wanglab/gogpt-training-data huggingface dataset:
Protein: Protein indeterminate-domain 6, chloroplastic (Q8RWX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:16934950}.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 4
- RING/FYVE/PHD zinc finger superfamily protein
- Probable serine/threonine-protein kinase PBL15
- Probable protein phosphatase 2C 47
- Beta-glucosidase 32
- NAC domain containing protein 38
- Peroxidase 22
- Trihelix transcription factor GT-3a
- Non-specific lipid transfer protein GPI-anchored 5
- Protein FAR1-RELATED SEQUENCE 9
Sequence:
MSSSYNTIALSSTPTFLLSSAAAGPGPNNFNRQEAAMTMVQQQPTSSVAPPPKKRRNQPGNPNPDAEVIALSPKTIMATNRFLCEVCNKGFQREQNLQLHRRGHNLPWKLKQKSNKEVRRKVYLCPEPSCVHHDPARALGDLTGIKKHYYRKHGEKKWKCDKCSKRYAVQSDWKAHSKTCGTKEYRCDCGTIFSRRDSYITHRAFCDALIQESARNPTVSFTAMAAGGGGGARHGFYGGASSALSHNHFGNNPNSGFTPLAAAGYNLNRSSSDKFEDFVPQATNPNPGPTNFLMQCSPNQGLLAQNNQSLMNHHGLISLGDNNNNNHNFFNLAYFQDTKNSDQTGVPSLFTNGADNNGPSALLRGLTSSSSSSVVVNDFGDCDHGNLQGLMNSLAATTDQQGRSPSLFDLHFANNLSMGGSDRLTLDFLGVNGGIVSTVNGRGGRSGGPPLDAEMKFSHPNHPYGKA
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase) (N-myristoyltransferase) (PfNMT) (Q9U419)
Organism: Plasmodium falciparum
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Myristoylates adenylate kinase AK2. During the asexual blood stage, may myristoylate proteins such as ARO, CDPK1 and GAP45 (By similarity). Probably by mediating protein myristoylation, plays a role in the assembly of the inner membrane complex during the early stages of schizogony and in the formation of rhoptries in the late stages and thus merozoite egress (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30419}.
Interaction partners:
Sequence:
MNDDKKDFVGRDLYQLIRNAKDKIKIDYKFWYTQPVPKINDEFDENVNEPFISDNKVEDVRKEEYKLPSGYAWCVCDITKENDRSDIYNLLTDNYVEDDDNVFRFNYSSEFLLWALSSPNYVKNWHIGVKYESTNKLVGFISAIPIDMCVNKNIIKMAEVNFLCVHKSLRSKRLAPVLIKEITRRINLESIWQAIYTAGVYLPKPISTARYFHRSINVKKLIEIGFSCLNTRLTMSRAIKLYRIDDTLNIKNLRLMKKKDIDGLQKLLNEHLKQYNLHAIFSKEDVAHWFTPIDQVIYTYVNEENGEIKDLISFYSLPSKVLGNNKYNILNAAFSFYNITTTTTFKNLIQDAICLAKRNNFDVFNALEVMDNYSVFQDLKFGEGDGSLKYYLYNWKCASCHPSKIGIVLL
Protein: Potassium channel subfamily K member 2 (Outward rectifying potassium channel protein TREK-1) (Stretch-activated potassium channel TREK-1) (TREK-1 K(+) channel subunit) (Two pore domain potassium channel TREK-1) (Two pore potassium channel TPKC1) (Q920B6)
Organism: Rattus norvegicus (Rat)
Function: Ion channel that contributes to passive transmembrane potassium transport. Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner. In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2. In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:31630908}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97438}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P97438}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:16248991}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000269|PubMed:31630908}.
Interaction partners:
- Potassium channel subfamily K member 10
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Potassium channel subfamily K member 1
- Piezo-type mechanosensitive ion channel component 1
- Popeye domain containing 2
- Piezo-type mechanosensitive ion channel component 2
- Transient receptor potential cation channel subfamily M member 8
Sequence:
MLASASRERPGYTAGVAAPDLLDPKSAAQNSKPRLSFSAKPTVLASRVESDSAINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPQEISQRTTIVIQKQNFIAQHACVNSTELDELIQQIVTAINAGIIPLGNNSNQVSHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAVIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKEEVGEFRAHAAEWTANVTAEFKETRRRLSVEIYDKFQRATSVKRKLSAELAGNHNQELTPCRRTLSVNHLTSEREVLPPLLKAESIYLNGLTPHCAAEDIAVIENMK
Protein: Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1) (P11796)
Organism: Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix.
Interaction partners:
Sequence:
MALRTLVSRRTLATGLGFRQQLRGLQTFSLPDLPYDYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISKGDAPTVAKLHSAIKFNGGGHINHSIFWKNLAPVREGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLGVDKELKRLVIETTANQDPLVSKGANLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVMNWKYANEVYEKECP
Protein: Nuclear transcription factor Y subunit C-4 (OsNF-YC4) (Transcriptional activator HAP5B) (OsHAP5B) (Q655V5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor involved in the regulation of flowering time under long day (LD) conditions. Functions as repressor of flowering, independently of HD1 and GHD7. Controls flowering time by negatively regulating the expression of EHD1 and HD3A. Component of the NF-Y/HAP transcription factor complex (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26542958}. Cytoplasm {ECO:0000269|PubMed:26542958}.
Interaction partners:
- Nuclear transcription factor Y subunit B-11
- Nuclear transcription factor Y subunit B-10
- Nuclear transcription factor Y subunit B-8
- Os09g0568200 protein
- HAP3 subunit of HAP complex
- Nuclear transcription factor Y subunit B-3
- HAP3 subunit of HAP complex
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit
- HAP3 subunit of HAP complex
Sequence:
MEPSSQPQPAIGVVAGGSQVYPAYRPAATVPTAPAVIPAGSQPAPSFPANPDQLSAQHQLVYQQAQQFHQQLQQQQQRQLQQFWAERLVDIEQTTDFKNHSLPLARIKKIMKADEDVRMISAEAPVIFAKACEIFILELTLRSWMHTEENKRRTLQKNDIAAAITRTDMYDFLVDIVPRDDLKEEGVGLPRAGLPPLGVPADSYPYGYYVPQQQVPGAGIAYGGQQGHPGYLWQDPQEQQEEPPAEQQSD
Protein: Cytochrome P450 3A41 (EC 1.14.14.1) (Q9JMA7)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Sulfotransferase 1E1
- Cytochrome P450 1A1
- Aromatase
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Cytochrome P450 26C1
- Polyunsaturated fatty acid lipoxygenase ALOX15
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
Sequence:
MNLFSALSLDTWVLLAIILVLLYRYGTRTHGLFKKQGIPGPKPLPFLGTVLNYYKGLWKFDMECYEKYGKTWGLFDGQMPLFVITDPEMIKNVLVKECFSVFTNRREFGPVGIMSKAISISKDEEWKRYRALLSPTFTSGKLKEMFPVIEQYGDILVKYLMQEAEKGKPVTMKDVLGAYSIDVITSTSFGVNVDSLNNPEDPFVEKAKGILRVDFFDPLVFSVVLFPFLTPVYEMLNICMFPKDSIEFFKKFVNRMKESRLDSKQKHRVDFLQLMMNAHNNSKDKDSHKALSDMEITAQSIVFIFAGYETTSSTLSFTLYCLATHPDIQKKLQEEIDETLPNKAPPTYDTVMEMEYLDMVLNETLRLYPIGNRLERFCKKDVELNGVYIPKGSTVMIPSYALHHDPQHWPEPEEFQPERFSKENKGSIDPYLYMPFGIGPRNCIGMRFAFMTMKLALTKVMQNFSFQPCQETQIPLKLSRQGLLQPEKPIVLKVVPRDVVITGA
Protein: Transposon Ty1-ER2 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q03619)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQQSNDLNIESDHDFQSDIELHPEQLRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTGSGGMHRLDVPLLAPMSQSNTHESSHASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDPGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Interleukin-1 receptor-associated kinase 1 (Predicted) (Irak1 protein) (B2RYH5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Interleukin-1 receptor-associated kinase 4
- Myeloid differentiation primary response protein MyD88
- TNF receptor-associated factor 6
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Interleukin-1 receptor-associated kinase-like 2
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-interacting protein
- NF-kappa-B essential modulator
- Interleukin-1 receptor type 1
- Interferon regulatory factor 7.
Sequence:
MAGGPGPGEPVVPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSEQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPASVLPPSTGAPRPSSISAGSETEDWSPRKLQSSASTFLSPAFPGSQTHSESELLQVPLSDSLGPPLQSSAPSSIKPSPESPVSGLQRARPSPFCWPFCEISQGTCNFSEELRIGEGGFGCVYRAVMRNTTYAVKRLKEEADLEWTVVKQSFLTEVEQLSRFRHPNIVDFAGYCAESGFYCLVYGFLPNGSLEDQLHLQTQACSPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLMPKLGDFGLARFSRFAGANPSQSSTVARTCTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVILETLAGQRAVRTQGAKTKYLKDLIEDEAEEVGVTLKSTQPTLWMGVATDAWTAPIAAQIYKKHLDSRPGPCPPQLGLALAQLACCCMHRRAKKRPPMTQVYKRLEGLQAVPPWKLEVAGHGSPSPQENSYMSTTGSAQSGDEPWQPLVVTTRAPAQAAQQLQRSPNQPVESDESVPGLSATLHSWHLTPDSHPSPVSFREASCTQGGTTRESSLRSGPGFQPTTMEGSSMGSSSLLSSEPPQIIINPARQKMVQKLALYEEGVLDSLQLLSSGFFPGLDLEPEKRKRPEESDEFQS
Protein: Eps-15 protein (SD09478p) (Q8WQ61)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNVDFARVCGKHIGVYEAYYKLIDPKGTGAIEAMTAAKFLKKSGLSDVVLSRIWDLSDPSGKGFLDKPGFFVALKLVSLSQAGQVASMANIYLDIANPPKLGELPKTMPSRIQTVPVASGGVANGDWSIGVIDRLKYEQLFESLHPSNGMLPGNKVKGVLMDSKLPMSILGTIWDLADQDKDGNLDMHEFVVAMHLVYQTLQKRTIPSVLPPELRKPGGAGPPPKPAMPPPPAGAAMPRAPSGEGFGDGGFVANFPKDIAPPAAIPPLPVAVPPMTRIPPVGAVSSQPLIQTDPLIPIGAPVMANADWVVTPADLKRFEEIFRQSDLDKDGLVSGLEVKDIFIKSGIPQRSLADIWALCDTNQSGKLTVEQFALAMWFVERKQRGVDPPHVLNANMVPPSMRATVAGVDLQPQEVKPTYSNPELEMISKEIEELARERRVLETEIAQKEADVRIKNGEVRSLQSELDTLTATLKQLENQRGEAQKRLDDLQAQVSHNTAVLANVSLDISRTNEQVTKIRDQCHMQEVTINEQEGELNAKRSELQKLKDEEASLQKEYDSNNRELSKLTNHLQATQLQISSVRSMVTQLLETQRQMTDALLICRAAMENQNAELVSEYQLKIEPDFDEARKTLTKQVQLPKDDPFEENNSGAANQATNGFGSDPFSGQPVNKPAISTGFDDSFNMSSGFDSGFDAFGQSGAGSAFGQTQRDPFGSDAFAANKSNAITPEPGKDDFGSDPFAALHAPTGQGQVLSPNAQKSGPPPRPESPSPALPPKKSKVPPPRPAPPRAAQPTGGFGSGGGGGFADFDDFDNKLHHIPSAPSPSATALSPLPPTLPAPIPVVSGSSLLDSFTLFDDPGQIHKQAASTPNPTPITVPTVHTLLQTSLSTPAAPSPALASLSTSGSGSVAGAGAHLPSSVTITTAPSLNNQHLSRSNTPLQNQRTADVKLETKAVVSVFDAFGEIGTRKAPTPSLITGPTDFKDDPFKDYRYEDPFSIKDPFAEEGEEELSEGKGADHKRNFAEDFSSGDEIGSAAKTLSNIVNNNSIKPKAATPLNNDLLQQFDAFNLNSSPTPSHHSGTSYHSNSKPNHDSQTALDAFADFDDFAATLATTGGSGAATTATTTGNTKLNNSFFDAFNDNFSVIQSSSVPTGVVRPNDQRAKAFDAFNDNFEDQFKTSPNANFAKFDGFEAHNFSSDFGNASFGTTGKEKQNGQVDKKFQSKEPVKDKFAADYSKPESFDADLEEALKRSVLDN
Protein: Occludin (Q16625)
Organism: Homo sapiens (Human)
Function: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:9175707}; Multi-pass membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:9175707}.
Interaction partners:
- Claudin-5
- Tight junction protein 2
- Claudin-1
- Tight junction protein 1
- Claudin-7
- Tight junction protein ZO-3
- Junctional adhesion molecule A
- Claudin-3
- Claudin-4
- Cingulin
Sequence:
MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGGSVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIYALCNQFYTPAATGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEVVQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYETDYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT
Protein: Folylpolyglutamate synthase, mitochondrial (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) (Q05932)
Organism: Homo sapiens (Human)
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Unsubstituted reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates.
Subcellular location: [Isoform 1]: Mitochondrion inner membrane {ECO:0000269|PubMed:16169100}. Mitochondrion matrix {ECO:0000269|PubMed:16169100, ECO:0000269|PubMed:8408020, ECO:0000269|PubMed:8662720}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:8662720}.
Interaction partners:
- Dihydrofolate reductase 2, mitochondrial
- Dihydrofolate reductase
- Thymidylate synthase
- Gamma-glutamyl hydrolase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
Sequence:
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRDPAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEEQASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSPPKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
Protein: Sulfhydryl oxidase 1 (rQSOX) (rSOx) (EC 1.8.3.2) (FAD-dependent sulfhydryl oxidase-2) (SOx-2) (Quiescin Q6) (Q6IUU3)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration (By similarity).
Subcellular location: [Isoform 1]: Golgi apparatus membrane {ECO:0000250|UniProtKB:O00391}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00391}. Secreted {ECO:0000250|UniProtKB:O00391}. Note=A small proportion is secreted, probably via a proteolytic cleavage that removes the membrane anchor. {ECO:0000250|UniProtKB:O00391}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:11278790, ECO:0000269|PubMed:12354420}.
Interaction partners:
Sequence:
MRRCGRHSGPPSLLLLLLLLPPLLLSVPGAYAARLSVLYSSSDPLTLLDADTVRPAVLGSSSAWAVEFFASWCGHCIAFAPTWKELANDVKDWRPALNLAVLDCADETNSAVCREFNIAGFPTVRFFKAFSKNGTGTALPAAGANVQTLRMRLIDALESHRDTWPPACPPLEPAKLKDINEFFTRSKAEYLALIFEREDSYLGREVTLDLSQFHAVAVRRVLNSESDVVSKFAVTDFPSCYLLLRNGSVSRVPVLVESRPFYTSYLRGLPGLTREAPPTTAAPVTPDKIAPTVWKFADRSKIYMADLESALHYILRVEVGKFSVLEGQRLVALKKFVAVLAKYFPGQPLVQNFLHSINDWLQKQQKKKIPYSYFKAALDSRKENAVLAEKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAHRYSEAHPQEPADGQEVLQAMRSYVQSFFGCRDCANHFEQMAAASMHQVKSPSNAVLWLWTSHNRVNARLSGALSEDPQFPKVQWPPRELCSACHNEVNGQVPLWDLGATLNFLKAHFSPANIVRDPPAPGPASRRGTQDPEASPNLVMDTLKLETGNSVLGHEQAASAASPGATALDVPAGKPEASGPQELNAGLSMGGASPGQGPPEHTEELLRDVQENAQGQQHLSKRDTEALLLPEVNHLQGPLAPRRGGHSPKQLASILEGEPEALAIQGRRQWLQVLGGGVSFLDISLCVGLYSVSFMGLLAMYTYFRARMRTPKGHVSYPTA
Protein: Cilia- and flagella-associated protein 65 (A8JFU2)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: May play a role in flagellar formation and mobility.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:15998802}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q3V0B4}.
Interaction partners:
Sequence:
MSSSRGSLRALLLAAAAAAAAAAGAVSNKLGYWFSCRRFGLDCPEQLEWRHWNPGTEYVKQLVLKNVSTSVLKIRFKQPTSKAFGMDFPEPFKLRPGMSQPLKVVFRPLKQQHYSDNVELFVGNVSCLVPVHAYTPVTHIEVPPALDFGFTPTKETVTAQLPVRNTGDVRVDVLWKLDAPFSISPLFASLAPGEVVAFTASFTPPEACSYTASAACQLESGAAAICKISGIGKFPYLSVEQAGVDFGAVVVGQRVERLVRFGNHSVVPAHFAVTHDEAGPDDGVFTVGPARGTLGPEEYSMLKLSYTPRATGTFSSETFHIGTAGGNRVALNLRGTAVAPLVTLSTRAFNFGNVAAGATASRVLYIRNHSAVPVPYDFQVDPLDVFAISRTRGVLAPDSTAHVTITFRPMAGLAANLWRRVTLLLKDAEPQGVDLVATAYTDKSRPPPLSQRHVERYMARVLSGGPAVEESQLDSKPPSAATGDPAAALTVDSDALDFGSCSRLSASEYRSVTVTNHTPAKLTAFVLVPEWADPGAAPGDAPQRVFQVFPESADMRPYGQATFKVAFRPPRDAAFFSQQLALVAHTKSQRNFRLVAEHQVLPAWCVPLRATGNTFLHSNPEFGPKVELSSRAVAFPPCRPGERVHQTLLIANSGDTPVAFSFGAAGAALGPLFSAKPAAGVVPPQGHVLVALRFAPTDTRPAAANALVTFNGVASNAVSVSLRGAAHTPRLTTDLPSSTLYFRPTCVGASSQRAVTLHNPSRVPVAFRWRLPARLQGLVTVSPAAGALRGNESVQLQWSFTPAAQKLYEARAACLVMSPPEAANGNAAGATASAASLFPGAGLATGIEWYEGAGATAALAGMGEEEAADAVLLSLVGEGTQGAVALEPPSLELGDLRVGHPVRRPLLLQNCSDGVLRYSLEVGPAEDDQPPAGDATLVDFTAGLDSAAEGGVGGGAGGAGGAALECWVDEPEGALPARASKTVMVTLFPRYRKRYSLQVRCRSSTVAPLLTGPNRPPSGGAGPRPLDAGSEAAAAAAAAAAAAAAPLPPPVIAPLTASTTFPTLEVTDVYCEGLPKQLLWQLLGLNDLNHHLRTEVTATELRLRAAQDRGALTTEAASAAMRPFLMEFGTHGLGGRPRVVHVEISNPTPLPASWQLHSFDDPDGVELENWVEPGRPRTEGERMRDLIAEYKLFEMRPRSGELEPGARCTVTIEFRPSVEGSFELPVFLHITDGKRLRLQLQAVTTPEPLQLLALPPPLRTFRLEPVALGERAPPLQMYVLRNGGPAPLHWRLDTAPLAALAEASWGHPVLELVGPEEGDIEEGGVAAINWRFSPLEAKEYRVEVPVLLGDGGIEVIELLGRGFAPPPAPPHGAAAVQLIGPGAATSPAAPTTAAEDDDTPAAALDSVGGDAEAEAARAAAAADRDWITWRGLSSAPSAGMAGRLALVDHDLVSLGVTPVRGLTRRIIVLTNKSRYPLAFDWDLGCLAPPPPPGLAATQRAAAASAMMGLGGGSLLPASQLQLLAGRPLQGALAISPAAGSLEPGERLVCRVSLHAGVTPQVFEGEVRCHVRIDDDAVAEAEAAAAAAAAAGAAAVAAELPFVEQVEEVIAEAPVRGPPAPPPAVAAAQRASRLRSRLPVHQYMTTAVRTRIEPLNAAFTATMEARTRRLADATRPPSWPEPQSISVTLRGRILDERQLGALRYVPPHERAAARAAVVAGAAWVPPAMVPFWEEEGRSTPAVSAQPSSQGGGGYGVGGYGGGYGSGGSQGGEASVAPSGGDPGGYSPRGGMADSWPSLEPGLGMEETVVGPPTVGLDLSLSLQHAGGAGGAPGGDGDSDSRPGTPSMTAAAHHHHHHPRHAGPAPGSGTAEVMEVTFSGDQQPTGGPMPSPPSISGAPDPDSATPDDDFATSDAAVNAAAAVRAAGGGMGSPQPVDPGGSAAAAASELAPPALPPAPPRGGDIEYDALVSAREVLAGLFAELMEDADVVRAVAFLPEHEVPSFAEVRATPPPCYDPAVRAAAEAARAEAEARAAAEAATKAAAEAEAGAAFAIPAAAAQAATEPPALEDELAADTELARVLVAPEWRAFADFVLESAVLGLMQESAAGDWEMPEEEVGR
Protein: S-adenosylmethionine synthase (EC 2.5.1.6) (A0A1D8PF68)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine-homocysteine S-methyltransferase
- S-adenosylmethionine decarboxylase proenzyme
- Adenosylhomocysteinase
- 6,7-dimethyl-8-ribityllumazine synthase
- aromatic-amino-acid transaminase
- L-methionine
- Histidine biosynthesis trifunctional protein
- Adenylyl-sulfate kinase
- Methylenetetrahydrofolate reductase
Sequence:
MTTSKETFLFTSESVGEGHPDKICDQVSDAILDACLAVDPLSKVACETAAKTGMIMVFGEITTKAQLDYQKIIRDTIKHIGYDDSEKGFDYKTCNVLVAIEQQSPDIAQGLHYEKALEELGAGDQGIMFGYATDETDEKLPLTILLAHKLNAALASARRSGSLPWLRPDTKTQVTIEYEKDGGAVIPKRVDTIVISTQHAEEITTENLRKEIIEHVIKKVIPEHLLDDKTIYHIQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDFSKVDRSAAYAARWVAKSLVTAGLAKRALVQFSYAIGVAEPTSIYIDTYGTSKLSTEALVEIIKNNFDLRPGVIVKELDLARPIYFKTASYGHFTNQENSWEQPKKLKF
Protein: Transcription factor, putative (Q387K4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor TFIIIB component B'' Myb domain-containing protein
- TATA box-binding protein-like 1
- Uncharacterized protein
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC3
- Plastid-encoded RNA polymerase subunit alpha
- RNA polymerase III subunit Rpc25 domain-containing protein
- DNA-directed RNA polymerase subunit
Sequence:
MSSCSHPTSAQYVDRARGTITCTLCGDIVQDPQLELDPIFARGDKGGRLRALGHLRPTRGSVSVRMPSARPSIEAARRGMATIARQLDVSDDMVEAALGLYKLAVSLNAVSGARPAILCAVLYAMCRRERTSHMVFDFADATGESPYDILSYMHLVCEATRTEVPVIDPSCVVHRFAEQMNLGQMTRSVVVCALKVLRAMHDDWIACGRRPLGVCVAALLVACYMFNIPRSPDEVCGFVRLTAGTISRRLDEFAATSTAALDSIDKYTRDDSSLPPAFTSATKKYDGDKRDAELRQLSAMYYELVAEAKVSTPSTPDRCEKWRHFLLCHCALEGKTPSDASLDLTTLTPQQQLQILGLPNTKPIDSSKARASVKEEEDKIMVKLERVKQEPVRQEPSTPEKGAPPVPNAGMSLSEMTDYYRMLMTRDPNVLDIRRDFDMEAVNPDDVVPAPQLPEEEAVVKTEGAAEAKFKIDPCLAEVLYDNERTLALPWEFIVLQDPELDDMTDLEPYLVLDNEERLRRQKVGEALYGESWNLGAARTKEEIERLEESHSTRKRRREPIREHLTVQDAVSQALRRRGASTINVSQIDELIPGLAGLENSAEDEWVA
Protein: Heat shock factor binding protein 1 (Heat shock factor-binding protein 1b) (Q6PBV8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Heat shock factor protein 1 isoform X1
- WASH complex subunit 3
- Uncharacterized protein.
- DnaJ homolog subfamily C member 11
- DnaJ
Sequence:
MAETDPKSVQDLTAVVQTLLQQMQDKFQTMSDQIIGRIDEMSTRIDDLEKNIADLMTQAGVEEIEGENKVKEGDAS
Protein: Esterase/lipase (EC 3.1.1.3) (Triacylglycerol lipase) (P77909)
Organism: Mycobacterium tuberculosis
Interaction partners:
Sequence:
MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA