wanglab/gogpt-training-data huggingface dataset:
Protein: Lipase (EC 3.1.1.3) (G8BKP1)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MRYFAIAFLLINTISAFVLAPKKPSQDDFYTPPQGYEAQPLGSILKTRNVPNPLTNVFTPVKVQNAWQLLVRSEDTFGNPNAIVTTIIQPFNAKKDKLVSYQTFEDSGKLDCAPSYAIQYGSDISTLTTQGEMYYISALLDQGYYVVTPDYEGPKSTFTVGLQSGRATLNSLRATLKSGNLTGVSSDAETLLWGYSGGSLASGWAAAIQKEYAPELSKNLLGAALGGFVTNITATAEAVDSGPFAGIISNALAGIGNEYPDFKNYLLKKVSPLLSITYRLGNTHCLLDGGIAYFGKSFFSRIIRYFPDGWDLVNQEPIKTILQDNGLVYQPKDLTPQIPLFIYHGTLDAIVPIVNSRKTFQQWCDWGLKSGEYNEDLTNGHITESIVGAPAALTWIINRFNGQPPVDGCQHNVRASNLEYPGTPQSIKNYFEAALHAILGFDLGPDVKRDKVTLGGLLKLERFAF
Protein: Germ cell-less protein-like 2 (Germ cell-less protein-like 1-like) (Q8NEA9)
Organism: Homo sapiens (Human)
Function: Possible function in spermatogenesis. Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:Q920G9}.
Interaction partners:
Sequence:
MGSSSSRVLGQPRRALAQQEQGARARGSARRPDTGDDAASYGFCYCPGSHKRKRSSGACRYCDPDSHREEHEEEGDKQQPLLNTPARKKLRSTSKYIYQTLFLNGENSDIKICALGEEWRLHKIYLCQSGYFSSMFSGSWKESSMNIIELEIPDQNIDVDALQVAFGSLYRDDVLIKPSRVVAILAAACMLQLDGLIQQCGETMKETINVKTVCGYYTSVEIYGLDSVKKKCLEWLLNNLMTHQNVKLFKELGINVMKQLIGSSNLFVMQVEMDVYTTLKKWMFLQLVPSWNGSLKQLLTETDVWFSKQRKDFEGMAFLETEPGKPFVSVFRHLRLQYIISDLASARIIEQDGIVPSEWLSSVYKQQWFAMLRAEQDREVGPQEINKEDLEGNSMRCGRKLAKDGEYYWCWTGFNFGFDLLVIYTNGYIIFKRNTLNQPRSGSVSLRPRRSIAFRLRLASFDSSGKLVCSRTTGYQILILKKDQEQVVMNLDSRFLTFPLYICCNFLYISPEKGIENNRHPENPEN
Protein: Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase) (O25533)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can also utilize CTP or GTP instead of ATP as a phosphoryl donor, albeit to a lesser extent.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pantothenate synthetase
- Phosphopantetheine adenylyltransferase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- Plasminogen-binding protein PgbB
- Urease accessory protein UreH-like transmembrane domain-containing protein
- Transcription elongation factor GreA
- 50S ribosomal protein L22
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- ADP-L-glycero-D-mannoheptose-6-epimerase
Sequence:
MPARQSFTDLKNLVLCDIGNTRIHFAQNYQLFSSAKEDLKRLGIQKEIFYISVNEENEKALLNCYPNAKNIAGFFHLETDYVGLGIDRQMACLAVNNGVVVDAGSAITIDLIKEGKHLGGCILPGLAQYIHAYKKSAKILEQPFKALDSLEVLPKSTRDAVNYGMVLSVIACIQHLAKNQKIYLCGGDAKYLSAFLPHSVCKERLVFDGMEIALKKAGILECK
Protein: Calmodulin (A0A1D8PMF8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Tubulin beta chain
- Mlc2p
- Calcium-channel protein CCH1
- Serine/threonine-protein phosphatase
- FK506-binding protein 1
- Myosin-5
- Actin
- Transcriptional regulator CRZ1
- calcium/calmodulin-dependent protein kinase
- Myosin 2
Sequence:
MAEKLSEQQIAEFKEAFSLFDKDSDGKITTKELGTVMRSLGQNPSESELTDMINEVDVNSDGSIDFPEFLTMMARKMKDTDSEAEIAEAFKVFDRNGDGKISAAELRHVLTSIGEKLSDADVDQMIKEADTNNDGEIDIQEFTSLLAAK
Protein: Nogo receptor homolog 1a (Reticulon-4 receptor-like 2a precursor) (Q6WZD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Cell projection {ECO:0000256|ARBA:ARBA00004316}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
Interaction partners:
Sequence:
METSTFTRSQRSSFAHNFKSALSLWLVVWLVVVKPVPAQNCPHRCVCYPTPMTVSCQAQNFTIVPHGMPYESQRVFLQNNRITELRVGSFAFGTQVLWLFSNNITWIEAGAFSELRDLEELDLGDNPNLHRLEGGAFRGLEKLQSLHMHRCKLAALPHDIFHKLYSLQFLYLQENQLHFIQDDLFADLINLSQLFLHGNRIRTLSENVFRGLVNLDRLLLHDNRVRQVNRRAFRDLGQLTMLFLFNNSLAELPGQAMRDVSSIEFLRLNNNPWACGCEARPLWEFFRGARLSSSEVLCASPASRRGQDLRFLREMDFALCPLPDPGSLAGTTTTTFSTKTRWWFSKNKPVSTSKGIFEKSSETKAHPYTGGKSSVTSTSTKYELGEEEALLPKLDPEEYWANYGNEDAGITSLRCFELECPPEFDSLPPSSSSSRSSSSTFLLLSMSVLTVCIHLLFG
Protein: Zinc-binding dehydrogenase family protein (F4KFK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Histone-lysine N-methyltransferase SETD1B-like protein
- At4g33840/F17I5_30
- Glycosyl hydrolase family 10 protein
- FAD-dependent oxidoreductase domain-containing protein 1
- Glycosyl hydrolase family 10 protein
Sequence:
MTTATNKQVILKDYVSGFPTESNFDFTTTTVELRVPEANRRVRSVYSDRIWAFRLQKRRPTLGYSCMGGVQCYHLTHEHFKIQHTDVPLSYYTGLLGMPGMTAYVGFYEICSPKKGETVYVSAASGAVGQLVGQFAKMMGCYVVGSAGSKEKVDLLKTKFGFDYAFNYKEEPDLSAALKRCFPNGIDIYFENVGGKMLDAVLMNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDEYSKFLEFLHPHIKEGKITYVEDVADGLEKGPEALVGLFHGKNVGKQVVVIARE
Protein: Secreted protein (H0ZT53)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Interaction partners:
- Alpha-synuclein
Sequence:
VFSSLWLLSTVSIWGCAVALAVASSAAGVVVAVVSAAGTSACLGSSLSWASSAFKDGEFSVEALVALSLSGAAAAAVFSSEEAAGVAACGAGCSEPVSAAPSPFFSSAGALLSLLPSSCWALSAAAASVAAGASLSLFSAAPPAGPSSFLSAASVSDAGASPFFSPLSFFLVMCPRKLAWILVAAL
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7 (Q61016)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- 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
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 7
- C-X-C chemokine receptor type 4
Sequence:
MSGTNNVAQARKLVEQLRIEAGIERIKVSKASSDLMGYCEQHARNDPLLVGVPASENPFKDKKPCIIL
Protein: Diabetes and obesity regulated, isoform G (Diabetes and obesity regulated, isoform H) (M9NFM7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}. Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
- Ecdysone receptor
Sequence:
MLSSLASYLFGSATSDSISQEANPAQNRTNASNANSSSSPGPTSDPAAGDVIEVTSSTPSVAGSSRGAVRASNGKRGKNRRGKQQRTNQQQRKQQPAITKLLTPSGEIVDEDFDEDEWYIVEKEDEEDDSLPRSDSEEELSVVEVSQPRGGSNNASSPMVTVATGTAFNCRRRQGVNSCSLYSGPRPQQQRNYLQRSRVSRPLSISTLSPPRSVPALGAGDHDTLTQSLYVASPSGSDQGQDHGQGANVLMEESWYVTPPPCFTSIGPINMETSPFENLLIEHPSMSVYHSIRSTQEGTDSFVNLDLGVSTEVPQQREEPEPEAEPQDQRQALQEQQRAPNARFDSHAAVQLKQQTLARQSQKSKNKKEHQQLCRSAIKRANKVRDFQAKANRPRRSEMQHCKLVSGANNNRSKCCY
Protein: Thiol peroxidase (Tpx) (EC 1.11.1.24) (Peroxiredoxin tpx) (Prx) (Scavengase p20) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin) (P0A862)
Organism: Escherichia coli (strain K12)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Has a preference for alkyl hydroperoxides and acts as lipid peroxidase to inhibit bacterial membrane oxidation. Acts as principal antioxidant during anaerobic growth.
Subcellular location: Periplasm {ECO:0000269|PubMed:7499381}. Cytoplasm {ECO:0000269|PubMed:19054092}. Note=Forms a mixed disulfide with cytoplasmic thioredoxin (trx1). {ECO:0000269|PubMed:19054092}.
Interaction partners:
- Thioredoxin reductase
- Alkyl hydroperoxide reductase C
- Thioredoxin 1
- Outer membrane protein A
- Elongation factor Tu 1
- Protein YobF
- Cell division topological specificity factor
- NADP-dependent 3-hydroxy acid dehydrogenase YdfG
- Cold shock-like protein CspC
- Ribosome-associated inhibitor A
Sequence:
MSQTVHFQGNPVTVANSIPQAGSKAQTFTLVAKDLSDVTLGQFAGKRKVLNIFPSIDTGVCAASVRKFNQLATEIDNTVVLCISADLPFAQSRFCGAEGLNNVITLSTFRNAEFLQAYGVAIADGPLKGLAARAVVVIDENDNVIFSQLVDEITTEPDYEAALAVLKA
Protein: Tetratricopeptide repeat protein 19, mitochondrial (TPR repeat protein 19) (Q6DKK2)
Organism: Homo sapiens (Human)
Function: Required for the preservation of the structural and functional integrity of mitochondrial respiratory complex III by allowing the physiological turnover of the Rieske protein UQCRFS1. Involved in the clearance of UQCRFS1 N-terminal fragments, which are produced upon incorporation of UQCRFS1 into the complex III and whose presence is detrimental for its catalytic activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:21278747}.
Interaction partners:
- Zinc finger FYVE domain-containing protein 26
- Complex III assembly factor LYRM7
- Mitochondrial chaperone BCS1
Sequence:
MFRLLSWSLGRGFLRAAGRRCRGCSARLLPGLAGGPGPEVQVPPSRVAPHGRGPGLLPLLAALAWFSRPAAAEEEEQQGADGAAAEDGADEAEAEIIQLLKRAKLSIMKDEPEEAELILHDALRLAYQTDNKKAITYTYDLMANLAFIRGQLENAEQLFKATMSYLLGGGMKQEDNAIIEISLKLASIYAAQNRQEFAVAGYEFCISTLEEKIEREKELAEDIMSVEEKANTHLLLGMCLDACARYLLFSKQPSQAQRMYEKALQISEEIQGERHPQTIVLMSDLATTLDAQGRFDEAYIYMQRASDLARQINHPELHMVLSNLAAVLMHRERYTQAKEIYQEALKQAKLKKDEISVQHIREELAELSKKSRPLTNSVKL
Protein: Mitochondrial import receptor subunit TOM70 (Mitochondrial precursor proteins import receptor) (Translocase of outer membrane 70 kDa subunit) (Translocase of outer mitochondrial membrane protein 70) (Q75Q39)
Organism: Rattus norvegicus (Rat)
Function: Acts as receptor of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex). Recognizes and mediates the translocation of mitochondrial preproteins from the cytosol into the mitochondria in a chaperone dependent manner. Mediates TBK1 and IRF3 activation induced by MAVS in response to Sendai virus infection and promotes host antiviral responses during virus infection (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11956321}; Single-pass membrane protein {ECO:0000269|PubMed:11956321}.
Interaction partners:
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM7 homolog
- Translocase of outer mitochondrial membrane 5
- Mitochondrial import receptor subunit TOM40B
- Mitochondrial antiviral-signaling protein
- Translocase of outer mitochondrial membrane 6.
- TOMM20-like protein 1
- Sorting and assembly machinery component 50 homolog
Sequence:
MAASKPVEAAMAAAAAPASGNGVGSSGGTAAPGSGAGTLPRWHVALAIGAPLLLGAGAMYLWSRRRRRREAGGRGDASGLKRNSERKTPEGRASPALGSGPDGSGDSLEMSSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNADLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNEQSMLLADKVLKLLGKENAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAQGKYMAEALLLRATFYLLIGSANAAKPDLDKVISLKEANVKLRANALIKRGTMCMQQQQPMLSTQDFNMAAEIDPMNSDVYHHRGQLKILLDLVEEAVADFDACIRLRPKFALAQAQKCFALYRQAYTANNSSQVQAAMKGFEEVIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDKGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL
Protein: LIM domain binding 3 (A0A096MKD4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGAARADISVDSILSQLFLGALHSLTRQQGTQQARPEEATAVGTSMSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKVGAGHWYADYQERFNPSVLKDSALSTHKPIEVKGLGGKATIIHAQYNTPITPSHSTCLRSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSSTPIEHAPVCTSQATSPLLPASAPSPAAASPIAASPTLATAAAAHAVAASAAGPASSPVENPRPQASAYSPAAATSPAPAAHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASPYSPSPGANYSPTPYTPSPAPAYTPSPAPTYTPSPAPTYSPSPAPAYTPSPAPNYNPTPSAAYSGGPSESASRPPWVTDDSFSQKFAPGKSTTSVSKQTLPRGAPAYNPTGPQVTPLARGTFQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFNCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPICAKCNTKIMGEVMHALRQTWHTTCFICAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDKPLCKKHAHAINV
Protein: Tubulin alpha-2 chain (EC 3.6.5.-) (P06604)
Organism: Drosophila melanogaster (Fruit fly)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-3 chain
- Tubulin beta chain
- Tubulin beta-2 chain
- beta-Tubulin at 65B
- Serine/threonine-protein kinase CG17528
- non-specific serine/threonine protein kinase
- Tubulin beta chain
- Echinoderm microtubule-associated protein-like CG42247
- Dynein heavy chain, cytoplasmic
- Dynein heavy chain
Sequence:
MRECISVHIGQAGVQIGNACWELYCLEHGIQPDGHMPSDKTVGGGDDSFSTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDVVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYMNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISVEKAYHEQLTVAEITNACFEPANQMVKCDPRRGKYMACCMLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFAEAREDLAALEKDYEEVGIDSTTELGEDEEY
Protein: Zinc finger CCCH domain-containing protein 37 (AtC3H37) (ENHANCER OF AG-4 protein 1) (Q941Q3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in flower development. Functions in floral reproductive organ identity by binding AGAMOUS (AG) pre-mRNA and promoting its processing. Functions in association with HUA2 and HEN4.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11595801, ECO:0000269|PubMed:12530963}. Note=Nuclear with a speckled distribution pattern.
Interaction partners:
- KH domain-containing protein HEN4
- ENHANCER OF AG-4 protein 2
- Zinc finger CCCH domain-containing protein 47
- Zinc finger CCCH domain-containing protein 17
- Flowering locus K homology domain
- Zinc finger CCCH domain-containing protein 54
- Zinc finger CCCH domain-containing protein 15
- Zinc finger CCCH domain-containing protein 29
- DExH-box ATP-dependent RNA helicase DExH10
- Protein HUA2-LIKE 1
Sequence:
MAHRQLYSYALQPSYAAAASTVSPAPPPPQQPLPPKTGLSSLYGSSADHYFPDTTYRFLARDGSEALSNYSGTLASSSSMYHHLPNTTASHLAYPQLLQHQEVAWPPGVEVPGAASAVEPLPPGVKRTSEALYYPTLLGAHNTIGQTEAWYTTDYFTKRPKLESTSHLPIYPQRAGEKDCTHYMQTRTCKFGESCRFDHPIWVPEGGIPDWKEAPVVPNEEYPERPGEPDCPYYIKTQRCKYGSKCKFNHPREEAAVSVETQDSLPERPSEPMCTFYMKTGKCKFGLSCKFHHPKDIQLPSSSQDIGSSVGLTSEPDATNNPHVTFTPALYHNSKGLPVRSGEVDCPFYLKTGSCKYGATCRYNHPERTAFIPQAAGVNYSLVSSNTANLNLGLVTPATSFYQTLTQPTLGVISATYPQRPGQSECDYYMKTGECKFGERCKFHHPADRLSAMTKQAPQQPNVKLSLAGYPRREGALNCPYYMKTGTCKYGATCKFDHPPPGEVMAKTTSEADAAGATNTDTTQ
Protein: Jacalin-related lectin 35 (JA-responsive protein 1) (Myrosinase-binding protein-like At3g16470) (O04309)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Beta-D-glucopyranosyl abscisate beta-glucosidase
- Phenazine biosynthesis PhzC/PhzF protein
- GDSL esterase/lipase 22
- 1-aminocyclopropane-1-carboxylate oxidase homolog 9
- 1-aminocyclopropane-1-carboxylate oxidase homolog 4
- TSA1-like protein
Sequence:
MAKKLEAQGGRGGEEWDDGGAYENVKKVYVGQGDSGVVYVKFDYEKDGKIVSHEHGKQTLLGTEEFVVDPEDYITSVKIYYEKLFGSPIEIVTALIFKTFKGKTSQPFGLTSGEEAELGGGKIVGFHGSSSDLIHSVGVYIIPSTTPLTPPVSGGLTKLEAQGGRGGDVWDDGGAYDNVKKVYVGQGDSGVVYVKFDYEKDGKIVSLEHGKQTLLGTEEFEIDPEDYITYVKVYYEKLFGSPIEIVTALIFKTFKGKTSQPFGLTSGEEAELGGGKIVGFHGTSSDLIHSLGAYIIPSSTPLTPSSNTIPAQGGDGGVAWDDGVHDSVKKIYVGQGDSCVTYFKADYEKASKPVLGSDHGKKTLLGAEEFVLGPDEYVTAVSGYYDKIFSVDAPAIVSLKFKTNKRTSIPYGLEGGTEFVLEKKDHKIVGFYGQAGEYLYKLGVNVAPIAK
Protein: UDP-glucuronosyltransferase 1A1 (UGT1A1) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-1) (UDPGT 1-1) (UGT1*1) (UGT1-01) (UGT1.1) (UGTBR1) (Q63886)
Organism: Mus musculus (Mouse)
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 (By similarity). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (By similarity). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol (By similarity). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (By similarity). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (By similarity). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (By similarity). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22309}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- Sulfotransferase 1E1
- UDP-glucose 6-dehydrogenase
- Cytochrome P450 1B1
- Cytochrome P450 1A2
- Beta-glucuronidase
- Aromatase
- 11-beta-hydroxysteroid dehydrogenase 1
- Aldo-keto reductase family 1 member D1
Sequence:
MTVVCWSSRLLLLLPYLLLCVFGPSASHAGRLLVFPMDGSHWLSMLGVIQQLQQKGHEVVVIAPEASIHIKEGSFYTLRKFPVPFQKENVTATLVELGRTAFNQDSFLLRVVKIYMKVKRDSSMLLAGCSHLLHNAEFMASLEESHFDALLTDPFLPCGSIVAQYLTVPTVYFLNKLPCSLDSEATQCPVPLSYVPKSLSFNSDRMNFLQRVKNVLLAVSENFMCRVVYSPYGSLATEILQKEVTVQDLLSPASIWLMRSDFVKDYPRPIMPNMVFIGGINCLQKKPLSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTVLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKTRAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVFKCCAYGCRKCFGGKGRVKKSHKSKTH
Protein: Glideosome associated protein with multiple membrane spans 2 (Q8IFN1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Rhomboid-like protease
Sequence:
MGSYGMDVDDAYLHQGQYAAPYDNQYQQDDDTPSPRGENHTPFVGYFSSHLLRTGFFLQCVSLVLMFVFYWAFGGTGIFIFDLYAGPECVKVSSTFHLTISILMALYLLGTLYIAMFQVFVADNSKWCRGFRAGSKLLSAAVTLDLLSSILRLVQYLYAYFYMSMRWWARYQQTKSDWTLLHFGSIVHSFALFIYGAAFFYMEAYHDEGTYEELAWSNLTLFKLAGLAELIMVFSGFGAFFSILLLGAIVCATVWAFSFEPLLEKWSPELHSRDINADVLPEIKHEDEQCAYNEENIYEPYSVNPDNVEYGEEMVAKNMNEKYIDGNTYDSNIYSANNGIPTTYDYTQIEGQLKKNVEMGVTENNYIKTAQY
Protein: Deadenylation-dependent mRNA-decapping factor PAT1 (DNA topoisomerase 2-associated protein PAT1) (Decapping activator and translational repressor PAT1) (Topoisomerase II-associated protein PAT1) (mRNA turnover protein 1) (P25644)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10779343, ECO:0000269|PubMed:23706738}. Nucleus {ECO:0000269|PubMed:23706738}. Cytoplasm, P-body {ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:23222640}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:23893485}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23222640}. Note=Shuttles between cytoplasm and nucleus. Exported in complex with LSM1. {ECO:0000269|PubMed:23706738}.
Interaction partners:
- ATP-dependent RNA helicase DHH1
- LSM complex subunit LSM4
- LSM1-LSM7 complex subunit LSM1
- LSM complex subunit LSM2
- LSM complex subunit LSM7
- LSM complex subunit LSM6
- LSM complex subunit LSM3
- m7GpppN-mRNA hydrolase
- LSM complex subunit LSM5
- 5'-3' exoribonuclease 1
Sequence:
MSFFGLENSGNARDGPLDFEESYKGYGEHELEENDYLNDETFGDNVQVGTDFDFGNPHSSGSSGNAIGGNGVGATARSYVAATAEGISGPRTDGTAAAGPLDLKPMESLWSTAPPPAMAPSPQSTMAPAPAPQQMAPLQPILSMQDLERQQRQMQQQFMNFHAMGHPQGLPQGPPQQQFPMQPASGQPGPSQFAPPPPPPGVNVNMNQMPMGPVQVPVQASPSPIGMSNTPSPGPVVGATKMPLQSGRRSKRDLSPEEQRRLQIRHAKVEKILKYSGLMTPRDKDFITRYQLSQIVTEDPYNEDFYFQVYKIIQRGGITSESNKGLIARAYLEHSGHRLGGRYKRTDIALQRMQSQVEKAVTVAKERPSKLKDQQAAAGNSSQDNKQANTVLGKISSTLNSKNPRRQLQIPRQQPSDPDALKDVTDSLTNVDLASSGSSSTGSSAAAVASKQRRRSSYAFNNGNGATNLNKSGGKKFILELIETVYEEILDLEANLRNGQQTDSTAMWEALHIDDSSYDVNPFISMLSFDKGIKIMPRIFNFLDKQQKLKILQKIFNELSHLQIIILSSYKTTPKPTLTQLKKVDLFQMIILKIIVSFLSNNSNFIEIMGLLLQLIRNNNVSFLTTSKIGLNLITILISRAALIKQDSSRSNILSSPEISTWNEIYDKLFTSLESKIQLIFPPREYNDHIMRLQNDKFMDEAYIWQFLASLALSGKLNHQRIIIDEVRDEIFATINEAETLQKKEKELSVLPQRSQELDTELKSIIYNKEKLYQDLNLFLNVMGLVYRDGEISELK
Protein: Cytochrome P450 monooxygenase (EC 1.14.14.1) (Q4KCD5)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- Polyketide synthase RzxC
- Polyketide synthase RzxE
- Polyketide synthase RzxD
- Polyketide synthase RzxF
- Polyketide synthase/nonribosomal peptide synthetase hybrid RzxA
- AMP-binding enzyme
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Polyketide synthase PltB
- Non-ribosomal peptide synthetase OfaC
- Non-ribosomal peptide synthetase PvdJ
Sequence:
MSQIEDTTVPAQSTADAAQPQLKAARPLAANIKIKDGFPVMPGKIPLLGHVHKIGKDALGELRQAEAACGPMFWTYFGSQLPVLQIVDEAGLAILQNKYTDNSFLREQMPVITGEAMNAFDGPRHRNARKASTDAFTPKGLTRAKVGQFIMETIDQRLKHWSRENQLAIFPQTKDIALEVVFRILGIATHELELWRHQYEEFFLGMIPLKINLPGFPAWRCRKARGWLEQRVAQIVATTRANNDHDSLVGAMILGRDEQGNGLSEVELVHNILGLGFAGSETTAAVMAWSALMLSQHPDVWQQLCEQVAGLESLPVTHEELVRQVPLAEGIFRETMRLYPPAPFEMRKVHTEFELLGQRIPAGVMAGVSLLHVSRNPERYPDPDSWRPERWLGLDRALNQVETCQFGGGPHACLGRHVAALEITLFIAMLARELGPKGNVPRLVGKMPPPAYLPFLRPSNKAFLDFSGA