wanglab/gogpt-training-data huggingface dataset:
Protein: Thiol peroxidase (Tpx) (EC 1.11.1.24) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin) (P9WG35)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Interaction partners:
- Superoxide dismutase
- Alkyl hydroperoxide reductase C
- Glutamine amidotransferase
- Superoxide dismutase
Sequence:
MAQITLRGNAINTVGELPAVGSPAPAFTLTGGDLGVISSDQFRGKSVLLNIFPSVDTPVCATSVRTFDERAAASGATVLCVSKDLPFAQKRFCGAEGTENVMPASAFRDSFGEDYGVTIADGPMAGLLARAIVVIGADGNVAYTELVPEIAQEPNYEAALAALGA
Protein: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase (EC 1.13.11.80) (G4V4T6)
Organism: Amycolatopsis orientalis (Nocardia orientalis)
Function: Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester bond to generate free CoA. It can also use phenylacetyl-CoA (PA-CoA) as substrate.
Interaction partners:
- Enoyl-CoA-hydratase
- 3,5-dihydroxyphenylacetyl-CoA synthase
- Enoyl-CoA-hydratase
- Aminotransferase
- (S)-3,5-dihydroxyphenylglycine transaminase (p-hydroxyphenylglycine transaminase)
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase
Sequence:
MTTDSPTLSLSPGLDHRALAKAAQRVDELLDGLPSPSARTPAQREAASSALDEIRAARTEYVEAHAEEIYDRLTDGRTRYLRLDELVRAAASAYPGLVPTEAQMAAERSRRQAEKEGREIDQGIFLRGILSAPKAGPHLLDAMLRPTARALELLPEFVETGVVRMEAASLERRDGVAYLTLCRDDCLNAEDAQQVDDMETAVDLALLDPAVRVGMLRGGVMSHPRYAGRRVFCAGINLKKLSSGDIPLVDFLLRRELGYIHKIVRGVATDGSWRARVIDKPWLAAVDSFAIGGGAQLLLVFDHVVAASDAYFSLPAATEGIIPGAANYRLSRFTGPRLARQVILGGRRITADEPDARLLVDQVVPPEEMDAAIESALAALDGDAVRANRRMVNLAEEPPDGFRRYMAEFALQQALRIYGADVIGKVGGFAAGSR
Protein: Urocortin 3 (A1YKY5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLMPTYFLLLLLLLLGGPRTSLSHKFYNAGPVFSCLNTALSEVKKNKLEDVPVLSKKNFGYLPTQDPSGEEEDEQKHIKNKRTFSDAVGGNGGRSIRYRYQSQAQPKGKLYPDKVKNDRGTKFTLSLDVPTNIMNILFNIDKAKNLRAKAAANAQLMAQIGKKK
Protein: Septin (Q9U334)
Organism: Caenorhabditis elegans
Interaction partners:
- Septin-type G domain-containing protein
- Anillin-like protein 1
- Myosin-11
- Calponin-homology
- WAPL domain-containing protein
Sequence:
MSSRTANSSSRNDESLRTGQHKENPNYWGFANFPNQVFRRAVKNGFDFTLMVVGRSGLGKSTFINTLFLAEINNLNEKESAPTHPHPSTVRVEEKLVKLVENSVSLNLTLVDTPGFGDAVNNSKCWEPIVNYVESKFFEQFCEETRIDRGEKIVDKCVHLCLYFIEPSGHGLKPIDIELMKHLHGRVNIVPVISKADCLTRDELLRFKKQIVKDAETAEIKLYKFPELEDPYTDKVAIEKLRKALPFAIIGSNMLKEKDGKKIRYREYPWGTVEVENMQHNDFLTLRDMIIRTNLIDMIDVTRNVHYENFRFRQMEGLPKNEKNRDPFTHLEEERRQKEQDLDEKRNTLEKVFTEKTSARKKRSDERMSALEELEQQNKQKIDAKRAEIIRLRHEISELKNGNLTSSQTSLAMYNENNHSQNSTLNSTTKSSPPPTSATSSSSGTMKKRMGGLGLFNRN
Protein: Group IIE secretory phospholipase A2 (GIIE sPLA2) (sPLA2-IIE) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 2E) (Q9NZK7)
Organism: Homo sapiens (Human)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines. In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (By similarity). May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria. Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (By similarity). May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes. Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:11922621}. Cytoplasm {ECO:0000269|PubMed:11922621}. Note=Through binding to heparan sulfate proteoglycan, may be localized to cytoplasmic compartments enriched in anionic phospholipids. {ECO:0000269|PubMed:11922621}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Cytochrome P450 2E1
- Phospholipase A and acyltransferase 3
- Phospholipase B1, membrane-associated
- Lysosomal phospholipase A and acyltransferase
- Acyl-protein thioesterase 1
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Platelet-activating factor acetylhydrolase
- Platelet-activating factor acetylhydrolase IB subunit alpha2
Sequence:
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLGTYNRKYAHYPNKLCTGPTPPC
Protein: Adenylyl cyclase-associated protein (CAP) (P54654)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Twinfilin
- Cofilin-1A
- Actin-interacting protein 1
- F-box domain-containing protein
- Ankyrin repeat-containing protein
- Uncharacterized protein
- Guanylyl cyclase, membrane
- Adenylate cyclase, germination specific
- Adenylate cyclase, aggregation specific
- Fork-head domain-containing protein
Sequence:
MSEATIVELLKRLDQATTRLEAVEKSIASGVASSSSSSSPSSGAAGPSSASVKEFQNLVDQHITPFVALSKKLAPEVGNQVEQLVKAIDAEKALINTASQSKKPSQETLLELIKPLNNFAAEVGKIRDSNRSSKFFNNLSAISESIGFLSWVVVEPTPGPHVAEMRGSAEFYTNRILKEFKGVNQDQVDWVSNYVNFLKDLEKYIKQYHTTGLTWNPKGGDAKSATPAPASSAPAAPVAPAVSSTPVESKKGPGLGAVFGELSKGDGVTSGLKKVTNDMKSKNFTDKSSVVKAADTKVAKVDAPSRPAVFALQGNKWSIEYQVNNKEIVIAEPDSRQTVYIFQCVNSLVQIKGKVNAITLDGCKKTSIVFENAISSCEVVNCNGVEIQVTGRVPSIAIDKTSGCQIYLSKDSLETEIVSSKSSEMNVLIPGATENDDLVELAIPEQYKTSVKGNKLHTESTSHI
Protein: Glutamate-rich protein 1 (Q86X53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAHRKHVFVEKVLQRLFPPVPSGQGKREPQTLAVQNPPKKVTSEKVSQKHAEPLTDTGSETPTARRLYTASGPPEGYVPCWPEPSSCGSPENASSGDDTEDQDPHDQPKRRRIRKHKSKKKFKNPNNVLIEQAELEKQQSLLQEKSQRQHTDGTTISKNKKRKLKKKQQIKRKKAAGLAAKAAGVSFMYQPEDSSNEGEGVGEACEEDGVDTSEEDPTLAGEEDVKDTREEDGADASEEDLTRARQEEGADASEEDPTPAGEEDVKDAREEDGVDTIEEDLTRAGEEDGKDTREEDGADASEEDPTWAGEEEGADSGEEDGADASEEDDTITNEKAHSILNFLKSTQEMYFYDGVSRDAASAALADAAEELLDRLASHSMLPSDVSILYHMKTLLLLQDTERLKHALEMFPEHCTMPPDHARVISAFFSYWITHILPEKSSD
Protein: Guanine-nucleotide exchange factor Cdc24 (D1MYR8)
Organism: Epichloe festucae
Interaction partners:
Sequence:
MAHAPLLRNNTAPVFQSNQSGFKNITQAKTMSSAPRGSQLSGSTAYAGSSTSLSSLASAATVVPGQNGGPIMATTNIINQKADASRSLYQICVSLKQRLSQVPDFTPFLEQLDPSDPVDPLWNLLRTGYPLLTIYNSLQPTEPLKVEDQIASEAKKSKIAIFKFVQACMKELQVPPAQSFVITDLMGNDTSGFVKVTQVVNYVLDLADQRGLLLQLQPYPEDEPAATTGSAQMSYRDHIVKELVDTERKYVQDLENLHDLKKTLEQKGLIPGDIVHQIFLNINAILDFQRRFLIRVETTNSMPKAVQRWGAPFCFYEDAFDIYQPFIANQRKAAQIANIVFDKIQQSGHPVATDFNTLDGFLLKPMQRLVKYPLLLKDLAKKSDDPQVKDDLCTGCEAAERVLQKANEAVNRDLLDEALEELITRVDDWKSHKVESFGKLLLHGVYGVITGKSDQEKEYEIYLFECILLCCKESSGKKDKTRSTGPKIKNRNGKLQLKGRIFMTNVTDVVSLSKPGSHSVQIWWRGDPGVENFTIKFLNEEMMRKWAVGLETQRKENAPRHSQSQESISNDFAWTRDHAGGLENPYLSQQEDDEEDHGPATAPTQYPVPRTSSSGNLRQRSATGDSTQSLAGIARAPPPRFPMPIPPASLSLQTQSSGAQSPSSRGGDSYFSPVAESPASSRTSTASGIFPGPAYQFPPKAGTPQSVWDDPRYAPGAMPRAPSRDGSSSSNTHGMAGGGRNARGPSLPAMATHSQTAAQQQQQQQRSRSYSTPDVNGAGISRQRQPSQSNIPAVPGIPQHLHPAHDGNIPRSQTGSPRNDLPIRTSTQSPGAQRERMHQHSGSLGGAMSHFATQPLYSRGNTPGPTGGDLLRVDSAAANSRNASPSIGTGSLTSTGNPLATPDLPMPTQLKVRVNCDSGNYVTLVVAFNITYQSLIDRIDAKLARFMTSSIGKGTLKLRYRDEDGDSVTIESDDDIQIAFMEWREGVRNMYSGGVGEIELFCVGEGQ
Protein: Putative U-box domain-containing protein 47 (EC 2.3.2.27) (Plant U-box protein 47) (RING-type E3 ubiquitin transferase PUB47) (Q3E9F6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- Putative U-box domain-containing protein 42
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- Ferrochelatase-2, chloroplastic
- Translation initiation factor IF-2
- Membrane-associated protein VIPP1, chloroplastic
Sequence:
MADSTADESTNADTLWRELHKVLPEIWYDGGGKDHCEIDEAIRILTCLRKIESKNPESDISPVEVPKEFICTLSNKIMIEPMLIASGQTFEKSYILEWLKHERTCPRTKQVLYHRFMIPNHLINEVIKEWCLIHNFDRPKTSDEVIDLFTGDLESLLQRISSPSSVEDQTEAAKELALKAKRFSSVCVYFVAKIPDSITRLLTPLSISEDSNPEFLENIVTALHIFSTSEKNKTLVAENPLVLPLLAKYMKQGTVLTRIHSAATVNSLSYTDSNKIIIGNSEVLKALIHVIEEGDSLATSEAFSALSNLCPVKEISEKAVSEGLIRAAIKKIKAGSNVSMLLSLLAFVSTQNHQTTEEMDNLGLIYDLFSILRNSNSLVNDENAVVIVYNICKSYKALQNVVLREEKRDVVLEEENKHGTFTRLENQEAGRATSLAKRILEWILR
Protein: TNF receptor-associated factor 6-B (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6-B) (Q6DJN2)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4K3}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9Y4K3}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K3}. Lipid droplet {ECO:0000250|UniProtKB:P70196}.
Interaction partners:
Sequence:
MSILNPRTSLEAGDSDDACCAAMASACCLNTKEDCDSPSTALPSGTPQSLEVEEVQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIVKSLRDAGHKCPVDNEILMENQLFPDNFAKREILSLKVKCPSQGCTETMELRHLERHLGQCQFASVECSQCQGSFPKSRLEKHMEHECGRRKIFCDNCGLAMAYEDMSGHELICPLAYVTCEYCQTNLIREQMPSHYSMDCTMAPIPCMYYEFGCTEKMQRNDLARHLQDFTQAHMRMMFQTLRSFSTTPTSHISDISFCDPNQFEPVPLSVAPAHPSHMPSHQDCSQETRNLRETIEQLEGRLVRQDHQIRELIAKMETQCTYVNELKHTIRSLEDKLLDVDGHHCNGVFIWKIKGFSGLQKTQEEEKPVVIHSPGFYTGKPGYKLCLRLHLQLPSAQRCANYISLFVHTMQGEYDSLLPWPLHGTIRLSILDQSEGAIIQDQEEVMDTKPDLLAFQRPTTQRNPKGFGYVTFMHLNTLKQRQYVKNDTLFVRCAVNIHLDVISPRREGFQPRSGDGAQ
Protein: Rho guanine nucleotide exchange factor 15 (D3ZPJ8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPPHNGSSPKALPQISNDASASVCTSIFWEPPTGSLKPPALLPPSVSRASLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPLGPVPLQDGSASAPGTVRRLAGKFEWGAEGKAQSADSLERCSQGSTDVNGEKETLQVGLSGNGSQENGTPAKPGLELRWVPVGSSDDILRAPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTRVRQDTSTSGELPQPDLELPSEDGIQAAPKAWEGDRPEEAPQNAPPPVALEGREEEGLEGLKELQWELPLQDEPLYQTYRAAVLSEELWGVGEDGGPSPANPGEAPTFSRLPGPRNTLWQELPAVRGSGLLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHISDLCDVVHAHAVGPFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKVGLRGFLELSLPNWCVKSQENMKGESIFASIRSSLRLQDPLQTLLTPLNLRAA
Protein: Putative transferase CAF17 homolog, mitochondrial (EC 2.1.-.-) (Iron-sulfur cluster assembly factor homolog) (B8JMH0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for normal heme biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Iron-sulfur cluster assembly 2.
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Lipoyl synthase, mitochondrial
- Cysteine desulfurase
- Frataxin.
- Glutaredoxin 3
- Serine hydroxymethyltransferase
- LYR motif-containing protein 4
- BolA family member 1
Sequence:
MQRMILFGGALREIVVRSGGLQAHYFLCTSRTRIKTHSQTRAASSTAHFSCYRLPHRTVLNVSGQDTSSFLQGIITNDMNLLGEDSLNAMYAHVLNVQGRTLYDIILYSLKGNPDGLNGVLLECDSTVQDSVMQLLKVYKIRRKVNLSVCPSLSLWALLPHSKEAVLGRPDVTTTDKVLVLEKDPRTELMGWRMITSAQDNPLDIVSACRLGNTEEYHRHRYEIGLPEGVGDLPPGEALPLEANLVYMQGISFSKGCYIGQELTARTHHTGVIRKRLMPVSLSAPAEKLNQGSALQTEGGKPAGKYRTGVDKLGLSLVRLAHAKETLQLKSSGDETVTVLASVPDWWPKTPQEK
Protein: Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (EC 1.1.1.300) (NADPH-dependent carbonyl reductase) (CR) (PHCR) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (Peroxisomal carbonyl reductase) (PerCR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) (Short chain dehydrogenase/reductase family 25C member 2) (Protein SDR25C2) (Q8WNV7)
Organism: Sus scrofa (Pig)
Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces all-trans-retinal and 9-cis retinal (Probable). Reduces 3-ketosteroids and benzil into 3alpha-hydroxysteroids and S-benzoin, respectively, in contrast to the stereoselectivity of primates DHRS4s which produce 3beta-hydroxysteroids and R-benzoin. In the reverse reaction, catalyzes the NADP-dependent oxidation of 3alpha-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3alpha-hydroxysteroids, retinoid, isatin and xenobiotic carbonyl compounds.
Subcellular location: Peroxisome {ECO:0000269|PubMed:12604222, ECO:0000269|PubMed:18334214}.
Interaction partners:
- Aldehyde dehydrogenase 1A1
- Dehydrogenase/reductase 9
- Aldehyde dehydrogenase 1 family member A2
- Aldehyde dehydrogenase 1A1
- Cytochrome P450 26A1
- All-trans-retinol 13,14-reductase
- Beta-carotene oxygenase 1
- Aldehyde oxidase 1
- aldehyde oxidase
- Short-chain dehydrogenase/reductase 3
Sequence:
MRAAGQLLRACSQTWKSVRMASTGVERRKPLENKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQENVDRTVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVNLHGGVDILVSNAAVNPFFGNIIDATEEVWDKILHVNVKATVLMTKAVVPEMEKRGGGSVLIVSSVGAYHPFPNLGPYNVSKTALLGLTKNLAVELAPRNIRVNCLAPGLIKTNFSQVLWMDKARKEYMKESLRIRRLGNPEDCAGIVSFLCSEDASYITGETVVVGGGTASRL
Protein: Bone morphogenetic protein 4 (A5HMF9)
Organism: Anas platyrhynchos (Mallard) (Anas boschas)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MIPGNRMLMVILLCQVLLGGTNHASLIPETGRKKVAELQGQQAGSGRRSAQSHELLRGFETTLLQMFGLRRRPQPSKSAVIPTYMLDLYRLQSGEEEESLQEISLQYPERSTSRANTVRSFHHEEHLETVPGPSEAPWIRFVFNLSSVPENEVISSAELRLYREQVEEPSAAWERGFHRINIYEVMKPLSERAQAITRLLDTRLVHHNVTRWETFDVSPAVIRWTKDKQPNHGLVIEVTHLHHAQTHQGKHVRISRSLPQGRGDWAQLRPLLVTFGHDGRGHALTRRARRSPKHQRSRKNKKNCRRHALYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR
Protein: G protein-regulated inducer of neurite outgrowth 1 (GRIN1) (Q7Z2K8)
Organism: Homo sapiens (Human)
Function: May be involved in neurite outgrowth.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Highly enriched in growth cone. {ECO:0000250}.
Interaction partners:
- Methyl-CpG-binding protein 2
- Guanine nucleotide-binding protein G
Sequence:
MDTAEDPAWLQLLQKDSSPPGPRPTAFFCPQDGSLGAGSSAMRDYCPSQQKASPAPPRHTPDQSPGMESRHRSPSGAGEGASCSDGPRGSLACPSPTCFSPQESPSKETLEAHGASISGTPEATTSGKPEPVSSVKTEPKSSDDRNPMFLEKMDFKSSKQADSTSIGKEDPGSSRKADPMFTGKAEPEILGKGDPVAPGRMDPMTVRKEDLGSLGKVDPLCSSKTYTVSPRKEDPGSLRKVDPVSSDKVDPVFPRKEEPRYSGKEHPVSSEKVAPTSAEKVDLVLSGKRDPGPSGKADPMPLESMDSASTGKTEPGLLGKLIPGSSGKNGPVSSGTGAPGSLGRLDPTCLGMADPASVGNVETVPATKEDSRFLGKMDPASSGEGRPVSGHTDTTASAKTDLTSLKNVDPMSSGKVDPVSLGKMDPMCSGKPELLSPGQAERVSVGKAGTVSPGKEDPVSSRREDPISAGSRKTSSEKVNPESSGKTNPVSSGPGDPRSLGTAGPPSAVKAEPATGGKGDPLSSEKAGLVASGKAAPTASGKAEPLAVGKEDPVSKGKADAGPSGQGDSVSIGKVVSTPGKTVPVPSGKVDPVSLGKAEAIPEGKVGSLPLEKGSPVTTTKADPRASGKAQPQSGGKAETKLPGQEGAAAPGEAGAVCLKKETPQASEKVDPGSCRKAEPLASGKGEPVSLGKADSAPSRKTESPSLGKVVPLSLEKTKPSSSSRQLDRKALGSARSPEGARGSEGRVEPKAEPVSSTEASSLGQKDLEAAGAERSPCPEAAAPPPGPRTRDNFTKAPSWEASAPPPPREDAGTQAGAQACVSVAVSPMSPQDGAGGSAFSFQAAPRAPSPPSRRDAGLQVSLGAAETRSVATGPMTPQAAAPPAFPEVRVRPGSALAAAVAPPEPAEPVRDVSWDEKGMTWEVYGAAMEVEVLGMAIQKHLERQIEEHGRQGAPAPPPAARAGPGRSGSVRTAPPDGAAKRPPGLFRALLQSVRRPRCCSRAGPTAE
Protein: Photosystem II reaction center protein I (PSII-I) (PSII 4.8 kDa protein) (P0C405)
Organism: Oryza sativa (Rice)
Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01316}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01316}.
Interaction partners:
Sequence:
MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGRDE
Protein: DNA mismatch repair protein Msh2 (MutS protein homolog 2) (P43247)
Organism: Mus musculus (Mouse)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P43246}. Chromosome {ECO:0000250|UniProtKB:P43246}.
Interaction partners:
- DNA mismatch repair protein Msh3
- DNA mismatch repair protein Msh6
- DNA mismatch repair protein Mlh1
- Mismatch repair endonuclease PMS2
- MutL homolog 3
- Exonuclease 1
- DNA polymerase delta catalytic subunit
- Proliferating cell nuclear antigen
- DNA ligase 4
- DNA excision repair protein ERCC-1
Sequence:
MAVQPKETLQLEGAAEAGFVRFFEGMPEKPSTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGSKTLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNKAGNKASKENEWYLAFKASPGNLSQFEDILFGNNDMSASVGVMGIKMAVVDGQRHVGVGYVDSTQRKLGLCEFPENDQFSNLEALLIQIGPKECVLPGGETTGDMGKLRQVIQRGGILITERKRADFSTKDIYQDLNRLLKGKKGEQINSAALPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELATFDFSQYMKLDMAAVRALNLFQGSVEDTTGSQSLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKYEGRHQALLLAVFVTPLIDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREVMDGLEKKMQSTLINAARGLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSELSSLNEEYTKNKGEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIVSFAHVSNAAPVPYVRPVILEKGKGRIILKASRHACVEVQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALELEEFQNIGTSLGCDEAEPAAKRRCLEREQGEKIILEFLSKVKQVPFTAMSEESISAKLKQLKAEVVAKNNSFVNEIISRIKAPAP
Protein: Serine/threonine-protein kinase 38 (EC 2.7.11.1) (NDR1 protein kinase) (Nuclear Dbf2-related kinase 1) (Q15208)
Organism: Homo sapiens (Human)
Function: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2.
Subcellular location: Nucleus {ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:7761441}. Cytoplasm {ECO:0000269|PubMed:17906693, ECO:0000269|PubMed:7761441}. Chromosome {ECO:0000269|PubMed:32537488}. Note=Localizes to DNA double-strand breaks in response to DNA damage. {ECO:0000269|PubMed:32537488}.
Interaction partners:
- MOB kinase activator 1A
- MOB kinase activator 2
- MOB kinase activator 1B
- Protein furry homolog-like
- Serine/threonine-protein kinase 38-like
- [F-actin]-monooxygenase MICAL1
- Protein S100-B
- Dual specificity protein phosphatase CDC14A
Sequence:
MAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKSNSFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILKPTVATSNHPETDYKNKDWVFINYTYKRFEGLTARGAIPSYMKAAK
Protein: Replication protein A 70 kDa DNA-binding subunit C (OsRPA70c) (Replication factor A protein 1C) (Replication protein A 1C) (Q65XV7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Probably involved in repair of double-strand DNA breaks (DSBs) induced by genotoxic stresses (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication protein A 32 kDa subunit B
- Replication protein A 32 kDa subunit A
- Replication protein A 32 kDa subunit C
- Replication protein A 70 kDa DNA-binding subunit B
- Replication protein A 70 kDa DNA-binding subunit A
- ATP-dependent DNA helicase
- Os01g0660500 protein
- Replication protein A 14 kDa subunit
- DNA polymerase delta catalytic subunit
- DNA replication ATP-dependent helicase/nuclease
Sequence:
MEPQLTPGAVQAIAEHPDGTGTIQPVLQVVDVRPVTTKNAPPTPKPAERFRMMLSDGVNTQQSMLATALNPLVKDATLRPGTVVQLTDFMCNTIQGKRIIIVVKLDVLQNDCIVIGNPKHYEPKSLTKEQDPNLQASVAQTNNGTYSGGASMLGPSVAPRAEQAASNSSYGGPYNSAQGMLGSSIGRTVEPGPANVSAVGSYGAISAQNTTNANMMQPTSQLNIMNANTMQPTSQLNTMNANTMQPTSQLSSLNPNQNQRFAAPASGGVFGPPGNAYGQPSRPSYQQPPPVYMNRGPASRNDSATRIIPITALNPYQPKWTIKARVTAKSDIRHWSNARSSGTVFSFDLLDAQGGEIRAQCWKESADKFFGQIEVGRVYLISRGSLKPAQKKYNTLNHDYEITLDIGLSTVEVCSDDDNSIPRLQYNFRQISELENMANETIVDLLGVVTSVSPSATIMRKIGTETRKRSIQLKDLSGRSIEVTLWGNFCDAEGQQLQLQCDSGSNPIIAFKGARVGDFNGKSVSTIGSTQLIINPDFPEVERLRQWYMTEGKTAPCISLSREMLNMGRTDARKTIAQIKDENLGRLEKPDWITVKAAISHVTTESFCYPACPKLLPVGRQCNKKAINNGDGMWHCDRCDESFQNPEYRYMLRFQIQDHTGSTYASAFDEAGEQIFGRKAGELFSIRNVDQDDAQFAEIIEGVRWHLYLFKLKVKEETYNDEQSLKCTAVKVEKLDPSKESNVLLGAIDNLLLDPKGQSDLAPNAGFTDPVGGHGAPTSSNAYAMNTGGVNQFGQQASISAGMSTPLAATRNLQTCSICGANGHSAQICHVGADMDMQETSAGGSSMGNYNSIAGNGSSECYKCKQPGHYARDCPGQSTGGLECFKCKQPGHFSRDCPVQSTGGSECFKCKQPGHFARDCPGQSTGAQHQTYGNNVAASRGYNRQSFVGGY