wanglab/gogpt-training-data huggingface dataset:
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A8I5ZML8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKRLAARCFAGLLILSPLTVISDSRSADSGKCGWLWFKASVRRPSKTEILEEMEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEEESNEEEEEEDEEESEAEAKSVKVKIKLNKKEEKGRDTGKGKKRPNRGKAKPVVSDFDSDEEQDENEQSEASGTDDE
Protein: Cytosolic sulfotransferase 8 (AtSOT8) (EC 2.8.2.-) (Sulfotransferase 4b) (AtST4b) (Q9FX56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. No activity with brassinosteroids.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- At2g15730
Sequence:
MGEKDIPRNLKEEEEEEEENQSEETKSLISSLPSDIDCSGTKLYKYQGCWYDKDILQAILNFNKNFQPQETDIIVASFPKSGTTWLKALTFALAQRSKHTSDNHPLLTHNPHELVPYLELDLYLKSSKPDLTKLPSSSPRLFSTHMSFDALKVPLKESPCKIVYVCRNVKDVLVSLWCFENSMSGENNLSLEALFESLCSGVNLCGPLWENVLGYWRGSLEDPKHVLFLRYEELKTEPRVQIKRLAEFLDCPFTKEEEDSGGVDKILELCSLRNLSGLEINKTGSLSEGVSFKSFFRKGEVGDWKSYMTPEMENKIDMIVEEKLQGSGLKL
Protein: Peroxidase 70 (Atperox P70) (EC 1.11.1.7) (ATP45) (Q9FMI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Large ribosomal subunit protein eL22y
- RING-type E3 ubiquitin transferase
- Cinnamyl alcohol dehydrogenase 2
Sequence:
MRSFTNLNPCYVLLPFFLVLATNATHTNNFLPRPRTGYYGSACWNVESIVRSVVESNYLANPANAPGILRMHFHDCFVQGCDASVLLAGPNSERTAIPNLSLRGFNVIEEAKTQLEIACPRTVSCADILALAARDFVHLAGGPWWPVPLGRLDGRISLASNVILPGPTDSVAVQKLRFAEKNLNTQDLVVLAAGHTIGTAGCIVFRDRFFNYDNTGSPDPTIAPSFVPLIQAQCPLNGDPATRVVLDTGSGDQFDTSYLNNLKNGRGLLESDQVLWTNLETRPIVERLLGLRFPFLIFGLEFARSMTKMSQIEIKTGLDGEIRRVCSAVN
Protein: Beta-glucosidase BoGH3A (EC 3.2.1.21) (Glycosyl hydrolase family protein 3A) (BoGH3A) (A7LXS8)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Catalyzes the hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose in xyloglucan degradation, leading to remove the backbone 'G' units.
Subcellular location: Periplasm {ECO:0000305}. Note=Periplasmic localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MIIGIMKTFLLTICFLSVQTGMVAIAQDKEQTPVYLDDTQPIEVRVQDALNRMTVEEKTRLSYAQGKFSSPGCPRLGIPELWMSDGPHGVRAEINWNDWGYAGWTNDSCTAFPALTCLAASWNPLLAAKYGYAIGEEARYREKDVLLGPGVNIYRTPLNGRNFEYMGEDPYLASELCVPYIQGVQKNGVAACVKHYALNNQELWRGHIDVQLSDRALYEIYLPAFKAAVERGKAWSIMGAYNKVRGTHATHHKLLNNDILKGEWNFDGCVITDWGAAHDTYEAAMYGLDIEMGSYTNGLTSESEFGYDDYYLGKSYLKMVREGKIPMEVVNDKAARVLRLIFRTAMNRRKPFGALTSEEHYRTAYEIATEGIVLLKNGTGKKQPALLPVPQGKYKRILVVGDNATRNLMLGGGSSELKVQKVISSLDGIKAKFGDGVVYAQGYTSGRPMYGRADVIPQVTVDSLRNDAVEKAMNSDLVIFVGGLNKNHFQDCEGGDRLSYELPFAQNELIEALLKVNKNLVAVIVSGNAVEMPWVKEIPSIVQSWYLGSVGGEALADVLSGEVTPSGKLPFSYPVKLEDCPAHFFGEISYPGDSIRQEYKEDILVGYRWYDTKKVQPLFPFGYGMSYTTFEYSKPVISAQTMNTDGSIDVSVKVKNTGKVAGKEIIQLYIGDEECSVLRPVKELKDFRKVQLLPNEEKEVKFTIKPEALQFFDDKQRTWVAEPGKFKAYIAASSSDIRGTVTFEYIQ
Protein: Glucan endo-1,3-beta-glucosidase 3 (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase 3) ((1->3)-beta-glucanase 3) (Beta-1,3-endoglucanase 3) (Beta-1,3-glucanase 3) (Q9ZU91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Beta-glucosidase 31
- alpha-D-xyloside xylohydrolase
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase MMS21
- Non-structural maintenance of chromosomes element 4 homolog B
- Non-structural maintenance of chromosomes element 4 homolog A
- Structural maintenance of chromosomes protein 6B
- Structural maintenance of chromosomes protein 6A
- Cyclin-J18
Sequence:
MAALLLLFLFLFASSALSQDSLIGVNIGTEVTNMPSPTQVVALLKSQNINRVRLYDADRSMLLAFAHTGVQVIISVPNDQLLGISQSNATAANWVTRNVAAYYPATNITTIAVGSEVLTSLTNAASVLVSALKYIQAALVTANLDRQIKVSTPHSSTIILDSFPPSQAFFNKTWDPVIVPLLKFLQSTGSPLLLNVYPYFDYVQSNGVIPLDYALFQPLQANKEAVDANTLLHYTNVFDAIVDAAYFAMSYLNFTNIPIVVTESGWPSKGGPSEHDATVENANTYNSNLIQHVINKTGTPKHPGTAVTTYIYELYNEDTRPGPVSEKNWGLFYTNGTPVYTLRLAGAGAILANDTTNQTFCIAKEKVDRKMLQAALDWACGPGKVDCSALMQGESCYEPDDVVAHSTYAFNAYYQKMGKASGSCDFKGVATVTTTDPSRGTCVFPGSAKSNQTLGNNTSALAPSANSTTSGCIPKYYHHPHASFGDLTLLSLLLIIALVFL
Protein: GRB10 interacting GYF protein 2 (E7ESB6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAETQTLNFGPEWLRALSSGGSITSPPLSPALPKYKLADYRYGREEMLALFLKDNKIPSDLLDKEFLPILQEEPLPPLALVPFTEEEQRNFSMSVNSAAVLRLTGRGGGGTVVGAPRGRSSSRGRGRGRGECGFYQRSFDEVEGVFGRGGGREMHRSQSWEERGDRRFEKPGRKDVGRPNFEEGGPTSVGRKHEFIRSESENWRIFREEQNGEDEDGGWRLAGSRRDGERWRPHSPGWREHMERRRRFEFDFRDRDDERGYRRVRSGSGSIDDDRDSLPEWCLEDAEEEMGTFDSSGAFLSLKKVQKEPIPEEQEMDFRPVDEGEECSDSEGSHNEEAKEPDKTNKKEGEKTDRVGVEASEETPQTSSSSARPGTPSDHQSQEASQFERKDEPKTEQTEKAEEETRMENSLPAKVPSRGDEMVADVQQPLSQIPSDTASPLLILPPPVPNPSPTLRPVETPVVGAPGMGSVSTEPDDEEGLKHLEQQAEKMVAYLQDSALDDERLASKLQEHRAKGVSIPLMHEAMQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGRVPFSPGPAPPPHMGELDQERLTRQQELTALYQMQHLQYQQFLIQQQYAQVLAQQQKAALSSQQQQQLALLLQQFQTLKMRISDQNIIPSVTRSVSVPDTGSIWELQPTASQPTVWEGGSVWDLPLDTTTPGPALEQLQQLEKAKAAKLEQERREAEMRAKREEEERKRQEELRRQQEEILRRQQEEERKRREEEELARRKQEEALRRQREQEIALRRQREEEERQQQEEALRRLEERRREEEERRKQEELLRK
Protein: Pyruvate carboxylase (EC 6.4.1.1) (P95127)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDIGHPVHAYLSVDEIVATARRAGADAIYPGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPSASVDELLSVAAGMPFPLFVKAVAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVIELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGETLEQLGLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDLPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTARASADRGTKILNFLADVTVNNPYGSRPSTIYPDDKLPDLDLRAAPPAGSKQRLVKLGPEGFARWLRESAAVGVTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTMPQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGSAIAEVAMCYTGDLTDPGEQLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAGVSADEFASDPARFGIPESVLGFLRGELGDPPGGWPEPLRTAALAGRGAARPTAQLAADDEIALSSVGAKRQATLNRLLFPSPTKEFNEHREAYGDTSQLSANQFFYGLRQGEEHRVKLERGVELLIGLEAISEPDERGMRTVMCILNGQLRPVLVRDRSIASAVPAAEKADRGNPGHIAAPFAGVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVVS
Protein: Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) (Q6FMU9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03125}.
Interaction partners:
- Adenylosuccinate lyase
- Candida glabrata strain CBS138 chromosome A complete sequence
- Inosine-5'-monophosphate dehydrogenase
- AMP deaminase
- Histidine biosynthesis trifunctional protein
- Inosine triphosphate pyrophosphatase
- Argininosuccinate synthase
- Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase
- Candida glabrata strain CBS138 chromosome F complete sequence
- asparagine synthase
Sequence:
MVNVVLGSQWGDEGKGKLVDILVSHYDVVARCAGGNNAGHTIVVDGVKYDFHMLPSGLVNPNCKNLLGNGVVIHIPSFFKELETLESKGLNDARGRLFISSRAHLVFDFHQRTDKLRELELAGRSKDGKNIGTTGKGIGPTYSTKASRSGLRVHHLVNDNPGAWELFESRYRRLLETRKQRYGDFDYDAEEELNRFKQYKESLKPFVVDSVDFLHKSIANNEKILVEGANALMLDIDFGTYPYVTSSNTGIGGVITGLGIPPQKIQEVYGVVKAYTTRVGEGPFPTEQLNEQGEKLQSIGAEFGVTTGRKRRCGWLDLVLLKYSTLINGYTSLNITKLDVLDTFTEIPVGVSYKYKGETLNSFPEDLLTLGNVEVEYVTLPGWNQDITQIKKYDDLPENAKKYLKFIEDFVKVPVQWVGTGPARDSMLEKQI
Protein: Transmembrane protein 79 (Mattrin) (Q9D709)
Organism: Mus musculus (Mouse)
Function: Contributes to the epidermal integrity and skin barrier function. Plays a role in the lamellar granule (LG) secretory system and in the stratum corneum (SC) epithelial cell formation.
Subcellular location: Lysosome {ECO:0000269|PubMed:24060273}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24060273}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Colocalized with TGOLN2 in the trans-Golgi network. Colocalized with LAMP1 in the lysosome.
Interaction partners:
Sequence:
MTEPETLALLDMKEPETPEKSPPQALVLQSEEEGGTESPGTESLRVGSSVGSPIVREGPEDGPDSTISEAATLPWGTDPHPSAPLPDPPGWRDIEPEPLESEAPTKSEEPFKEDANLLPEKTVRAFVPIDLQCIERKPQEERILHRDAGPGELRNFLPARLSHPEPPERKWAEAVVRPPGRSCGGCGSCGGREALRAVASVVAALIFFPCLLYGAYAFLPFDAPRLPTMSSRLVYTLRCGVFATFPIVLGLLVYGLSLLCFSALRPFGEPRREVEIHRQYVAQSVQLFILYFFNLAVLSTYLPQDTLKLLPLLTGLFAISRLIYWLTFAVGRSFRGFGYGLTFLPLLAMLVWNLYYMFVVEPERMLTASESRLDYPDHARSVSDYRPRSWG
Protein: Calcium/calmodulin-dependent protein kinase II inhibitor 1 (Camk2n1 protein) (Q503R1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSEVLPYGEGKMSGYGADTDVSQMSFSCGLQDTNSFFGASQAKRPPKLGQIGRAKRVVIEDDRIDEVLKGMTDKSSPGV
Protein: Serpinb3c (Q6UKZ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MILSPEADGKFTVEMYRQLRESDKNIFYSPISMITALGMLKLGAKGNTEIQIEKVLQCNETTEKSTEKSAHCDDEDNVHEQFQKLITQLNKSNDGYDLKAANSIYGAKGFPLLQTFLEDIKECYHANVESLDFEHAAEESEKKINFWVKNETNGKIKDLFPSGSLSSSTKLALVNAVYFKGRWNHKFDENNTIEEMFWLNKNTSTPVLMVKQSNKFMFSFLEDVQAQIVEIPYKGKELSMFVLLPMEIDGLKQLEKQLTAAKLLEWTRAENMHLTELYLWLPRFKVEEKYDLPVPLECMGMVNAFDPQKADFSGMSSTQGLVVSKVLHKSFVEVNEEGTEADPASGEEVILRLAQVADFRCDHPFLFFIIHSKTNSILFFGRISSP
Protein: Putative uncharacterized protein YER097W (P40062)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MRFLPRKSRLLMSMRDFYYGLKKLHFCSFPNDIRPPHKKTFLLHSIRSIEAVFGTSDFIKLLGANSTFRLNKLECVENLSSILKKVFALSVINRKLKHLPKATSLPYEK
Protein: (R)-linalool synthase 2, chloroplastic (EC 4.2.3.26) (Terpene synthase TPS-Lin 2) (PsTPS-Lin-2) (PsTPS-Linl) (C0PPR1)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (mono-TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (R)-linalool.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAFVSIAPLASRCCVHKSFVSSREVKPLCRTIPTLGRCRRGKTVTPSISMCWTATVLDDGVQRRIANHHSNLWDDSFIQSLSTPYGETSYLERADKLIGEVKEIINSISVEDGELITPLNDLIQRLSIVDNIERLGIDRHFKNEIKSALDYVYSYWNEKGIGCGRESVITDLNSTALGLRTLRLHGYPVSSDVFEQFKEQNGQFACSAIQTEGEIKKVLNLFRASLIAFPGEKVMEEAEIFSTIYLKEALLKIPVCSLSREIAYVLEYGWHMNLPRLEARNYIDVFGQDPIYLTLNMRTQKLIELAKLEFNIFHSLQQEELKHVSRWWKDSGFSQMAYARHRHVEFYTLASCIAIDPQHSSFRLGFTKITYLGTVLDDIYDTFGTMDELELFTAAVKRWHPSAAEGLPEYMKGVYMMFYETVNEMAREAEKCQGRDTLNYARQALEAYIDSYMKEAKWISSGFLPTFEEYLDNGKVSFGYRIGTLQPILTLGIPFPHHILQEIDFPSRLNDLAGSILRLKGDIHSYQAERSRGEESSGISCYMKDNPESTEEDAVTYINAMINRLLKELNWEFLKPHSNVPITSKKHAFDILRAFYHLYKDRDGFSVTRNEIRNLVMTTVIEHVPL
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (P38972)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthetic protein ADE5,7
- Amidophosphoribosyltransferase
- Adenylosuccinate lyase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Phosphoribosylaminoimidazole carboxylase
- Bifunctional purine biosynthesis protein ADE17
- Bifunctional purine biosynthesis protein ADE16
- Dihydroorotase
- Adenylosuccinate synthetase
Sequence:
MTDYILPGPKALSQFRVDNLIKDINSYTNSTSVINELRSCYIHYVNGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLNDAVANNLPSSALGEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQDKVQRIERGLALLIKTVPGFPLLENLNDISLKCVYDRMTQQLYLTEPPNTMSIFTHEEPKPLVHVPLTPKDTKQSPKDILSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDDSVLVLVDLSAKQETKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKIINSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG
Protein: Ly6/PLAUR domain-containing protein 6B (Q8NI32)
Organism: Homo sapiens (Human)
Function: Likely acts as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro acts on nAChRs in a subtype- and stoichiometry-dependent manner. Modulates specifically alpha-3(3):beta-4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced maximal current response and increasing the rate of desensitization to ACh; has no effect on alpha-7 homomeric nAChRs; modulates alpha-3(2):alpha-5:beta-4(2) nAChRs in the context of CHRNA5/alpha-5 variant Asn-398 but not its wild-type sequence. However, according to another report in vitro it can weakly inhibits alpha-7 nAChRs.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MLYKSSDRPAHKVSMLLLCHALAIAVVQIVIFSESWAFAKNINFYNVRPPLDPTPFPNSFKCFTCENAGDNYNCNRWAEDKWCPQNTQYCLTVHHFTSHGRSTSITKKCASRSECHFVGCHHSRDSEHTECRSCCEGMICNVELPTNHTNAVFAVMHAQRTSGSSAPTLYLPVLAWVFVLPLL
Protein: 5-aminolevulinate synthase, non-specific, mitochondrial (ALAS-H) (EC 2.3.1.37) (5-aminolevulinic acid synthase 1) (Delta-ALA synthase 1) (Delta-aminolevulinate synthase 1) (P13196)
Organism: Homo sapiens (Human)
Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Glycine dehydrogenase
- Serine hydroxymethyltransferase, mitochondrial
- Alanine--glyoxylate aminotransferase
- D-amino-acid oxidase
- Porphobilinogen deaminase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Peroxisomal sarcosine oxidase
Sequence:
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
Protein: Hid-1 family protein P27G11.12 (Down-regulated in multiple cancers 1 homolog 1) (Q9P7M6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MGSQQSKLDFRNAVLRLHEERNIPKFDLIWERLWTLPETTEDVFHLMSIDDLTKVKDNAPENLQTIIAVLWDKLEDLQKETLFDDPAAPTTKCALNCMRLLTRLMPIIFEDKSMLEWFDYFAWTVPKDPNINTPRGASFLNTVVDYLFLINFTIPAHNDLTHGVHYCIWETGVVYHPTMLKERSYELHRVEVLRLLLSLFSEEIYRTDGNGSSCCAYVASIANRRLVLCLLSSLINTAMRFNTMFWKPEFLPLDNSVAHMSLIEYCFSVLLILMSEENNNGTPCYNNYRSSKNTLPKNYFSILLSKLQPYSDFQIILDGMSRLLYPPMQSTIPKRSSLIMFDYYPLVLIFCKLFIHYNERFFHYLIDTDRAIDLFIFLLYLSFEYLGDPSTYNHLKLCVILLKRLTAEKYFCKRLNKPFQQQTALPISMPVPFEGGTYADFTIIAISLLVQYTKDYHSEIAQMLCCSLCYLCLYAQNLNSHSSQSLFELFQSASYPGFLISNDVNHKILKYVIGAINNAIQYAQKYNAPLLYFFSMHKDYIEAVSALSFDAIMSVRNSSAEGDSAYWTRNGKTFSSKAFDSILLSRLRYVRSKSPTPYYPIESSEFGFTNLKDVTSKDEITDGFDKALRSNSLRTHRDSRPVQPLLKQRPQLHRALTESATLHGNDRSLEDTDEAKVEPIAHSVDYTFKPTVEWWNKWWPSLNFRTMLDIFTDLSLKISDMKKAGHPASEIMAMIKTQKYPATNQPYIPKYRTKEWRQQLANFARLFAWQVSCDLDSHKREGPGIFEGTDVKIFDSF
Protein: Glutamate receptor ionotropic, kainate 3 (GluK3) (Glutamate receptor 7) (GluR-7) (GluR7) (B1AS29)
Organism: Mus musculus (Mouse)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17620617}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42264}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor 1
- Metabotropic glutamate receptor 2
- Lysine--tRNA ligase
- Disks large homolog 4
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MTAPWRRLRSLVWEYWAGFLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQSLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWAMERLQAAPRAESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRTLTADYALLMESTTIEYITQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFIYKLRKTAEREQRSFCSTVADEIRFSLTCQRRLKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMSCSTSLAPVFP
Protein: RCS-specific HTH-type transcriptional activator RclR (Reactive chlorine resistance protein R) (P77379)
Organism: Escherichia coli (strain K12)
Function: Involved in reactive chlorine species (RCS) stress resistance. Up-regulates, in response to hypochlorous acid (HOCl), the expression of three genes essential for survival of RCS stress (rclA, rclB and rclC) and its own expression.
Interaction partners:
- Inner membrane protein RclC
- HTH-type transcriptional regulator YjiE
- Probable pyridine nucleotide-disulfide oxidoreductase RclA
- HTH-type transcriptional repressor NemR
- Uncharacterized protein RclB
- Uncharacterized HTH-type transcriptional regulator YdiP
- Melibiose operon regulatory protein
- Uncharacterized HTH-type transcriptional regulator YidL
- Regulatory protein SoxS
- Multiple antibiotic resistance protein MarA
Sequence:
MDALSRLLMLNAPQGTIDKNCVLGSDWQLPHGAGELSVIRWHALTQGAAKLEMPTGEIFTLRPGNVVLLPQNSAHRLSHVDNESTCIVCGTLRLQHSARYFLTSLPETLFLAPVNHSVEYNWLREAIPFLQQESRSAMPGVDALCSQICATFFTLAVREWIAQVNTEKNILSLLLHPRLGAVIQQMLEMPGHAWTVESLASIAHMSRASFAQLFRDVSGTTPLAVLTKLRLQIAAQMFSRETLPVVVIAESVGYASESSFHKAFVREFGCTPGEYRERVRQLAP
Protein: Probable polyol transporter 3 (Q9ZNS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plasma membrane sugar-proton symporter.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- AP2-like ethylene-responsive transcription factor AIL6
- WUSCHEL-related homeobox 5
- AP2-like ethylene-responsive transcription factor AIL7
- AP2-like ethylene-responsive transcription factor BBM
- LOB domain-containing protein 16
- AP2-like ethylene-responsive transcription factor AIL5
- Protein WUSCHEL
- AP2-like ethylene-responsive transcription factor PLT2
- Floral homeotic protein APETALA 2
- Auxin response factor 5
Sequence:
MVHADGHNFPGSDPNPHMNKFAFGCAIVASIISIIFGYDTGVMSGAQIFIRDDLKINDTQIEVLAGILNLCALVGSLTAGKTSDVIGRRYTIALSAVIFLVGSVLMGYGPNYPVLMVGRCIAGVGVGFALMIAPVYSAEISSASHRGFLTSLPELCISLGILLGYVSNYCFGKLTLKLGWRLMLGIAAFPSLILAFGITRMPESPRWLVMQGRLEEAKKIMVLVSNTEEEAEERFRDILTAAEVDVTEIKEVGGGVKKKNHGKSVWRELVIKPRPAVRLILIAAVGIHFFEHATGIEAVVLYSPRIFKKAGVVSKDKLLLATVGVGLTKAFFIIIATFLLDKVGRRKLLLTSTGGMVFALTSLAVSLTMVQRFGRLAWALSLSIVSTYAFVAFFSIGLGPITWVYSSEIFPLRLRAQGASIGVAVNRIMNATVSMSFLSMTKAITTGGVFFVFAGIAVAAWWFFFFMLPETKGLPLEEMEKLFGGGGPRGDRDGLEIQTKTISIGGFS
Protein: BCL2 associated agonist of cell death b isoform 1 (BCL2 associated agonist of cell death b isoform X1) (BCL2-antagonist of cell death) (BCL2-associated agonist of cell death b) (Bad protein) (Q4V925)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Apoptosis regulator Bcl-2
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Non-specific serine/threonine protein kinase.
- V-akt murine thymoma viral oncogene homolog 2,-like.
- Raf-1 proto-oncogene, serine/threonine kinase a.
- Raf-1 proto-oncogene, serine/threonine kinase b.
Sequence:
MAHMFNISDDSETETMEDSEDSSLDKHKSGSAQKKQHLTVPDRLKGEQLGRQRNLSMNEEDLLETGVAEDPHMLGDPFRPRSRSAPPALWAAKKYGQQLRRMSDEFDKGQMKRVKSAGTARQMSQSPSWLAFLWSHKESDAESRPAE
Protein: AT3g56750/T8M16_80 (Plant/protein) (Q9LET2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g26950
- At1g61240
- Rhamnogalacturonan I rhamnosyltransferase 4
- O-fucosyltransferase 23
- Protein MANNAN SYNTHESIS-RELATED 1
- Trimethylguanosine synthase
- O-fucosyltransferase 29
- AT4g38500/F20M13_60
- AT5g42660/MJB21_3
- Transmembrane protein
Sequence:
MATMSKAQRTKPTSGSQRLVLFCIVVFSFLLLFSSVISTGKLGLPYQQTLIDYFVWSPRGKRQHSLSEKYLYWGNRIDCPGKNCETCAGLGHQESSLRCALEEAMFLNRTFVMPSGMCINPIHNKKGILNRSDNKTTEEGWLGSSCAMDSLYDIDLISEKIPVILDDSKTWHIVLSTSMKLGERGIAHVSGVTRHRLKESHYSNLLIINRTASPLAWFVECKDRSNRSAVMLPYSFLPNMAAAKLRNAAEKIKAQLGDYDAIHVRRGDKLKTRKDRFGVERIQFPHLDRDTRPEFILRRIEKRIPRGRTLFIGSNERKPGFFSPLAVRYKLAYSSNFSEILDPIIENNYQLFMMERLVMMGAKTYFKTFKEYETDLTLTDDPKKNKNWEIPVYTMDERREEAS