLYPDATPEELQAVDNVCIICREEMVTGAKRLPCNHIFHTSCLRSWFQRQQTCPTCRMDVLRASLPAQSPPPPEPADQGPPPAPHPQPLLPQPPNFPQGLLPPFPPGMFPLWPPMGPFPPVPPPPSSGEAAAPPPTSTAVSRPSGAATTTAAGTSTSAPAPGSVPGPEAGPAPGFPFPPPWMGMPLPPPFAFPPMPVPPAGFAGLTPEELRALEGHERQHLEARLQSLRNIHTLLDAAMLQINQYLTVLASLGPPRPATSVNPTEETASTVVSAAPSTSAPSSEAPTPSPGASPPIPEAEKPPAPESVGIVEELPEDGEPDAAELRRRRLQKLESPVAH