wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein mL60 (54S ribosomal protein L31, mitochondrial) (YmL31) (P14063)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL58
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL57
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL49
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS42
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein mL40
Sequence:
MFGPFKLTSPVAGGLLWKIPWRMSTHQKTRQRERLRNVDQVIKQLTLGLHVQRCQDKGLTYQEAMESKKKYKPRSKSLRLLNKPSVFPKENQMSSKDKYWTFDKKAVGYRKGIHKVPKWTKISIRKAPKFF
Protein: Gamma-crystallin A (Gamma-A-crystallin) (Gamma-crystallin 4) (P04345)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
Sequence:
MGKITFYEDRGFQGRCYECSSDCPNLQTYFSRCNSIRVDSGCWMLYERPNYQGYQYFLRRGDYPDYQQWMGFSDSIRSCRSIPYTSSHRIRLYERDDYRGLVSELMDDCSCIHDRFRLHEIYSMHVLEGCWVLYEMPNYRGRQYLLRPGDYRRYHDWGAMDAKVGSLRRVMDLY
Protein: Endoglucanase (EC 3.2.1.4) (CaCel) (Cellulase) (Endo-beta-1,4-glucanase) (D3GDK4)
Organism: Cryptopygus antarcticus (Antarctic springtail)
Function: Hydrolyzes carboxymethylcellulose (CMC). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin.
Subcellular location: Secreted {ECO:0000269|PubMed:24848382}.
Interaction partners:
Sequence:
MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP
Protein: Meiosis regulator and mRNA stability factor 1 (Limkain-b1) (G8JLP4)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MMEGNGTENSCSRTRGWLQQDNDAKPWLWKFSNCFSRPEQTLPHSPQTKEYMENKKVAVELKDVPSPLHAGSKLFPAVPLPDIRSLQQPKIQLSSVPKVSCCAHCPNEPSTSPMRFGGGGGGSGGTSSLIHPGALLDSQSTRTITCQVGSGFAFQSASSLQNASARNNLAGIASDFPSMCLESNLSSCKHLPCCGKLHFQSCHGNVHKLHQFPSLQGCTSAGYFPCSDFTSGAPGHLEEHISQSELTPHLCTNSLHLNVVPPVCLKGSLYCEDCLNKPARNSIIDAAKVWPNIPPPNTQPAPLAVPLCNGCGTKGTGKETTLLLATSLGKAASKFGSPEVAVAGQVLENLPPIGVFWDIENCSVPSGRSATAVVQRIREKFFKGHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDKLRQSLRRFANTHTAPATVVLVSTDVNFALELSDLRHRHGFHIILVHKNQASEALLHHANELIRFEEFISDLPPRLPLKMPELCRMESKTGHRNSEHQQGHLRLVVPTHGNSSAAVSTPKNSGVAEPVYKTSQKKENLSARSVTSSPVEKKDKEETVFQVSYPSAFSKLVASRQVSPLLASQSWSSSEADCPDPFANGADVQVSNIDYRLSRKELQQLLQEAFARHGKVKSVELSPHTDYQLKAVVQMENLQDAIGAVNSLHRYKIGSKKILVSLATGAASKSLSLLSAETMSVLQDAPACCLPLFKFTDIYEKKFGHKLNVSDLYKLTDTVAIREQGNGRLVCLLPSSQARQSPLGSSQSHDGSSTNCSPIIFEELEYHEPVCRQHCSNKDFSEHEFDPDSYKIPFVILSLKTFAPQVHSLLQTHEGTVPLLSFPDCYIAEFGDLEVVQENQGGVPLEHFITCVPGVNIATAQNGIKVVKWIHNKPPPPNTDPWLLRSKSPVGNPQLIQFSREVIDLLKSQPSCVIPISHFIPSYHHHFAKQCRVSDYGYSKLIELLEAVPHVLQILGMGSKRLLTLTHRAQVKRFTQDLLKLLKSQASKQVIVREFSQAYHWCFSKDWDVTEYGVCELIDIVSEIPDTTICLSQQDNEMVICIPKRERTQDEIERTKQFSKDVVDLLRHQPHFRMPFNKFIPSYHHHFGRQCKLAYYGFTKLLELFEAIPDTLQVLECGEEKILTLTEVERFKALAAQFVKLLRSQKDNCLMMTDLLTEYAKTFGYTFRLQDYDVSSISALTQKLCHVVKVADIESGRQIQLINRKSLRSLTAQLLVLLMSWEGTTHLSVEELKRHYESTHNTPLNPCEYGFMTLTELLKSLPYLVEVFTNDKMEECVKLTSLYLFAKNVRSLLHTYHYQQIFLHEFSMAYTKYVGETLQPKTYGHSSVEELLGAIPQVVWIKGHGHKRIVVLKNDMKSRLSSLSLSPANHENQPSEGERILEVPESHTASELKLGADGSGPSHTEQELLRLTDDSPVDLLCAPVPSCLPSPQLRPDPVILQSADLIQFEERPQEPSEIMILNQEEKMEIPIPGKSKTLTSDSSSSCISAAVPVPPCPSSETSESLLSKDPVESPAKKQPKNRVKLAANFSLAPITKL
Protein: Small ribosomal subunit protein uS14 (30S ribosomal protein S14) (P0AG59)
Organism: Escherichia coli (strain K12)
Function: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Interaction partners:
- Large ribosomal subunit protein bL33
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL30
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein bS6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL15
- Alternative ribosome-rescue factor A
Sequence:
MAKQSMKAREVKRVALADKYFAKRAELKAIISDVNASDEDRWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHGFLRKFGLSRIKVREAAMRGEIPGLKKASW
Protein: Flavin-containing monooxygenase 2 (EC 1.14.13.-) (Dimethylaniline oxidase 2) (FMO 1B1) (Pulmonary flavin-containing monooxygenase 2) (FMO 2) (Q99518)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation. Specifically catalyzes S-oxygenation of sulfur derived compounds such as thioureas-derived compounds, thioetherorganophosphates to their sulfenic acid. In vitro, catalyzes S-oxygenation of the second-line antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA), forming a sulfinic acid and a carbodiimide via a postulated sulfenic acid intermediate. Also catalyzes S-oxygenation of the thioether-containing organophosphate insecticides, phorate and disulfoton.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 2D6
- Cytochrome P450 3A4)
- Cytochrome P450 2C9
Sequence:
MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDGRASIYQSVVTNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRKCPDFSSSGQWKVVTQSNGKEQSAVFDAVMVCSGHHILPHIPLKSFPGMERFKGQYFHSRQYKHPDGFEGKRILVIGMGNSGSDIAVELSKNAAQVFISTRHGTWVMSRISEDGYPWDSVFHTRFRSMLRNVLPRTAVKWMIEQQMNRWFNHENYGLEPQNKYIMKEPVLNDDVPSRLLCGAIKVKSTVKELTETSAIFEDGTVEENIDVIIFATGYSFSFPFLEDSLVKVENNMVSLYKYIFPAHLDKSTLACIGLIQPLGSIFPTAELQARWVTRVFKGLCSLPSERTMMMDIIKRNEKRIDLFGESQSQTLQTNYVDYLDELALEIGAKPDFCSLLFKDPKLAVRLYFGPCNSYQYRLVGPGQWEGARNAIFTQKQRILKPLKTRALKDSSNFSVSFLLKILGLLAVVVAFFCQLQWS
Protein: Putative transport protein YhhT (P0AGM0)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
METPQPDKTGMHILLKLASLVVILAGIHAAADIIVQLLLALFFAIVLNPLVTWFIRRGVQRPVAITIVVVVMLIALTALVGVLAASFNEFISMLPKFNKELTRKLFKLQEMLPFLNLHMSPERMLQRMDSEKVVTFTTALMTGLSGAMASVLLLVMTVVFMLFEVRHVPYKMRFALNNPQIHIAGLHRALKGVSHYLALKTLLSLWTGVIVWLGLELMGVQFALMWAVLAFLLNYVPNIGAVISAVPPMIQVLLFNGVYECILVGALFLVVHMVIGNILEPRMMGHRLGMSTMVVFLSLLIWGWLLGPVGMLLSVPLTSVCKIWMETTKGGSKLAILLGPGRPKSRLPG
Protein: Ring-infected erythrocyte surface antigen (Q8I0U6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Ring-infected erythrocyte surface antigen
- Knob-associated histidine-rich protein
- Erythrocyte membrane protein 3
Sequence:
MRPFHAYSWIFSQQYMDTKNVKEKNPTIYSFDDEEKRNENKSFLKVLCSKRGVLPIIGILYIILNGNLGYNGSSSSGVQFTDRCSRNLYGETLPVNPYADSENPIVVSQVFGLPFEKPTFTLESPPDIDHTNILGFNEKFMTDVNRYRYSNNYEAIPHISEFNPLIVDKVLFDYNEKVDNLGRSGGDIIKKMQTLWDEIMDINKRKYDSLKEKLQKTYSQYKVQYDMPKEAYESKWTQCIKLIDQGGENLEERLNSQFKNWYRQKYLNLEEYRRLTVLNQIAWKALSNQIQYSCRKIMNSDISSFKHINELKSLEHRAAKAAEAEMKKRAQKPKKKKSRRGWLCCGGGDIETVEPQQEEPVQTVQEQQVNEYGDILPSLRASITNSAINYYDTVKDGVYLDHETSDALYTDEDLLFDLEKQKYMDMLDTSEEESVKENEEEHTVDDEHVEEHTADDEHVEEPTVADDEHVEEPTVADEHVEEPTVAEEHVEEPTVAEEHVEEPASDVQQTSEAAPTIEIPDTLYYDILGVGVNADMNEITERYFKLAENYYPYQRSGSTVFHNFRKVNEAYQVLGDIDKKRWYNKYGYDGIKQVNFMNPSIFYLLSSLEKFKDFTGTPQIVTLLRFFFEKRLSMNDLENKSEHLLKFMEQYQKEREAHVSEYLLNILQPCIAGDSKWNVPIITKLEGLKGSRFDIPILESLRWIFKHVAKTHLKKSSKSAKKLQQRTQANKQELANINNNLMSTLKEYVGSSEQMNSITYNFENINSNVDNGNQSKNISDLSYTDQKEILEKIVSYIVDISLYDIENTALNAAEQLLSDNSVDEKTLKKRAQSLKKLSSIMERYAGGKRNDKKAKKYDTQDVVGYIMHGISTINKEMKNQNENVPEHVQHNAEANVEHDAEENVEHDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEEYDEENVEEVEENVEEYDEENVEEVEENVEENVEENVEENVEEYDEENVEEVEENVEENVEENVEENVEENVEEVEENVEENVEENVEENVEENVEENVEEYDEENVEEHNEEYDE
Protein: UDP-glucuronosyltransferase 2B17 (UDPGT 2B17) (UGT2B17) (EC 2.4.1.17) (17-beta-hydroxysteroid-specific UDPGT) (RLUG38) (Testosterone, dihydrotestosterone, and beta-estradiol-specific UDPGT) (UDP-glucuronosyltransferase 2B5) (UDPGT 2B5) (UDPGTr-3) (P08542)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75795}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPGKWISALLLLQISCCFQSGNCGKVLVWPMEFSHWMNIKTILDELVQRGHEVTVLKPSAYYVLDPKKSPDLKFETFPTSVSKDELENYFIKLVDVWTYELQRDTCLSYSPLLQNMIDGFSDYYLSLCKDTVSNKQLMAKLQESKFDVLLSDPVAACGELIAEVLHIPFLYSLRFSPGYKIEKSSGRFILPPSYVPVILSGMGGPMTFIDRVKNMICTLYFDFWFHMFNAKKWDPFYSEILGRPTTLAETMGKAEMWLIRSYWDLEFPHPTLPNVDYIGGLQCRPPKPLPKDMEDFVQSSGEHGVVVFSLGSMVSSMTEEKANAIAWALAQIPQKVLWKFDGKTPATLGPNTRVYKWLPQNDLLGHPKTKAFVTHSGANGVYEAIYHGIPMVGIPMFGEQHDNIAHMVAKGAAVTLNIRTMSKSDLFNALKEIINNPFYKKNAVWLSTIHHDQPMKPLDKAVFWIEFVMRHKGAKHLRPLGHDLPWYQYHSLDVIGFLLTCSAVIAVLTVKCFLFIYRLFVKKEKKMKNE
Protein: E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CHIP) (Q9XYW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- Ubiquitin-conjugating enzyme E2-17 kDa
- Hsc70Cb, isoform G
- Ubiquitin-conjugating enzyme E2 N
- Mothers against decapentaplegic homolog
- AT16033p
- LD01461p
- E2 ubiquitin-conjugating enzyme
- Heat shock protein 83
- Microtubule-associated protein
Sequence:
MTTKHIYSTTNLSDLQLKEQGNCLFAARKYDDAINCYSKAIIKNPTNATYFTNRALCNLKLKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSKEQKQNFGDDITLQLRLARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVHDEQLKDKQQEIEQECDDHIKELNNIFSKVDERRKKREVPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIAENEWSLDY
Protein: Probable ATP-binding protein YheS (P63389)
Organism: Escherichia coli (strain K12)
Function: Genetic data indicate it may be involved in ribosome assembly or function.
Interaction partners:
- Putative esterase YheT
- UPF0270 protein YheU
Sequence:
MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGSWQLAWVNQETPALPQAALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWSIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSMFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFRFSFRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEYLRADESPIQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIEFEGALVVVSHDRHLLRSTTDDLYLVHDRKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENANSAQARKDQKRREAELRAQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQMLLEGQSN
Protein: Homeobox protein cut (P10180)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of cell fate decisions in multiple lineages. Specifically, functions as a determination factor that specifies sensory organ identity in precursor cells. Probably also involved in cell type specification of Malpighian tubules. In absence of cut gene external sensory organs are transformed into chordotonal organs.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein su
- Modifier of mdg4
- Origin recognition complex subunit 3
Sequence:
MQPTLPQAAGTADMDLTAVQSINDWFFKKEQIYLLAQFWQQRATLAEKEVNTLKEQLSTGNPDSNLNSENSDTAAAAATAAAVAAVVAGATATNDIEDEQQQQLQQTASGGILESDSDKLLNSSIVAAAITLQQQNGSNLLANTNTPSPSPPLLSAEQQQQLQSSLQQSGGVGGACLNPKLFFNHAQQMMMMEAAAAAAAAALQQQQQQQSPLHSPANEVAIPTEQPAATVATGAAAAAAAAATPIATGNVKSGSTTSNANHTNSNNSHQDEEELDDEEEDEEEDEDEDDEEENASMQSNADDMELDAQQETRTEPSATTQQQHQQQDTEDLEENKDAGEASLNVSNNHNTTDSNNSCSRKNNNGGNESEQHVASSAEDDDCANNNTNTSNNNNTSNTATSNTNNNNNNNSSSGNSEKRKKKNNNNNNGQPAVLLAAKDKEIKALLDELQRLRAQEQTHLVQIQRLEEHLEVKRQHIIRLEARLDKQQINEALAEATALSAAASTNNNNNSQSSDNNKKLNTAAERPMDASSNADLPESTKAPVPAEDDEEDEDQAMLVDSEEAEDKPEDSHHDDDEDEDEDREAVNATTTDSNELKIKKEQHSPLDLNVLSPNSAIAAAAAAAAAAACANDPNKFQALLIERTKALAAEALKNGASDALSEDAHHQQQQHHQQQHQHQQQHHQQQHLHQQHHHHLQQQPNSGSNSNPASNDHHHGHHLHGHGLLHPSSAHHLHHQTTESNSNSSTPTAAGNNNGSNNSSSNTNANSTAQLAASLASTLNGTKSLMQEDSNGLAAVAMAAHAQHAAALGPGFLPGLPAFQFAAAQVAAGGDGRGHYRFADSELQLPPGASMAGRLGESLIPKGDPMEAKLQEMLRYNMDKYANQALDTLHISRRVRELLSVHNIGQRLFAKYILGLSQGTVSELLSKPKPWDKLTEKGRDSYRKMHAWACDDNAVMLLKSLIPKKDSGLPQYAGRGAGGAGGDDSMSEDRIAHILSEASSLMKQSSVAQHREQERRSHGGEDSHSNEDSKSPPQSCTSPFFKVENQLKQHQHLNPEQAAAQQREREREQREREQQQRLRHDDQDKMARLYQELIARTPRETAFPSFLFSPSLFGGAAGMPGAASNAFPAMADENMRHVFEREIAKLQQHQQQQQAAQAQAQFPNFSSLMALQQQVLNGAQDLSLAAAAAKDIKLNGQRSSLEHSAGSSSCSKDGERDDAYPSSLHGRKSEGGGTPAPPAPPSGPGTGAGAPPTAAPPTGGASSNSAAPSPLSNSILPPALSSQGEEFAATASPLQRMASITNSLITQPPVTPHHSTPQRPTKAVLPPITQQQFDMFNNLNTEDIVRRVKEALSQYSISQRLFGESVLGLSQGSVSDLLARPKPWHMLTQKGREPFIRMKMFLEDENAVHKLVASQYKIAPEKLMRTGSYSGSPQMPQGLASKMQAASLPMQKMMSELKLQEPAQAQHLMQQMQAAAMSAAMQQQQVAQAQQQAQQAQQAQQHLQQQAQQHLQQQQHLAQQQHPHQQHHQAAAAAAALHHQSMLLTSPGLPPQHAISLPPSAGGAQPGGPGGNQGSSNPSNSEKKPMLMPVHGTNAMRSLHQHMSPTVYEMAALTQDLDTHDITTKIKEALLANNIGQKIFGEAVLGLSQGSVSELLSKPKPWHMLSIKGREPFIRMQLWLSDANNVERLQLLKNERREASKRRRSTGPNQQDNSSDTSSNDTNDFYTSSPGPGSVGSGVGGAPPSKKQRVLFSEEQKEALRLAFALDPYPNVGTIEFLANELGLATRTITNWFHNHRMRLKQQVPHGPAGQDNPIPSRESTSATPFDPVQFRILLQQRLLELHKERMGMSGAPIPYPPYFAAAAILGRSLAGIPGAAAAAGAAAAAAAVGASGGDELQALNQAFKEQMSGLDLSMPTLKRERSDDYQDDLELEGGGHNLSDNESLEGQEPEDKTTDYEKVLHKSALAAAAAYMSNAVRSSRRKPAAPQWVNPAGAVTNPSAVVAAVAAAAAAAADNERIINGVCVMQASEYGRDDTDSNKPTDGGNDSDHEHAQLEIDQRFMEPEVHIKQEEDDDEEQSGSVNLDNEDNATSEQKLKVINEEKLRMVRVRRLSSTGGGSSEEMPAPLAPPPPPPAASSSIVSGESTTSSSSSSNTSSSTPAVTTAAATAAAGWNY
Protein: ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) (P9WPS1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit b-delta
- ATP synthase epsilon chain
- ATP synthase subunit b
- ATP synthase subunit beta
- ATP synthase subunit alpha
- ATP synthase gamma chain
- Uncharacterized protein Rv1507c
- Probable cytoplasmic peptidase PepQ
- Uncharacterized protein Rv1303
Sequence:
MDPTIAAGALIGGGLIMAGGAIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPVK
Protein: FI19481p1 (Xyloside xylosyltransferase) (Q9W1D1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase
- FI12101p)
- O-glucosyltransferase rumi
- N-alpha-acetyltransferase 20
Sequence:
MAKNSFKTLISQKHKTFPADLNMYGMKCKSQLLEDQENVTLIINRRNSIRQKPKSWAWTLLRCRWQKKLVLLLIFICVCVLIVFANTHLLVRGNILSAFLSSRLNKHSHAEKQEARYPDIPATTPSVPPVLRPTHYLLNYSSTQLELSSHLNGLSSDYNIFVIYTRENYHLNLKFDLFAHSLLKHTSAQLHLHVITDSESQPSVLEILQRQIRRFRRTVIYTIYDVKVCSSIIQDIAAKLSPYFSSTPNSYYSDSLFFLSLGLHRIADRSLNRAILLDCDIVFRSDVRLLFNEFDNFLPHQLYGLAPELTPVYRHILYRYRVRYPKTSFGNPYYPINNEGGNQHSRVHHGYPGLNSGVVLLLLNRIRNSKSYLEKLTHSEVHTLVAKYSFKGHLGDQDFFTLLGYEYPNLIYRLDCIWNRQLCTWWKDHGYSQIFDAYFRCEGNIKMYHGNCNTRIPE
Protein: 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS) (Q9S400)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
Interaction partners:
Sequence:
MKLKTNIRHLHGSIRVPGDKSISHRSIIFGSLAEGETKVYDILRGEDVLSTMQVFRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNMGNSGTSIRLISGVLAGADFEVEMFGDDSLSKRPMDRVTLPLKKMGVSISGQTERDLPPLRLKGTKNLRPIHYELPIASAQVKSALMFAALQAKGESVIIEKEYTRNHTEDMLKQFGGHLSVDGKKITVQGPQKLTGQKVVVPGDISSAAFWLVAGLIAPNSRLVLQNVGINETRTGIIDVIRAMGGKLEITEIDPVAKSATLIVESSDLKGTEIGGALIPRLIDELPIIALLATQAQGVTVIKDAEELKVKETDRIQVVADALNSMGADITPTADGMIIKGKSALHGARVNTFGDHRIGMMTAIAALLVADGEVELDRAEAINTSYPSFFDDLESLIHG
Protein: Interleukin enhancer binding factor 2 (cDNA FLJ51660, highly similar to Interleukin enhancer-binding factor 2) (B4DY09)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE
Protein: Kv channel interacting protein 3, calsenilin (A2AHT3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIRWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRLSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI
Protein: Carotenoid-cleaving dioxygenase, mitochondrial (EC 1.13.11.-) (EC 1.13.11.71) (B-diox-II) (Beta,beta-carotene 9',10'-oxygenase) (Beta-carotene dioxygenase 2) (Q99NF1)
Organism: Mus musculus (Mouse)
Function: Broad specificity mitochondrial dioxygenase that mediates the asymmetric oxidative cleavage of carotenoids. Cleaves carotenes (pure hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin, lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-carbon double bond. Through its function in carotenoids metabolism regulates oxidative stress and the production of important signaling molecules.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21106934}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MLGPKQSLPCIAPLLTTAEETLSAVSARVRGHIPEWLNGYLLRVGPGKFEFGKDRYNHWFDGMALLHQFRMERGTVTYKSKFLQSDTYKANSAGGRIVISEFGTLALPDPCKSIFERFMSRFEPPTMTDNTNVNFVQYKGDYYMSTETNFMNKVDIEMLERTEKVDWSKFIAVNGATAHPHYDPDGTAYNMGNSYGPRGSCYNIIRVPPKKKEPGETIHGAQVLCSIASTEKMKPSYYHSFGMTKNYIIFVEQPVKMKLWKIITSKIRGKPFADGISWEPQYNTRFHVVDKHTGQLLPGMYYSMPFLTYHQINAFEDQGCIVIDLCCQDDGRSLDLYQLQNLRKAGEGLDQVYELKAKSFPRRFVLPLDVSVDAAEGKNLSPLSYSSASAVKQGDGEIWCSPENLHHEDLEEEGGIEFPQINYGRFNGKKYSFFYGCGFRHLVGDSLIKVDVTNKTLRVWREEGFYPSEPVFVPVPGADEEDSGVILSVVITPNQSESNFLLVLDAKSFTELGRAEVPVQMPYGFHGTFVPI
Protein: Regulator of G-protein signaling 8 (RGS8) (P49804)
Organism: Rattus norvegicus (Rat)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12880183}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane {ECO:0000269|PubMed:9394004}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:12880183}. Cell projection, dendrite {ECO:0000269|PubMed:12880183}. Nucleus {ECO:0000269|PubMed:12880183}. Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1. {ECO:0000269|PubMed:12880183}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 7-binding protein
Sequence:
MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVTKAHRIFEEFVDVQAPREVNIDFQTREATRKNMQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS
Protein: Activating transcription factor 1 (F7FD47)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Cyclic AMP-dependent transcription factor ATF-2
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-responsive element-binding protein 1
- non-specific serine/threonine protein kinase
- cAMP responsive element binding protein 5
- Cyclic AMP-dependent transcription factor ATF-4
Sequence:
MEDSHKSNTSETASQPGSTVPGIISQIVHQVSSLSESEESQDSSDSIGSSQKAHGILARRPSYRKILKDLSSEDTRGRKGDGENPSISAVTSMSVPTPIYQTSSGQYIAIAPNGALQLASPGPDGVQALQTLTMTNSSSAQQGAILQYAQTSDGQQILVPSNQVVVQTASGDMQTYQIRTTPSATSLPQTMVMTSPVTLTSQTTKTDDPQLKREIRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKTLKDLYSHKSV
Protein: Glycolate oxidase 1 (AtGLO1) (GOX1) (EC 1.1.3.15) ((S)-2-hydroxy-acid oxidase GLO1) (Short chain alpha-hydroxy acid oxidase GLO1) (Q9LRR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants (Probable).
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
- Glycerate dehydrogenase HPR, peroxisomal
- Phosphoglycolate phosphatase 1A, chloroplastic
- Serine--glyoxylate aminotransferase
- Glutamate--glyoxylate aminotransferase 2
- Glutamate--glyoxylate aminotransferase 1
- Glyoxylate/hydroxypyruvate reductase A HPR2
- Malate synthase
- Isocitrate lyase
- Glyoxylate/hydroxypyruvate reductase HPR3
- Catalase-2
Sequence:
MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTEWDTPRPSARL