wanglab/gogpt-training-data huggingface dataset:
Protein: 3-hydroxy-4-methyl-anthranilyl-[aryl-carrier protein] 5-monooxygenase (EC 1.14.13.223) (FAD/NADH-dependent hydroxylase SibG) (C0LTM1)
Organism: Streptosporangium sibiricum
Function: Involved in the biosynthesis of the antitumor antibiotic sibiromycin. Hydroxylates the C5 position of the peptidyl carrier protein (PCP)-bound 4-methyl-3-hydroxyanthranilic acid (4-MHA or 3H4MAA), leading to the formation of the fully substituted anthranilate moiety found in sibiromycin.
Interaction partners:
Sequence:
MRILVNGGGPAGMAFAMFAARSGRGDEITVRDWTGPGDTYGFGVILPPAAVEVFRDAEPDLADELNSHITAWDRLSVHRHGRTASIPAPRLGAMDRRTLLKVLRRRCAERGVRFEHGAVDPALGDHDLVVAADGARSVTRRHRAAAFGTTTREIGPAYIWLGADRALEHLRFLVAETPDGPAVAHAYPYSPDRSTFLVEADGAPPPAVLAEWFAGPLGGARLLENRSRWSRFQEIHNRTWSAGNVVLIGDAAHTAHYSIGSGTRLALDDARALADALCAQPRLADALKGYEDARRPIVEHTQRIGRLSATWFTRLPDVPMERLLDDLATRGGQISWRDLATEGSGAVPVRG
Protein: Protocadherin beta-6 (PCDH-beta-6) (Q91XZ4)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27161523}; Single-pass type I membrane protein {ECO:0000269|PubMed:27161523}.
Interaction partners:
- Protocadherin beta-8
- Protocadherin beta 11
- Protocadherin beta 10
Sequence:
METTLAKTPEKRQVVFLAILLLLWEAGSEAIRYSIPEETESGYLVAHLAKDLGFRVGELATRRARIHHRGNKELLQLDVETGNLLLKEKPDREALCGATEPCVLHFQIILENPVQFFQTELQLTDINDHSPEFPDTEMLLKIQESTQPATVFLLKAAQDSDIGSNAVQNYTVSPNLHFHVVTLSRSDGRKYPELVLDRALDREEQPELTLILTALDGGAPPKSGTTTVRIEVVDINDNAPEFVQSLYSVEVPENSPLDALVVTVSARDLDAGIHGNVAYSLFQGGGGPQPFVIDEITGEIRLKGALDFEATSYYTMEIVATDSGGLSGKCTVAIQVLDVNDNAPKLTISSLTSSIPENAPEAVVAVFSVSDPDSGDNGRMVCSIQNELPFLLKPTFENYYTLAAEGPLDREIREEYNITIIVSDLGTPRLTTQHTITVQVVDINDNAPAFTQTSYTMFVHENNNPALHIGTISATDSDSGSNAHITYSLLPPHDLQLSLASLVSINADNGQLFALRAMDYEALQAFEFHVVARDGGSPALSSQALVRVVVLDDNDNAPFILYPMQNASAPCTELLPRAAEPGYLVTKVVAVDSDSGQNAWLSFQLLKATEPGLFSVWAHNGEVRTTRLLSERDVPKHRLLLLVKDNGEPPRSASVTLHVLLVDGFSQPYLPLPEVQHDSSQDEDMLTLYLVIALASVSSLFLLSVLLFVGVRLCRRVREASLGACSVPEGHFSGHLVDVSGMGTLSQSYQYEVCLSGDSGTTDFKFLNHYSQ
Protein: Stationary phase gene 1 protein (P50088)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKLDSGIYSEAQRVVRTPKFRYIMLGLVGAAVVPTAYMRRGYTVPAHSLDNINGVDTTKASVMGTEQRAAMTKGKSLQEMMDDDEVTYLMFSSIM
Protein: Insulin-like growth factor 3 (B0Z6G1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MPTCHAKRLQIMPGFMLKVPSWRSVCVLYSLCCVLILPDNTEGARARCGRELVDDLEFVCGDRGFYIGKPGAARSGGPRSRGKGIVDQCCVRGCDLQHLELYCAKSKKVRRDVPASVLQTPEDQFWLVFQRRYQKLADLQRDEESASQRIRERTLYQQNLLNTKTSTQTSSTHLSSTTETPTFISHIR
Protein: Chorismatase (EC 3.3.2.13) (Q54305)
Organism: Streptomyces rapamycinicus (strain ATCC 29253 / DSM 41530 / NRRL 5491 / AYB-994) (Streptomyces hygroscopicus (strain ATCC 29253))
Function: Involved in the biosynthesis of the macrocyclic amino acid-linked polyketides rapamycin which is a potent immunosuppressant that prevents T-cell proliferation through initial binding to the immunophilin FKBP12. Catalyzes the hydrolysis of chorismate via a 1,4-conjugate elimination of water to yield (4R,5R)-4,5-dihydroxycyclohexa-1,5-dienecarboxylic acid (DCDC).
Interaction partners:
- Full equals 3-hydroxybenzoate synthase
- Chorismate synthase
- Chorismate mutase
- Chorismate mutase
- chorismate mutase
- chorismate mutase
- Anthranilate synthase component 1
- aminodeoxychorismate synthase
- Aminodeoxychorismate synthase
- Aminodeoxychorismate synthase
Sequence:
MTPPVTAPYCRFEKLGASDLDGDETLLGVIEHRTGHTGVSLAEGCPRTAVHTTTREDESFAEAWHAEGPKESGSHDGVAWARTPDYLFGVARVPEGGRYAAGTAAVYTGIFDLIGTLGYPSLARTWNYVSGINTPNADGLEVYRDFCVGRAEALDARGIDPATMPAATGIGAHGGGITCYFIAARAGDRVNMENPAVLTAHRYPQRYGPRPPVFSRATWLSPPGADDGRLFVSATAGIVGHETVHHGDVAAQCEVSLENIARVIGAENLGRHGLRRGYALADVDHLKVYVRHREDISTVRRICAERLSREATVAVLHTDIARTDLLVEIEGVVA
Protein: LD15680p (Q95RQ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALCEVSTGESSPVHDKDCDDNSTSATDVTIGNDLVLPDAVVGDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRIKLQKERAEKEKLVHQRRAEYLQNLQFQGQQEMLVYHENNISAPSSGNTNASNNNNLHQIQSNQ
Protein: Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase) (P00489)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Interaction partners:
- Glycogen debranching enzyme
- 1,4-alpha-glucan-branching enzyme
- Phosphoglucomutase-1
- UTP--glucose-1-phosphate uridylyltransferase
- Alpha-amylase
- Alpha-amylase
- Alpha-amylase
- Alpha-amylase
- Phosphoglucomutase 2 like 1
- Phosphoglucomutase 2
Sequence:
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEKIP
Protein: Cellulose-binding domain-containing protein (Q54DJ1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Multiple inositol polyphosphate phosphatase 1
Sequence:
MFKKLLFFTLTFALFALAICDNSIKITQTLSSAWEGHSTWNVVIENIGDKPIFGATIVAESGLSLERPDNLWSLDSLGNNRFGLPSWITQNGGLKAFNGTHTFGYTNAQPTSAVFSATDIRY
Protein: F-actin-capping protein subunit beta (CapZ beta) (P47756)
Organism: Homo sapiens (Human)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization. Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A9XFX6}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:A9XFX6}.
Interaction partners:
- F-actin-capping protein subunit alpha-2
- F-actin-capping protein subunit alpha-1
- Dynactin subunit 2
- Dynactin subunit 4
- F-actin-capping protein subunit alpha-3
- Alpha-centractin
- Dynactin subunit 1
- Twinfilin-1
- Dynactin subunit 6
- WASH complex subunit 5
Sequence:
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLLCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYLWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNKSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVNGLRSVQTFADKSKQEALKNDLVEALKRKQQC
Protein: Pyruvate kinase (EC 2.7.1.40) (C6KTA4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Enolase
- Glucose-6-phosphate isomerase
- Pyruvate dehydrogenase E1 component subunit beta
- Phosphoenolpyruvate carboxylase
- Pyruvate dehydrogenase E1 component subunit alpha
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L11a, putative
- 40S ribosomal protein S19
- 60S ribosomal protein L23
- Guanylate kinase
Sequence:
MSSFKYKNSAAGASMQSAANITLRQILEPNNVNLRSKKTHIVCTLGPACKSVETLVKLIDAGMDICRFNFSHGSHEDHKEMFNNVLKAQELRPNCLLGMLLDTKGPEIRTGFLKNKEVHLKEGSKLKLVTDYEFLGDETCIACSYKKLPQSVKPGNIILIADGSVSCKVLETHEDHVITEVLNSAVIGERKNMNLPNVKVDLPIISEKDKNDILNFAIPMGCNFIAASFIQSADDVRLIRNLLGPRGRHIKIIPKIENIEGIIHFDKILAESDGIMIARGDLGMEISPEKVFLAQKLMISKCNLQGKPIITATQMLESMTKNPRPTRAEVTDVANAVLDGTDCVMLSGETAGGKFPVEAVTIMSKICLEAEACIDYKLLYQSLVNAIETPISVQEAVARSAVETAESIQASLIIALTETGYTARLIAKYKPSCTILALSASDSTVKCLNVHRGVTCIKVGSFQGTDIVIRNAIEIAKQRNMAKVGDSVIAIHGIKEEVSGGTNLMKVVQIE
Protein: Prespore protein Dd31 (Q02465)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Spore coat. Note=Associated with the inner face of spore coat.
Interaction partners:
Sequence:
MEHNNNPGTPQMSSEFPASTTQTSSSAAAYDNSSHFEKEQSLMRWEQDLKLRERALANNQSAADITGPHVVVPAPATAHPRQANFPSSYPMIRLNLEEDIAIREYRQIVKFGIFVFLWEAAALVYNWVVSIGTIVYSAVDNFFLALFYMIVGVPTLYFLTRKLYRAASVPERARKSYAYLMALLGVVLFNIIFFVGFKRSGMNGLIWVISLFHNDHNAVGAMATVSLFFWFVGVFLTIALFIMYLRLNNTKRQRGEIQNAGFREYIKSR
Protein: DNA helicase 2 (S5YPI0)
Organism: Bacillus phage Troll
Interaction partners:
Sequence:
MKITVGIMYTHIDFQGDTLKAEKVRGHMHHKLGVKEEGVFHSRAYKAGVWDGITDFYDMKEDKFPTGLLQLFLEGVREMQEKYASLTYELDDTRPGALLHHDSMDKEIQLVKNGETITLRDYQYDSVKQILKEQVGIVNLATNAGKTMTAAGIIKQLFPLVARGERIAFMVHSKEILRQAKESISEALQLKPREIGMVGDGKFDIKNKKLVFVMIPTLHSALKDPTKGVTYTQKDRLVKQMAEDIAPKFLDTVNTRTLIKNYLKNWTPKTKNDLEIENILTTLAYDNAYTDKKVQMVLRSYKGELEKILMKKNKKNFEKWKTAHDFVESIRVFIGDEAHRSKGESWYSTALQCSNAQYRIALTGTVNQKDVILYQRIRALFSGVVSKVSNDDMVKRGVSSKPVIRMIEIKEPRGIELADNYLEAYKMGIVNNEYRNRFAVKVGASFYKQKKAGVLISVNHIDHGEQLKELIEAEGHECVFLKGELSSEERQEVLRRFGSGEVPFMIGTTLIDEGLDLNSIGCLILAGAGKSLRQVLQRIGRGLRLNGIDGNQTLVLDFIDRTHEILLNHSKERMKIYKDENFDMKLLGK
Protein: Aprataxin (EC 3.6.1.71) (EC 3.6.1.72) (Forkhead-associated domain histidine triad-like protein) (FHA-HIT) (Q7Z2E3)
Organism: Homo sapiens (Human)
Function: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:14755728, ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:15276230, ECO:0000269|PubMed:15380105}. Nucleus, nucleolus {ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:16777843}. Note=Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage (PubMed:15380105). Colocalizes with MDC1 at sites of DNA double-strand breaks (PubMed:20008512). Interaction with NCL is required for nucleolar localization (PubMed:16777843). {ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:15380105, ECO:0000269|PubMed:20008512}.; SUBCELLULAR LOCATION: [Isoform 12]: Cytoplasm {ECO:0000269|PubMed:15276230}.
Interaction partners:
- DNA repair protein XRCC1
- DNA repair protein XRCC4
- Aprataxin and PNK-like factor
- DNA ligase 3
- Tyrosyl-DNA phosphodiesterase 1
- Probable helicase senataxin
- Poly [ADP-ribose] polymerase 1
- DNA polymerase beta
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Atypical kinase COQ8A, mitochondrial
Sequence:
MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKDQEVKLQPGQVLHMVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ
Protein: V-type proton ATPase subunit B 1 (V-ATPase subunit B 1) (Vacuolar proton pump subunit B 1) (Q19626)
Organism: Caenorhabditis elegans
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (Probable). Essential for the proper assembly and activity of V-ATPase (By similarity). Required maternally for early embryogenesis and zygotically during morphogenesis. Specifically, involved in the clearance of apoptotic cell corpses in embryos. Also, during embryonic development, the V-ATPase is required to repress fusion of epidermal cells probably by negatively regulating eff-1-mediated cell fusion. In neurons, required for necrotic cell death by promoting intracellular acidification. Required for cell death induced by hypoxia. Required for acidification of synaptic vesicles and the release of neurotransmitters from adult neurons.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E
- Probable V-type proton ATPase subunit H 2
- V-type proton ATPase subunit C
- Probable V-type proton ATPase subunit G
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
Sequence:
MAAVDVNQPITGHKSAIIRNYNTNPRLIYQTVCGVNGPLVILNDVKFPQFSEIVKITLPDGSKRSGQVLEISKNKAVVQVFEGTSGIDAKNTICEFTGDILRTPVSEDMLGRIFNGSGKPIDKGPPVLAEDFLDINGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSASGLPHNEIAAQIVRQGGLVQLPDRPHEQTNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRIALTSAEFLAYQCKKHVLVVLTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRDGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRLIYPPINVLPSLSRLMKSAIGEGMTREDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSDDLLYLEFLTKFEKNFITQGHYENRSVFESLDIGWQLLRIFPREMLKRIPESTLEKYYPRGGAKE
Protein: Protein SEC13 homolog (A8MXL6)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}. Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
MIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKEELQMQPQIDHLP
Protein: Protein TANC2 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2) (A2A690)
Organism: Mus musculus (Mouse)
Function: Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines.
Subcellular location: Cell projection, dendritic spine {ECO:0000250|UniProtKB:F1LTE0}.
Interaction partners:
Sequence:
MFRNSLKMLLTGGKSSRKNRSSDGGSEEPPDRRQSSVDSRQSRSGQGGISTESDCAFEPDYAVPPLPVSEGDVEQELGPPPSVDEAANTLMTRLGFLLGEKVTEVQPSDQYSMEVQDENQTSAITQRISPCSTLTSSTASPPASSPCSTLPPVSTNAAAKDCSYGAVTSPTSTLESRDSGIIATLTNYSENMERTKYVGEGSKELGSGGNLKPWQSQKSSMDSCLYRVDENMAASTYSLNKIPERNLETVLSQSVQSIPLYLMPRPNSVAATSSAHLEDLAYLDEQRHTPLRTSLRMPRQSLSGARTQQDLRVRFAPYRPPDISLKPLLFEVPSITTESVFVGRDWVFHEIDAQLQSSNASVNQGVVIVGNIGFGKTAIISRLVALSCHGTRMRQIASDSPHASPKHVDANRELPLTQAPSAHSSITSGSCPGTPEMRRRQEEAMRRLASQVVAYHYCQADNAYTCLVPEFVHNVAALLCRSPQLTAYREQLLREPHLQSMLSLRSCVQDPMASFRRGVLEPLENLHKERKIPDEDFIILIDGLNEAEFHKPDYGDTIVSFLSKMIGNFPSWLKLIVTVRTSLQEITKLLPFHRIFLDRLEENEAIDQDLQAYILHRIHSSSEIQNNISLNGKMDNTTFGKLSSHLKTLSQGSYLYLKLTFDLIEKGYLVLKSSSYKVVPVSLSEVYLLQCNMKFPTQSSFDRVMPLLNVAVASLHPLTDEHIFQAINAGSIEGTLEWEDFQQRMENLSMFLIKRRDMTRMFVHPSFREWLIWREEGEKTKFLCDPRSGHTLLAFWFSRQEGKLNRQQTIELGHHILKAHIFKGLSKKVGVSSSILQGLWISYSTEGLSMALASLRNLYTPNIKVSRLLILGGANINYRTEVLNNAPILCVQSHLGYTEMVALLLEFGANVDASSESGLTPLGYAAAAGFLSIVVLLCKKRAKVDHLDKNGQCALVHAALRGHLEVVKFLIQCDWTMAGQQQGVFKKSHAIQQALIAAASMGYTEIVSYLLDLPEKDEEEVERAQINSFDSLWGETALTAAAGRGKLDVCRLLLEQGAAVAQPNRRGAVPLFSTVRQGHWQIVDLLLTHGADVNMADKQGRTPLMMAASEGHLGTVDFLLAQGASIALMDKEGLTALSWACLKGHLSVVRSLVDNGAATDHADKNGRTPLDLAAFYGDAEVVQFLVDHGAMIEHVDYSGMRPLDRAVGCRNTSVVVTLLKKGAKIGPATWAMATSKPDIMIILLSKLMEEGDMFYKKGKVKEAAQRYQYALKKFPREGFGEDLKTFRELKVSLLLNLSRCRRKMNDFGMAEEFATKALELKPKSYEAYYARARAKRSSRQFAAALEDLKEAIKLCPNNREIQRLLMRVEEECRQMQQQQQQQPPPPPQQPPQELPEEETEPEPQHEDIYSVQDIFEEEYLEQDVENVSIGLQTEARPSQGLPVIQSPPSSPAHRDSAYISSSPLGSHQVFDFRSNSSVGSPTRQGYQSTSPALSPTHQNSHYRPSPPHTSPAHQGASYRFSPPPVGGQSKEYPSPPPSPLRRGPQYRASPPAESMSVYRSQSGSPVRYQQETNVSQLPGRPKSPLSKMAQRPYQMPQLPVAVPQQGLRLQPAKAQIVRSNQPSSAVHSSTVIPTGAYGQVAHSMASKYQSSQGDMGVSQSRLVYQGSIGGIVGDGRPVQHVQASLSAGAICQHGGLTKEDLPQRPSSAYRGGMRYSQTPQIGRSQSASYYPVCHSKLDLERSSSQLGSPDVSHLIRRPISVNPNEIKPHPPTPRPLLHSQSVGLRFSPSSNSISSTSNLTPTFRPSSSIQQMEIPLKPAYDRSCDELSPVSPTQGGYPSEPTRSRTTPFMGIIDKTARTQQYPHLHQQNRTWAVSSVDTVLSPTSPGNLPQPESFSPPSSISNIAFYNKTNNAQNGHLLEDDYYSPHGMLANGSRGDLLERVSQASSYPDVKVARTLPVAQAYQDNLYRQLSRDSRQGQTSPIKPKRPFVESNV
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FU99)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Lysophospholipase 1
Sequence:
MKVSTIFSVSLIAGALAAPAVVTVTKEAPPARVTVQAVVNVEDGGRQSSLSTLEKKTKTKSQKKTKPTPSTDLDKRAQKKRSNLSEWQQKMLDQHNKKRELHKDTDSLVWNDNLAILAQSYADRYDCSGNLAHNPEFIEAIGENLAVGYDDIDAIDAWYDEIQHYDYSNPVHQGRTAHFTQLVWKDTKNVGCAYKTCGGDLYNYIVCEYDPAGNWAGEFADNVKPLK
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit A (EC 2.4.1.198) (GlcNAc-PI synthesis protein) (Phosphatidylinositol-glycan biosynthesis class A protein) (PIG-A) (P37287)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Polymeric immunoglobulin receptor
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- CD59 glycoprotein
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
Sequence:
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRERVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGIDLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLEKAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHCGPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEISETR
Protein: Transmembrane protein (Q38BQ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIKGSDPLHHGLSEGAGGNSRGDENDTVVNSNVEVMCLDMSRSSLLANSTKPPSSSCSDTPSSCSDSNMSGIDFYCRQVPIFSQGVGVDYFVNGMGGYEGHLHQQPQGGELGFDQRNKQGGKSSSSPSNFHHNVNEECSATVATRLAGGLSDDCSGNNTRRRNFNHSMCNSPELRSCGDEYAAEARRNVPGSSRGVMAAVSQTQSLGKRKIAEGNVQANLPLLRVSDCGTKTVHIIPLGNTNVTSQFKCSCCDHVFELSFVTNHADSSAKEKDQERGRNTEVGLTCTYGNGLDSNTGEATAVDRSAEFLFRQQPDRESTSLSLLGMKFDKGFRVSAGSVRGNYGSHPVQNETNASQGAVRHSLEDRRRRYQSGRFSQGTPKEIKANDSLFPSLPTFSPTSFVRAYVGEGNLPWEATLDNVPAVTVSCCVAALNLIAVQFLRHHVIDTRDHFCLFATGTYMIFASYFVAYYFLGHYTESFRRISRDKQFYIIANLIKAGILASLVPFATLHLSRIILFDEWDTNTLRNLGCIYTIPDFVSMLIVKRMSWSTWTHHLCVLLFNFFSTMNDYTQENVCRCVVVYAAFSTFAYCVNVLLASRFLGVKPGVARILSHVSVVAYLFFCGLNWVWQTYYIHRLLYGGNGHWTVYVYIALVGLVMYDDVTLCQWLIHNARNTAFAAAHHKEQRRRQ
Protein: Protein tortoise (Q8T133)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for efficient chemotaxis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11157987}.
Interaction partners:
- Probable serine/threonine-protein kinase tsuA
- DNA topoisomerase 2, mitochondrial
Sequence:
MNKTIIINNVSKYIKFKNYYSSSSTILKKKTSEIYKIKGLDIKDRKELYSLNNDSIKKKLNQLKDETNQLLKERGEELMKDLSKTLNLTSDNLKYNITKSPFTLRAYLLAANQGISFYHHELRKQINPTDDYERQKRKDLVYKLQSQEIDSLTSGGANKKKSPFLEDNNNKKSMSIEREMEIIREQQQEQQHFDQQMSNSTKWEMSQLEIQPRIDTFRQDELFVSFNPYESMSTNSQSYQLVSRLSKFVWNKELTNWEMFSSSKLNQLIPQLQLHILDKINLNNDNDNDNSIIINQFLESIKFISNEINSTDLNIFKTLNSSNNNNNSSENIIEVENGGDFKKIINNSIVDSLIYMKGHHFRITSDPFILFFQQLKENQDYFTSNEDYKQFLEKLLDTLLFETIEFDPTSTTTINGNRQFEYKLKLDLLQREAFRQFKVYQVFNTSPDAKRHEESDLRKLAHLCKTLQKRSTSDFIQESKKYLSPQILSNGLLNSNKLLVATSSSNELNQSKTSISISQLTDGLHSCIPATMSLLEFSIKNSSKDNILFDTFDGKLKNINSLDDLITKFANSKYIYLRESLSQRFSMFIQSSNNTTDNNTTTDTNDNDIIIGLNNPIYKLLIDLEDKVLELSQNNFEENPIENWIGCLSIELGDEDDNIEYKDTDQFNVIASQNFNLVRINNQMLAQLHKTFSEDLDFQIEELELMIKNKKILEREIKAHNEKISKIIKDSRDSTTPTFYFIGIQDDQVYTLEIPNEWEPVWNLLKSYPNGLLLKDFIDKQTFVTKEAFLSTLTDLNKYGVVGLFPKN
Protein: CYCLIN D41 (F4KHY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAEENLELSLLCTESNVDDEGMIVDETPIEISIPQMGFSQSESEEIIMEMVEKEKQHLPSDDYIKRLRSGDLDLNVGRRDALNWIWKIRGLCRTDREACEVHQFGPLCFCLAMNYLDRFLSVHDLPSGKGWILQLLAVACLSLAAKIEETEVPMLIDLQVGDPQFVFEAKSVQRMELLVLNKLKWRLRAITPCSYIRYFLRKMSKCDQEPSNTLISRSLQVIASTTKGIDFLEFRPSEVAAAVALSVSGELQRVHFDNSSFSPLFSLLQKERVKKIGEMIESDGSDLCSQTPNGVLEVSACCFSFKTHDSSSSYTHLS
Protein: Proteasome 26S subunit, ATPase 6 (A0A8I6AGB8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQVMPSVCIRFVTEKNTFV
Protein: ATP synthase F(0) complex subunit f, mitochondrial (ATP synthase membrane subunit f) (P56135)
Organism: Mus musculus (Mouse)
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. Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MASLVPLKEKKLMEVKLGELPSWIMMRDFTPSGIAGAFRRGYDRYYNKYINVRKGSISGISMVLAAYVVFSYCISYKELKHERRRKYH