wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase subunit S1 (V-ATPase subunit S1) (C7-1 protein) (V-ATPase Ac45 subunit) (V-ATPase S1 accessory protein) (Vacuolar proton pump subunit S1) (O54715)
Organism: Rattus norvegicus (Rat)
Function: Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15904}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q15904}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15904}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Note=Not detected in trans-Golgi network. {ECO:0000250|UniProtKB:Q15904}.
Interaction partners:
- V-type proton ATPase subunit
- Renin receptor
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit D
- V-type proton ATPase subunit e 2
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit d 2
Sequence:
MMAATVVSRIRTGTRWAPVLWLLLSLVAVAAAVAAEQQVPLVLWSSDRDLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLATLKELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLESEDVPYTAALTAVRPSRVARDVAMVAGGLGRQLLQTQVASPAIHPPVSYNDTAPRILFWAQNFSVAYKDEWKDLTSLTFGVENLNLTGSFWNDSFAMLSLTYEPLFGATVTFKFILASRFYPVSARYWFTMERLEIHSNGSVAHFNVSQVTGPSIYSFHCEYVSSLSKKGSLLVTNVPSLWQMTLHNFQIQAFNVTGEQFSYASDCAGFFSPGIWMGLLTTLFMLFIFTYGLHMILSLKTMDRFDDRKGPTITLTQIV
Protein: Conserved protein (P71898)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Uncharacterized protein Rv2313c
- Probable sugar-transport integral membrane protein ABC transporter UspA
- Probable sugar-transport integral membrane protein ABC transporter UspB
- Probable periplasmic sugar-binding lipoprotein UspC
Sequence:
MIEPQHAVNIVLKEAARSGRADETMVLVTEKVEATLRWAGNSMTTNGVSHSRNVTVISIVRRGDSAFVGSVVSAEVDPSVLPGLVVSSQDAARSAPEAGDAAPLLADTGEPDDWDAPVPGTGAGVFTGIAGSLSRGFRGADRLYGYAHRSVSTTFLASSTGLRRRYTQPTGAIEINAKRGDASAWVGIGTPDFVEVPIDLMLERLSTRLRWAQRTVELPAGRYQTIMPPSTVADMMIYLGWSMAGRGAQEGRTAFSAPGGGTRVGERLTELPLTLFTDPAAPGLACTPFVAVSNSSETQSVFDNGMEISQVDWIRSGVINALAYPRATAAKFDAPVAVAADNLIMTGGSADLADMIAGTERGLLLTTLWYIREVDPTTLLLTGLTRDGVYLVEDGEVSAAVNNFRFNESPLDLLRRATEAGVSEPTLPREWSDWVTRTAMPPLRIPDFHMSSVSQAQ
Protein: Cytochrome c oxidase subunit NDUFA4 (Complex I-MLRQ) (CI-MLRQ) (NADH-ubiquinone oxidoreductase MLRQ subunit) (O00483)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. NDUFA4 is required for complex IV maintenance.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:23746447, ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 6C
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 7C, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 7A2, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
Sequence:
MLRQIIGQAKKHPSLIPLFVFIGTGATGATLYLLRLALFNPDVCWDRNNPEPWNKLGPNDQYKFYSVNVDYSKLKKERPDF
Protein: Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.4.19.12) (Deubiquitinating enzyme 3) (Ubiquitin thioesterase 3) (Ubiquitin-specific-processing protease 3) (Q01477)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Plays a role in regulation of silencing by interacting with SIR4. Also, in conjunction with BRE5, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of SEC23. Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation.
Interaction partners:
- UBP3-associated protein BRE5
- U1 small nuclear ribonucleoprotein A
- Protein NAM8
- Proteasome activator BLM10
- Autophagy-related protein 19
- Ubiquitin carboxyl-terminal hydrolase 2
- E3 ubiquitin-protein ligase RSP5
- Protein DOA1
- DNA-directed RNA polymerase II subunit RPB1
- Cell division control protein 48
Sequence:
MNMQDANKEESYSMYPKTSSPPPPTPTNMQIPIYQAPLQMYGYTQAPYLYPTQIPAYSFNMVNQNQPIYHQSGSPHHLPPQNNINGGSTTNNNNINKKKWHSNGITNNNGSSGNQGANSSGSGMSYNKSHTYHHNYSNNHIPMMASPNSGSNAGMKKQTNSSNGNGSSATSPSYSSYNSSSQYDLYKFDVTKLKNLKENSSNLIQLPLFINTTEAEFAAASVQRYELNMKALNLNSESLENSSVEKSSAHHHTKSHSIPKHNEEVKTETHGEEEDAHDKKPHASKDAHELKKKTEVKKEDAKQDRNEKVIQEPQATVLPVVDKKEPEESVEENTSKTSSPSPSPPAAKSWSAIASDAIKSRQASNKTVSGSMVTKTPISGTTAGVSSTNMAAATIGKSSSPLLSKQPQKKDKKYVPPSTKGIEPLGSIALRMCFDPDFISYVLRNKDVENKIPVHSIIPRGIINRANICFMSSVLQVLLYCKPFIDVINVLSTRNTNSRVGTSSCKLLDACLTMYKQFDKETYEKKFLENADDAEKTTESDAKKSSKSKSFQHCATADAVKPDEFYKTLSTIPKFKDLQWGHQEDAEEFLTHLLDQLHEELISAIDGLTDNEIQNMLQSINDEQLKVFFIRNLSRYGKAEFIKNASPRLKELIEKYGVINDDSTEENGWHEVSGSSKRGKKTKTAAKRTVEIVPSPISKLFGGQFRSVLDIPNNKESQSITLDPFQTIQLDISDAGVNDLETAFKKFSEYELLPFKSSSGNDVEAKKQTFIDKLPQVLLIQFKRFSFINNVNKDNAMTNYNAYNGRIEKIRKKIKYGHELIIPEESMSSITLKNNTSGIDDRRYKLTGVIYHHGVSSDGGHYTADVYHSEHNKWYRIDDVNITELEDDDVLKGGEEASDSRTAYILMYQKRN
Protein: Dynein axonemal intermediate chain 4 (WD repeat-containing protein 78) (Q8T0V3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}. Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}.
Interaction partners:
Sequence:
MTPKSIQDDTYVEQFMKYNLNVMHQMTNFTTMVAKSTTRSRTRSSVRAGIGGNKQSIDDLMNGILYETINWEPYSTVEALEEAYEPKPYTKSFLKITLRKSDFFEIHSQTQTTVAKGSPEGDDAERDNRNYEYLTIGKGKIRRRSDNDAQTDTLLFTTRAVNTILITKATVSSYVSNFEMYDTLNNITKEFATATMSSVKDLTSALAQTEDADTFEDDEAVAEKDKVSSQIERLFRSPEFRNAIMYMGRTLSSNTNEAGLRRFRNFDQVERWNAEAEYVYSMNLLFRLVPEPSKDERKAVSDIDFCRSNGDILAVAYGLYSFSSQHVPTSGSVFLWSIKNPGEPERAYYYDVPVTAINFSPFLPSLLAIGLYDGSVEVRDVSSLQDTPVAVSQRSTSPGSSPVVAIRWIKQVSDDDHETDIDPFLSLSQDGSVTRFRIIKSPFLLGFTQMILERVEGHPEGIFVHPSSRIPCESNRHPQGLSITTHPLHKDIYYVLTDEGCIHKCSINYQHQYLEVLRCHDGGVTVMEFSPWSPKLFLTCGNDWFVRIWVDGITRPLLELLDEMTPVHWAKWSPTHSTIIVTVNRETANVWDFRRNLLRPMSKHKMDSSFNTVARFSHCGRTLVIGNERGNTLFNALNDMPFSPHFQYDELEKAIFKAIGNDHELLMELKSIGFFGYPNKKAVF
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A8I6GMA3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEEYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQACKPHHPNTEPVLGLSQTPISQQSLPLHMIPPSQVDDLSSPAKRKRTSSPTKNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Lipase 1 (EC 3.1.1.3) (Arylesterase) (EC 3.1.1.-) (Q9S2A5)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes the hydrolysis of fatty acid esters with a preference for mid-length acyl chain (C10-C16). Is able to hydrolyze the triacylglycerol triolein and mixed triacylglycerols from a wide range of natural oils; better activity is obtained with corn-, wheat germ- and olive oil that have higher content of linoleic and/or oleic acid (C18:2; C18:1, cis). Tween detergents are also substrates for this enzyme. Displays arylesterase activity towards p-nitrophenyl alkanoate esters and alpha- and beta-naphthyl esters.
Subcellular location: Secreted {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}.
Interaction partners:
- Bifunctional protein
- ATPase
Sequence:
MRRFRLVGFLSSLVLAAGAALTGAATAQAAQPAAADGYVALGDSYSSGVGAGSYISSSGDCKRSTKAHPYLWAAAHSPSTFDFTACSGARTGDVLSGQLGPLSSGTGLVSISIGGNDAGFADTMTTCVLQSESSCLSRIATAEAYVDSTLPGKLDGVYSAISDKAPNAHVVVIGYPRFYKLGTTCIGLSETKRTAINKASDHLNTVLAQRAAAHGFTFGDVRTTFTGHELCSGSPWLHSVNWLNIGESYHPTAAGQSGGYLPVLNGAA
Protein: (thale cress) hypothetical protein (A0A178UNT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDEEATSWIRRAKFSQTVSYRLNSSKLASLPFMINQDKFSGLKAIPQRSSSSSSASSSDPKLVSSNSQTTGDTSSLEAADVYVVDSEIQTNPVTHKQRSVSPSPQMAVPDVFKEARSERKRFSTPHPRRVESEKGMKPKLSHKNSFDKRSFNLRSPSGPIRDLGTLRIQERVKSKKDTGWSKLFDNTGRRVSAVEASEEFRVDMSKLFFGLKFAHGLYSRLYHGKYEDKAVAVKLITVPDDDDNGCLGARLEKQFTKEVTLLSRLTHPNVIKFVGAYKDPPVYCVLTQYLPEGSLRSFLHKPENRSLPLKKLIEFAIDIARGMEYIHSRRIIHRDLKPENVLIDEEFHLKIADFGIACEEEYCDMLADDPGTYRWMAPEMIKRKPHGRKADVYSFGLVLWEMVAGAIPYEDMNPIQAAFAVVHKNIRPAIPGDCPVAMKALIEQCWSVAPDKRPEFWQIVKVLEQFAISLEREGNLNLSSSKICKDPRKGLKHWIQKLGPVHAGGGGGSSSSGLGGSALPKPKFA
Protein: Protein FAM163A (Cebelin) (Neuroblastoma-derived secretory protein) (Q96GL9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTAGTVVITGGILATVILLCIIAVLCYCRLQYYCCKKSGTEVADEEEEREHDLPTHPRGPTCNACSSQALDGRGSLAPLTSEPCSQPCGVAASHCTTCSPYSSPFYIRTADMVPNGGGGERLSFAPTYYKEGGPPSLKLAAPQSYPVTWPGSGREAFTNPRAISTDV
Protein: Putative polypeptide N-acetylgalactosaminyltransferase 9 (pp-GaNTase 9) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 9) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9) (Q8MRC9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties.
Subcellular location: [Isoform A]: Golgi apparatus membrane {ECO:0000269|PubMed:30158631}; Single-pass type II membrane protein {ECO:0000269|PubMed:30158631}.; SUBCELLULAR LOCATION: [Isoform B]: Golgi apparatus membrane {ECO:0000269|PubMed:30158631}; Single-pass type II membrane protein {ECO:0000269|PubMed:30158631}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MAFIWRRRSTTIVKLVAFALAIWFCIAFLVYTDDTRRRAAQEGAGASGAGSAPGVGGGAGGLGDPIALALRNEPAGEDFGINGNVIGGGGQKQAHDEADIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDPPANFEENPGELGKPVRLPKEMSDEMKKAVDDGWTKNAFNQYVSDLISVHRTLPDPRDAWCKDEARYLTNLPKTDVIICFHNEAWTVLLRTVHSVLDRSPEHLIGKIILVDDYSDMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANHAKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIDVISDETLEYHYRDSGGVNVGGFDWNLQFSWHPVPERERKRHNSTAEPVYSPTMAGGLFSIDREFFDRLGTYDSGFDIWGGENLELSFKTWMCGGTLEIVPCSHVGHIFRKRSPYKWRSGVNVLKKNSVRLAEVWMDEYSQYYYHRIGNDKGDWGDVSDRRKLRNDLKCKSFKWYLDNIYPELFIPGDSVAHGEIRNLGYGGRTCLDAPAGKKHQKKAVGTYPCHRQGGNQYWMLSKAGEIRRDDSCLDYAGKDVTLFGCHGGKGNQFWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLENYDSSKL
Protein: Golgi apparatus membrane protein-like protein ECHIDNA (Q8LEK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates trans-Golgi-network trafficking and cell elongation. Required for keeping the appropriate balance between secretory trafficking and vacuolar targeting of a subset of proteins. The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins and cell wall components (e.g. pectin and hemicellulose) to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane; Multi-pass membrane protein.
Interaction partners:
- Protein YIP
- Protein YIP4a
- Protein YIP
- Serine/threonine-protein kinase ATG1c
- Serine/threonine-protein kinase ATG1a
- Serine/threonine-protein kinase ATG1t
- Serine/threonine-protein kinase ATG1b
- V-type proton ATPase subunit a1
- Syntaxin-61
- Ras-related protein RABA2a
Sequence:
MDPNNQIQAPVENYANPRTCLFHVLFKGAALAFYILSALFFNSFVIIFVVTVLLAALDFWVVKNVSGRILVGLRWWNEINDLGESVWKFESLDQESLARMNKKDSWLFWWTLYLAAAAWFILGVFSLIRFQADYLLVVGVCLSLNVANIIGFTKCKKDAKKQFQQFASQTIASRFQSTVQSAFTLV
Protein: Neuronal acetylcholine receptor subunit alpha-9 (Nicotinic acetylcholine receptor subunit alpha-9) (NACHR alpha-9) (Q9UGM1)
Organism: Homo sapiens (Human)
Function: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion.
Subcellular location: Synaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:25282151}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit alpha-10
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-7
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit alpha-4
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit alpha
- Acetylcholine receptor subunit beta
Sequence:
MNWSHSCISFCWIYFAASRLRAAETADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWARVVILKYMSRVLFVYDVGESCLSPHHSRERDHLTKVYSKLPESNLKAARNKDLSRKKDMNKRLKNDLGCQGKNPQEAESYCAQYKVLTRNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFIMVFVMTILIIARAD
Protein: S-phase cyclin A associated protein in the ER (H3BS25)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQSTAVDCKITSSTTGDKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIPSPSTDRINVTSNARRSLNFGGSTGTVPAPRLAPTGVSWADKVKAHHTGSTASSEITPAQSCPPMTVQKASRKNERKDAEGWETVQRGRPIRSRSTAVMPKVSLATEATRSKDDSDKENVCLLPDESIQKGQFVGDGTSNTIESHPKDSLHSCDHPLAEKTQFTVSTLDDVKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDPSDISNVSAANLSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQI
Protein: Phagosome assembly factor 1 (O08654)
Organism: Rattus norvegicus (Rat)
Function: Plays a regulatory role in autophagic activity. In complex with BCAS3, associates with the autophagosome formation site during both non-selective and selective autophagy.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BSU1}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q9BSU1}. Note=The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner. {ECO:0000250|UniProtKB:Q9BSU1}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Kinesin-like protein KIF17
- Protein lin-7 homolog A
Sequence:
MLDLEVVPERSLGNEQWEFTLGMPLAQAVAILQKHCRIIKNVQVLYSEQSPLSHDLILNLTQDGIKLLFDAFNQRLKVIEVYDLTKVKLKYCGVHFNSQAIAPTIEQIDQSFGATHPGVYNSAEQLFHLNFRGLSFSFQLDSWTEAPKYEPNFAHGLASLQIPHGATVKRMYIYSGNSLQDTKAPMMPLSCFLGNVYAESVDVIRDGTGPSGLRLRLLAAGCGPGVLADAKMRVFERAVYFGDSCQDVLSMLGSPHKVFYKSEDKMKIHSPSPHKQVPSKCNDYFFNYFTLGVDILFDANTHKVKKFVLHTNYPGHYNFNIYHRCEFKIPLAIKKENAGGQTEICTTYSKWDSIQELLGHPVEKPVVLHRSSSPNNTNPFGSTFCFGLQRMIFEVMQNNHIASVTLYGPPRPGAHLRTAELP
Protein: T-complex protein 1 subunit alpha (TCP-1-alpha) (CCT-alpha) (P12612)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- Phosducin-like protein 2
- Actin
- Tubulin beta chain
Sequence:
MSQLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKMLVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVVIIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTLGKETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDVKRRSYRNYGLDLIRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPEPPKEDPHDH
Protein: Adenosine receptor A3 (P0DMS8)
Organism: Homo sapiens (Human)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q28309}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Kininogen-1
- Guanine nucleotide-binding protein G
- Adenosine receptor A1
Sequence:
MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE
Protein: Uncharacterized protein C688.12c (Q9P6L4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000269|PubMed:10759889}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889}.
Interaction partners:
Sequence:
MSEEESPYQLTKTFSNPKNNKIGLAIFLIGAFINLIHIYKPKGPSNNPTKRNYHISFGPPGKIRWFPLGIRKEVRSNVSGREIIIKMIITFILVQTTLITLDLYVFGATGLGLILSWKLFEVACANPEDEALLAERKQRLKEQREKKEQKKEQKKEKKTERRKKKKL
Protein: RPA1 related single stranded DNA binding protein, X-linked (B1AQ74)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
NNEDPYGDIWLTDKQPEEHNFSDTKIISLSHLEMTWTNRRNFPALLVRILHKSKLRYYGKPDKKMIEPYQTFLEVADSSGTVSVIMWNALCPEWYKSLRVGLVLLLQDYSVKKSYPFRIQPVPVDPQIKLISTMEICLNLRDPPTNIIIIPEKQVKPEWRLPKLNHRFTTRSELDDMPENCICDVIGLLVFVGRVQRSKKKENREDFWSYRWIHIADGTSEQPFIVELFSTSQPEIFENIYPMAYFVCTQLKVVRNDNQVPKLLYLTTTNESGVFITGHRGQPYTYDAKNANRPSTSQAARVEIQERNGKRHQDDEPVNSQYFQTTSTNLSLSNKIRILQGPHANPVAVPQPGASVQTKGIKPGMPSIFNRRANINANLQGKARKTISDRWESQLWREKKFGLIDHLHYSRVYPESIPRKFMFEHRKFLSDQYNSQPAKYVPPEGRPPKLDDFKSARSLGHFEVTILGLNHEIAIDVAFLPMYCPEDIRTSQIDTLLTSMNYSCAYPQDTTGNDRLPGPRAVAGDIIKAATELDRVHIVGILDICNLGNNKVEVYLHKIYSPENTS
Protein: Putative cytochrome P450 137 (EC 1.14.-.-) (P9WPM5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Polyketide synthase Pks13
- Putative cytochrome P450 141
- Mycocyclosin synthase
- Cytochrome P450 130
- Peptide synthetase MbtE
- Possible oxygenase
- Possible electron transfer protein FdxB
- Transmembrane protein
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
- DNA polymerase I
Sequence:
MVLRSLASPAALTDPKRCASVVGVAAFAVRREHAPDALGGPPGLPAPRGFRAAFAAAYAVAYLAGGERRMLRLIRRYGPIMTMPILSLGDVAIVSDSALAKEVFTAPTDVLLGGEGVGPAAAIYGSGSMFVQEEPEHLRRRKLLTPPLHGAALDRYVPIIENSTRAAMHTWPVDRPFAMLTVARSLMLDVIVKVIFGVDDPEEVRRLGRPFERLLNLGVSEQLTVRYALRRLGALRVWPARARANTEIDDVVMALIAQRRADPRLGERHDVLSLLVSARGESGEQLSDSEIRDDLITLVLAGHETTATTLAWAFDLLLHHPDALRRVRAEAVGGGEAFTTAVINETLRVRPPAPLTARVAAQPLTIGGYRVEAGTRIVVHIIAINRSAEVYEHPHEFRPERFLGTRPQTYAWVPFGGGVKRCLGANFSMRELITVLHVLLREGEFTAVDDEPERIVRRSIMLVPRRGTRVRFRPAR
Protein: Homeobox protein SIX6 (Optic homeobox 2) (Sine oculis homeobox homolog 6) (Six9 protein) (Q9QZ28)
Organism: Mus musculus (Mouse)
Function: May be involved in eye development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Visual system homeobox 2
- Homeobox protein OTX2
- Paired box protein Pax-6
- Ventral anterior homeobox 2
- Dachshund homolog 1
Sequence:
MFQLPILNFSPQQVAGVCETLEESGDVERLGRFLWSLPVAPAACEALNKNESVLRARAIVAFHGGNYRELYHILENHKFTKESHAKLQALWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRHLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQQQVLSQGPGRVLRSEGEGTPEVLGVASSPAASLSSKAATSAISITSSDSECDI