wanglab/gogpt-training-data huggingface dataset:
Protein: Inositol 1,4,5-triphosphate receptor associated 1 (Inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate) (JAW1-related protein MRVI1) (Murine retrovirus integration site 1 protein) (Protein MRVI1) (Q9WUX5)
Organism: Mus musculus (Mouse)
Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15388327}. Sarcoplasmic reticulum {ECO:0000269|PubMed:15388327}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- cGMP-dependent protein kinase 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- cGMP-dependent protein kinase 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
Sequence:
MGRSLTCPFGISPACGAQASWSIFGVGTAEVPGTHSHSNQAAAMPHIPEDEEPPGEPQAAQTQDSPSAGPFPSPPTIVLTGDASSPEGETDKNLVNRAPSPHRRLSHRHLKVSTASLTSVDPSGHVIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSLGDSPSAVSPNLSSGASPASSRSCSLTISTSPGLDICSGPQSPLPGAPPQQKGHEDGVSSPCPGEPNVSKGLADLKQNDQRKVSQGRLAPRSPTVEKTKELTVEQKENFDPLQHVEATPMAQASGASISGKMALNSPQPGPAEMELGRQLLKTAREGNPLPRTTAQGSGGTVSPHSLGQGSAGEPMGPKAGSKAELRSPVSRPPLIRGVSWDSSPEEPGPLLQKVLAKLPLAEEEKRFPGKAKPAKPPGLKDFQIQVQPVRMQKLTKLREEHILMRNQNLVGFKLPELSEAAEQDKGVSPELAPAAEEEESKSGLDVMPNISDILLRKLRVHKSLTGSAPPLTEKEVENVFVQLSLAFRNDSYTLESRINQAERERNLTEENTEKELENFKASITSSANIWYHCEHRETYQKLLEDIAVLHRLAARLSSRAEVVGAVRQEKRMSKATEVMMQYVENLKRTYEKDHAELMEFKKLANQNSSRSCGPSEDGVPRTARSMSLTMGKNMPRRRVSVAVVPKFNALNLPGQAPSSSPMPSLPALSESSNGKSSISVSPALPALLENGKTNAEANCEVGAPVPLPSCLEETSQETKAKAEEEAYSKGYQEGVKKTEELQDLKEEEEEEQKTESPEEPEEVEETQEDEKDQGSSKLEELVHFLQVMYPKLCQHWQVIWMMAAVMLVLSVVLGLYSSYNSCTEEADGPPGRSTCSAAQRDSWWSSGLQQELPAEQ
Protein: Flavonol 3-O-glucosyltransferase UGT71C1 (EC 2.4.1.91) (Flavonol 7-O-beta-glucosyltransferase UGT71C1) (EC 2.4.1.237) (UDP-glycosyltransferase 71C1) (O82381)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses quercetin 7-O-glucosyltransferase and 3'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives. Glucosylates other secondary metabolites in vitro like trans-resveratrol, curcumin, vanillin and etoposide.
Interaction partners:
Sequence:
MGKQEDAELVIIPFPFSGHILATIELAKRLISQDNPRIHTITILYWGLPFIPQADTIAFLRSLVKNEPRIRLVTLPEVQDPPPMELFVEFAESYILEYVKKMVPIIREALSTLLSSRDESGSVRVAGLVLDFFCVPMIDVGNEFNLPSYIFLTCSAGFLGMMKYLPERHREIKSEFNRSFNEELNLIPGYVNSVPTKVLPSGLFMKETYEPWVELAERFPEAKGILVNSYTALEPNGFKYFDRCPDNYPTIYPIGPILCSNDRPNLDSSERDRIITWLDDQPESSVVFLCFGSLKNLSATQINEIAQALEIVDCKFIWSFRTNPKEYASPYEALPHGFMDRVMDQGIVCGWAPQVEILAHKAVGGFVSHCGWNSILESLGFGVPIATWPMYAEQQLNAFTMVKELGLALEMRLDYVSEDGDIVKADEIAGTVRSLMDGVDVPKSKVKEIAEAGKEAVDGGSSFLAVKRFIGDLIDGVSISK
Protein: At4g19350 (Embryo defective 3006) (Q8LAF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEKPGHETDIAGSRRTHLKKSFKSTLRHLLTACSKQDFVDIFSKFSGAEQELLFQLYTRVVVNLHQTIEEEFDEQCHETQVGPILDTVEELVEEQSLDPLFSDKTDVMAIAYDLTTSKKNEIQKLTVLLQRAEEQNRQKEARISMLKKQTQDLSGTADRIEKLNAGVSGYFEGKDKLPPI
Protein: X-linked lymphocyte-regulated gene 4 (Q9JJQ4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASKIKGRPPKQPKVTPALPSNDSQQLHENNPGNNLALETCGESSSSHGTGGPKPGPSKKTLNERKRKYGVSVNKTVQNIEWNVDHFLKVQHERRQELYKDYSHQFLTLVMMWNIDVDQIKKQAGKLSDILDEQQKLFQQFQSIHMQKIEEFKELCDRHLKNLQAIKCCRRKAIIEEARKLMDYLGKRVTEETVHVTSRKQRMVFNHHFYPC
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (C0PVB3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO12235p1
- Sulfhydryl oxidase
- Cytochrome c oxidase assembly factor 5
- Cytochrome c oxidase copper chaperone
Sequence:
MRMLFMIFTIAERSFKILELPTTPTLLLRRQSHNYGYDYISPTHIELSREATRLVIRRLQRTVLRLIRDPDFIMSAEANPEMDKEHHESPFAANRKAGASGAGKQDSNCRTCNDFKSWSKQQRLISNVQSAKVKHMAAAEKLTVNAAEDPLPRDDCPLDKVRLGISTWGLLHTMAAFYSDNPTDTEKRDMKTFFEVLSRLYPCEFCAKDFRTDLDVNPINVNSQKELALWLCKFHNRVNDKLGKPLFDCTKVNERWRDGWLDGSCD
Protein: ORF 23 (Q98141)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MLRVPDVKASLVEGAARLSTGERVFHVLTSPAVAAMVGVSNPEVPMPLLFEKFGTPDSSTLPLYAARHPELSLLRIMLSPHPYALRSHLCVGEETASLGVYLHSKPVVRGHEFEDTQILPECRLAITSDQSYTNFKIIDLPAGCRRVPIHAANKRVVIDEAANRIKVFDPESPLPRHPITPRAGQTRSILKHNIAQVCERDIVSLNTDNEAASMFYMIGLRRPRLGESPVCDFNTVTIMERANNSITFLPKLKLNRLQHLFLKHVLLRSMGLENIVSCFSSLYGAELAPAKTHEREFFGALLERLKRRVEDAVFCLNTIEDFPFREPIRQPPDCSKVLIEAMEKYFMMCSPKDRQSAAWLGAGVVELICDGNPLSEVLGFLAKYMPIQKECTGNLLKIYALLTV
Protein: Arabinose 5-phosphate isomerase KdsD (API) (L-API) (EC 5.3.1.13) (P45395)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). KdsD is not essential in the KDO biosynthesis and can be substituted by GutQ. Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
Interaction partners:
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
- 2-dehydro-3-deoxyphosphooctonate aldolase
- Inner membrane protein YrbG
- 3-deoxy-manno-octulosonate cytidylyltransferase
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipopolysaccharide export system ATP-binding protein LptB
- Tetraacyldisaccharide 4'-kinase
- Lipopolysaccharide export system protein LptC
- Lipid-A-disaccharide synthase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
Sequence:
MSHVELQPGFDFQQAGKEVLAIERECLAELDQYINQNFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMVTPQDVVIAISNSGESSEITALIPVLKRLHVPLICITGRPESSMARAADVHLCVKVAKEACPLGLAPTSSTTATLVMGDALAVALLKARGFTAEDFALSHPGGALGRKLLLRVNDIMHTGDEIPHVKKTASLRDALLEVTRKNLGMTVICDDNMMIEGIFTDGDLRRVFDMGVDVRQLSIADVMTPGGIRVRPGILAVEALNLMQSRHITSVMVADGDHLLGVLHMHDLLRAGVV
Protein: Peroxidase 51 (Atperox P51) (EC 1.11.1.7) (ATP37) (Q9SZE7)
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:
- At4g25315
- WAT1-related protein At5g40240
- Similarity to Ta11-like non-LTR retroelement protein
- At4g01000
- Berberine bridge enzyme-like 11
- Pentatricopeptide repeat-containing protein At4g13650
Sequence:
MVVMNKTNLLLLILSLFLAINLSSAQLRGDFYAGTCPNVEQIVRNAVQKKIQQTFTTIPATLRLYFHDCFVNGCDASVMIASTNTNKAEKDHEDNLSLAGDGFDTVIKAKEAVDAVPNCRNKVSCADILTMATRDVVNLAGGPQYAVELGRRDGLSSSASSVTGKLPKPTFDLNQLNALFAENGLSPNDMIALSGAHTLGFAHCTKVFNRLYNFNKTNNVDPTINKDYVTELKASCPQNIDPRVAINMDPNTPRQFDNVYYKNLQQGKGLFTSDQVLFTDSRSKPTVDLWANNGQLFNQAFISSMIKLGRVGVKTGSNGNIRRDCGAFN
Protein: Proteasome subunit alpha type-7-A (20S proteasome alpha subunit D-1) (Proteasome component 6A) (Proteasome subunit alpha type-4) (TAS-G64) (P30186)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the association of the SCF(TIR1) E3 ubiquitin ligase complex with the proteasome.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11387208}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-2-B
- Proteasome subunit beta type-1
- Proteasome subunit beta type-3-B
- Proteasome subunit beta type-3-A
- Proteasome subunit beta type-7-B
- Proteasome subunit beta type-7-A
- Proteasome subunit alpha type-2-A
Sequence:
MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLAVEKKSTPKLQDSRSARKIVSLDNHIALACAGLKADARVLINKARIECQSHRLTLEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTRIPALYQTDPSGTFSAWKANATGRNSNSIREFLEKNYKESAGQETVKLAIRALLEVVESGGKNIEVAVMTREEGVLKQLEEEEIDIIVAEIEAEKAAAEAAKKGPAKET
Protein: Neural cell adhesion molecule 2 (H9KV31)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
ALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVVVQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTISDNRFAMLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAISMPQKSFNATAERGEEMTFSCRASGSPEPAISWFRNGKLIEENEKYILKGSNTELTVRNIINSDGGPYVCRATNKAGEDEKQAFLQVFVQPHIIQLKNETTYENGQVTLVCDAEGEPIPEITWKRAVDGFTFTEGDKSLDGRIEVKGQHGSSSLHIKDVKLSDSGRYDCEAASRIGGHQKSMYLDIEYAPKFISNQTIYYSWEGNPINISCDVKSNPPASIHWRRDKLVLPAKNTTNLKTYSTGRKMILEIAPTSDNDFGRYNCTATNHIGTRFQEYILALADVPSSPYGVKIIELSQTTAKVSFNKPDSHGGVPIHHYQVDVKEVASEIWKIVRSHGVQTMVVLNNLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKLSITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAVIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERVTNHEDGSPVNEPNETTPLTEPEKLPLKEEDGKEALNPETIEIKVSNDIIQSKEDDSKA
Protein: Mitogen-activated protein kinase PMK1 (MAPK PMK1) (EC 2.7.11.24) (Q92246)
Organism: Pyricularia oryzae (Rice blast fungus) (Magnaporthe oryzae)
Function: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. Central regulator of appressorium development that acts downstream of the cAMP signal. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. Regulates expression of secreted fungal effector proteins implicated of host immune defenses, preventing reactive oxygen species generation and excessive callose deposition at plasmodesmata. Furthermore, controls the hyphal constriction required for fungal growth from one rice cell to the neighboring cell, enabling host tissue colonization and blast disease. Targets downstream of the PMK1-MAPK pathway include transcription factor MST12 and pathogenicity-related genes GAS1 and GAS2, both of which are expressed during appressorium formation, even if regulation of MST12 is not associated with expression of GAS1 or GAS2.
Interaction partners:
Sequence:
MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQENNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDDEPTAPPIPEEFFDFDKHKDNLSKEQLKQFIYQEIMR
Protein: Phosphatidylserine synthase 2 (PSS-2) (PtdSer synthase 2) (EC 2.7.8.29) (Serine-exchange enzyme II) (Q9Z1X2)
Organism: Mus musculus (Mouse)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine. Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position. Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein {ECO:0000269|PubMed:10938271}. Membrane {ECO:0000269|PubMed:23071296}. Note=Highly enriched in the mitochondria-associated membrane (MAM).
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Ethanolaminephosphotransferase 1
- Phosphatidylserine synthase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase A1 member A
- Phospholipase D1
- Group XIIA secretory phospholipase A2
- Lysophospholipid acyltransferase LPCAT4
Sequence:
MRRGERRVAGGSGSESPLLKGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCALGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQARAVNNRDGHPGPDDDLLGTGTAEEEGTTNDGVTAEEGTSAAS
Protein: Neuronal membrane glycoprotein M6-b (M6b) (Q13491)
Organism: Homo sapiens (Human)
Function: May be involved in neural development. Involved in regulation of osteoblast function and bone formation. Involved in matrix vesicle release by osteoblasts; this function seems to involve maintenance of the actin cytoskeleton. May be involved in cellular trafficking of SERT and thereby in regulation of serotonin uptake.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Colocalizes with SERT at the plasma membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MKPAMETAAEENTEQSQERKGCFECCIKCLGGVPYASLVATILCFSGVALFCGCGHVALAGTVAILEQHFSTNASDHALLSEVIQLMQYVIYGIASFFFLYGIILLAEGFYTTSAVKELHGEFKTTACGRCISGMFVFLTYVLGVAWLGVFGFSAVPVFMFYNIWSTCEVIKSPQTNGTTGVEQICVDIRQYGIIPWNAFPGKICGSALENICNTNEFYMSYHLFIVACAGAGATVIALLIYMMATTYNYAVLKFKSREDCCTKF
Protein: DNA replication ATP-dependent helicase/nuclease DNA2 (DNA replication ATP-dependent helicase-like homolog) [Includes: DNA replication nuclease DNA2 (EC 3.1.-.-); DNA replication ATP-dependent helicase DNA2 (EC 3.6.4.12)] (Q8QHA5)
Organism: Xenopus laevis (African clawed frog)
Function: Key enzyme involved in DNA replication and DNA repair in nucleus and mitochondrion. Involved in Okazaki fragments processing by cleaving long flaps that escape fen1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit dna2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA, while the 3'-ssDNA cleavage is prevented by the presence of RPA. Also involved in DNA replication checkpoint independently of Okazaki fragments processing (By similarity). Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is subject to debate. According to various reports, the helicase activity is weak and its function remains largely unclear. Helicase activity may promote the motion of dna2 on the flap, helping the nuclease function.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51530}. Mitochondrion {ECO:0000250|UniProtKB:P51530}.
Interaction partners:
Sequence:
MEPVSAECHLPPEDDLLEMMMEQSFTEPEEKSQDKPTRKIIPKTKLCKGVNNRYCVLHIKEVYAQREEKHLTITASQEGDDLELCILKDDWVALQIKPGDIIHLEGNCSVDNTWTISRDTGYLILYPDLLISGTSIANGIRCLRRSVLSEKFKVCDKGSRQMLNGTMLHDIFQRATTCGFTDSVLQELAHHTVHGPKYLKEMYQLKLNQADVMGEIQEYLPSLSKWATDFMTHPLNQQQINRTKSTAGDPTETTKVSEFLDIEENIWSPRFGLKGKIDVTARVKIHQKSKAHLKIMPLELKTGKESNSIEHRSQVVLYTLLSQERREDPEAGLLLYLKTGNMYTVPGNRLDRRELLKIRNELSYYLTNVLHKSDNGSKETTLASLPAMIADRQACKYCSQMRNCALYNRSVEQQTENCYIPPEMIPVVQKETEHLTEDHLQYFRLWYLMCTLEANSKDSKMGRKNIWMMSSSEREEDGQCIGNLIRTGHVQTISDVQYLHSFQRRSGSVPATNLASGDRVVVSGEERFLALSTGYIKEVKDENITCILDRSLVKLPEDLLFRLDHEEGGGGLEFHLGNLSRLMENSSVSEKLRKLIIDFSKPNFVQHLSSILPPDAKDIVASILRGLNKPQKQAMKRVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLKKFQVGFLRLGRTQKLHPDVQEFSEEEICKAKSIKSLSALEELYNSQPVVATTCMGVNHPIFTRRRFDFCIVDEASQISQPICLGPLFFADRFVLVGDHQQLPPLVKSAEARELGMSESLFKRLERNQEAVVQLTVQYRMNSKIMALSNKLVYEGRLECASDRVSNAVVQLPHIKTLLLELEFRESQESMWIKDVLEPSNPVCFLNTEKIPALETEEKGGISNWIEAKLVFHLTKLYLKAGCRPSDIGIIAPYRQQLKMISNYFNSLSASAVEVNTVDKYQGRDKSVIIVSFVRSNIDGKLGDLLKDWRRLNVALTRAKHKLIMLGCVPTLNRFDCLEQLICNLKTENQIYDLPEGAHEHFPV
Protein: Oxaloacetate acetylhydrolase (EC 3.7.1.1) (Q7Z986)
Organism: Aspergillus niger
Interaction partners:
Sequence:
MKVDTPDSASTISMTNTITITVEQDGIYEINGARQEPVVNLNMVTGASKLRKQLRETNELLVCPGVYDGLSARIAINLGFKGMYMTGAGTTASRLGMADLGLAHIYDMKTNAEMIANLDPYGPPLIADMDTGYGGPLMVARSVQQYIQAGVAGFHIEDQIQNKRCGHLAGKRVVTMDEYLTRIRAAKLTKDRLRSDIVLIARTDALQQHGYDECIRRLKAARDLGADVGLLEGFTSKEMARRCVQDLAPWPLLLNMVENGAGPVISVDEAREMGFRIMIFSFACITPAYMGITAALERLKKDGVVGLPEGMGPKKLFEVCGLMDSVRVDTEAGGDGFANGV
Protein: ETS domain-containing protein Elk-1 (P19419)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to purine-rich DNA sequences. Forms a ternary complex with SRF and the ETS and SRF motifs of the serum response element (SRE) on the promoter region of immediate early genes such as FOS and IER2. Induces target gene transcription upon JNK-signaling pathway stimulation (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
- Serum response factor
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 11
- Protein kinase C alpha type
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
Sequence:
MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSTMPNVAPAAIHAAPGDTVSGKPGTPKGAGMAGPGGLARSSRNEYMRSGLYSTFTIQSLQPQPPPHPRPAVVLPSAAPAGAAAPPSGSRSTSPSPLEACLEAEEAGLPLQVILTPPEAPNLKSEELNVEPGLGRALPPEVKVEGPKEELEVAGERGFVPETTKAEPEVPPQEGVPARLPAVVMDTAGQAGGHAASSPEISQPQKGRKPRDLELPLSPSLLGGPGPERTPGSGSGSGLQAPGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP
Protein: Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase) (Q9NRD8)
Organism: Homo sapiens (Human)
Function: Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15591162, ECO:0000269|PubMed:26301257}; Multi-pass membrane protein {ECO:0000269|PubMed:15591162}. Cell junction {ECO:0000269|PubMed:26301257}. Note=Localizes to the apical membrane of epithelial cells. Localizes on internal membrane structures under resting conditions, translocates to the plasma membrane and cell-cell junctions upon challenge with enteric pathogens, such as Escherichia coli. {ECO:0000269|PubMed:26301257}.
Interaction partners:
- Dual oxidase maturation factor 2
- Dual oxidase maturation factor 1
- NADPH oxidase 1
- Dual oxidase 1
- Neutrophil cytosol factor 2
- NADPH oxidase 3
- Cytochrome b-245 light chain
- Iodotyrosine deiodinase 1
- NADPH oxidase 4
- Neutrophil cytosol factor 4
Sequence:
MLRARPEALMLLGALLTGSLGPSGNQDALSLPWEVQRYDGWFNNLRHHERGAVGCRLQRRVPANYADGVYQALEEPQLPNPRRLSNAATRGIAGLPSLHNRTVLGVFFGYHVLSDVVSVETPGCPAEFLNIRIPPGDPVFDPDQRGDVVLPFQRSRWDPETGRSPSNPRDLANQVTGWLDGSAIYGSSHSWSDALRSFSGGQLASGPDPAFPRDSQNPLLMWAAPDPATGQNGPRGLYAFGAERGNREPFLQALGLLWFRYHNLWAQRLARQHPDWEDEELFQHARKRVIATYQNIAVYEWLPSFLQKTLPEYTGYRPFLDPSISPEFVVASEQFFSTMVPPGVYMRNASCHFRKVLNKGFQSSQALRVCNNYWIRENPNLNSTQEVNELLLGMASQISELEDNIVVEDLRDYWPGPGKFSRTDYVASSIQRGRDMGLPSYSQALLAFGLDIPRNWSDLNPNVDPQVLEATAALYNQDLSQLELLLGGLLESHGDPGPLFSAIVLDQFVRLRDGDRYWFENTRNGLFSKKEIEDIRNTTLRDVLVAVINIDPSALQPNVFVWHKGAPCPQPKQLTTDGLPQCAPLTVLDFFEGSSPGFAITIIALCCLPLVSLLLSGVVAYFRGREHKKLQKKLKESVKKEAAKDGVPAMEWPGPKERSSPIIIQLLSDRCLQVLNRHLTVLRVVQLQPLQQVNLILSNNRGCRTLLLKIPKEYDLVLLFSSEEERGAFVQQLWDFCVRWALGLHVAEMSEKELFRKAVTKQQRERILEIFFRHLFAQVLDINQADAGTLPLDSSQKVREALTCELSRAEFAESLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEDKSRLMFTMYDLDENGFLSKDEFFTMMRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSELRFTQLCVKGGGGGGNGIRDIFKQNISCRVSFITRTPGERSHPQGLGPPAPEAPELGGPGLKKRFGKKAAVPTPRLYTEALQEKMQRGFLAQKLQQYKRFVENYRRHIVCVAIFSAICVGVFADRAYYYGFASPPSDIAQTTLVGIILSRGTAASVSFMFSYILLTMCRNLITFLRETFLNRYVPFDAAVDFHRWIAMAAVVLAILHSAGHAVNVYIFSVSPLSLLACIFPNVFVNDGSKLPQKFYWWFFQTVPGMTGVLLLLVLAIMYVFASHHFRRRSFRGFWLTHHLYILLYALLIIHGSYALIQLPTFHIYFLVPAIIYGGDKLVSLSRKKVEISVVKAELLPSGVTYLQFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAVGPWTTRLREIYSSPKGNGCAGYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSLGSQMLCKKIYFIWVTRTQRQFEWLADIIQEVEENDHQDLVSVHIYVTQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLVNRQDRAHFMHHYENF
Protein: Family with sequence similarity 64 member A isoform 2 (Family with sequence similarity 64, member A, isoform CRA_c) (A0A0S2Z5C7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASRWQNMGTSVRRRSLQHQEQLEDSKELQPVVSHQETSVGALGSLCRQFQRRLPLRAVNLNLRAGPSWKRLETPEPGQQGLQAAARSAKSALGAVSQRIQESCQSGTKWLVETQVKARRRKRGAQKGSGSPTHSLSQKSTRLSGAAPAHSAADPWEKEHHRLSVRMGSHAHPLRRSRREAAFRSPYSSTEPLCSPSESDSDLEPVGAGIQHLQKLSQELDEAIMAEESGDIVSLIHD
Protein: Transcription activator, putative (Q57Z97)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proliferating cell nuclear antigen
- Histone H2A
- Histone H3 variant
- Histone H3, putative
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- Histone H4
- Histone H4
- Histone H2A
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
Sequence:
MKFENPVAAFLESRNPARASLKRNRTFVDFSALNSEAETPVADVGASDHDVTSLVGAAEEEDWTNVATVSSSPVKVLLLPDDGEEEEEELRLLLGDRGKVFVRPKDPPVRQESSTDVTSEENDVANVSADVDDKVKQNQVSLGDVLWEKLSNADREELAERFERHFLWELSKDVELACTYQPFFTSKTMRLIQDGVQSSQFLPPKILSRETTNSPDGYVLRPYQFDGVQFLVNRFHSGMPSVLGDDMGLGKTAQVSAFLNGLKTLYNVGGPHLIVVPLNTVTGWARELSRWAPTLHVVSYNGDGKERAMLRGGRGSKRGVFVTTPAILRRDRGFFCKRSWVVAVVDEAHMLKESTATISHVARRITACFRLAMTGTPIQNSVKEVWSIMMFLYPSFCALYERNGGDTISAANNCAKLLQHVMLRRTKSTTDLGIPPRVDEPVIMVEPTRIQRALLLRMTERALREDGGVFQNHLAHQRVICSHPLALRLLTMEGRDSLTRVEDRLSACGISLDERSIIAPSGKMIELDRMLREFHMNGHRCLIFSNFTCVLDLLQGLCILRDYSHERIDGSAQRVERELSMARFNGPASKVFVFLISTMSGGVGITLTGADIVILFDANFNPQMDRQAADRAHRIGQTRTVRVFRLCCKETVEERIQDIALRRLSLGEFVVDGAAVGDDNSATEIPGSYIQQLFSTSTSGENREEHWSVGSKDHRDGLTEEQQGMKKDDPVVIDSGAGEGVESAQVPFVSPQDQSNAEDDAIVDDILRMEAGGASTMLSAKPIGRVARVTIGVTHECFVCGEGMRPLQPLFHCSWCTKAYHAECANERVLPEGVSAPRNWTCPRHRCDLCEKVATTDGALFMCYECPAAFCFDCLDKDYLDLDNDGVNFLHIHRNYPGMETEGMDVRRNVYYIRCFRCSGVLSSSSTSVSGSTEEDTTSIDGSFSESH
Protein: IP21085p (IP21385p) (Lectin-21Ca) (Q9VPS2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFQHANFFLHVFMACGLYGIRAKDVCPRMSTDKEVCLVELAPVLKYISNNHKSHWNSANEVQVNETRKQLAKIEGQEKETNDKIKVIHDNVDNEFNALSAKIKNVKNIQRHLASLELQLQETKKALNLSVEAKKVMPKTEIPSQFQKIGWRHFFIEKKHKVDWFKATSMCHKMGAHLLTIQSEDELDAIRTELKDINDGSHDFWLDINDIAKWGEFISLATGMNPPFLKWHKHRPQVQIHQRCVHLRGGEMMDGKCSEQFLFICQLAVN