wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 (Complex I-PDSW) (CI-PDSW) (NADH-ubiquinone oxidoreductase PDSW subunit) (Q9DCS9)
Organism: Mus musculus (Mouse)
Function: Accessory subunit that is involved in the functional assembly of the mitochondrial respiratory chain complex I. Complex I has an NADH dehydrogenase activity with ubiquinone as an immediate electron acceptor and mediates the transfer of electrons from NADH to the respiratory chain.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
Sequence:
MPDSWDKDVYPEPPSRTPAPSPQTSLPNPITYLTKAYDLVVDWPVTLVREFIERQHAKNRTYYYHRQYRRVPDITECKEGDVLCIYEAEMQWRRDFKVDQEIMNIIQERLKACQQREGENYQQNCAKELEQFTKVTKAYQDRYLDLGAYYSARKCLAKQKQRMLEERKAARQEAAA
Protein: Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma) (Q5BJR8)
Organism: Rattus norvegicus (Rat)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48443, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P48443}.
Interaction partners:
- Retinoic acid receptor, gamma
- Retinoic acid receptor beta
- Retinoic acid receptor, alpha
- Nuclear receptor corepressor 2
- Thyroid hormone receptor beta
- Oxysterols receptor LXR-alpha
- Nuclear receptor coactivator
- Peroxisome proliferator-activated receptor gamma
- Mediator of RNA polymerase II transcription subunit 1
- Nuclear receptor coactivator 2
Sequence:
MYGNYSHFMKFPTGFGGSPGHTGSTSMSPSVALPTGKPMDSHPSYTDTPVSAPRTLSAVGTPLNALGSPYRVITSAMGPPSGALAAPPGINLVVPPSSQLNVVNSVSSSEDIKPLPGLPGIGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKDCLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECASTGHEDMPVERILEAELAVEPKTESYGDMSVESSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVILLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKDMRMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLETPLQIT
Protein: LD05664p (Meiotic central spindle, isoform A) (Zinc finger motif protein) (O96395)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVGRSSGKMERSVDASMGKNCRACAEHSSILVDLFSKEISDPPIWEMLNSILPEICRVKRDEMPQKICPTCLVAAQNAFHFRHKCEQSFQFFSQLLQLDKSNSNLSRSHCRRGTMNPLIPFEIVGCEDPLDTNVTKLDANRPDVKTDIDEPTDGKATNGQESEPLQEVFEITMNDIKTEDEVSIQETFEDAFDEENDNNNTDSEREDSDQWTVGSTEDQDEPWIPGGGGRQTVGGNNQSLLCTECGVSYSTQKALARHVAKHKEQGDTQKPHLCDFCGRGFRTNAQLTTHRRRHTGERPFKCPLCPKAYTHGPTLKSHMHTHDEEKGHKCPQCDKTFYTRGNLRAHIQRHTGERPYKCPDCPQTFAKNSGLKLHSRLHKEERPFKCELCGKGFVQNQHLITHLRVHNGDRQFKCPDCDKSFFEKSNMMKHQRTHSGIKPFKCEECGQAFSHNHHLKSHLRIHTGEKPYKCDQCGKGFSANQSLMKHTLWHVDNNDRPFKCSQCPKAYDTQQSLRGHEKTHKNPDEPKTLHQCPHCDVRFALKKTLDKHITSHKIRPHPCPQCPEGFFSQKSLKKHLRLHNLKK
Protein: FI21420p1 (Loner ISO1) (Schizo, isoform B) (Q9VP80)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- ADP-ribosylation factor 6
- Kin of irre, isoform A
Sequence:
MSEADLKNLSQNSDGDQELLLHQTTQSLLMASSIMFVGNQGGPGGSAGGVAPPGPVSLPLPLSINMPHHHVHAMPYNVDELLRENNALHAKIKELSLERDRLLCEVSNLRLELDMSELKRLPVDLDDNFPQKSLERSGSTQYELAGAQQPGSANASTCTDSGSVGGYVYLQNHYAPGAHSSSAAINYPAQQHPQMVYQIQQYPTCHQQQQQQHLQQQQHLHQTGAGHYMQVTATGGGQYHHHHMLHGHGHHAHHHGGAVVIAGSGVGTGLGSGATSVIMQHQQQQQQQQNMHKKNSIRNGGDVLKRTRAQSAYELSQDLLEKQIELLERKYGGVRARNAAVTIQRAFRHYMMVKKFASITAMAKAEKRLSRRMVVTASSLGLAEEGASSSSAYGSATESQLTEQQQQQQAQQQQQPRVTIMAGPAGAASPGLSRTPPTRSLSMRERRQLDCSPIPRSQSGASPASISSSTVSTSALASHPHVNLLHAAEPHYYNAQALPQGAAYYTSYHGSPHDLSYASSADTSLNASWVNTSGHSPHTPYYSAAQIYMRPKGGSTTPTPSCSGSTGSGSGGSGSGSSKKVPPEVPKRTSSITAQQQTQLLLLQRQTPPPPSLLRTNGLCKTAENGSLTSVQSSGSDSSVTSAERNLNSDLGSDRSNSPHTWKRGTALNSSQQFSTHSADSAGAVSGGGVGVAGGAGVYAAQMQAAVAAATAAGGMPPADDHAISSHTSAAQYEQHEQQQHEQQQLQAAAAAAGVAQNYKMSETIRKRQYRVGLNLFNKKPEKGITYLIRRGFLENTPQGVARFLITRKGLSRQMIGEYLGNLQNQFNMAVLSCFAMELDLSGRQVDVALRKFQAYFRMPGEAQKIERLMEIFSQRYCECNADIVGRLRSSDTIFVLAFAIIMLNTDLHTPNLKPERRMRVEDFIKNLRGIDDCHDIDKDMLMGIYDRVKSDEFKPGSDHVTQVMKVQATIVGKKPNLALPHRRLVCYCRLYEIPDVNKKERPGVHQREVFLFNDLLVITKIFSKKKTSVTYTFRNSFPLCGTVVTLLDMPNYPFCIQLSQKVDGKILITFNARNEHDRCKFAEDLKESISEMDEMESLRIEAELERQKSARNRAPGNAENRDSGVADVEVCPCPYQQGSQASGEQAPNSADNSQQLKRSALSNSLLDMHEQFGNEKPQRRGSVGSLDSGMSISFQSTTTSSASRENAAAIAAAANAAAAAKMRFNMPPTAAIATPSNVYAAPGMQAYTHANFVQQSQAAYMLQQQQMLQQQAQMQAQAQAQAQAQAQAQAQAQAQAQAQPLTGRIPGRERKASRTDENGRSTEV
Protein: Hd1 (Heading day 1) (Q9FE92)
Organism: Oryza sativa (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00357}.
Interaction partners:
Sequence:
MNYNFGGNVFDQEVGVGGEGGGGGEGSGCPWARPCDGCRAAPSVVYCRADAAYLCASCDARVHAANRVASRHERVRVCEACERAPAALACRADAAALCVACDVQVYSANPLARRHQRVPVAPLPAITIPATSVLAEAVVATATVLGDKDEEVDSWLLLSKDSDNNNNNNNNNDNDNNDNNNSNSSNNGMYFGEVDEYFDLVGYNSYYDNRIENNQDRQYGMHEQQEQQQQQQEMQKEFAEKEGSECVVPSQITMLSEQQHSGYGVVGADQAASMTAGVSAYTDSISNSISFSSMEAGIVPDSTVIDMPNSRILTPAGAINLFSGPSLQMSLHFSSMDREARVLRYREKKKARKFEKTIRYETRKAYAEARPRIKGRFAKRSDVQIEVDQMFSTAALSDGSYGTVPWF
Protein: L-lactate permease (P33231)
Organism: Escherichia coli (strain K12)
Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate. Seems to be driven by a proton motive force.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- L-lactate dehydrogenase
- Putative L-lactate dehydrogenase operon regulatory protein
- Quinone-dependent D-lactate dehydrogenase
- Aspartate aminotransferase
Sequence:
MNLWQQNYDPAGNIWLSSLIASLPILFFFFALIKLKLKGYVAASWTVAIALAVALLFYKMPVANALASVVYGFFYGLWPIAWIIIAAVFVYKISVKTGQFDIIRSSILSITPDQRLQMLIVGFCFGAFLEGAAGFGAPVAITAALLVGLGFKPLYAAGLCLIVNTAPVAFGAMGIPILVAGQVTGIDSFEIGQMVGRQLPFMTIIVLFWIMAIMDGWRGIKETWPAVVVAGGSFAIAQYLSSNFIGPELPDIISSLVSLLCLTLFLKRWQPVRVFRFGDLGASQVDMTLAHTGYTAGQVLRAWTPFLFLTATVTLWSIPPFKALFASGGALYEWVINIPVPYLDKLVARMPPVVSEATAYAAVFKFDWFSATGTAILFAALLSIVWLKMKPSDAISTFGSTLKELALPIYSIGMVLAFAFISNYSGLSSTLALALAHTGHAFTFFSPFLGWLGVFLTGSDTSSNALFAALQATAAQQIGVSDLLLVAANTTGGVTGKMISPQSIAIACAAVGLVGKESDLFRFTVKHSLIFTCIVGVITTLQAYVLTWMIP
Protein: Large ribosomal subunit protein mL49 (54S ribosomal protein IMG2, mitochondrial) (Integrity of mitochondrial genome protein 2) (P25642)
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, ECO:0000269|PubMed:14576278}. 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 bL19m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL30m
Sequence:
MISSCVTRCFGRGKCLPGPATASIYQTIRCISTNSNKAAEAPIFPKLEDVKMHELIGNNNFGKKTYYVERSRTGNLPVYSAYKNGGNKIITEIRKIEGDVIQLRNDLQEQLPFIPKKSWSVVMQSKKIIIKGNAVEAVKRVLTKKF
Protein: Peptidyl-prolyl cis-trans isomerase 3 (PPIase 3) (EC 5.2.1.8) (Cyclophilin-3) (CYP-3) (Rotamase 3) (P52011)
Organism: Caenorhabditis elegans
Function: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Plays a role in protein folding, transport and assembly.
Interaction partners:
- Nsp1_C domain-containing protein
- Probable cytochrome P450 CYP44
- peptidylprolyl isomerase
Sequence:
MSRSKVFFDITIGGKASGRIVMELYDDVVPKTAGNFRALCTGENGIGKSGKPLHFKGSKFHRIIPNFMIQGGDFTRGNGTGGESIYGEKFPDENFKEKHTGPGVLSMANAGPNTNGSQFFLCTVKTEWLDGKHVVFGRVVEGLDVVKAVESNGSQSGKPVKDCMIADCGQLKA
Protein: Cleavage stimulation factor 64 kD subunit (Cleavage stimulation factor 64 kilodalton subunit) (FI01908p) (Q9VE52)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein suppressor of forked
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage stimulation factor subunit 1
- Probable cleavage and polyadenylation specificity factor subunit 2
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor 73
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Pre-mRNA cleavage complex 2 protein Pcf11
- Factor interacting with poly
Sequence:
MADKAQEQSIMDKSMRSVFVGNIPYEATEEKLKEIFSEVGPVLSLKLVFDRESGKPKGFGFCEYKDQETALSAMRNLNGYEIGGRTLRVDNACTEKSRMEMQQLLQGPQVENPYGEPCEPEDAPELITKTVASLPPEQMYELMKQMKLCIVSNPSEARQMLMLNPQLAYALLQAMVVMRIVDPQQALGMLFKANQMPPVLGGNPHQGPGNHTMMGQQQVPQQQVQIPQQQQQAPQPPMPVPGPGFPANVHPNDIDLRMVPGGPMPMDPRMMGRGMDQDLRASLPNPVPPPLMDPRARAQMPPQQQQGVPQAPPAPYPSDPRQRPMDPRLRAGPGPQQQAPPQGIPQAPPPTQQQQAAAQQLQSRLGAHGVLPSDASDQEKAALIMQVLQLSDEQIAQLPSEQRVSIVMLKEQIAKSTQR
Protein: Tyrosine 3-monooxygenase (EC 1.14.16.2) (Tyrosine 3-hydroxylase) (TH) (P07101)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa. In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When phosphorylated at Ser-19 shows a nuclear distribution and when phosphorylated at Ser-31 as well at Ser-40 shows a cytosolic distribution (By similarity). Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P04177}.
Interaction partners:
- Alpha-synuclein
- Aromatic-L-amino-acid decarboxylase
- Pterin-4-alpha-carbinolamine dehydratase
- Pterin-4-alpha-carbinolamine dehydratase 2
- Dopamine beta-hydroxylase
- Dihydropteridine reductase
- Sepiapterin reductase
- Synaptic vesicular amine transporter
- Tyrosinase
- Phenylethanolamine N-methyltransferase
Sequence:
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
Protein: Peptidyl-prolyl cis-trans isomerase CYP23 (PPIase CYP23) (EC 5.2.1.8) (Cyclophilin of 23 kDa) (Cyclophilin-23) (Q8LDR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- AT1G01800 protein
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Pre-mRNA-splicing factor SYF2
- Peroxidase 7
- At3g05070
- Pre-mRNA-splicing factor SLU7-B
- Pre-mRNA-splicing factor SLU7-A
- Pre-mRNA-splicing factor SLU7
- Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial
Sequence:
MGITRNLILGLACLAFVSIAKALPHEPELGSARVVFQTSYGDIEFGFYPTVAPKTVDHIFKLVRLGGYNTNHFFRVDKGFVAQVADVASGRSAPMNEEQRKEAEKKIVGEFSDVKHVRGTLSMGRYDDPNSAQSSFSMLLGNAPHLDRQYAVFGKVTKGDETLSKLEEVPTRREGIFVMPTERITILSTYYYDTKMESCEEERSVLKRRLQASFVEVERQRMKCFP
Protein: BTB and MATH domain-containing protein 41 (P41886)
Organism: Caenorhabditis elegans
Function: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-3
Sequence:
MEINNGAQPENAAVSIPSRSPSGKSEKRKSPSIVSGCRTVMNERSFTNYWSVERFTVQLELHNPAEFMLAPKFGDGDYEFVMKLFPNGKDEETAGYLSLFLLINKCPNPRLRFRVSFTVETADGPRSCHLNKNLVTINRSGIVTASKFFSLDILRSAMNVYIPNDILTIGCELTIFGECTTQISSLFKPYQRTHSASSTSRSLSSPNTKCLKIDESSAHDAFTEFLSTGEFSDFIIVASCGREFPTHMCILAARSEYFKVLLRNHSTKEFMSKRLQFDDISARTLDVLLRHMYASAAGRVVKLEEDQLTEDLISAMDRLMINSLRDEVARLIGSKVTVDNVLTRISMAAELRLDDTYDVLLDFFSNHKHECMKLTAWDELESAKPPLAIKILRDAFSNTDSPSTTSMDSRIIDRITLT
Protein: Four and a half LIM domains 1 (A0A0D9SFB0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVT
Protein: Kre9p (Q5ANN9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Beta-glucan synthesis-associated protein
- Skn1p
- Protein ROT1
- Protein KRE1
- Kre5p
Sequence:
MRQFQIILISLVVSIIRCVVADVDITSPKSGETFSGSSGSASIKITWDDSDDSDSPKSLDNAKGYTISLCTGPTSDGDIQCLDPLVKNEAISGKSKTVSIAQNSVPNGYYYFQIYVTFTNGGTTIHYSPRFKLTGMSGPTATLDVTETGSVPADQASGFDTATTADSKSFTVPYTLQTGKTRYAPMQMQPGTKVTATTWSMKFPTSAVTYYSTKAGTPNVASTITPGWSYTAESAVNYASVAPYPTYWYPASERVSKATISAATKRRRWLD
Protein: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD) (E2QE90)
Organism: Escherichia coli
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445}.
Interaction partners:
Sequence:
MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATADLGVSVRPRWPLAELPAA
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (Q9ZQY2)
Organism: Zea mays (Maize)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit alpha
- 3-methyl-2-oxobutanoate dehydrogenase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyl dehydrogenase
Sequence:
MLGAARRQLGSGPMLGQVLRRLRPAVAAEVARGYSAAAKEMTVRDALNSALDEEMSADPSVFLMGEEVGEYQGAYKISKGLLDRYGPDRVLDTPITEAGFTGIGVGAAYHGLRPIIEFMTFNFSMQAIDHIINSAAKSNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCYAAWFAHVPGLKVLTPYSSEDARGLLKAAIRDPDPVIFLENELLYGESFPVSAEVLDSSFCLPIGKAKIEREGKDVTITAFSKMVGYALQAAEILSKEGISAEVINLRSIRPLDRAAINASVRKTNRLVTVEEGFPQHGIGAEICMSVVEESFAYLDAPVERIAGADVPMPYAANLERMAVPQVDDIVRAAKRACYRAVPMAAAA
Protein: Contig An02c0390, genomic contig (A2QET8)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRRKIEIKAIKDDRNRSVTFLKRKGGLFKKAHELAVLCSVDVAVIIFGHNKKLYEFSSCDMREALTRYQYFGPPHEHKGPEDFNGKRDDDDDEDETTPAPEDVHPTPPNPPMIPAHLPGHPGFQHVTHAPSASPPIGNGMAFAPRHGTPQPQGVSRPSSRNHLRRVSSNMGPQQHHHATPPPPPPPPQNGFTYIPNPSVYNPNAAHAMAQPPRPPQFTHYGPPGPHHQPPPPPQHHPAMPPHSMPPQSMPPHTMAPQAMPPHHQAPPHMPHPPHALSQQPPPMAMTQPPHAAIPQVAQAFLPEQGRNSMPPTFTTEQQPPPPRTVSLPEGTAPTDAMPGPMKTEGTPSPPHQRSLSSKSRSIFTPIDDRGSVLARHFGVGPPTEAGENAQTKAEGATLGPNEGKPAGLTAKPPPPPPRAATEAPRPQPVVDLKPPVRTNSGQFPPKRPQLKVQIPSENSDRGSATADSSSRDSAGNKTLTPAKANPDTGHSSVVLPPPSPSAGAILSAGAQGPPNPFARPPPPGAAPQNNSAYNNNSNIDTPISALPSRFVSDALLPSPSSFFPEWGFGRSGPDSNMLPSPLTFPTPAVQSGPGFGREDEQDKKRKSPDSGPNAEGVVKKPKT
Protein: Mitochondrial import inner membrane translocase subunit Tim10B (Mitochondrial import inner membrane translocase subunit Tim9B) (Tim10b) (Q9Y0V3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import inner membrane translocase subunit Tim8
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim22
- GEO02620p1
- Acylglycerol kinase, mitochondrial
- RE03721p
- GEO12235p1
Sequence:
MDSNLRNLKDFFTLYNKVTELCFSRCVDNLSQRDLGGHEDLCVDRCVTKFARFNQNMMKVYVDVQTTINAKRMEEMEENARKAEQQQREQEKERLKEAAATAVLTPVQPPVAGNLSM
Protein: Hyaluronan and proteoglycan link protein 1 (Cartilage-linking protein 1) (Proteoglycan link protein) (E7FBW8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Aggrecan core protein
Sequence:
MTFLLLFLLVLSESRADNFEEAYSDLETYRTIYISENGPRLSVDTAQPKVISQRGGNATLPCKFNRDSSLPPNPKLRIKWTKLTSDYLKEIDVFVAMGFHKKSYGRFHGRVHLQAASESDATLVITEITLEDYGKYKCEVIDGLEDDTAVVSLDLQGIVFPYFPRLGRYNLNFLEAEKACRDQDAIVASFEQLYDAWRDGLDWCNAGWLSDGSVQYPITKPREPCGGKNTIPGVRNYGIRDKQKEQYDVFCFTSNYKGRFYYLIHSSKLTYDEAVQACQKDGAQIAKVGQMYAAWKLLGYDRCDAGWLADGSVRYPISKPRRRCSPTEAAVRFSGFPDKKHKLYGVYCYKSNN
Protein: Uncharacterized membrane protein YPR027C (Q12079)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Putative UPF0377 protein YIR040C
- Uncharacterized protein YLR296W
- Uncharacterized protein YDR215C
- Uncharacterized protein YBL044W
Sequence:
MVGIYRILASFVPLLGLLFAFHDDDMIDTVTIIKTVYETVTSTSTAPAPAATKSVSEKKLDDTKLTLQVIQTMVSCFSVGENPANMISCGLGVVILMFSLIIELINKLENDGINEPQRLYDLIKPKYVELPSNYVNEKIKTTFEPLDLYLGVNMNTSGSELNQNCLILKLGEKTALPFPGLAQQICYTKGASNEFTNYKLSDIQGNLNENSQGIANGVFQKISNIRKISGNFKSQLYQISEKITDENWDGSAVGFTAHGREKGPNKSQISVSFYRDN
Protein: Thiosulfate dehydrogenase [quinone] large subunit (EC 1.8.5.2) (Thiosulfate:quinone oxidoreductase) (TQO) (P97207)
Organism: Acidianus ambivalens (Desulfurolobus ambivalens)
Function: TQO plays a role in sulfur oxidation and is proposed to couple sulfur oxidation to dioxygen reduction; caldariellaquinone or sulfolobus quinone seem to serve to transfer electrons to the electron transport chain terminal oxidase formed by DoxBCE.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15306018}; Multi-pass membrane protein {ECO:0000269|PubMed:15306018}.
Interaction partners:
Sequence:
MSGKQSEEFKRTEKMTRMEYLFPVRFAVGWMFLDGGLRKAVLKPAKLDPNSASFVGGKLVNFLPHAGPFKGLLLMTLENRSLDVTFLTVFSYIEIIAGLFIIIGLLTRLAALGALAMSVGFAPAYWLGSTCEDEWQIGALLTAGSVTLMLTAAGRVWGLDYFLYKKLGDRPIANVPILKWIKLW
Protein: CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)] (P29965)
Organism: Homo sapiens (Human)
Function: Cytokine that acts as a ligand to CD40/TNFRSF5. Costimulates T-cell proliferation and cytokine production. Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation. Induces the activation of NF-kappa-B. Induces the activation of kinases MAPK8 and PAK2 in T-cells. Induces tyrosine phosphorylation of isoform 3 of CD28. Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By similarity). Involved in immunoglobulin class switching (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:8626375}; Single-pass type II membrane protein {ECO:0000303|PubMed:8626375}. Cell surface {ECO:0000269|PubMed:15067037, ECO:0000269|PubMed:7678552}.; SUBCELLULAR LOCATION: [CD40 ligand, soluble form]: Secreted {ECO:0000269|PubMed:8626375}. Note=Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and a matrix metalloproteinases (MMP) inhibitor-sensitive pathway. {ECO:0000269|PubMed:15193700}.
Interaction partners:
- Inducible T-cell costimulator
- Tumor necrosis factor receptor superfamily member 5
- T-lymphocyte activation antigen CD80
- T-cell-specific surface glycoprotein CD28
- T-lymphocyte activation antigen CD86
- ICOS ligand
- Ig-like domain-containing protein
- P-selectin glycoprotein ligand 1
- T-cell surface glycoprotein CD4
- CD70 antigen
Sequence:
MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL