wanglab/gogpt-training-data huggingface dataset:
Protein: L-gicerin (Q90880)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAGGRRAAPRCGWGWGGGWGCCPFLCLLLCCGAAGRPEVYMPSSAGSGDREHSQAGVQLLHPWECLLHLRRVVLCQPRPLRSGEAVRHHASGVRIDETEYSERLSVGEDKALSISKVTRQDNARTFICQVGADSQGVGESRTELYTYKIPAPPEITPNSAGIPAQSNDMLKIAQCTSENSFPSPNITWYKNGEPLLQEEDKTKILTTLVRESNGLYTVVSTLFSKVTREDRNSLFHCTVHYWLQGQMRTKDSPRVNVTVFYPTEHVELRVATNAGIVKEGDDVKLVCDADGNPAPVFSFFRRELGDSWQDMTSLADTNDGVLMLHNVSKSSSGLYRCQTLDLDDMTQHEGDVELVVNYIEGVQVKMEPSSPLHEGDSVRLSCTAHSPVKLDYQWRDARGRKVAEGNQLLLTNLTFETSSNFSCRVKARSVPGLEQSKQVAVAVKGKPRIVAISAPLYVRQDEVINLTCKAIAFPQPSFHWSVNGTTHEYMENQHMASNLTVRVSHDLLRAGAMCRVSNALGVSEKHIQLLDQKPSESKGIIIVAIIVCILVVAVLGSIIYFLHKKGKISCGRSGKQDITKPEARKDKNVVEVKSDKLSEEAGLLQGANAEKRSPADQSEKYIDLRN
Protein: Probable pectinesterase/pectinesterase inhibitor 35 [Includes: Pectinesterase inhibitor 35 (Pectin methylesterase inhibitor 35); Pectinesterase 35 (PE 35) (EC 3.1.1.11) (Pectin methylesterase 35) (AtPME35)] (Q9LYT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Pectate lyase
- Pectinesterase inhibitor 3
Sequence:
MATTSFSLPNHKFGIKLMLFLVLNLLSLQTSVFAHSSNSKFTKISRHPNSDSSSRTKPSTSSNKGFLSSVQLSLDHALFARSLAFNLTLSHRTSQTLMLDPVNDCLELLDDTLDMLYRIVVIKRKDHVNDDVHTWLSAALTNQETCKQSLSEKSSFNKEGIAIDSFARNLTGLLTNSLDMFVSDKQKSSSSSNLTGGRKLLSDHDFPTWVSSSDRKLLEASVEELRPHAVVAADGSGTHMSVAEALASLEKGSGRSVIHLTAGTYKENLNIPSKQKNVMLVGDGKGKTVIVGSRSNRGGWNTYQSATVAAMGDGFIARDITFVNSAGPNSEQAVALRVGSDRSVVYRCSIDGYQDSLYTLSKRQFYRETDITGTVDFIFGNSAVVFQSCNLVSRKGSSDQNYVTAQGRSDPNQNTGISIHNCRITGSTKTYLGRPWKQYSRTVVMQSFIDGSIHPSGWSPWSSNFALKTLYYGEFGNSGPGSSVSGRVSWAGYHPALTLTEAQGFTVSGFIDGNSWLPSTGVVFDSGLL
Protein: RNA-binding protein Raly (Autoantigen p542) (Heterogeneous nuclear ribonucleoprotein C-like 2) (hnRNP core protein C-like 2) (hnRNP associated with lethal yellow protein homolog) (Q9UKM9)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that acts as a transcriptional cofactor for cholesterol biosynthetic genes in the liver. Binds the lipid-responsive non-coding RNA LeXis and is required for LeXis-mediated effect on cholesterogenesis (By similarity). May be a heterogeneous nuclear ribonucleoprotein (hnRNP).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q64012}.
Interaction partners:
- CUGBP Elav-like family member 1
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Eukaryotic translation initiation factor 2 subunit 2
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoprotein K
- Matrin-3
- Heterogeneous nuclear ribonucleoprotein D0
- Agouti-signaling protein
- Heterogeneous nuclear ribonucleoprotein M
Sequence:
MSLKLQASNVTNKNDPKSINSRVFIGNLNTALVKKSDVETIFSKYGRVAGCSVHKGYAFVQYSNERHARAAVLGENGRVLAGQTLDINMAGEPKPDRPKGLKRAASAIYSGYIFDYDYYRDDFYDRLFDYRGRLSPVPVPRAVPVKRPRVTVPLVRRVKTNVPVKLFARSTAVTTSSAKIKLKSSELQAIKTELTQIKSNIDALLSRLEQIAAEQKANPDGKKKGDGGGAGGGGGGGGSGGGGSGGGGGGGSSRPPAPQENTTSEAGLPQGEARTRDDGDEEGLLTHSEEELEHSQDTDADDGALQ
Protein: Uncharacterized protein (Q38FF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSESSATKKHVYGYELYSKNVHQYPSITDVKTVKGAIAGNIHDYLNHLGAFEGNARRERGEVLAYSLLAGALSLACAIYFAKDVLLPYKLLTLSLIGVTGAATLCAYVCDCRQKSDNIAFLATCSASTEAKDYLRTLKGHRVCIRLGEVPNSSALTMEAQVVGPPCFFGAPEVHSSSSKVVPYGRYFTKSGYFFPPPLMNDVDNLLSSLKTSTSKKKRQS
Protein: Prolactin-releasing peptide (A0A060VMC1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Prolactin releasing hormone 2 receptor
- Prolactin-releasing peptide receptor
- G-protein coupled receptors family 1 profile domain-containing protein
- Prolactin-releasing peptide receptor
- Prolactin-releasing peptide receptor
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- Coiled-coil domain-containing protein 61
- Centrosomal protein CCDC61
- Neuropeptide Y receptor type 2
Sequence:
MNNLARGKLSTDPPQQATNVYVPCRPSTMTPETTAACPVMVRECVLGSRWLMAALTILLLLSTTVTCVHSTTVEHDFHIVHNVDNRSPEIDPFWYVGRGVRPIGRFGKRQSGGGGSGGLRHPGAMVSTLEILLDIIRNQENIGKTLSGEDADWLP
Protein: Apple domain-containing protein (Q2U7K1)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MKFQAPLAMLSLAGVAYANAPHARPEYKRICDTPSSGEVEVQPGLHATFSCGKYTTDGSRTGLNVANPEACIGECASSDGCVGAIWTAKTTLPYPCYLVQHGSEPSIKTGSDNMWITYRKDEEEAGEDPFGGSGCEADLETMEAELKKCKGLAARTCTNGLQVQTYSTGSKKYKIACGHTVSAAVGSGANMNIVKDVDSFQECADLCASTAGCARATVDTKADKNTCHLYRNPSSQIRASNVDRSVIYLV
Protein: Indole-3-acetic acid-amido synthetase GH3.17 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 17) (AtGH3-17) (Q9FZ87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp, Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Appears to favor Glu over Asp while the other GH3 favor Asp over Glu. Little or no product formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic and butyric acid analogs of IAA, PAA and the synthetic auxin naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be used as substrates.
Interaction partners:
- Auxin transporter protein 1
- Auxin efflux carrier component 8
- Auxin efflux carrier component 5
- Two-component response regulator ARR1
Sequence:
MIPSYDPNDTEAGLKLLEDLTTNAEAIQQQVLHQILSQNSGTQYLRAFLDGEADKNQQSFKNKVPVVNYDDVKPFIQRIADGESSDIVSAQPITELLTSSGTSAGKPKLMPSTAEELERKTFFYSMLVPIMNKYVDGLDEGKGMYLLFIKPEIKTPSGLMARPVLTSYYKSQHFRNRPFNKYNVYTSPDQTILCQDSKQSMYCQLLCGLVQRSHVLRVGAVFASAFLRAVKFLEDHYKELCADIRTGTVTSWITDSSCRDSVLSILNGPNQELADEIESECAEKSWEGILRRIWPKAKYVEVIVTGSMAQYIPTLEFYSGGLPLVSTMYASSECYFGINLNPLCDPADVSYTLLPNMAYFEFLPVDDKSHEEIHFATHSNTDDDDDALKEDLIVNLVNVEVGQYYEIVITTFTGLYRYRVGDILKVTGFHNKAPQFRFVQRRNVVLSIDTDKTSEEDLLNAVTQAKLNHLQHPSSLLLTEYTSYADTSSIPGHYVLFWELKPRHSNDPPKLDDKTMEDCCSEVEDCLDYVYRRCRNRDKSIGPLEIRVVSLGTFDSLMDFCVSQGSSLNQYKTPRCVKSGGALEILDSRVIGRFFSKRVPQWEPLGLDS
Protein: Eukaryotic translation initiation factor 4C (Q9VEA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation initiation factor eIF1
- Small ribosomal subunit protein uS12
- Ribosomal protein
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS17
Sequence:
MPKNKGKGGKNRRRGKNENEFEKRELIFKEDQQEYAQVTKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINQGDIILVGLRDYQDSKADVILKYTPDEARNLKTYGEFPESVRINETVTFVEDGFDEDIEFGDEISSEDDADSVDNI
Protein: Cytochrome c-552 (EC 1.7.2.2) (Ammonia-forming cytochrome c nitrite reductase) (Cytochrome c nitrite reductase) (P0ABK9)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).
Subcellular location: Periplasm {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:7934939, ECO:0000269|PubMed:9593308}.
Interaction partners:
- Cytochrome c-type protein NrfB
- Protein NrfD
- Protein NrfC
- Nitrite reductase large subunit
- Periplasmic nitrate reductase
- Respiratory nitrate reductase 1 alpha chain
- Hydroxylamine reductase
- Periplasmic nitrate reductase, electron transfer subunit
- Nitrite reductase small subunit
- Formate-dependent nitrite reductase complex subunit NrfG
Sequence:
MTRIKINARRIFSLLIPFFFFTSVHAEQTAAPAKPVTVEAKNETFAPQHPDQYLSWKATSEQSERVDALAEDPRLVILWAGYPFSRDYNKPRGHAFAVTDVRETLRTGAPKNAEDGPLPMACWSCKSPDVARLIQKDGEDGYFHGKWARGGPEIVNNLGCADCHNTASPEFAKGKPELTLSRPYAARAMEAIGKPFEKAGRFDQQSMVCGQCHVEYYFDGKNKAVKFPWDDGMKVENMEQYYDKIAFSDWTNSLSKTPMLKAQHPEYETWTAGIHGKNNVTCIDCHMPKVQNAEGKLYTDHKIGNPFDNFAQTCANCHTQDKAALQKVVAERKQSINDLKIKVEDQLVHAHFEAKAALDAGATEAEMKPIQDDIRHAQWRWDLAIASHGIHMHAPEEGLRMLGTAMDKAADARTKLARLLATKGITHEIQIPDISTKEKAQQAIGLNMEQIKAEKQDFIKTVIPQWEEQARKNGLLSQ
Protein: Interleukin-1 receptor type 2 (IL-1R-2) (IL-1RT-2) (IL-1RT2) (CD121 antigen-like family member B) (IL-1 type II receptor) (Interleukin-1 receptor beta) (IL-1R-beta) (Interleukin-1 receptor type II) (CD antigen CD121b) [Cleaved into: Interleukin-1 receptor type 2, membrane form (mIL-1R2) (mIL-1RII); Interleukin-1 receptor type 2, soluble form (sIL-1R2) (sIL-1RII)] (P27931)
Organism: Mus musculus (Mouse)
Function: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competitive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250}. Secreted {ECO:0000250}.
Interaction partners:
- Interleukin-1 alpha
- Interleukin-1 beta
- Interleukin-1 receptor type 1
- Interleukin-1 receptor antagonist protein
- Interleukin-1 receptor accessory protein
- Tumor necrosis factor
- Interleukin-10
- Interferon gamma
- Interleukin-6 receptor subunit alpha
Sequence:
MFILLVLVTGVSAFTTPTVVHTGKVSESPITSEKPTVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLTWSKLDSSQLIPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTSSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVSLIFDPVTREDLHTDFKCVASNPRSSQSLHTTVKEVSSTFSWSIALAPLSLIILVVGAIWMRRRCKRRAGKTYGLTKLRTDNQDFPSSPN
Protein: Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase (Ch1CoA dehydrogenase) (EC 1.3.8.10) (Q2LQN9)
Organism: Syntrophus aciditrophicus (strain SB)
Function: Mediates the conversion of cyclohex-1-ene-1-carbonyl-CoA into (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA in biosynthesis of cyclohexane-1-carboxylate, a by-product produced during fermentation of benzoate and crotonate to acetate. Also able to further convert (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA to benzoyl-CoA.
Interaction partners:
- Cyclohexane-1-carbonyl-CoA dehydrogenase
- Electron transfer flavoprotein subunit alpha
- Enoyl-CoA hydratase
- Electron transfer flavoprotein subunit beta
- 3-hydroxyacyl-CoA dehydrogenase
- Acetyl-CoA acetyltransferase
- Pyruvate:ferredoxin oxidoreductase
- Enoyl-CoA hydratase
Sequence:
MKGPIKFNALSLQGRSVMSNQSNDTTITQRRDTMNELTEEQKLLMEMVRNLAVREIAPRAIEIDENHSFPVHARDLFADLGLLSPLVPVEYGGTGMDITTFAMVLEEIGKVCASTALMLLAQADGMLSIILDGSPALKEKYLPRFGEKSTLMTAFAATEPGAGSDLLAMKTRAVKKGDKYVINGQKCFITNGSVADILTVWAYTDPSKGAKGMSTFVVERGTPGLIYGHNEKKMGMRGCPNSELFFEDLEVPAENLVGEEGKGFAYLMGALSINRVFCASQAVGIAQGALERAMQHTREREQFGKPIAHLTPIQFMIADMATEVEAARLLVRKATTLLDAKDKRGPLIGGMAKTFASDTAMKVTTDAVQVMGGSGYMQEYQVERMMREAKLTQIYTGTNQITRMVTGRSLLFPS
Protein: BCL2 associated X, apoptosis regulator (A0A0D9S330)
Organism: Chlorocebus sabaeus (Green monkey) (Simia sabaea)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- BCL2 like 11
- BH3-interacting domain death agonist
- Apoptosis regulator Bcl-2
- Cytochrome c
- Bcl-2 homologous antagonist/killer
- Bcl-2-like protein 1
- Cellular tumor antigen p53
- Parkin RBR E3 ubiquitin protein ligase
- Apoptosis-inducing factor 1, mitochondrial
- protein acetyllysine N-acetyltransferase
Sequence:
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGETPELALDPVPQDASTKRLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTILVAGVLTASLTIWKKMG
Protein: V-type proton ATPase subunit d 1 (V-ATPase subunit d 1) (Vacuolar proton pump subunit d 1) (Q6PGV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Subunit of the V0 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 (By similarity). May play a role in coupling of proton transport and ATP hydrolysis (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P61421}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61421}; Cytoplasmic side {ECO:0000250|UniProtKB:P61421}. Lysosome membrane {ECO:0000250|UniProtKB:P61421}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000269|PubMed:21844891}.
Interaction partners:
- V-type proton ATPase subunit H
- V-type proton ATPase subunit G
- V-type proton ATPase subunit F
- Vacuolar proton pump subunit B
- Vacuolar proton pump subunit B
- ATPase H+-transporting V1 subunit E1b.
- ATPase H+-transporting V1 subunit E1a
- V-type proton ATPase subunit D
- V-type proton ATPase 21 kDa proteolipid subunit c''
- H
Sequence:
MPFSELYFNVDNGYLEGLVRGFKAGILSQADYLNLVQCETLEDLKLHLQSTDYGSFLANEASPLTVSVIDDKLKEKMVVEFRHMRNQSYEPLASFMDFITYSYMIDNVILLITGTLHQRAISELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLEAFYKFCTTLGGTTADTMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGKLYPEGLAQLARADDYEQVKAVAEYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFSVFYAYVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Ube2l3 protein (Ubiquitin-conjugating enzyme E2L 3) (D3Z8W5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD
Protein: Calcium-regulated heat stable protein 1 (Calcium-regulated heat-stable protein of 24 kDa) (CRHSP-24) (Q9WU49)
Organism: Rattus norvegicus (Rat)
Function: Binds mRNA and regulates the stability of target mRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9712905}. Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Detected at cytoplasmic stress granules and P-bodies. Detected at exosome granules where mRNA is degraded (By similarity). {ECO:0000250}.
Interaction partners:
- DIS3-like exonuclease 1
- Exosome complex exonuclease RRP44
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Exosome complex component RRP41
- Exosome complex component MTR3
- Exosome complex component RRP46
- Exosome complex component 10
- Exosome complex component RRP45
- Exosome complex component RRP43
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
Sequence:
MSSEPPPPPQPPTHQTSIGLLDTPRARDRSPSPLRGNVVPSPLPTRRTRTFSATVRASQGPVYKGVCKCFCRSKGHGFITPADGGPDIFLHISDVEGEYVPVEGDEVTYKMCSIPPKNEKLQAVEVVITHLAPGTKHETWSGHVISS
Protein: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (3-ketoacyl-[acyl-carrier-protein] reductase beta subunit) (KAR beta subunit) (Carbonyl reductase family member 4) (CBR4) (Quinone reductase CBR4) (EC 1.6.5.10) (Q91VT4)
Organism: Mus musculus (Mouse)
Function: Component of the heterotetramer complex KAR (3-ketoacyl-[acyl carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)-hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis. The homotetramer has NADPH-dependent quinone reductase activity (in vitro), hence could play a role in protection against cytotoxicity of exogenous quinones. As a heterotetramer, it can also reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N4T8}.
Interaction partners:
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8)
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Fatty acid synthase
Sequence:
MDKVCAVFGGSRGIGRAVAQLMAQKGYRLAIVSRNLEVAKVTAGELGGNHLAFRCDVAKEQDVQSTFQEMEKHLGPVNFLVNAAGINRDSLLVRTKTEDMISQLHTNLLGSMLTCKAAMKTMIQQGGSIVNVGSIIGLKGNVGQSAYSATKGGLVGFSRSLAKEVARKKIRVNVVAPGFIRTDMTRHLKEEHFKKNIPLGRFGETLEVAHAVVFLLESPYITGHVLIVDGGLQLTV
Protein: Leucine-rich repeat receptor-like serine/threonine-protein kinase SKM1 (EC 2.7.11.1) (Protein STERILITY-REGULATING KINASE MEMBER 1) (O82318)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor with a serine/threonine-protein kinase activity (By similarity). Together with SKM2, LRR-rich receptor-like kinase (LRR-RLK) required for male fertility by the perception of CLE43 and CLE45 peptides and the transduction of their promoting action in pollen tubes, especially under relatively high temperature (at 30 degrees Celsius), thus conferring tolerance against high temperature probably through the maintenance of mitochondrial activity. Seems to not be involved in the perception of CLE45 peptide in roots.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9SYQ8}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein
- Membrane-associated kinase regulator 5
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MSTSHHHHHPPYLITTLFFLFLNFSCLHANELELLLSFKSSIQDPLKHLSSWSYSSTNDVCLWSGVVCNNISRVVSLDLSGKNMSGQILTAATFRLPFLQTINLSNNNLSGPIPHDIFTTSSPSLRYLNLSNNNFSGSIPRGFLPNLYTLDLSNNMFTGEIYNDIGVFSNLRVLDLGGNVLTGHVPGYLGNLSRLEFLTLASNQLTGGVPVELGKMKNLKWIYLGYNNLSGEIPYQIGGLSSLNHLDLVYNNLSGPIPPSLGDLKKLEYMFLYQNKLSGQIPPSIFSLQNLISLDFSDNSLSGEIPELVAQMQSLEILHLFSNNLTGKIPEGVTSLPRLKVLQLWSNRFSGGIPANLGKHNNLTVLDLSTNNLTGKLPDTLCDSGHLTKLILFSNSLDSQIPPSLGMCQSLERVRLQNNGFSGKLPRGFTKLQLVNFLDLSNNNLQGNINTWDMPQLEMLDLSVNKFFGELPDFSRSKRLKKLDLSRNKISGVVPQGLMTFPEIMDLDLSENEITGVIPRELSSCKNLVNLDLSHNNFTGEIPSSFAEFQVLSDLDLSCNQLSGEIPKNLGNIESLVQVNISHNLLHGSLPFTGAFLAINATAVEGNIDLCSENSASGLRPCKVVRKRSTKSWWLIITSTFAAFLAVLVSGFFIVLVFQRTHNVLEVKKVEQEDGTKWETQFFDSKFMKSFTVNTILSSLKDQNVLVDKNGVHFVVKEVKKYDSLPEMISDMRKLSDHKNILKIVATCRSETVAYLIHEDVEGKRLSQVLSGLSWERRRKIMKGIVEALRFLHCRCSPAVVAGNLSPENIVIDVTDEPRLCLGLPGLLCMDAAYMAPETREHKEMTSKSDIYGFGILLLHLLTGKCSSSNEDIESGVNGSLVKWARYSYSNCHIDTWIDSSIDTSVHQREIVHVMNLALKCTAIDPQERPCTNNVLQALESTSSSSSSCTTYLSKILSLA
Protein: Uncharacterized protein YjiH (P39379)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inner membrane protein YjiG
- RNA 2'-phosphotransferase
- Isoaspartyl dipeptidase
- D-galactonate dehydratase
- D-galactonate transporter
- Galactonate operon transcriptional repressor
Sequence:
MTQQGDAVAGELATEKVGIKGYLAFFLTIIFFSGVFSGTDSWWRVFDFSVLNGSFGQLPGANGATTSFRGAGGAGAKDGFLFALELAPSVILSLGIISITDGLGGLRAAQQLMTPVLKPLLGIPGICSLALIANLQNTDAAAGMTKELAQEGEITERDKVIFAAYQTSGSAIITNYFSSGVAVFAFLGTSVIVPLAVILVFKFVGANILRVWLNFEERRNPTQGAQA
Protein: Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) (P00683)
Organism: Mus musculus (Mouse)
Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Ribonuclease inhibitor
- Inactive pancreatic lipase-related protein 1
- Anionic trypsin-2
- Chymotrypsin-like elastase family member 3B
- Bile salt-activated lipase
- Chymotrypsin-like elastase family member 2A
- Colipase
- Carboxypeptidase A1
Sequence:
MGLEKSLILFPLFFLLLGWVQPSLGRESAAQKFQRQHMDPDGSSINSPTYCNQMMKRRDMTNGSCKPVNTFVHEPLADVQAVCSQENVTCKNRKSNCYKSSSALHITDCHLKGNSKYPNCDYKTTQYQKHIIVACEGNPYVPVHFDATV
Protein: Peptidyl-prolyl cis-trans isomerase CYP71 (PPIase CYP71) (EC 5.2.1.8) (Cyclophilin of 71 kDa) (Cyclophilin-71) (AtCYP71) (Q8W4D0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Histone proline isomerase that increases the rate of cis-trans isomerization of the synthetic histone H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (RKme3-SAP30F-p-nitroanilide) in the histone H3 N-terminal tail, in vitro. Histone remodeling factor involved in chromatin-based gene silencing. Reinforces H3K27 methylation. Involved in fundamental processes of chromatin assembly and histone modification by mediating the targeting of FAS1 and LHP1 on the chromatin. Required for the formation and development of leaves, for normal phyllotaxy and for the formation, maintenance and activity of root and shoot apical meristems.
Subcellular location: Nucleus {ECO:0000269|PubMed:17704213}.
Interaction partners:
- Cytochrome P450 86A1
- Cytochrome P450 89A2
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- At2g20330/F11A3.12
- Peptidyl-prolyl cis-trans isomerase CYP59
- At1g80930/F23A5_23
- Initiation factor eIF-4 gamma, MA3
- 3beta,22alpha-dihydroxysteroid 3-dehydrogenase
Sequence:
MEEESKNGGTTIPTEELAVVAVPPVVEEEEPMVGPGPAPRGKRKRPLQFEQAYLDSLPSANMYEKSYMHRDVVTHVAVSAAEFFISGSMDGHLKFWKKKGVGIEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDMMAMIRLPYIPGAVEWVYKQGDVKAKLAVSDRDSLFVHIYDPRSGSNEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGIIEYWSATTLQFPEDEVNFKLKSDTNLFEIIKCKTTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYDESLVVAQDLQRSDAPLYRLEAIDFGRRMAVEKELEKTESAPQPNAVFDESSNFLIYATFLGIKVINLHTNTVARILGKVESNERYLRVALYQGDQGGKKVRKIPAAAANVNESKEPLTDPTILCCAFKKHRIYMFSRREPEEPEDASQGRDVFNEKPAADELMSVSDIGNSATTSLPENVIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTVPKS
Protein: Aldo-keto reductase family 1, member C1 (A0A8I6AV33)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MNSKQQTVRLSDGHFIPVLGFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPERVQPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPVLLADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQVMSCCGC
Protein: Mcf.2 transforming sequence (A2AET8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAEANPPRGKMRFRRNAASFPGSLHLVLVLRPTSFLQRTFTDIGFRFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIEKFAVTVKEMAQMLQSFGTELAETELPQDILSIEEILAGRAERYHLLKNDLTAVTKEGKVLLMNLQVPATEETVSSSLECTQHINGDWQTIKKLLAQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQEAVTQVEFLLSQQRELGDITGNLAQVKQRLKKLEILDDKSQELLTKARIVILRGHKLASNHHYALDLICQRCNELRYLSDILVNEIRTKRVQLSRTFKVHRLLQQARQCCDQGECLLASQGMDKFQTKEDAQKALQDVDNFLQMAMPFINYDIESLQYEFDVLLSPELKAQMQNIQLKLENIRSAFQNQQAGCKSLKEVPEGAFQNLVPASENVMRSRMIFFSPKHVGIGYSFFQACRIFLKVKKSWRQIHAQSNVKVEAVEDSQEKNSDQSPKLDNSLDILKNHVLNELIQTERAYVRELFTVLLGYRSEMDNPQMFDLMPPLLRNKKDVLFGNMAEIYEFHNNIFMSRLEDCSDAPERVGPCFLERKDDFQMYAKYCQNKPRSELIWRKYSECAFFQECQRKLKHRLGLDSYLLKPVQRITKYQLLLKELLKYSKEGEGTTKLKEALDSMLELLKSVNDSMHQTAINGYVGNINELGKMVLQGSFNVWLGHRKGATKMKDFARFKPMQRHLFLYEKAVMFCKRRFESGEGADRYPSYSFKHCLKMEDVGITEHVKGDNRKFEIRYSEKEEIYIVQAPNVDVKMLWLKEIRKILVQQKELMTAKTQQDQALDQDQLFPQQQNAELCKSSPFCVCEETLFNATEAGAEVEQAGALIKVREAAVLAQAEASSAAWNGMLPSAEGAAAIAEHSYNYFSSNNDHGEDRTQMRHMSEVTF