wanglab/gogpt-training-data huggingface dataset:
Protein: G-protein-signaling modulator 1 (Activator of G-protein signaling 3) (Q86YR5)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction.
Subcellular location: Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Nuclear mitotic apparatus protein 1
- Partitioning defective 3 homolog B
- Guanine nucleotide-binding protein G
- FERM and PDZ domain-containing protein 1
- Protein inscuteable homolog
- Dexamethasone-induced Ras-related protein 1
Sequence:
MAGPAPPVADELPGPAARRLYSRMEASCLELALEGERLCKAGDFKTGVAFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLKEHGRALEYHKHDLLLARTIGDRMGEAKASGNLGNTLKVLGRFDEAAVCCQRHLSIAQEQGDKVGEARALYNIGNVYHAKGKQLSWNAANATQDPGHLPPDVRETLCKASEFYERNLSLVKELGDRAAQGRAYGNLGNTHYLLGNFTEATTFHKERLAIAKEFGDKAAERRAYSNLGNAHVFLGRFDVAAEYYKKTLQLSRQLRDQAVEAQACYSLGNTYTLLQDYERAAEYHLRHLLIAQELADRVGEGRACWSLGNAYVSMGRPAQALTFAKKHLQISQEIGDRHGELTARMNVAQLQLVLGRLTSPAASEKPDLAGYEAQGARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSLPLPVRSRKYQEGPDAERRPREGSHSPLDSADVRVHVPRTSIPRAPSSDEECFFDLLTKFQSSRMDDQRCPLDDGQAGAAEATAAPTLEDRIAQPSMTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRITHSNAGHLRGHGEPQEPGDDFFNMLIKYQSSRIDDQRCPPPDVLPRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGGPEQGAGGPPEPQQQCQPGAS
Protein: Probable phosphoadenosine phosphosulfate reductase (EC 1.8.4.8) (3'-phosphoadenylylsulfate reductase) (PAPS reductase, thioredoxin dependent) (PAdoPS reductase) (Q10270)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier (By similarity). Required for methionine synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenylyl-sulfate kinase
- Sulfite reductase subunit beta
- Probable sulfite reductase flavoprotein component
- Sulfate adenylyltransferase
- 3'
- Siroheme biosynthesis protein met8
- Probable 3-mercaptopyruvate sulfurtransferase
- Probable uroporphyrinogen-III C-methyltransferase
- Probable sulfate permease C869.05c
- Homoserine O-acetyltransferase
Sequence:
MSSIDTPANKLQAKTLFHPEHLEYINKQLSELSPQDILKWCRWTLPSLFQTSALGLSGLVIMDMLSKMDMNVPLIFINTLHHFPETLDLLEKVKTKYPNVPVHVYRCAEAANEKEFAQKFGEKLWETDESRYDFLVKVEPASRAYSDLNVLAVFTGRRRSQGGERGSLPIVQLDGPVLKINPLANWSFTEVHNYIITNNVPYNELLNKGYRSVGDWHSTQPVREGEDERAGRWRGREKTECGLHSHPQSKFAQYMAELKKKETADQ
Protein: DNA replication complex GINS protein PSF3 (GINS complex subunit 3) (Q7ZT01)
Organism: Xenopus laevis (African clawed frog)
Function: Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730133}. Chromosome {ECO:0000269|PubMed:12730133}. Note=Associates with chromatin. {ECO:0000269|PubMed:12730133}.
Interaction partners:
Sequence:
MWEPYMPVEPGLGREENFLSLEDLLMSQEKLPCCIESGFPRLGFLDKGGDSDSIPEGSKMELPLWLAKGLYDNKRRVLSVELPKIYREGWRTVFSADANVVDLHKMGPHYYGFGSQLLNFDSPENPEIAKTILQTFVGRFRRIMDSSQNAYNEDTSGLVARLDELERSLFRAGQRGLNAFQSWERGKAAQITASNLVQNYKKRKFNEADA
Protein: MPL proto-oncogene, thrombopoietin receptor (Q5JUY5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MPSWALFMVTSCLLLAPQNLAQVSSQDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAWISLVTALHLVLGLSAVLGLLLLRWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANHSYLPLSYWQQP
Protein: Uncharacterized protein C8E4.05c (O42889)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Bifunctional purine biosynthetic protein ADE1
- Adenylosuccinate synthetase
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylglycinamide formyltransferase
- Amidophosphoribosyltransferase
- Bifunctional purine biosynthesis protein ade10
- Phosphoribosylformylglycinamidine synthase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Uncharacterized urease accessory protein ureD-like
- Methylenetetrahydrofolate dehydrogenase [NAD
Sequence:
MPVSVSDSFVFRNIFGDAEIRKIWSDENRTQEYLNWEAALARAEASLGIIPKYAGEEIQRVCKVENIDFSKLEEETINIGYPVLGVVHQLANLCSGDSGKYCHWGATTQDVTDSATVRQMIDSFKIIKGYLEKAIELATVLVIKHRETTMAGRSNLQQAVPITFGFKMARFVATLRRHHQRLCELLPRVSVLEFGGACGTLASLENKGLMVQQKLAEELGLLQPEIAWHTERDRIAEAGCFLGMLTGTLAKFATDIKLLMQTEVAEVFEPFKANRGSSSTMPQKRNPISCVYITASTSFVRQGVAALLDAMVEDHERATGAWEIEWIVLPDVFVHTVGTLKQTVFLLEGLEVHPSRMNENLSITNGLIVSEAVMMALAPKLGRDEAHDLVYRLCHLSIQENKPLVELLLAERQVTNYLSKEEVTSLLNPENYLGSTFEMIERALQIP
Protein: SXP/RAL-2 family protein Ani s 5-like cation-binding domain-containing protein (O16948)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKSYLSIIALFAVVFADFDGPMFLRYQPRNIQQSYFAIAKNYQLSQMQKNQQLQQWAQMNNLSNEYSSYTQQRSQQEQQVSQQTSQIISQLSTVQNQLESILNNDNQTGAQKRQAIQSLRYQYPQEVSVLFHIREVSMKRMGIDDDHDDSYESF
Protein: Tryptophanyl-tRNA synthetase (G3V277)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAY
Protein: Zinc finger protein 446 (Zinc finger protein with KRAB and SCAN domains 20) (Q9NWS9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger protein 24
- Zinc finger protein 397
- Zinc finger and SCAN domain-containing protein 32
- PiggyBac transposable element-derived protein 1
- Zinc finger protein 396
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein 444
- Zinc finger protein 483
- Zinc finger and SCAN domain-containing protein 9
- Zinc finger protein 232
Sequence:
MPSPLGPPCLPVMDPETTLEEPETARLRFRGFCYQEVAGPREALARLRELCCQWLQPEAHSKEQMLEMLVLEQFLGTLPPEIQAWVRGQRPGSPEEAAALVEGLQHDPGQLLGWITAHVLKQEVLPAAQKTEEPLGSPHPSGTVESPGEGPQDTRIEGSVQLSCSVKEEPNVDGQEVAPSSPPLAAQSPEGNHGHQEPASTSFHPPRIQEEWGLLDRSQKELYWDAMLEKYGTVVSLGLPPHQPEAQAQSELGMLLTGTGVCRSLRSGNESEGPPGCPEAQPPQGPGPAAWEGLSGAATPAPTVRPGTPPVPTQPTPAETRLEPAATPRKPYTCEQCGRGFDWKSVFVIHHRTHTSGPGVQSPGLATGESTEKPPQGEVAFPHHPRRSLTGPRSYPCEECGCSFSWKSQLVIHRKSHTGQRRHFCSDCGRAFDWKSQLVIHRKGHRPEVP
Protein: PdpA (B3VTA7)
Organism: Francisella tularensis subsp. novicida (strain U112)
Interaction partners:
Sequence:
YIINYNLSNINLINTQLKNTKILYRKGLISKLDYEKYKRYCIISRFKNNIDEFILYFSTNYKDSQSLKIAENIYGINGWLTFDLAYINNHKDFNFLLSPNQPILLDIQINDSFNFYKKE
Protein: Thiol S-methyltransferase TMT1A (EC 2.1.1.9) (Methyltransferase-like protein 7A) (N6-adenosine-methyltransferase TMT1A) (EC 2.1.1.348) (Protein AAM-B) (Thiol methyltransferase 1A) (Q9H8H3)
Organism: Homo sapiens (Human)
Function: Putative methyltransferase.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18477614, ECO:0000269|PubMed:19773358, ECO:0000269|PubMed:26185986}. Endoplasmic reticulum {ECO:0000269|PubMed:19773358}. Membrane {ECO:0000269|PubMed:18477614}. Microsome {ECO:0000269|PubMed:37137720}. Cytoplasm, cytosol {ECO:0000269|PubMed:37137720}. Note=Inserted in the ER membrane and migrates from the inserted site to lipid droplet. {ECO:0000269|PubMed:18477614, ECO:0000269|PubMed:19773358}.
Interaction partners:
Sequence:
MELTIFILRLAIYILTFPLYLLNFLGLWSWICKKWFPYFLVRFTVIYNEQMASKKRELFSNLQEFAGPSGKLSLLEVGCGTGANFKFYPPGCRVTCIDPNPNFEKFLIKSIAENRHLQFERFVVAAGENMHQVADGSVDVVVCTLVLCSVKNQERILREVCRVLRPGGAFYFMEHVAAECSTWNYFWQQVLDPAWHLLFDGCNLTRESWKALERASFSKLKLQHIQAPLSWELVRPHIYGYAVK
Protein: Large ribosomal subunit protein uL10 (60S acidic ribosomal protein P0) (60S ribosomal protein L10E) (P05388)
Organism: Homo sapiens (Human)
Function: Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Subcellular location: Nucleus {ECO:0000269|PubMed:19188445}. Cytoplasm {ECO:0000269|PubMed:19188445}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661, PubMed:19188445). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19188445}.
Interaction partners:
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein uL1
Sequence:
MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
Protein: DNA polymerase delta interacting protein 3 (Polymerase delta interacting protein 46) (Q6R954)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQVGLRAVPLLCLVSGGAWVGSRSQASCPLPSGSRPH
Protein: U6 snRNA-associated Sm-like protein LSm3 (P62310)
Organism: Homo sapiens (Human)
Function: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm6
- Small nuclear ribonucleoprotein G
Sequence:
MADDVDQQQTTNTVEEPLDLIRLSLDERIYVKMRNDRELRGRLHAYDQHLNMILGDVEETVTTIEIDEETYEEIYKSTKRNIPMLFVRGDGVVLVAPPLRVG
Protein: NADH-ubiquinone oxidoreductase 49 kDa subunit (EC 7.1.1.2) (NADH dehydrogenase subunit 7) (Q23883)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O75306}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75306}; Matrix side {ECO:0000250|UniProtKB:O75306}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Ribosomal protein/NADH dehydrogenase domain-containing protein
- Deoxyguanosine kinase
- NADH dehydrogenase iron-sulfur protein 7
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MLNISKIFEEVKVMKNFTLNFGPQHPAAHGVLRLIVELESENVVRVEPHIGLLHRGTEKLIEGKTYTQALPYFDRLDYVSMNVQEHAYSLAVERLYLDSLDIELEIPQRAKVIRVLFSEITRVLNHIMATTTHAMDVGALTPFLWAFEEREKLMEFYERVSGARMHAAYIRPGGVAFDLPMNISEDIYKFVIQYRKRLEEIEDMLINNRIWKQRLVDIGIVSAEEALNYGFTGPLLRGAGIVYDIRKNYPYDDYDKYDFKIIIGEENNSYTRFIIRMKEMYQSLSIIEQALNNLRPGLIKLEGVNITAPDRAFVKKDMESCINHFKFFSEGFIIPANENYTIVEAPKGEFGIYLNANDTAKPYRCRIKAPGFLHLQGLNMMSKDHLLADVVTLIGTQDIVFGEVDR
Protein: T-cell-specific surface glycoprotein CD28 (CD antigen CD28) (P31041)
Organism: Mus musculus (Mouse)
Function: Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27460989}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P10747}.
Interaction partners:
- T-lymphocyte activation antigen CD80
- T-lymphocyte activation antigen CD86
- Tumor necrosis factor receptor superfamily member 5
- Protein kinase C theta type
- ICOS ligand
- CD40 ligand
- Cytotoxic T-lymphocyte protein 4
- Growth factor receptor-bound protein 2
- Inducible T-cell costimulator
- Phosphatidylinositol 3-kinase regulatory subunit alpha
Sequence:
MTLRLLFLALNFFSVQVTENKILVKQSPLLVVDSNEVSLSCRYSYNLLAKEFRASLYKGVNSDVEVCVGNGNFTYQPQFRSNAEFNCDGDFDNETVTFRLWNLHVNHTDIYFCKIEFMYPPPYLDNERSNGTIIHIKEKHLCHTQSSPKLFWALVVVAGVLFCYGLLVTVALCVIWTNSRRNRLLQSDYMNMTPRRPGLTRKPYQPYAPARDFAAYRP
Protein: Putative pumilio homolog 8, chloroplastic (APUM-8) (AtPUM8) (Q9LM20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Subcellular location: Plastid, chloroplast {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:20214804}.
Interaction partners:
- Pumilio homolog 24
- Pumilio homolog 23
- Pumilio homolog 26
- Nucleolin 2
- Large ribosomal subunit protein P2v
- Putative pumilio homolog 22
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Putative pumilio homolog 25
Sequence:
MMRGEFGEASSLSRSPSSPLQTEPHPQSPKFYRNHYVFSGDHSSYNSSSRFCLRSPSDYSLSSYFSNGLCSSEDGSSQFASPPLDGLMTKYNFGGDDLGLCESFDLLNVGEEDKTHHQTQRSSFGNYEANGDGGFRYYSGFGVDQKDHQISNSWNLGMQSCNMNNYSVPVHGKSGVGALFDHQGISSNPNESLPKVSEFQGYVYFMAKDQHGCRFLQWIFEDGSALDALVIFSEVIPHVVELMMDPFGNYLMQKLLDVCNEEQRTQIILMVTSEPGQLIRISLNAYGTRVVQRLVESIKTRKQISLVKSALRPGFLNLIRDLNGNHVIQRCLQCLSTEDNEFIFEDATKFCIDIATHRHGCCVLQKCIAYSSGLQREKLVTEISRNSLFLAQDPYGNYAVQFVLELRDFSAIAAMLAQLKGHYVELSMQKFSSHMVERCLTHCPESRPQIVRELISVPHFDILIQDPYANFVIQAALAVTKGSLHATLVEVIRPHSILRNNPYCKRIFSRNLLKN
Protein: Reticulon (Q4G5W2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Reticulon 4 receptor.
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1-B
- Oligodendrocyte myelin glycoprotein b
- Atlastin-1
- Myelin-associated glycoprotein
- Atlastin GTPase 2.
- Atlastin 3
- Receptor expression-enhancing protein.
Sequence:
MDDQISSTTPSYDVHHDDEGEFRAEKQANSLMDEDFSSSEAQAHVPEVEGILDLAGGAKDALERHRSTMPRKEEPLLDFGEPEPEPSSTIKPEPEAPKPAPISSFGDASPKQAKPEEKEEKPTVAPYKCNSSCSLVELLYWRDLQRTGVVFGAGLFLLLSLSMCSIISVLSYVALALLSVTVSFRIYKGILQAVQKSEDGHPFKMYLDKDTALPAEMVHKYSDSTLVHINTVIKELRRLFLVEDLVDSLKFAVLMWILTYVGALFNGLTLIILGFIGAFSCPVIYEKHQAQIDHYYGLVNKQFKDVVGKIQAKIPGAKPKTE
Protein: Protein SCO1 homolog, mitochondrial (O75880)
Organism: Homo sapiens (Human)
Function: Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9878253}. Mitochondrion inner membrane {ECO:0000269|PubMed:15229189}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase copper chaperone
- Heme A synthase COX15
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Surfeit locus protein 1
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase assembly factor 6 homolog
- Cytochrome c oxidase subunit 6B1
Sequence:
MAMLVLVPGRVMRPLGGQLWRFLPRGLEFWGPAEGTARVLLRQFCARQAEAWRASGRPGYCLGTRPLSTARPPPPWSQKGPGDSTRPSKPGPVSWKSLAITFAIGGALLAGMKHVKKEKAEKLEKERQRHIGKPLLGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSITTLPDLTPLFISIDPERDTKEAIANYVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMRPYRKKS
Protein: T. brucei spp.-specific protein (Q384E5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPFGCRNSRIFVTPQSIYTNCPLWPVIPIPQIPRVAHGFPTLHAPLFRKSMRTRRRHHLVKRLQPAAGLGYPRPGCAGFGCFRFQTFLEQGQMGSLVQPLFRSVDCQPRPFQRRFSYCVFSTASTVWPVHAGSPHHGSSVPTSNSILTNTKPLLSSTTIANGVLGSRAPKLIGEGG
Protein: RPGR interacting protein 1 (A0A8I6APX2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLHLLDHMPEDRPVRDTDSIPLSKGTSGKNVKAQSRSGRMNREKLNYRPFQLHEDPMVVKELSPKQRDKSRRPRTNMKRSTTTQPDLRTLAVLQEPVRQRPPWVSASLRSLVTRHAQVPRRKAHMQRQCPSTAAGSTQSRVHVGRRPGPNDRRSHTAPPTFKDYVMDENPSMEVTSEPSQPTHIMTTDSTHAEETSRSPEKMSKVEKLEQRSSLECAEKAAELRATIKENVELIRLKKLLYERSASLAATEAQLTRVQEAYEDLLQKNQGILDATHDAFLSQVNELKAELSEESKKAVSLRIQLGDVSILQKTLKEFQVRVEDLESERKLLSDSYDRLLENMLESSHQPLESSHQPHWNRELMAEQLPQQVCPLLDQVGAELEETKVLLQVTNQVAQDEQLTFQVTSILCQHKQEEENLQSTATIPLFPEELFELAVQPTLLAQTVQRESSEPRVQEESSLSQVLNELQVSHAETALELEKTRDMLLLQRKINLCYQEELEATLTKADKENRDHEETMERLTHLLDFKNSRIMQLEGAGGEDLGVLEYWMRLCLPLKSSLQACNKRKKAQAYLSVNVLGGWKAQNDESRSEAWAPQNELRIEITRCCGLRSRWGGRQPSPYVMYRFFTFPDHATTVIPASSDPYFKDQALFPVPVTSDLDEYLRREALSLYVFDDEDPEPGSFLGRVQVPLLPLAQNKSLKGDFNLTDAGEMSNGSIQVQLDWKSHHLPPESLQMSEAEKPEEEEEEEEEDEEKEEREEEEKEEEKEEEEEEEEEKEEENKDGLEVSFTEEQTPFLPQAQIASTEIPIEAGQYQEKRKPPVIAERKEKERQVTSYSRRKHSKKPGVQGKNRMEYLSCNILNGDIQQMRYTEWKFSGLKMYEDDGLKVQQKEEEQPSPHSALRQDQPSHSINASSPTDQESSEQASEVSEAHTPDSDDIVVTPQSQTCPKADSEKMCIEIVSLAFCPEADVMADENIRQVYVEYKFCDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPVEHQDRRQFLFAMLQAQNSDEGRLKFTVVSDPLDEEKKECQDIGYAYLELWQIFQSGKDILEQELEIVSPGNQAIQIGRLKVSLQATAALHGIYKEMTEDLFS
Protein: 3-methylornithine synthase (EC 5.4.99.58) ((2R,3R)-3-methylornithine synthase) ((3R)-3-methyl-D-ornithine synthase) (Pyrrolysine biosynthesis protein PylB) (Q46E78)
Organism: Methanosarcina barkeri (strain Fusaro / DSM 804)
Function: Catalyzes the isomerization of L-lysine to (2R,3R)-3-methylornithine via a radical-based mechanism, a step in the biosynthesis pathway of pyrrolysine.
Interaction partners:
- 3-methyl-D-ornithine--L-lysine ligase
- Pyrrolysine--tRNA ligase
- Diaminopimelate decarboxylase
- Pyrrolysine synthase
- Monomethylamine methyltransferase MtmB1
- L-lysine 2,3-aminomutase
- Biotin synthesis BioY protein
- Biotin--
- Methylcobamide:CoM methyltransferase MtaA
Sequence:
MIQKMALDEFDSLGDKVIEGYQLTDNDLRTLLSLESKEGLERLYSAARKVRDHYFGNRVFLNCFIYFSTYCKNQCSFCYYNCRNEINRYRLTMEEIKETCKTLKGAGFHMVDLTMGEDPYYYEDPNRFVELVQIVKEELGLPIMISPGLMDNATLLKAREKGANFLALYQETYDTELYRKLRVGQSFDGRVNARRFAKQQGYCVEDGILTGVGNDIESTILSLRGMSTNDPDMVRVMTFLPQEGTPLEGFRDKSNLSELKIISVLRLMFPKRLIPASLDLEGIDGMVLRLNAGANIVTSILPPDSQLEGVANYDRDLEERDRDIKSVVRRLEIMGMKPARQADFEAVLGC
Protein: Ferric uptake regulation protein (Q92LL6)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
Sequence:
MSQSKNRIEELEGILREGGVRVTRQRAAILKILAEAEDHPDASELHRRAKEIDATVSLSTVYRTLSALEQQGVVQRHAFENATARFETADAPHHDHLIDIETGAVIEFRSDKIEQLQAEIAAELGYDLVRHRLELYCRKRKD
Protein: Phospholipid-transporting ATPase VA (EC 7.6.2.1) (ATPase class V type 10A) (Aminophospholipid translocase VA) (P4-ATPase flippase complex alpha subunit ATP10A) (O60312)
Organism: Homo sapiens (Human)
Function: Catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. Initiates inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in membrane tubulation and cell trafficking. Facilitates ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell spreading on extracellular matrix. Has low flippase activity toward glucosylceramide (GlcCer).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30530492}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B.
Interaction partners:
- Cell cycle control protein 50A
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase VD
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase IC
- E3 ubiquitin-protein ligase makorin-3
- Ubiquitin-protein ligase E3A
- Small nuclear ribonucleoprotein-associated protein N
- MAGE-like protein 2
Sequence:
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLADNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILAITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPADILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDLSRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRSKLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVYSFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQIQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQRGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEKVSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELKSPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQPTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHDQVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCSSVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENSEELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIAYACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPPSTSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRSKLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHWCYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGVLDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDLFTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSNPYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSAPKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVREHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNWISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ