wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication licensing factor mcm7-A (EC 3.6.4.12) (CDC47 homolog A) (CDC47p) (Minichromosome maintenance protein 7-A) (xMCM7-A) (p90) (Q91876)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development.
Subcellular location: Nucleus {ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
Interaction partners:
Sequence:
MPRDYQTEKEKCKTFLQEFYKDDEIGKKHFKYGVQLANIAHREQVALYIDLDDLAEEDPELVDAICENTRRYTNLFADAVQELLPQYKEREVVHKDALDVYIEHRLMMEQRGRDPNEMRDSQNQYPPELMRRFELYFKAPSSSKARVVRDVKADSIGKLVNIRGIVTRVTEVKPMMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSRECQTNRSGGRLYLQTRGSKFIKFQELKIQEHSDQVPVGNIPRCMSVYVRGENTRLAQPGDHVGITGVFLPMLRTGFRQVVQGLLSETYLECHRLVKMNKSEDDELGTEELSEEELRQITEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDNSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVMKDPVTGEMTLEGGALVLADQGVCCIDEFDKMMDTDRTAIHEVMEQQTISIAKAGIMTTLNARCSILAAANPAYGRYNPKKTVEQNIQLPAALLSRFDVLWLIQDKPDRDNDLRLAQHITYVHQHSKQPPSQFQPLDMKLMRRYITMCKRKQPAIPEALADYLTAAYVEMRKEARTNKDMTFTSARTLLSVLRLSTALARLRLEDVVEKEDVNEAMRLMEMSKDSLLGDKGHTSRTQRPADVIFSTIREMVPEKGARSVKYSEAEQRCVSKGFTPAQFEAALEEYEELNVWLVNQARTKITFV
Protein: SRP19 protein (Q388I9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Signal recognition particle subunit SRP68
- Signal recognition particle 54 kDa protein
- Signal recognition particle subunit SRP72
- Signal recognition particle receptor alpha subunit, putative
- Signal recognition particle receptor subunit beta
- 60S ribosomal protein L19, putative
- Large ribosomal subunit protein eL18
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L18a
Sequence:
MKPSQPSYDKRAYQTIYPQYLDAELTPHDGRRLTRTQAVDDPTTNEVVEALKELGYTDIFVEPSASFPRSQGSIKYIMPPKGCVKVAIKRPKGEHYIPKSDFDTQTRGVTVEDIPNKMELLRRVSALIKIQHALKKQAEAAAASQTANTRKK
Protein: Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Selectin ligand synthase) (Q712G6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Interaction partners:
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Alpha-
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- P-selectin
- E-selectin
- Hdc homolog, cell cycle regulator
Sequence:
MVQGCLCWRGCCDLKTSFPWVTNSRRLWMNCIGCNPVWRLRAWGCLAGGTTLMVIWLFWLLRSVPGGAPAPQPTLTILIWHWPFTNRSPELSSDTCTRYGMASCHLSANRSLLASADAVVFHHRELQTRHSRLPLDQRPHGQPWVWATMESPSNTHGLRHFRGIFNWVLSYRRDSDIFVPYGRLEPFSGPTPPLPAKSRMAAWVVSNFQERQQRAKLYRQLAPHLKVDVFGRASGRPLCPNCLLPTVARYRFYLSFENSQHRDYITEKFWRNALAAGAVPVVLGPPRTTYEAFVPPDAFIHVDDFSSARELAVFLVSMNESRYRGFFAWRDRLRVRLLNDWRERFCTICARYPYLPRSQVYEDLESWFQA
Protein: 3',5'-cyclic-AMP phosphodiesterase (EC 3.1.4.53) (G3UZ46)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNKAAAIVLSGDMKKGTCSQKRGTQLKKNQRGSIRVASFDVENGPSPGRSPLDPQAGSSSGLVLHAAFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVRNNFTLLTNLHGAPNKRSPAASQAPVSRVSLQVERNDV
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (Immunoglobulin heavy chain-binding protein homolog) (Q2ULV1)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Protein disulfide-isomerase
- Uncharacterized protein
- Hsp70 nucleotide exchange factor fes1
- non-specific serine/threonine protein kinase
- Endoplasmic reticulum chaperone BIP
- Calnexin
- Molecular chaperone
- Derlin
- Protein kinase domain-containing protein
- WW domain-containing protein
Sequence:
MARLSSRNGAAKPFTAWTTIFYLLLVFIAPLAFFGTAHAEEDSVQDNYGTVIGIDLGTTYSCVGVMQNGKVEILVNDQGNRITPSYVAFTDEERLVGDAAKNQYAANPVRTIFDIKRLIGRKYDDKDVTKDTKNFPFKVVNKDGKPVVKVDVNKTPKTFTPEEVSAMVLGKMKEIAEGYLGKSVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRVVNEPTAAAIAYGLDKTGDERQVIVYDLGGGTFDVSLLSIDNGVFEVLATAGDTHLGGEDFDHRVMDYFVKQYNKKNNVDITKDLKSMGKLKREVEKAKRTLSSQMSTRIEIESFHNGEDFSETLTRAKFEELNMDLFKKTLKPVEQVLKDAKVKKSEVDDIVLVGGSTRIPKVQALLEEFFGGKKASKGINPDEAVAFGAAVQGGVLSGEAGTEDVVLMDVNPLTLGIETTGGVMTKLIPRNTVIPTRKSQIFSTAADNQPTVLIQVYEGERSLTKDNNLLGKFELTSIPPAPRGVPQIEVSFDLDANGILKVSASDKGTGKAESITITNDKGRLSQEEIDRMVAEAEEFAEEDKAIKSKIEARNSLENYAFSLKNQVNDENGLGGQIDEDDKQTILDAVKEVTDWLEDNAAEATTEDFEEQKEQLSNVAYPITSKLYGSAPADEDDEPSGHDEL
Protein: BBSome complex member BBS5 (Q9I7P3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004309}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000256|ARBA:ARBA00004607}.
Interaction partners:
- Bardet-Biedl syndrome 1
- Bardet-Biedl syndrome 9
- BBSome complex member BBS4 homolog
- Bardet-Biedl syndrome 8
- BBSome interacting protein 1
- Outer segment 5
- Intraflagellar transport 20
- No mechanoreceptor potential B, isoform D
- Intraflagellar transport 52
- Putative inner dynein arm light chain, axonemal
Sequence:
MLKSLAPIEGNQQPVLQLLWEDKEVKFDVPQLHKNLRSGERVLDYIYHIEDSKGNPGDTGRLMVTNLRIIWHSLVHKKYNLSIGYARIGNTNTRVVHMHSKARIASQALYILAVSNETRFEFLFTDVSGETSRRDQPIFASVFDVYHLYQRTYLYRDLKLRGAIVQAGQLVILPDEEVFSHVQGVWNLSSDQGNLGSFVVTNIRLVWFADANETFNISLPYLQIESLRVRESKYGPALVIQTAETGGGYVLGFRVDPAERLNELFKELSSLHTVYGEHPNFGIQYNANDARRRLEAASEEAAQASQIKVDNFEELDERQEREINTKLNSYLAEGCLGKVPSQGERAPVYCKELGFAMEPIGDGYKLQDLWNVMPTKMETME
Protein: Signal peptide, CUB and EGF-like domain-containing protein 2 (Protein You) (Q5G872)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Lipid-binding protein required for SHH long-range signaling by binding to the dually lipid-modified SHH (ShhNp) and by promoting ShhNp mobilization, solubilization and release from the cell membrane. Acts by enhancing the proteolytic processing (shedding) of the lipid-modified N- and C- terminal of ShhNp at the cell surface. Synergizes with DISP1 to cause an increase in SHH secretion. Probable cell surface coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9NQ36}. Cell surface {ECO:0000250|UniProtKB:Q9NQ36}. Note=Secreted and tethered at the cell surface. {ECO:0000250|UniProtKB:Q9NQ36}.
Interaction partners:
- Sonic hedgehog protein
- Hedgehog acyltransferase
- Indian hedgehog B protein
- Tiggy-winkle hedgehog protein
Sequence:
MGAVWTVRLLCLFLLLLNTRQSAALPHNTDQCAEGSDACHIDAICQNTPTSYKCTCKTGFKGDGKHCEDIDECDVEYNGGCVHECNNIPGNYRCTCLDGFHLAHDGHNCLDVDECVFNNGGCQHVCVNTMGSYECRCKQGFFLSDNQHTCIHRSVEGLSCMNKEHGCGHICKESPKGGVACECRPGFELAKNQRGCILTCNHGNGGCQHICEDTEQGPICRCHVRYMLHADGRTCVERDEMAPTAPDHNATSLAEVDKRVKRRLLMETCAVNNGGCDSTCKDTSTGVRCSCPVGFTLQPDGKSCKDIDECELHNGGCDHYCRNTIGSFECSCRKGFKLLTDERSCQDIDECFFERTCDHTCVNSPGSFQCVCNKGYTLYGLAHCGDINECSFNNGGCEHTCENTMGSFGCHCRAGYKLHWNKKDCIEAEDSPLVPPPARPTLNCNKQGGGELCYLTCQSQVHISSGAEDSYTVTCGMPLPCHTGGQWNGSYCPGSGIKTIATFKSGQGKCNLKRSHENLAHSFKTALSDKRATENVQFSFVSLHCASSSRQQRSRHGRKAGEEEGSFITAQFELDVNLEEVTAEGCDLTCVRRRSEKRLRKTIRTLRKSINREQFHLHFAGSEYELAKKLVRPADTPDHCGTGQILLDKKCVKCSVGTYYDGEQGRCFLCPPGTYQDEEGQVSCDVCPGPEGRGIPETAGARNISECAGQCRPGQFSHDGFVPCLPCPQGTYQPEVGRTSCFTCGGSLTTKYDGSVSFQNCETKVQCSPGHYYNTSTHRCIRCPVGTYQMEFGQNYCIACPGNTTTDFDGSTNIMQCKNRHCGGELGEFTGYIESPNYPGNYPANIECTWTITPPPKRRILVVVPEIYLPIEDECGDYLVMRKSSLPNSVTTYETCQTYERPIAFTSRSKKLWIQFRSNEGNSGKGFQVPYVTYDEDYQELIEDIVRDGRLYASENHQEILKDKKLMRALFDVLAHPQNFFNYTAQESREMFPKSFIRFLRSKVLRFLRP
Protein: SD10041p (Q86PE7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSFLRGSVSYVWCTTSVLGKGATGSVFQGVNKITGESVAVKTFNPYSHMRPADVQMREFEALKKVNHENIVKLLAIEEDQEGRGKVIVMELCTGGSLFNILDDPENSYGLPEHEFLLVLEHLCAGMKHLRDNKLVHRDLKPGNIMKFISEDGQTIYKLTDFGAARELEDNQPFASLYGTEEYLHPDLYERAVLRKSIQRSFTANVDLWSIGVTLYHVATGNLPFRPFGGRKNRETMHQITTKKASGVISGTQLSENGPIEWSTTLPPHAHLSQGLKTLVTPLLAGLLEENREKTWSFDRFFHEVTLILRKRVIHVFFTNRTSSVEVFLEPDEQIDNFRERIFLQTEVPLEKQILLFNNEHLEKKVTPRTIAKAFPATTTEQPIFLYSNDDNNVQLPQQLDLPKFPVFPPNVSVENDASLAKSACSVGHECKRRVDIFTSMDILIKKGVEHFIEMLVTTITLLLKKTESFDNLLSTVIDYADVVHSMARVTKGDQEIKTLLTALENVKSDFDGAADVISQMHKHFVIDDELNDQWTSSMHGKKCPCKTRASAQAKYLVERLRDSWQHLLRDRATRTLTYNDEQFHALEKIKVDHNGKRIKALLLDNVNPTVAQIAECLADWYKLAQTVYLKTQILEKDVRDCERKLNGIRDELYHVKSELKLDVDTKTINNNNQLAKIEERNRLRVMQQQQQEVMAVMRTNSDIISLLSKLGITNGSLESS
Protein: LD17329p (Q86NY1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKPQNNDTLELDDILSQPVKDKERFAAFMMRKLAENKPAQNDNLFGNFKLDFDLDFEVPLIKKSQAKPKSKLPEVQPLGELVSKNSAATEKVNEPPVDQAPNENVPPRRSPTLSPNNRRSMRRSGNVPGSDKLRRHAIRRRSRSCGRQLLPEFEETVNLTRSISSPVNFLPEISSTPCTEKQKEEVAKNTTRVETDKPAEKPMELSQEPEPENPLQTKVTSPARNPILAAEIEQICKERQSSFHKNVLQLDYSGRAPYSRPPTPSSPSVAGLRRTYTMEKGPAPGQLLLSPSHRYDTPSKMPVVKAKRFNQELMVPDTPERQSHDPAWQSEPQPEFVVPETQPQDLGELVQTLSRSAISPIVVINTSNSNRSVRRDAVAMKSVPTSPVTALSSPPIAPSPRRSAAASPQKSIAQLPRVEENMDAIMTDDESDEHPSTVPLNLAPSGGNTTRQRRLRSSNRARATIESQESSMRLLNLHKSVNAKKSKPRKTAIPLNKAPSAPINGEQFARELTRMSNYEILDLRKRNSLNEIYPLNGHRNHRSEKLILEEEIQRELLRRNLMDEAEGLPKQQSSDDSNEDYIPVPPKTQSLRTKSNDRSQGRGRPRSTRRDLPMTTELVNYLGLSQTLETRRKSSKDGKRCLYTKGSSDHEDNDSLSPVKLPRLSKSIQIVPPPPVSLRYSQSLQNLPCSGKFDFDNVVMAAPPDFHDSVNSDAIEIAPPPPEYVVNTRGRSTSGRKSNKNDLVLPPPGYEGGQEEEHDERPSQPRCTAKELQQSTQNGRRAMENELVPPPIEYVEEENRNNEQSRRSTKNGNLVDRNTHNAVEYCEPPEPPEYDDSDHGQASILRRSGKKLQHSKQSVQKSNKEQIIAPSYENNEDYDSDEEPIYNEEYGKEESQNKNVTRRKSDKDEMASHTLECIEGPDPNWNSSCNKQNRNHQNASKKKKK
Protein: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 5) (NADH-plastoquinone oxidoreductase subunit 5) (P0C328)
Organism: Oryza sativa subsp. japonica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase iron-sulfur protein 2
Sequence:
MEHTYQYAWVIPLLPLPVIMSMGFGLFLVPTATKNLRRIWAFPSVLLLSIAMVFSVHLSIQQINGSSIYQYLWSWTVNNDFSLEFGYLIDPLTSIMLILITTVGILVLIYSDDYMSHDEGYLRFFVYISFFNTSMLGLVTSSNLIQIYFFWELVGMCSYLLIGFWFTRPIAASACQKAFVTNRVGDFGLLLGILGFFWITGSLEFRDLFKIANNWIPNNEINSLLTILCAFLLFLGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLIARLLPLFISLPLIMSFISLIGTLTLFLGATLALAQRDIKRSLAYSTMSQLGYMMLALGIGSYQAALFHLITHAYSKALLFLGSGSVIHSMEPLVGYSPDKSQNMVLMGGLRKYIPITRTCFLWGTLSLCGIPPLACFWSKDEILSNSWLYSPFFGIIASFTAGLTAFYMFRIYLLTFDGYLRVHFQNYSSTKEDSLYSISLWGKRISKGVNRDFVLSTAKSGVSFFSQNLSKIHVNTGNRIGSFSTSLGTKNTFVYPHEPGNTMLFPLLILLLCTLFIGSIGIHFDNEIGELTILSKWLTPSINFFQESSNSSINSYEFITNAISSVSLAIFGLFIAYMFYGSAYSFFQNLDLINSFVKGGPKKYFFHQLKKKIYSWSYNRGYIDIFYTRTFTLGIRGLTELTQFFDKGVIDGITNGVGLASFCIGEEIKYVGGGRISSYLFFFLCYVSVFLFFFLS
Protein: Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE (P08293)
Organism: Azotobacter vinelandii
Function: This protein may play a role in the biosynthesis of the prosthetic group of nitrogenase (FeMo cofactor).
Interaction partners:
Sequence:
MKAKDIAELLDEPACSHNKKEKSGCAKPKPGATDGRCSFDGAQIALLPVADVAHIVHGPIACAGSSWDNRGTRSSGPDLYRIGMTTDLTENDVIMGRAEKRLFHAIRQAVESYLPPAVFVYNTCVPALIGDDVDAVCKAAAERFGTPVIPVDSAGFYGTKNLGNRIAGEAMLKYVIGTREPDPLPVGSERPGIRVHDVNLIGEYNIAGEFWHVLPLLDELGLRVLCTLAGDARYREVQTMHRAEVNMMVCSKAMLNVARKLQETYGTPWFEGSFYGITDTSQALRDFARLLDDPDLTARTEALIAREEAKVRAALEPWRARLEGKRVLLYTGGVKSWSVVSPLQDLGMKVVATGTKKSTEEDKARIRELMGDDVKMLDEGNARVLLKTVDEYQADILIAGGRNMYTALKGRVPFLDINQEREFGYGGYDRMLELVRHVCITLECPVWEAVRRPAPWDIPASQDARPSGGPFGER
Protein: Surfactant protein C (SP-C) (Pulmonary surfactant-associated protein C) (Pulmonary surfactant-associated proteolipid SPL(Val)) (P11685)
Organism: Rattus norvegicus (Rat)
Function: Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces.
Subcellular location: Secreted, extracellular space, surface film.
Interaction partners:
- Pulmonary surfactant-associated protein B
- Pulmonary surfactant-associated protein A
- Uteroglobin
- Pulmonary surfactant-associated protein D
- Aquaporin-5
- Advanced glycosylation end product-specific receptor
- Napsin A aspartic peptidase, isoform CRA_a
- Adhesion G protein-coupled receptor F5
- Pro-cathepsin H
- Homeobox protein Nkx-2.1
Sequence:
MDMGSKEVLMESPPDYSTGPRSQFRIPCCPVHLKRLLIVVVVVVLVVVVIVGALLMGLHMSQKHTEMVLEMSIGGAPETQKRLALSEHTDTIATFSIGSTGIVLYDYQRLLTAYKPAPGTYCYIMKMAPESIPSLEALARKFKNFQAKSSTPTSKLGQEEGHSAGSDSDSSGRDLAFLGLAVSTLCGELPLYYI
Protein: Amine oxidase (EC 1.4.3.-) (Q9JJK6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSFRTMAKKSGILVWGILLCVSSCLALYENLVKCFQDPDYEAFLLIAQNGLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPMRIPESHKLIHTYVQKLGLKLNKFNQYDSNTWYLLNGQRYRASEVMANPGILGYPLRPSEKNKTVTDLFYQAITKIKPHRKTSNCSQLLSLYDSYSTKAYLMKEGTLSKRAHRDDRGYNDENAGYYKSLLGVSEDCKHLLQKCPIFRDHRWLCPIPNGLSASLKPGTIRLWSKVERVVRDGPKVKVMYRTDGPTSALHKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQDGIRGGYSITDRPSRFIYYPSHSLPGGKGVLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKRMCPKSAIKHWSLDPLTIGAFTEFTPYQFVDYSKQLSQPEGRIYFAGEHTCLPHSWIDTAIKSGIRASCNIQAAVDKEATRGHTAL
Protein: Uncharacterized amino-acid permease PB2B2.01 (Q9HDV2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNAYVRDSESVYSESYPPENFISNEPEKSKDKDNFNGEEVISYVGEVETVPAKEENVFRRFINGFKIEKNQQDSAGQGLKRRLKSRHIQMIGIGGAIGTGVWVGSSKSLYRGGAASVLIDYCIVGTMVFCTVYALGELAVAFPTRGSFVTHATRFIDESWGFALSWNYVFSFIVTIPLELTTGTMMIKYWTNLNSGIWVTVFIVFLFFINIFGVKGYGEMEFIMSTIKVVAMCGFIILGIIIDCGGVPTDHRGYMGTHIFRENAFRHKFKGFCAVFTSAAFSFSGTEYVGVAAAETENPAKAFPVAVRQTLFRIAIFYILSLFIVSLLISGADPRLTSYHGVDASPFVLAIKDANIKALPSILNAIILISVISSANAQLYAGSRAIHSLGCNGFAPKCFTLVDREGRPLVALLILFLFMFLGYLVETGQYDTVFDWMLSISGLGTLFCWGSICLAHIRYRAAMKHQNRSLKEVGFVSPFNVYASYYAFILVCLVLAAEFYVSIFPVGGKPDASAFFENYLSAPVILVFFICHKLYYKTKRITLSNMDLETDFAYKTPVEEEEEEEKSAGSLSIKQRMKKLSDMMC
Protein: FAD-binding monooxygenase stcW (EC 1.14.13.-) (Sterigmatocystin biosynthesis cluster protein W) (Q00730)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
- Versicolorin B desaturase stcL
- Norsolorinic acid synthase stcA
- Oxidoreductase stcQ
- Versiconal hemiacetal acetate esterase stcI
Sequence:
MTVHYVHEGPEPQESRYSIPQHTTWMDPNNRRLRVITIGAGFSGILMAYQIQKQCANIEHVVYEKNHDIGGTWLTNRYPNAGCDVPSHAYTYRFALYPDWPRYFSYASDIWEYLDKVCAAFKLRQYMQFRTEVIKACWNEEEGQWKVRLRRQRPGQEPEEFDDHCHILLNACGVLSNPKWPDTPGLHDRFKGRVIHTAAWPDDYGEVQWNSDRVAVIGSGASSIQAVAGIQPHVGHLDIFVRTGVWFGVLAGNTGAPTKIYSEAERAQFRSNPSALVEHTKSIEAEVNGMWGAFYRDSMAQKGASAFFRQRMASIIKDDRLAKGFTPTFGFGCRRITPGDPYMHAIQQANVDVHFTAVASCTEDGIVGADGIERLVDTIVCASGFDNTYRPQFPIIGRRGVDLRDKWKTNPEAYLGLAVPDMPNYITFIGPSWPIQNGSVMAPLHSVSEYAIQFLKKMQNENIRAWAPRQQITDRFNEHVQEWVKHTVWSDQCRSWYKNNETGRVNAIWPGSSLHYQAVIERPRYEDFEISYADANPWAHLGMGWTMLDRAGGKQADVSPHLCLENIDPVWFKSIGGDVDILRKQLEKGHTLPNNASHAEA
Protein: Protocadherin gamma B6 (Q8K499)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
VAVGTRIPLEPATDPDINLNSVKDYQISSNPYFSLMVRINPDGGKTPELSLEKLLDREEQRSHRLILTALDGGDPPRSATTQIEISVKDINDNPPVFSREEYRVSVSENLSPGSSVLQVTATDEDEGVNAEIRYYFRSTAQSTRHVFSL
Protein: Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase) (P54137)
Organism: Caenorhabditis elegans
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183}.
Interaction partners:
- exodeoxyribonuclease III
- Apurinic-apyrimidinic endonuclease
- Uracil-DNA glycosylase
- XPA C-terminal domain-containing protein
- Alcohol dehydrogenase class-3
- Flap endonuclease 1
- dUTP diphosphatase
- DNA polymerase theta
- Probable tyrosyl-DNA phosphodiesterase
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MHSFSMKRVVASSSVAAVATCDVEGTVVAWRRDVELIRKMRKDMIAPVDTMGCHKLADPLAAPPVHRFQVLVALMLSSQTRDEVNAAAMKRLKDHGLSIGKILEFKVPDLETILCPVGFYKRKAVYLQKTAKILKDDFSGDIPDSLDGLCALPGVGPKMANLVMQIAWGECVGIAVDTHVHRISNRLGWIKTSTPEKTQKALEILLPKSEWQPINHLLVGFGQMQCQPVRPKCGTCLCRFTCPSSTAKNVKSETEETSTSIEVKQEVEDEFEDEKPAKKIKKTRKTRTKIEVKTESET
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (Q57ZY1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- poly
- Flap endonuclease 1
- DNA-repair protein, putative
- KU80 protein
Sequence:
MAAKGKSTQRRSATGGANSKGASAKISPVKKSTARKGQQKTTKKTPVVTKPVPTKTTAAAGVKKKVDAAVTTQAPVTGGKRERFLRKGRGVVDVHSGKVDTCHVYERDGTVFQFTLNQTNISSNNNKFYITQLLEDDARKNYFIFARWGRVGAVGQYMLEPYLDARSAEQDFCSKFREKTRNDWVDRGRFKKVPGKYEYMEVDYGEDDDDDAGGEKPGKKKKAEKPVRESKLPKEVQDLMRLIGCRESMSQVLRELEVDTERMPLGKISKAQILRAYEVLKEIEKKLKRPLKQLEELSSRFYTLIPHAFGTRRPPVINTVDVVRQKREMLETLAELEVASTLVDMKDDEALHPLDNIYRKMKCAIQPLKPQSEVYKRIVQYVRNTQGPTHDAYTLQVVEVFTLRREDEEERYKPFKKMDNRQMLWHGSRITNFLGILSQGLRIAPPEAPCTGYMFGKGIYLSDVCSKSANYCHPPRDTNTGLLLLCEVALGKQKEYENAHYMLEPEKGTNSTKGVGRMYPDPKGAEVVKGVLWPKGCIKEDSRSTSLIYPEHIIYDVRQCVLRYLVRVSFEYK
Protein: Zinc finger/BTB domain protein (Q8L9M8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Outer envelope pore protein 21B, chloroplastic
- Rhodanese-like domain-containing protein 11, chloroplastic
- 6,7-dimethyl-8-ribityllumazine synthase
- YlmG homolog protein 2, chloroplastic
- Inner membrane localized protein
- Alpha/beta-Hydrolases superfamily protein
- Uncharacterized protein At5g03900
- Low-density receptor-like protein
- Protein CHLOROPLAST J-LIKE DOMAIN 1
- Ribosomal RNA small subunit methyltransferase J
Sequence:
MAKKKELLSKAPWRGDDEDDSDKFSNAKLKVTKDSDGMSKMHVPSRGTKKGSLADDDDDSLEIDPQLRYSFNRNYQFLQSVFTIDTLVKPLPPSMAFNVSRNLSFFTRIFTQFFDPEGIANAQKSLGLGQEEKARRVR