wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 526 (Q8TF50)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAEVVAEVAEMPTQMSPGAVEMSTPMSAEMMEMSTEVTEMTPGEALASSLFFQHHQFMCSECGSLYNTLEEVLSHQEQHMLAVSEEEALTTQNVGLEPELVPGAEGPFQCGECSQLILSPGELLAHQDAHLRESANQIQYQCWDCQELFPSPELWVAHRKAQHLSATVAEPPVPPPLPPPTPLPPPSPPSEVKMEPYECPECSTLCATPEEFLEHQGTHFDSLEKEERNGLEEEEEDDEEDEEDDEEMEDEEAMAEVGDDAVGGDESTAGWAQGCGDCPQHQPSAGARRQHRRTAHSPASATHPFHCSQCQRSFSSANRLQAHGRAHVGGTHECTTCSKVFKKAASLEQHLRLHRGEARYLCVDCGRGFGTELTLVAHRRAHTANPLHRCRCGKTFSNMTKFLYHRRTHAGKSGAPPTGATAPPAPAEPTPPPPPPAPPAQLPCPQCSKSFASASRLSRHRRAVHGPPERRHRCGVCGKGFKKLIHVRNHLRTHTGERPFQCHSCGKTFASLANLSRHQLTHTGARPYQCLDCGKRFTQSSNLQQHRRLHLRPVAFARAPRLPITGLYNKSPYYCGTCGRWFRAMAGLRLHQRVHARARTLTLQPPRSPSPAPPPPPEPQQTIMCTELGETIAIIETSQPLALEDTLQLCQAALGASEAGGLLQLDTAFV
Protein: PDZ and LIM domain protein 3 (Actinin-associated LIM protein) (Alpha-actinin-2-associated LIM protein) (Q53GG5)
Organism: Homo sapiens (Human)
Function: May play a role in the organization of actin filament arrays within muscle cells.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10063829}. Note=Localizes to myofiber Z-lines.
Interaction partners:
- Alpha-actinin-2
- Titin
- LIM domain-binding protein 3
- Smoothelin-like protein 1
- Sorbin and SH3 domain-containing protein 2
- Myozenin-2
Sequence:
MPQTVILPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAAAHQLCLKIDRGETHLWSPQVSEDGKAHPFKINLESEPQDGNYFEHKHNIRPKPFVIPGRSSGCSTPSGIDCGSGRSTPSSVSTVSTICPGDLKVAAKLAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPLMSEPTASVPPESDVYRMLHDNRNEPTQPRQSGSFRVLQGMVDDGSDDRPAGTRSVRAPVTKVHGGSGGAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFIEGELYCETHARARTKPPEGYDTVTLYPKA
Protein: Serine/threonine-protein kinase YabT (EC 2.7.11.1) (P37562)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Uncharacterized protein YabS
- Stage II sporulation protein E
- Serine/threonine-protein kinase PrkC
- Probable serine/threonine-protein kinase YbdM
- Tyrosine-protein kinase YwqD
- Tyrosine-protein phosphatase YwqE
- Chromosome-anchoring protein RacA
- Putative tyrosine-protein kinase YveL
- Stage IV sporulation protein FA
- Protein phosphatase PrpC
Sequence:
MMNDALTSLACSLKPGTTIKGKWNGNTYTLRKQLGKGANGIVYLAETSDGHVALKVSDDSLSITSEVNVLKSFSKAQSVTMGPSFFDTDDAYIPSANTKVSFYAMEYIKGPLLLKYVSDKGAEWIPVLMIQLLSSLSVLHQQGWIFGDLKPDNLIVTGPPARIRCIDVGGTTKEGRAIKEYTEFYDRGYWGYGTRKAEPSYDLFAVAMIMINSVHKKEFKKTNQPKEQLRSLIEGNPLLQKYKKALFSALNGDYQSADEMKKDMLDAGQKAAQRKQPIKASPQPATRQRQQKPRQGKITKTRYTPKQKPAKSGGLFETTLIVISVLALYFAYIIFFLI
Protein: Zinc finger protein CRM3 (Changed mutation rate protein 3) (Q12145)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transcription factor involved in the regulation of the transcription of genes involved in cell rescue and defense, as well as cell cycle and DNA processing.
Subcellular location: Nucleus {ECO:0000305|PubMed:18366603}.
Interaction partners:
Sequence:
MNFSLSKQSSEKQSSYTDKSRSPNIGMCTVNYKSNLPLQVSAVDQLSTGKGTQFYGHNSYKNERECYNSTKINLPPISSLLPNFENNTPPNVDSRVQFPPQQVYQSMNVVPIVNEIYTPISMNATSDQYPIYYTESQQPIPHSQSPHLTSSAPLMMPVMVPTVYKPLTPYDKEPITIASEPNFTAISMASHPNAALELCHDRPKSVPPGYGVLPTMQEASNGRTKSEPGAVLNGSATFSDWKTDTRISSTKLRKQCPVCGKICSRPSTLKTHYLIHTGDTPFKCTWEGCTKSFNVKSNMLRHLKSHERKRNKVLNTT
Protein: cyclic-guanylate-specific phosphodiesterase (EC 3.1.4.52) (Q9I025)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Diguanylate cyclase
- Diguanylate cyclase TpbB
- GGDEF domain-containing protein
- Diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- Sensor domain-containing diguanylate cyclase
- diguanylate cyclase
- GGDEF domain-containing protein
- diguanylate cyclase
Sequence:
MQIGRPRRDSLFHFGIVVAALAAVPLLMAPLVYQQARMRAEGEAAVTSVAILRQLDTLLGVVSDSLDKSQEAVGKPCREVLGRLTRMTMLSPYFRSLVLVERESVYCSSLRGELHDLPLQVAFKALGSLPAGQRITPSNATPQVPERASVIMSRGDENGSGVLAIIDGQYLLDIQQAASYDERFQVQMVLRQSQRQLPGGAPATGDGVAVAASARFPVEVRVAVAPALASAYRADAWRHYAPFILLAALLAGYLAHLFCRRRLSLVGDMYRAMRAREFHMVYQPIIHLDTGECRGVEALVRWQRPDRSQVRPDIFIPLAEDNGMIGDLTRHIFGLVAADLAQLGLGAGDHLGVNVSGSHLASHGFVDDVRRLLGAIGSEGPQLVLEVTEREALPHDAQLQHNIQQLRELGVQWALDDFGTGQSSLSHLQKLHADFLKIDRSFVSSVGSGSVNAVVLETIIALAQRLDLAMTAEGIETREQEQYLCGHSIQWGQGYLFSPPLKAAELWAWRNSRRGAEREARVAAS
Protein: Interleukin family protein (Q6FGW4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU368043}.
Interaction partners:
Sequence:
MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN
Protein: Protein Wnt-1 (XWnt-1) (XInt-1) (P10108)
Organism: Xenopus laevis (African clawed frog)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (By similarity). Plays an important role in patterning during embryonic development. Plays an essential role in the development of the embryonic brain and central nervous system (CNS) (By similarity). Has a role in osteoblast function, bone development and bone homeostasis (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P04628}. Secreted {ECO:0000250|UniProtKB:P04628}.
Interaction partners:
Sequence:
MRILTFLLGLKTLWVLAFSSLSNTIAVNNSGKWWGIVNVASAGNVLPGSDARPVPLVLDPSLQLLSRQKRLIRQNPGILQSITRGLHSAIRECKWHFRNRRWNCPTGTGNQVFGKIINRGCRETAFVFAITSAGVTHSVARSCSEGSIESCSCDYRRRGPGGPDWHWGGCSDNIEFGRFIGREFVDSSERGRDLKYLVNLHNNQAGRLTVLTEMRQECKCHGMSGSCSLRTCWMRLPPFRSVGDALKDRFDGASKVTYSNNGSNRWGSRSDPPHLEPENPTHALPSSQDLVYFEKSPNFCSPSEKNGTPGTTGRICNSTSLGLDGCELLCCGRGYRSLAEKVTERCHCTFNWCCHVTCLNCTSSQIVHECL
Protein: ADP-ribosylglycohydrolase (Q382Z4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Mitochondrial ribosomal protein S18
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Dehydrogenase-like protein
- PROP1-like PPR domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MVAKLQHNPAPTTLNFYEKSFQQLSDVQQRQTGLLIGAAVGDAAARALDGYTAEEVAAVAAESGSLQDEDEDPVVFASVTPREHKSGLLRHHSYTFYLFSQLLRVMATSRGDFPVQYVKNEWVATARAHPDCFVREHASLLHVLCITMQLPVIYPWADDSTLREYASDFLEFLTETPAERAVASREDVYAYTNSVLGVALRCLQSNPDPYRNAAFMAAPGTAHVFPDDLALYCPPALVGSSHSRTEELSEADSKTVPLFPARLLESDVRVVRECLVVARGAASFAEGIKAAIHLGGPVCQRSLIVGALLGARMGVRRIPISWLSATYDHVPLVTLALQVAQWSWNPPHH
Protein: ATP synthase F(1) complex catalytic subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (P56480)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17438143}; Peripheral membrane protein {ECO:0000269|PubMed:17438143}; Matrix side {ECO:0000250|UniProtKB:P00829}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLSLVGRVASASASGALRGLSPSAALPQAQLLLRAAPAGVHPARDYAAQASAAPKAGTATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRDSRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
Protein: DNA-binding protein (P71859)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTGVSDIQEAVAQIKAAGPSKPRLARDPVNQPMINNWVEAIGDRNPIYVDDAAARAAGHPGIVAPPAMIQVWTMMGLGGVRPKDDPLGPIIKLFDDAGYIGVVATNCEQTYHRYLLPGEQVSISAELGDVVGPKQTALGEGWFINQHIVWQVGDEDVAEMNWRILKFKPAGSPSSVPDDLDPDAMMRPSSSRDTAFFWDGVKAHELRIQRLADGSLRHPPVPAVWQDKSVPINYVVSSGRGTVFSFVVHHAPKVPGRTVPFVIALVELEEGVRMLGELRGADPARVAIGMPVRATYIDFPDWSLYAWEPDE
Protein: PPi-type phosphoenolpyruvate carboxykinase 1 (EhPEPCK1) (PPi-PEPCK1) (EC 4.1.1.38) (Diphosphate-dependent phosphoenolpyruvate carboxykinase 1) (PEP carboxyphosphotransferase 1) (C4LY96)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Inorganic pyrophosphate (PPi)-dependent phosphoenolpyruvate carboxykinase, which regulates the carbon flow of the central metabolism by fixing CO(2) to phosphoenolpyruvate to produce oxaloacetate. Can also produce pyruvate and diphosphate from phosphoenolpyruvate and phosphate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26269598}.
Interaction partners:
- Malate dehydrogenase
- Malate dehydrogenase
- Malate dehydrogenase
- Pyruvate kinase
- PPi-type phosphoenolpyruvate carboxykinase 3
- PPi-type phosphoenolpyruvate carboxykinase 2
- Pyruvate, phosphate dikinase
Sequence:
MFNQEKGTDYPILNIQELEALADLKLSAMGKEYPKHDKSDAIDVVAPLVDIIAEGDQESTAPIDARLQTFLNSYFAECGEEVPKIPDNTFILDREGLGRVLSFPPHKQEFFCETMKSYKIKQGVLHNPAKDKRTTVGVFHICQSDVPVPADKIECPKIAFLRMLKAAFYGAPDDHLIIPYTAECKEPTRSWVSLYMRPVVVPGVKGVKGFEHEKATEMHFFVPGNMVSCLDFVESVFGNAGNPRLSKNDAALDPLGWTGHSGMAILAPHLTRMTKKECGLPHISQATERQKRERMCWEKEDELYNDGKTFKMYCRDASGVICTIIADNYFGYCKKEVKTQISYSANLYGFAEEEHAGGAVTRPSYDLGEACKAVQYAEGYKFSEMVEKNKHSIIVKEEGYAVDKKYPEGIIYVPEDSVFTIEDASIKFNHNGKEESILLTPKVNYVLPNGYTIILHDTMTSRRWTLRGILPQYTLCHKPCTVSGGGKSEISKNISDAIFEGKMFVNNKEEEFKAVQKVFDHDFSRRYADGEIKSAHILDPNVTLGTVVKMLTPSSFFTEEHNEFVAAIPPMIVELALTIKSLYREEWKGDWQSRITVDKINGKEGHELKYRKMPLPSQYLRVGFERDETTWRVFQLRKDFFPAAKLQMEDDITASVIVPTKLLKTPINTNGKKACKIVKNCELRLFQRPDDAVFRGYDKQTEYDFSIPGHFISNYQPMTREEAKDFTKDVVRLYQYTEPMRKCLQDFVAGKDEAKYIVSSSHTRLVQDGDKLVGSKNPRYLQRRPDMLDPEYTYMTFKAIQLFRKISDEEPLYTPVDAVLSGRRNNPPQVAKNGMKLRPLSVFAPLHYFELPELLMECITSMTGASPSMFGAGSEGALTKGPFNSLPAVVDLNNYLLGMICCGYSGFVSSASYCGPHYKVAHDISLLIPEIWSRMRRYEQEPKYLIEHGYLEPCPDVTYNGKTYSGKRLGYRITKDFTVHYFSSIFSVPNSVMPEDFLKPELQDLAIYADSYEYIEQTDKGIAMNYVKDGTVEGACPPLKALIYIMANGEYNGMTRESKEFREMFDAKTILNSEWYKERLVTRQKLEVAKLNKDLAYLNKTIAEKPRLAETLNKQIAAVKEELQYVSSEEYLIDIDGSIGTDPYPYKCMKH
Protein: Serine protease snk (EC 3.4.21.-) (Protein snake) (P05049)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo.
Subcellular location: Secreted {ECO:0000269|PubMed:9477324}.
Interaction partners:
- Serine protease ea
- Serine protease gd
- Protein spaetzle
Sequence:
MIILWSLIVHLQLTCLHLILQTPNLEALDALEIINYQTTKYTIPEVWKEQPVATIGEDVDDQDTEDEESYLKFGDDAEVRTSVSEGLHEGAFCRRSFDGRSGYCILAYQCLHVIREYRVHGTRIDICTHRNNVPVICCPLADKHVLAQRISATKCQEYNAAARRLHLTDTGRTFSGKQCVPSVPLIVGGTPTRHGLFPHMAALGWTQGSGSKDQDIKWGCGGALVSELYVLTAAHCATSGSKPPDMVRLGARQLNETSATQQDIKILIIVLHPKYRSSAYYHDIALLKLTRRVKFSEQVRPACLWQLPELQIPTVVAAGWGRTEFLGAKSNALRQVDLDVVPQMTCKQIYRKERRLPRGIIEGQFCAGYLPGGRDTCQGDSGGPIHALLPEYNCVAFVVGITSFGKFCAAPNAPGVYTRLYSYLDWIEKIAFKQH
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (DNA 3'-5' helicase II) (Q9L7T3)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MNDDLSLLLNSLNDPQRQAVAAPLGRQLVLAGAGSGKTRVLVHRIAWLIQVEHASPYSILSVTFTNKAAAEMRHRIEQLLGINPAGMWVGTFHGLAHRLLRAHWREAGLSENFQILDSDDQQRLVKRVIRELGLDEQRWPARQAQWFINGQKDEGLRPQHIQPGGDLFLATMLKIYEAYEAACARAGVIDFSELLLRALDLWRDHPGVLEHYQRRFRHILVDEFQDTNAVQYAWLRILAKGGDSLMVVGDDDQSIYGWRGARIENIQQFSDDFADAEVIRLEQNYRSTASILKAANALIANNQGRLGKELWTDGEDGESLSLYAAFNEHDEARYVVESIESALKGGLARSEIAILYRSNAQSRVLEEALLREKIPYRIYGGQRFFERAEIKNAMAYLRLLDGRGNDAALERVVNVPARGIGEKTVESIREFARGNDVSMWEAIRLMIANKVLPGRAASALTGFVELIENLSAKVMDMPLHLMTQTVIEQSGLISYHKEEKGEKGQARVENLEELVSAARAFENSEEEEDLTPLQAFLSHASLEAGETQADAHEDSVQLMTLHSAKGLEFPLVFLVGMEEGLFPHKMSLEESGRLEEERRLAYVGVTRAMQRLVLTYAETRRLYGSETYNKVSRFIREIPPALIQEVRLSNTVSRPYGGTSRSAGGNLFSGAGVPETPFSLGQRVRHALFGEGTILNFEGAGAQARVQVNFESEGSKWLMLGYAKLEAL
Protein: Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] (Q71U36)
Organism: Homo sapiens (Human)
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. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P68369}.
Interaction partners:
- Tubulin beta-3 chain
- Tubulin beta-2A chain
- Tubulin beta-4B chain
- Tubulin beta-2B chain
- Tubulin beta chain
- Cytoplasmic dynein 1 heavy chain 1
- Tubulin beta-6 chain
- Tubulin beta-4A chain
- Microtubule-associated protein tau
- CAP-Gly domain-containing linker protein 1
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Vacuolar protein sorting-associated protein 52 (Q9UST3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 51
- Thioredoxin reductase
- Conserved oligomeric Golgi complex subunit 8
- t-SNARE affecting a late Golgi compartment protein 1
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 3
- t-SNARE affecting a late Golgi compartment protein 2
Sequence:
MQRASTQDVYDGSGDDLNKLDSLKSVLNDVLSSLERFQVDLDVATSDIYKVSERSNKIQVNLNNLKAVESALGAEIDGAILPPDLIKTISTGDMDHPSWNSALEKLTSFLEGGEDDSSLGNMFNSLQINKDQKKLVDKLRDKAIERIRNYIVVTIKMFRQAFVDVFPIRKHRLIANKNYYLFLFKFNRKLALELQRAYINTMNWFYLYHFEQYSRFLDKVHVLKGETIRVEEDRKGLFNLSKGAQQSYGNQMLSVNLRPQDFDMNSVLTASTMHHIESSPQYIERVYCSWELVLTEHVSSEYAFLLEYFNLSKDQQATVFAAIFEKTLHFSRKYITGLISSSIDCIGILKSIRFTQKLALQAQTNIVPVIEPHYNSMILFLWPRFQAVMDMHCESLRKTNLSVKPEEITSRPHPLSQRVAELLYSLSMLSVNVVEAEPVARSASRLAQDYVSMLQNLCKTVNDKRRQSRFLSNNYTLISTVLSGVSGNLAIEQKTYFEKLNENLTNFQ
Protein: Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein (O44183)
Organism: Caenorhabditis elegans
Interaction partners:
- Aminopeptidase ltah-1.1
- Peptidase M20 dimerisation domain-containing protein
- Uncharacterized protein
- C2H2-type domain-containing protein
- Putative serine/threonine-protein kinase K06H7.1
- Peptide transporter family 1
- BTB domain-containing protein
- Surfeit locus protein 4 homolog
Sequence:
MCQLHNFRPKRDPCSAANINEITVEHTAIKWTVSFQLKMIIGQATLRCRCLTDATKLVLDVRDLSIRSVSINGVDCDFRIAPNVYTFFGSKMSVYLPPQFQKAGTILQVTVAYGTSPDATALQWMKKEQTADKRMPYLFSQCQAIHARSIVPCMDTPSVKSTYEAEVTVPTGMTCLMSAIGQGSKGDDDTTTFFYKQPVAIPSYLIAIVVGCLEKRDISDRCAVWAEPSVVDKAHWEFAETEDILASAEEIAGKYIWGRYDMVCLPPSFPFGGMENPCLTFLTPTLIAGDRSLVSVIAHEIAHSWSGNLVTNSSWEHFWLNEGFTMFIERKICGRLVSEDYRQFMAFNGWTNSLIPAVYEQFTPTHQFTKLIQDHTNVDPDVAFSCVPYEKGSALLFYLEQKLGGSEIFEAYLKDYLKTFAHQAIDSWQWKDHLYKYFADQKEVLDTVNFDLWFNGVGMPPEKPNYGQSMVEACEVLLKKWLAADESTVGDITSEDYYAMQPLQQIELLSQLWQHDPPIEHYKLDALNKLYKLNDSQNSELLLNWLRLCIKSKWEECIPKALDFVNSQGRLKFCRPIYRDLAQWPIANKKARDVYLKGRSQMHPITAEMIAKDLHIRHSTHTVCF
Protein: COP9 signalosome complex subunit 4 (CSN complex subunit 4) (SGN4) (O13895)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11854407}. Nucleus {ECO:0000269|PubMed:11854407}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 7
- RING-box protein pip1
- Cullin-4
- Cullin-1
- Ubiquitin-like protein 1
- Cullin-3
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MEEVVHYFLEGNMPVAQFREALALHYTNEKELFEQAKRCLNICCGSNNFAKRNDVLFSLLDVAVSISSLELRKELISELYVPVQSLEEAPSEYLVSCCLQLATIYEAEQNFELLCSSLEAVEKHGHFENDLEQLLLLRIRLGDAYLKLGKAEKAILTVRTSIPLAFKVSNDQLLMELQLCNARALDETGQFLEAAKCYYRVLQYKVPGNELIYRENLCSVAQCLLLAIPSPIVLQFLQEISLQPSVREIPFYSLVEKYLKRKFIGKEDGAFLLPFLLPHQVIHMNRLIEDGRHFLETNILFLSEFFEVSSTSILAKHFKLSEEQVDTVVADMVIQERLNASIDQCEGYITFLPEYGKANNLPNYVNKIATVLQHYGS
Protein: Probable cyclase otaY (EC 5.-.-.-) (Ochratoxin A biosynthesis cluster protein Y) (A0A1R3RGJ9)
Organism: Aspergillus carbonarius (strain ITEM 5010)
Function: Probable cyclase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties. OtaY is probably involved in the polyketide cyclization (Probable). The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable).
Interaction partners:
Sequence:
MTTPTPTTLKHHATTILTTLVNDRQTAAIEHLLHPTITLKHNDLPAMSKSELIAFWPEVLAQSPHFRVQIRDVIAEGNKVWVYSRVEGRLGEGVMDDFHMMVFDEEGLVVRSTGVQRVVEGEM
Protein: ATP synthase subunit d, mitochondrial (Q59PV8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273, ECO:0000256|PIRNR:PIRNR005514}.
Interaction partners:
- Uncharacterized protein
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit beta
- ATP synthase subunit a
- ATP synthase subunit gamma
- ATP synthase subunit 4
- ATP synthase subunit alpha
- ATP synthase subunit 5
- F1F0 ATP synthase subunit h
- F1F0 ATP synthase subunit g
Sequence:
MSSVAKQAARKVDFNKLVNGLGLTGTTASSLTAFKKRHDEAKKEFIDLSSQSTDIDFNHYRSILKNSKVVDEIEKAVSGFKPVTIDVSKNLKNIEIFESKAIENAKLTEKSVLEEISVLQKTLKEIESARPFDQLTVDDVAAASDLEEKVTYMVKNGKWEVPGYREKFGDLAAM
Protein: Ubiquitin-like domain-containing protein (Q582Y0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tubulin-specific chaperone, putative
Sequence:
MASPEVSFMDAVRERYGAPDDSAAYSAESFLVGEASRRRNKKWELVGMEKTRQKQADHSKLVHVVLRGMNITVAESTTGELAQAALHRLEEVDLSENFQLTIREVGRMAQHLPALKVLQLSHSPELFPVGTAEISASPFESLLVAPHLRKLVLNHVGVQSIWQLRAVVQLPLLEELHLDNNSIKRLALFVDDNEEKTAHRILHEANKNDNNSGNDIKSGWFPAVNTLSLAQNELSSWGLESGLQESIGTAFPGLKRLFLTSNRMPNLSITRACASIVPHGGGNKRGDGDTSDGSLVDYAYLQPLELLCLNENPTITDACTLDAVRYLCPHLTTFRITYSAIFPQWNETLGRMYVVASLPSITTLNRGQVRAKERMDSEIFYIQRGMAAEQKQQVGEAQDGSQSKVTQETLRYPLLDVLREKHKDVITVIYREGETASHDGTMHMMLNIVLRCDGFEDTHKRVPSSMSVGKLKALVRAVYSVAPSHQHLSFVSGDAGVVEAPTQLDNELQSLSFYGMCDRAIVLVVDTSLRS
Protein: Golgi SNAP receptor complex member 1-1 (Golgi SNARE 11 protein) (AtGOS11) (Q9LMP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Syntaxin-31
- Membrin-11
- Syntaxin-32
- VAMP-like protein YKT62
- Membrin-12
- VAMP-like protein YKT61
- Bet1-like SNARE 1-1
- Bet1-like SNARE 1-2
- Syntaxin-23
- Bet1-like protein At4g14600
Sequence:
MDVPSSWDALRKQARKIEAQLDEQMHSYRRLVSTKALSKSDGNESDLEAGIDLLLRQLQQVNAQMQAWVSSGGSEMVSHTLTRHQEILQDLTQEFYRHRSSLRAKQEHASLLEDFREFDRTRLDLEDGYGSEQALIKEHMGINRNTAQMDGVISQAQATLGTLVFQRSTFGGINSKLSNVASRLPTVNTILAAIKRKKSMDTIILSLVAAVCTFLIFIYWITK