wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-related protein 3 (Actin-like protein 3) (P61158)
Organism: Homo sapiens (Human)
Function: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Plays a role in ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109554}. Cell projection {ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:16767080, ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29925947}. Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (PubMed:19109554).
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 4
- Actin nucleation-promoting factor WASL
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 5-like protein
- Actin nucleation-promoting factor WAS
Sequence:
MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Protein: Uncharacterized protein (Q583U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMELLQLPTTCECLLPLDAAVMAAYGPSAIYFFPLSQLFNAVTATATVTAPKGFHSVELSSHWGCCAPWHPPGASLERCGVFYEQSGLVRFRSCSFGDMPQQKRVDGKTKKGKKGEESVFDPAVKGLDGIEEMAVFFGTTLVVRTGAEALFFALDPASNPGEEKLPLIGRTALPQGKSISTTTPSNDVSADNLWYFMGASHPTSIVDEGDRYICVASFDRKERKLEAVLLAVSDTRAVQLKRTKVGGLKVSPDAGKFFCCAFNWSLRQLIVVFKGKKGKTSGTTLALSLESMSLTAENITVPPKAMDLTYTTAGEAWALTTANEDGALIIKNLMAADAGREVRLPSLKGRQASGNGNHDDQKKKKKEEEEEGEGEGEDVHTCLTAVGSTVCVLYGKAVAMVCTDDSANKGGAKSSKDSVTFSGHTQTGGEESLYAWLLKQQQRKVDESEEEEHQQELREVINFLQGTVKGPPTLIVRDCRYVSQKNGVYNHDVLDSIQANSKMKVYYKQLLRYIAIAQSLHPVTILLALHVENPSVRLSVAALLAVKPALAAGGLRLLEWGGPTRSHFNKSGDGNYKSNARREAKLFGAALLNSALDALSAGALGAVEVLCAVADITLMAALTPNSSCTVAGKSDSFRQAANHNRQDGNAVTREEVEAELTIVDCIAVLTSYARWALVTAAPSLGTITAHLAPPRTDESRRKEAMIRDRVAHAITTSRDIQIDVFPLRCR
Protein: Mitochondrial import inner membrane translocase subunit TIM16 (Mitochondria-associated granulocyte macrophage CSF-signaling molecule) (Presequence translocated-associated motor subunit PAM16) (Q9Y3D7)
Organism: Homo sapiens (Human)
Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}; Peripheral membrane protein {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}; Matrix side {ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit Tim17-A
- Stress-70 protein, mitochondrial
- DnaJ homolog subfamily C member 15
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit Tim17-B
- Mitochondrial import inner membrane translocase subunit Tim21
- GrpE protein homolog 1, mitochondrial
Sequence:
MAKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSKLSPEEVQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT
Protein: Bifunctional protein FolD 2 (Tetrahydrofolate dehydrogenase/cyclohydrolase 2) [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] (Q9LHH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Interaction partners:
- Formate--tetrahydrofolate ligase
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- 5-formyltetrahydrofolate cyclo-ligase-like protein COG0212
- 5-formyltetrahydrofolate cyclo-ligase, mitochondrial
- Formyltetrahydrofolate deformylase 1, mitochondrial
- Glycine cleavage system H protein 2
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Serine hydroxymethyltransferase 1, mitochondrial
- Formyltetrahydrofolate deformylase 2, mitochondrial
Sequence:
MASSSDHTAKIIDGKAIAHTIRSEIAEEVRGLSEKHGKVPGLAVVIVGSRKDSQTYVNTKRKACAEVGIKSFDVGLPEEVSEADLISKVHELNSNPDVHGILVQLPLPKHINEEHILGAISIDKDVDGFHPLNIGKLAMKGREPLFLPCTPKGCLELLARSGVKIKGQRAVVVGRSNIVGLPVSLLLLKADATVTTVHSHTKDPEAIIREADIVIAACGQAHMIKGNWIKPGAAVIDVGTNAVSDPSKKSGYRLVGDVDFAEASKVAGFITPVPGGVGPMTVAMLLRNTVDGAKRVFGE
Protein: 4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) (EC 2.6.1.22) ((S)-3-amino-2-methylpropionate transaminase) (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT) (H3BNQ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKALPACDFEKPRSSPTSCLFQVWCWVAVVTNPFVSVPRWSSGITTLTCSSIFSVTS
Protein: Probable inositol 3-phosphate synthase isozyme 3 (AtIPS3) (MIP synthase 3) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase 3) (AtMIPS 3) (MI-1-P synthase 3) (Q9LX12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18603618, ECO:0000269|PubMed:20215587}.
Interaction partners:
- Inositol-phosphate phosphatase
- Phosphatase IMPL1, chloroplastic
- Bifunctional phosphatase IMPL2, chloroplastic
- Inositol 3-kinase
- Inositol-3-phosphate synthase isozyme 2
- Inositol-3-phosphate synthase isozyme 1
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
Sequence:
MFIESFKVESPNVKYTENEIHSVYDYQTTELVHENKNGAFQWTVKPKTVKYEFKTDTHVPKLGVMLVGWGGNNGSTLTAGVIANREGISWATKEKVQQANYFGSLTQASSIRVGSFNGEEIYAPFKSLLPMVNPEEIVFGGWDISDMNLADAMARAKVLDIDLQKQMRPFMEHMVPLPGIFDPDFIAANQGSRANHVIKGTKKQQLEQVIKDIREFKEKNKVDKVVVLWTANTERYSNVVVGLNDTTENLMSSLDKDEAEISPSTLYAIACVLENVPFINGSPQNTFVPGLIELAIKRNCLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVGSNGILYEPGEHPDHVVVIKYVPCVGDSKRAMDEYTSEIFMGGKNTIVMHNTCEDSLLAAPIILDLVLLAELTTRIQFMSENEGKFHSFHPVATLLSYLSKAPLVPPGTPVVNALSKQRAMLENVLRACVGLAPENNMILEYK
Protein: Translocating chain-associated membrane protein 1-like 1 (Q8N609)
Organism: Homo sapiens (Human)
Function: Stimulatory or required for the translocation of secretory proteins across the ER membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Translocating chain-associated membrane protein 1
Sequence:
MGLRKKSTKNPPVLSQEFILQNHADIVSCVGMFFLLGLVFEGTAEASIVFLTLQHSVAVPAAEEQATGSKSLYYYGVKDLATVFFYMLVAIIIHATIQEYVLDKINKRMQFTKAKQNKFNESGQFSVFYFFSCIWGTFILISENCLSDPTLIWKARPHSMMTFQMKFFYISQLAYWFHAFPELYFQKTKKQDIPRQLVYIGLHLFHITGAYLLYLNHLGLLLLVLHYFVELLSHMCGLFYFSDEKYQKGISLWAIVFILGRLVTLIVSVLTVGFHLAGSQNRNPDALTGNVNVLAAKIAVLSSSCTIQAYVTWNLITLWLQRWVEDSNIQASCMKKKRSRSSKKRTENGVGVETSNRVDCPPKRKEKSS
Protein: Resistin (A0A8I6B465)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MQVGPPGCITPPIFPSAVPAAMKNTVLHCWSVSSRGRLASCPEGTTVTSCSCGSGCGSWDVREDTMCHCQCGSIDWTAARCCTLRVGS
Protein: Nuclear pore complex protein Nup107 (107 kDa nucleoporin) (Nucleoporin Nup107) (p105) (P52590)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. Involved in nephrogenesis.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:P57740}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P57740}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P57740}. Note=Located on both the cytoplasmic and nuclear sides of the NPC core structure. During mitosis, localizes to the kinetochores. Dissociates from the dissasembled NPC structure late during prophase of mitosis. {ECO:0000250|UniProtKB:P57740}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup133
- Nucleoporin Nup37
- Nucleoporin 205
- Nuclear pore complex protein Nup85
- Nucleoporin 160
- LOC683983 protein
- Nuclear pore complex protein Nup93
- AT hook containing transcription factor 1
- Nuclear pore complex protein Nup155
Sequence:
MDRSGFGGMSSPVIRDPEVTRTARKHSAHKRVLIQANQDENFGTTTPRSQIIPRTPSSFRQPFTPPSRSLLRHPDISYIFGTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGFYTNTEHHSMTEDINLSTVMLREDDPGEAASMSMFSDFLQSFLKHSSTTVFDLVEEYENICASQVNILSKIVSRATRWDWQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENMFAIAGINASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGDFSDNIEFYAKSVYWENTLHSLKQRQLLSYIGSTRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLHHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTLDETEELPREYMEANWTLEKVFEELQATDKKRVLEENQEHYHVVQKFLILGDIDGLMDEFSKWLSKSRSSLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLINEKHTNLIAFYTCHLPQDLAVAQYALFLEGVTECEQRHQCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPSLDTATTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDSIAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNERFKHMNSAPQKPTLLSQATFTEKVAHEHKEKKYEMDHNIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEEDPERAHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS
Protein: Down syndrome cell adhesion molecule (Down syndrome cell adhesion molecule a precursor) (Q53CM6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MWILAIIFFQCILNVLSEDLHSSLYFVNASLQEVVFASTTGTLVPCPAAAVPPATLRWYLATGEESYNVPGIRHVHPNGTLQIFHFPPSSFSKVIHDNTYYCTAENPSGKIRSQDVHIKAVLREPYTVRVADQTAMRGSVAVFKCIIPSSVENYITVVSWERDTVPLVSGARFLITSTGALYILDVQKEDELFNYRCMTRHRYTSETRQSNSARLFVPDPSNSAPAILDGFEKREVMASHRVELPCKASGHPAPKYRWLKNNRPLESDSRFRQSVTGLLIERAQPSDTGSYVCEVWNSYGNAEVIGRLTVKEPLKAVVSPRKVKGSVGSQVSLSCSVTGSDEFELSWYRNGDKINTGANIRMNGINKENLVMDGMAKSDGGVYQCFSRKAKMSAQDFVQVILEDGTPKILSAFSEKVVGPNDFVSLTCHVKGTPQPAITWTLDDEVVAKDSRHRIVHSITAEGNVVSYLNISHIQVRDSGVYRCTCNNSAGTVSYQARINVRGSADIRPMKNLTAIAGWDMYIHCHVIGYPYYSIKWFKNSNLLPFNDRQRAFENNGTLKLLNVQKELDEGEYSCHVQVQPQLFKNQSVHVTVKVPPFIQPFEFPRYSIGHRVFVPCVVRSGDLPISITWEKDGKSINASLGVTIDNIDFTSSLRISNLQRVHNGTYTCIAQNDAAVVKYQSQLIVRVPPRFKVQPQDQDGIYGKSVILNCSADGEPRPTIEWKYSKGAGVPQFQPIALNSGFRVQLLGNGSLLIKHVLEEDAGYYLCKVSNDVGADVSKSMYLNVKIPAMITSYPNNSLATKGEKIEMSCKAHGEKPIMVRWEKEVEKEKQSHMINPDMWRHTVTVKNVGDEVVSTLQIYPTMREDSGFFSCHAINSYGEDRGILQLTVQEPPEPPKVEIREVKERTIALRWTMGFDGNSLITGYDIECKNKTETWERARRTRDVSPTLNQATIIELHPSSTYNIRMFAKNHIGDSEPSNELTVTTDEADPEGPPQDVTLEAITSQSIKVTWKAPLKHLQNGVIRGYQVCHREHSTNGSHQFVCISVEATGETESLSLNNLKKFAEYEVVVQASNSAGPGPASSEVRATTMEDVPSRAPEKVVATAASPESISLSWQTPAREALNGVLQGFRIIYWANLPDGELGEIRNVTTHKAPLELEGLEKYTNYSIQVLAFTRAGDGVRSDQIYIRTKEDVPGPPGGVKAAAASSSVVYVSWLPPLKLNGVIRKYTVFCSSTSPTVVSEFEVAPDEFLHRVHNLSRNRKYNIWVMAVTAAGRGNSSDVITVEPLAKAPAKILTFSGTVTTPWMRDVVLPCRAVGDPPPAIKWLKESGSPAPAVIDGRRSIHGNGSFIIKTVKAEDSGYYTCVASNNYGTDEIILNLQVQVPPDQPRLTVTKTTTTSITVTWTPGDNGGSSIRGYILQYSEDNSEKWGSISISPSERSYRLENLNCGTWYKFTLTAQNAVGPGRISEIIEAKTHGKEPQFSKEQELFTSINGTSVKLNLIGWNDGGCPITSFTLEYRPLESPVWTKAKRTSLSKSYNLLDLQEATWYELQMKVYNSAGLAEKRVKFATLSYDGSTIPPLVKTLVKDPVKKTSNEGMKMMVTISCILVGMVLLFVLLMVLRRRRREQRLKRLRDAKSLAEMLMSKNTRPSDTMNKQQQTLRMHIDIPRAQLLIEERDTMETVDDRSTVLLTDNDFGETAKQKSATVTHSVHYQSLSQATGPLVDVSDVRPGTSKSSLSNPTSRRTAKAGPAARNRYASQWTLNRPHPPVSVHTLSTDWRLGTPRVAGSVDKESDSYSVSPSQDTDRARSSMVSTESASSTYEELARAYEHAKMEEQLRHAKFTITECFISDTSSEQMTAGTNDYTDSLTSSTPSESGICRFTASPPKPQDVCRVINMAVPKAHRPGGELVHLPPYLRMDFLLNRGVSGTSREAAMGQACLEPQKTRSLKRPALLEPTPMEVPTSRDVQQWQSGTASTLPQREAGTDLAQAAKISTSQESLLDSRGHLKQTNNPYAKSYTLV
Protein: Meiosis-specific protein SPO13 (Sporulation-specific protein 13) (P23624)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for meiosis I segmentation. Probably acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Meiosis-specific protein SPO11
- Meiosis-specific protein HOP1
- Shugoshin
- Meiosis-specific serine/threonine-protein kinase MEK1
- Monopolin complex subunit MAM1
- Meiotic recombination protein REC8
- Monopolin complex subunit LRS4
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Meiosis induction protein kinase IME2/SME1
- Protein RED1
Sequence:
MAPRKRFRLLELGSPTHSKRKVQKPLQEKTPNLRVSPLAFKIGKEIKNKEIRKTKKTESENIFNSKHVDLRLESPHPGLNFVSDAQQYSKAGDVRYLKNKSSNTLKNERQTIERPSFDNSLRFEDIEQPPKSTSTPVLSQSSQINVEREAPMFPVPYYIAPSPMYNFSPYQNFVGNPTFLTPSHNPNLNYAIPIQRPELLYPNVNVYDSPLFKKTRLPHQTKSLDKEKNYQYLPIYPVSISNNGDFVGQETPRAAPKLSKKRLSNTLDVNCSDYESSGQNATYNDSESSLN
Protein: Homeobox protein cut-like 2 (Homeobox protein Cux-2) (P70298)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in the control of neuronal proliferation and differentiation in the brain. Regulates dendrite development and branching, dendritic spine formation, and synaptogenesis in cortical layers II-III. Binds to DNA in a sequence-specific manner.
Subcellular location: Nucleus.
Interaction partners:
- DNA-binding protein SATB2
- Fez family zinc finger protein 2
- Nuclear receptor ROR-beta
- Transcription intermediary factor 1-alpha
Sequence:
MVAPVLKSFQAEVVALSKRSREAEAAFLSVYKQLIEAPDPVPSFEVARTLDDRLQRPSFDPSGQRLQDVHIAWKRCPEPPSAREQNEGTCPTGHTPANGNHLPGPEDTLVTDTLLQKNEAERQKGLQEVHITLAARLGEAEEKIKVLHSALKATQTELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRLACCSPQGPSGEKVSFALCSGPRLEAALASKDREILRLLKDAQQLRHSLQELEEVSANQIADLERQLAAKSEAIEKLQEKLEAQADYEEIKTELSILRAMKLASSTCSLPQTLAKPDDPLLVAKDVFFPTQKFLLEKPALLASPEEDPSEDDSIKGSLGTEPPYPPQLPPPPGPEDPLSPSPAQPLLGPSLGPDGPRTFSLSPFPSLAPGERLAGDSLLSKHMMGPAAFKGETGNLLAFPPTFYGGAKPPSAPAASVPCPEPTGAPEAVDGAGPEEEQLDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEPFIKMKQFLSDEQNVLALRTIQVRQRGSITPRIRTPETGSDDAIKSILEQAKKEIESQKGGESKNSPASVSIPNGTASSSTSEDAIKNILEQARREMQAQQQALLEMESGPRGRSVPPSPPERPSPATASQNGALTCVKQEDGGGGSGSSSTVQAPLAVLSPAAFVQRIIRKVKSEIGDAGYFDHHWASDRGLLSRPYASVSPSLSSSSSYSGQPNGRAWPRGDEATIAPEDEAAMGEDEAPRVGELKAEAGAPEVGGGRLPYYPAYVPRTLKPTVPPLTPEQYELYMYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLSDQLGQGQGQAPTQQPSASQASPTEPTSSPSPPPSPTEPEKTSQEPLGLSLESSKENQQPEGRASSSLGGKPFSSSQAAGGIQEMVAMSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREPFVRMQLWLSDPHNVEKLRDMKKLEKKAYLKRRYGLIGTGSDSESPAAHSECPSPCLQPQELSLMQAKKPRVVLAPAEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDDPDFDPSGGPNVLTPGHTHREPTPQSPDSETEDQKPPMKSLELQEPEGPLQRAAPDRALVKIKQEEGLEVDGDSQPQDVGDPDRGQDGPKEEHTHPLGNSDLSELAPGPFLSGTPNPDCPSLHNPQEKGTGEQVHSEPLSFKSTSESSCCSLEGPPNSPSVISSPDLTTCVSPAPSSSAPISPSLPGAPPAKVPSTSPTGDTAAALHPSTKVNPNLQRRHEKMANLNSIIYRLERAANREEVLEWEF
Protein: Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI (EC 1.14.11.-) (Fumigatonoid A synthase nvfI) (Novofumigatonin biosynthesis cluster protein I) (A0A2I1BSX0)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Fe(II)/2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Interaction partners:
Sequence:
MVGSRTWCESEMLFVQPDAGTKEELYYRVTPKPGQTQANFNWTPHKVRFHDARPQRDSFDLNTHGFTFVEDAISPQLIERIRADDTAAVEGDYFASVAALVKRVTGADHVVCFSPYTRKENSEKGIFGQPARTVHCDHTPAAAIELTHKLCGEDAVRLLQSRFRAFSVWRPLVEPVLDWPLAVVDGRTIAPDDLHPVHWLRYEKKDTEPPFQLSFSETQKWYYLSRQRSDEVSIVKNYDSEVVPSPRSAHCAFKHPFVPKDAPPRESIDVRCLVFGGR
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 10 (B5MBW9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MPRGSRSAASRPASRPAAPSAHPPAHPPPSAAAPAPAPSGQPGLMAQMATTAAGVAVGSAVGHVMGSALTGAFSGGSSEPSQPAVQQPLALYPQAPTPAAPQPLQMGPCAYEIRQFLDCSTTQSDLSLCEGFSEALKQCKYYHGLSSLP
Protein: 2mit, isoform A (2mit, isoform C) (2mit, isoform D) (Q9VFY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVKIVNQHCDLGLALLLAWTWLTRLVVAAHLVDIPTSSRLAAEREEQQLSRQDVGRLSYQSIHRMLRDENEPDSFRGELRYQQKRHKRELELNAPANKLNLTHRDLRTFNSTGGQWKGDFQVITAMDLSSNQLESLSLDNFNQLRQLDLGNNSLEVIPLSLADTNMSLPFVTLDLSCNKFSQISTSFFAQRLPQLKNLNLAHNELLNISRESFYNLLELQTLVLSHNNISDIDYETFLALPNLQYLDLSHNRLSGSAIRALQGIPDLVSLSIAYNPDVGVAMQEFVASWSLKELDASGTGLCQVPAALAQSVRTLKLSDNWLKAINCGDMDSYPLLQYLDLSHSRIAQVEDDALGRLELLESLFLDRNLLMRVPSSLPPSLEHLFLQHNQIMELPPQAFVGLVNLQTLDLSNNRLIFLPPLSLPKLLTLNLESSGVESVSQSIVHTLPQLRDLLLEDNPIKCSDLLGIAEWASPCRSVDAGQSNGASVSGRVDLKTEYLQFHNFYENFSSRECGIRKPENDTKPPSCSLTRASATLTTTPRSMSKVEKSQEAQATATSVEVAAATAATSEKTGIQATSAAQSTAAATTAEREAIATATSSDTTATPTLAAAAAIQSAGNIPAQLTTKTLRPTETTSLAQLQRRQQMPGMPAKTTETPAKNLPSLAQTKATTALPILATRDAATATTEINSDKPTNISGATKTVATSAAEIATPPAIEVPQTILAGKKSDKMPADKAHETLLKYPTRDTSGQVATTPHKHATLQLHVKDRHLIGTPLLMHKGDVLLVDAEQLLLPGTATVADADSEVLDPSQQHQSAEQEKHQSATDKRQADAINGDTKSPAKGHKKKPSLSIKKMTYSTKHAAKTVEDMAATSKTPQHQHSSVNTPKEAAPEELSTFAQLKAYVELKSESKPEHLMDQREENHHNLTGNHPGVMLLVACVLFIVLLAGLAHVYRCELPWQRSNRSGQLRPHHQRHLNETDDAHSFLHYQGSVNSNGGDPARLQKWHHSTRREAPYSSPLHNLQARELQQQRCQQFYSSSLADKSSSTSSSSSGSSRSSLHSPSRDDSYYIEMAPSSPPAANLPSLPMELLGSRSNALGCRTDRVAATDLGGTTEAVPSSAAAIKSVSSRLMTPSSRRLNIW
Protein: Probable glutathione peroxidase 8 (EC 1.11.1.9) (Q8LBU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May constitute a glutathione peroxidase-like protective system against oxidative stresses.
Interaction partners:
- Glutathione reductase, chloroplastic
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR2
- Glutathione synthetase, chloroplastic
- L-ascorbate peroxidase 3
- Monodehydroascorbate reductase 3
- Glutathione S-transferase F6
- Glutathione S-transferase U19
- Glutathione S-transferase F9
- Glutathione S-transferase F7
Sequence:
MATKEPESVYELSIEDAKGNNLALSQYKDKVLLIVNVASKCGMTNSNYTELNELYNRYKDKGLEILAFPCNQFGDEEPGTNDQITDFVCTRFKSEFPIFNKIEVNGENASPLYKFLKKGKWGIFGDDIQWNFAKFLVDKNGQAVQRYYPTTSPLTLEHDIKNLLNIS
Protein: Glutathione S-transferase (EC 2.5.1.18) (Q9MZB4)
Organism: Capra hircus (Goat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
RLLLEYTDSNYEEKKYTMGDAPDYDRSQWLNEKSKLGLDFPNLPYLIDGTHKLTQSNAILRHIARKYNMCGETEEEKIRVDLLENQVMDVRLHMARICYSPDFEKLKPGYLKEIPGRMKLFSVFLGKRCWFAGNKLTYVDFLAYDILDLQRIFEPRCLDEFRNLKDFLTRFEGLKKISGYMKSSRFLP
Protein: Sorbitol dehydrogenase 1 (SDH 1) (EC 1.1.1.-) (Polyol dehydrogenase) (Xylitol dehydrogenase) (EC 1.1.1.9) (P35497)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is active with D-sorbitol (D-glucitol) and xylitol as substrates, leading to the C2-oxidized product D-fructose and D-xylulose, respectively. Is likely involved in the utilization of D-sorbitol as a sole carbon source for growth. Has no activity on mannitol and primary alcohols such as ethanol.
Interaction partners:
- NADPH-dependent aldose reductase GRE3
- Xylulose kinase
- Sorbitol dehydrogenase 2
- Hexokinase-2
- Glucokinase-1
- Hexokinase-1
- Putative glucokinase-2
- N-acetylglucosamine kinase
- Mannitol dehydrogenase DSF1
- Transaldolase
Sequence:
MSQNSNPAVVLEKVGDIAIEQRPIPTIKDPHYVKLAIKATGICGSDIHYYRSGGIGKYILKAPMVLGHESSGQVVEVGDAVTRVKVGDRVAIEPGVPSRYSDETKEGRYNLCPHMAFAATPPIDGTLVKYYLSPEDFLVKLPEGVSYEEGACVEPLSVGVHSNKLAGVRFGTKVVVFGAGPVGLLTGAVARAFGATDVIFVDVFDNKLQRAKDFGATNTFNSSQFSTDKAQDLADGVQKLLGGNHADVVFECSGADVCIDAAVKTTKVGGTMVQVGMGKNYTNFPIAEVSGKEMKLIGCFRYSFGDYRDAVNLVATGKVNVKPLITHKFKFEDAAKAYDYNIAHGGEVVKTIIFGPE