wanglab/gogpt-training-data huggingface dataset:
Protein: Methylenetetrahydrofolate reductase (NADPH) (EC 1.5.1.53) (Q9WU20)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a cosubstrate for homocysteine remethylation to methionine. Represents a key regulatory connection between the folate and methionine cycles.
Interaction partners:
- Methionine synthase
- Serine hydroxymethyltransferase, cytosolic
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, mitochondrial
- Thymidylate synthase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Cystathionine gamma-lyase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Aminomethyltransferase, mitochondrial
- Methionine synthase reductase
Sequence:
MVNEARGSGSPNPRSEGSSSGSESSKDSSRCSTPSLDPERHERLREKMRRRMDSGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLFVDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCQQRPEEITGHLHRAKQLGLKNIMALRGDPVGDHWEAEEGGFSYATDLVKHIRTEFADYFDICVAGYPRGHPDAESFEDDLKHLKEKVSAGADFIITQLFFEASTFFSFVKACTEIGISCPILPGIFPIQGYTSLRQLVKLSKLEVPQKIKDVIEPIKDNDAAIRNYGIELAVSLCRELLDSGLVPGLHFYTLNREVATMEVLKQLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQDWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPREELLKMWGEELTSEESVFEVFEHYLSGEPNRHGYRVTCLPWNDEPLAAETSLMKEELLRVNRLGILTINSQPNINAKPSSDPVVGWGPSGGYVFQKAYLEFFTSRETVEALLQVLKTYELRVNYHIVDVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPISFMFWKDEAFALWIEQWGKLYEEESPSRMIIQYIHDNYFLVNLVDNEFPLDSCLWQVVEDTFELLNRHPTERETQAP
Protein: RuvB-like helicase (EC 3.6.4.12) (E7ETR0)
Organism: Homo sapiens (Human)
Subcellular location: Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363048}.
Interaction partners:
Sequence:
MAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQVP
Protein: Large ribosomal subunit protein uL14B (60S ribosomal protein L23-B) (P0CT61)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0CX42}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL36B
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL13
Sequence:
MSRGRGAASGTKYRMTLGLPVQAIMNCADNSGAKNLYIVSVFGTGARLNRLPAASCGDMVLATVKKGKPDLRKKIMPAIVVRQRKAWRRKDGVYLYFEDNAGVIVNPKGEMKGSAITGPVAKECADLWPRIASNAGTVV
Protein: Host cell factor 2 (HCF-2) (C2 factor) (Q9Y5Z7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10196288}. Nucleus {ECO:0000269|PubMed:10196288}.
Interaction partners:
- Host cell factor 1
- CREB/ATF bZIP transcription factor
- WD repeat-containing protein 5
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Cyclic AMP-responsive element-binding protein 3
- Histone-lysine N-methyltransferase 2B
- Histone-lysine N-methyltransferase SETD1A
- Histone-lysine N-methyltransferase 2A
- Biorientation of chromosomes in cell division protein 1-like 1
Sequence:
MAAPSLLNWRRVSSFTGPVPRARHGHRAVAIRELMIIFGGGNEGIADELHVYNTATNQWFLPAVRGDIPPGCAAHGFVCDGTRILVFGGMVEYGRYSNELYELQASRWLWKKVKPHPPPSGLPPCPRLGHSFSLYGNKCYLFGGLANESEDSNNNVPRYLNDFYELELQHGSGVVGWSIPVTKGVVPSPRESHTAVIYCKKDSGSPKMYVFGGMCGARLDDLWQLDLETMSWSKPETKGTVPLPRSLHTASVIGNKMYIFGGWVPHKGENTETSPHDCEWRCTSSFSYLNLDTTEWTTLVSDSQEDKKNSRPRPRAGHCAVAIGTRLYFWSGRDGYKKALNSQVCCKDLWYLDTEKPPAPSQVQLIKATTNSFHVKWDEVSTVEGYLLQLSTDLPYQAASSDSSAAPNMQGVRMDPHRQGSNNIVPNSINDTINSTKTEQPATKETSMKNKPDFKALTDSNAILYPSLASNASNHNSHVVDMLRKNEGPHTSANVGVLSSCLDVRTVIPETSVSSTVSSTQTMVTQQTIKTESSSTNGAVVKDETSLTTFSTKSEVDETYALPATKISRVETHATATPFSKETPSNPVATVKAGERQWCDVGIFKNNTALVSQFYLLPKGKQSISKVGNADVPDYSLLKKQDLVPGTGYRFRVAAINGCGIGPFSKISEFKTCIPGFPGAPSAVRISKNVEGIHLSWEPPTSPSGNILEYSAYLAIRTAQIQDNPSQLVFMRIYCGLKTSCIVTAGQLANAHIDYTSRPAIVFRISAKNEKGYGPATQVRWLQGNNKKAPLN
Protein: Regulatory protein SIR2 homolog 7 (SIR2-like protein 7) (A0A2R8QUG9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Glutamine-dependent NAD
- Nicotinamide phosphoribosyltransferase
- Nicotinamide phosphoribosyltransferase
- Nudix-type motif 12.
- Phosphate cytidylyltransferase 2, ethanolamine.
- NAD
- Nicotinamide nucleotide transhydrogenase 2.
- Uncharacterized protein LOC393330
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- Uncharacterized protein.
Sequence:
MDVRINSGVSARAERKEQEKAKIIQREKQRQTMKTISKILQKCESEWTEEERSMLQAHQDTVQELSRRQNRRHLLKRKQEEVFDDAENLKTKVKQLAEAVQRAKHLVIYTGAGISTAASIPDYRGPNGVWTQLQKGRSVSTSDLSQAEPTLTHMSIWMLHKMKMVQHVVSQNCDGLHLRSGLPRHALSELHGNMFIEVCDSCSPPREFIRLFDVTERTALHRHGTGRSCPHCRAELRDTIVHFGERGTLEQPLNWKGAAEAAQRADLILCLGSSLKVLKKYSCLWCMNRPASKRPKLYIVNLQWTPKDNLATLKIHGKCDAVMALLMEELALAVPVYSRLQDPIFSMAKPLSPQEQKSHSRKEIAPPSALEEVSQSAPPQGEGPAVQGGWFGRGYSKGRRKKKSS
Protein: Protein ttm-2 (Toxin-regulated target of MAPK 2) (Q19829)
Organism: Caenorhabditis elegans
Function: Involved in resistance to B.thuringiensis pore-forming toxin Cry5B downstream of the sek-1 and pmk-1 MAPK kinase pathway.
Interaction partners:
- Zinc transporter ttm-1
- Putative sphingolipid delta
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin domain-containing protein 15
Sequence:
MLDKIRFTVLLDRPFYQPGQTIQGHVVCEPHHPLEIDCVEGRLHGEIQYFQQLPPNHNRNGSPLPPSKTRVLIDEKAQLWKYQTVSEMLGLDVFYDENQNRHFSSESASASSSSLFTTAATFPIQIELPHFAPPSFYCPGSPVSIRFTLEIQLYNQGFKIASHEENLVVLNYESIKRQVTPKPVNFQKTFNFPKERSISLEMLLPTDVFTTTARLENCITICNRWKQSLKYVHLNIVRRISALNQNNEVIDTVKIDTTGVGLPSKTKIAVGETYSFRPTFNVPALPPNIHVNGLFKTEYSLKVTIGRAHNFVLASYEVPITIVTMDQSSRRSMQKEDILVDISASNNTLNNLPVDLLA
Protein: Deaminated glutathione amidase, chloroplastic/cytosolic (dGSH amidase) (EC 3.5.1.128) (Nitrilase-like protein 2) (Protein nitrilase 1 homolog) (AtNit1) (Protein Nit1 homolog) (Q94JV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione. Possesses amidase activity toward deaminated ophthalmate in vitro.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:30692244}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:30692244}.
Interaction partners:
- Amidase 1
- S-alkyl-thiohydroximate lyase SUR1
- Tryptophan N-monooxygenase 2
- Tryptophan N-monooxygenase 1
- Indole-3-acetaldehyde oxidase
- Agmatine deiminase
- Guanine nucleotide-binding protein subunit gamma 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- BTB/POZ domain-containing protein At3g44820
Sequence:
MNAYSVSLDFTKPSLFTRITLSSQIPLTMATTVNKTVRVAAAQMTSVNDLMTNFATCSRLVQEAALAGAKLICFPENFSFVGDKEGESVKIAEPLDGPVMERYCSLARDSNIWLSLGGFQERFDDTHLCNTHVVIDDAGMIRDTYQKMHLFDVDVPGGSSYKESSFTVPGTKIVSVDSPVGRLGLTVCYDLRFPKIYQQLRFEQKAQVLLVPSAFTKVTGEAHWEILLRARAIETQCYVIAAAQAGKHNEKRESYGDTLIIDPWGTVVGRLPDRVSTGIVVADIDFSLIDSVRTKMPIDKQRVSIDL
Protein: Maternal uncoordinated protein 2 (Cohesin loading complex subunit SCC4 homolog) (O17581)
Organism: Caenorhabditis elegans
Function: Plays an important role in the loading of the cohesin complex on to DNA (By similarity). Forms a heterodimeric complex (also known as cohesin loading complex) with scc-2/SCC2 which mediates the loading of the cohesin complex onto chromatin (By similarity). Required for normal development until the fourth larval stage. Functions cell autonomously to guide migrations during the development of the nervous system. Participates in the guidance of mechanosensory neuron AVM by a slt-1-independent mechanism. Regulates chromosome segregation in early embryos.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:15539489}. Cytoplasm {ECO:0000269|PubMed:15539489}. Note=Binds to chromatin from the end of mitosis until prophase. Localizes to the cytoplasm of neurons.
Interaction partners:
- Nipped-B-like protein scc-2
- Structural maintenance of chromosomes protein 3
- Wings apart-like protein homolog 1
- Structural maintenance of chromosomes protein 5
- Cohesin subunit scc-3
- separase
- Separin homolog sep-1
- Cnd1 domain-containing protein
- Structural maintenance of chromosomes protein 6 homolog smc-6
- N-acetyltransferase ESCO2
Sequence:
MNQDAVAKALLGMAEALRTQDPPKLKMAIKCARSTLSMEISDEMKAICNLQLGKLLFFYTDNFELAKNHLQCAYDKMSAMGTFYTRDKMNAISMLADLHIHYQQWPLTSIKATIRHEITTTRGFPALSNKLMFQLIELMKIDKDVEGAIEMCQLAINSSHADPKMELYFRIAKTLVTYQLMHEEPDISDVTRIGSMIKVMENSTTSDKAHLECIKDFYVCTKLAYMFYEGKSRTSRQLLRQIQKSQTSGETKIHGIRWLGEPSITLLACVMNQICALVQSNTDRVEKYYHLVIKHADEIIFKSTRSPQEPGVVRCINMIKMTTLEMMACCNVLACRPQKTLHNVRDMLEWSNRTSGPLLTRYFTPHIHYILGLQCCYFRQHENAENHFRAAMKKLHKEDITAHNTMALLNLNLAITYLNQLKMADYYEVSENLTAPKISSCSQMLKNNVKLLSAFFAYITNKLNECKLLSHEVLDDSKAEDFFRLHGLGLLLLSLVTDVDEKGVRPTVDWSKKSHDHVVILFSHSLYEKILLAAGYDPKSELMKMVVSEQLASRRMLSVENLTPLVANMPASKLLQWFDGDPFKLLPRDETVL
Protein: Protein DJ-1 homolog C (AtDJ1C) (Q8VY09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an essential role in chloroplast development and is required for chloroplast integrity and viability.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:20406884}.
Interaction partners:
- DJ-1 protein homolog F
- Protein DJ-1 homolog D
- DJ-1 protein homolog E
- Hydroxyacylglutathione hydrolase 1, mitochondrial
- Hydroxyacylglutathione hydrolase 2, mitochondrial
- Probable hydroxyacylglutathione hydrolase 2, chloroplastic
- Persulfide dioxygenase ETHE1 homolog, mitochondrial
- Hydroxyacylglutathione hydrolase cytoplasmic
- Lactoylglutathione lyase GLX1
- F22K20.6 protein
Sequence:
MGSLGYSISMIASLSPTLMESRLISSMGCVSMTVAPSFSSVSVVSSSLGTTRRDRTLKLRSSMSPGMVTTLDSDVGVGSSATTKKVLVPIGYGTEEIEAVVLVDVLRRAGADVTVASVEQKLEVEGSSGTRLLADVLISKCADQVYDLVALPGGMPGAVRLRDCEILEKIMKRQAEDKRLYGAISMAPAITLLPWGLLTRKRTTGHPAFFGKLPTFWAVKTNIQISGELTTSRGPGTSFQFALSLAEQLFGETTAKSIEEFLLLRDGYQNPKNKEFNSIDWSLDHTPRVLIPVANGSEAVELVSIADVLRRAKVDVTVSSVERSLRITAFQGTKIITDKLIGEAAESSYDLIILPGGHTGSERLQKSKILKKLLREQHESGRIYGATNSSSTVLHKHGLLKEKRTTVYPSESDEPMNQQMIEGAEVVIDGNVITSLGLATVTKFSLAIVSKLFGHARARSVSEGLVHEYPRQ
Protein: 2-oxoglutarate dehydrogenase-like, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1-like) (OGDC-E1-like) (Alpha-ketoglutarate dehydrogenase-like) (D3ZQD3)
Organism: Rattus norvegicus (Rat)
Function: 2-oxoglutarate dehydrogenase (E1-like) component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDHC) which mediates the decarboxylation of alpha-ketoglutarate in the tricarboxylic acid cycle. The OGDHC complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) while reducing NAD(+) to NADH. The OGDHC complex is mainly active in the mitochondrion. Involved in the inhibition of cell proliferation and in apoptosis (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9ULD0}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MSQLRLLLFRLGPQARKLLATRDIAAFGGRRRSSGPPTTIPRSRGGVSPSYVEEMYFAWLENPQSVHKSWDNFFQRATKEASVGPAQPQPPAVIQESRASVSSCTKTSKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSFVPSDLITTIDKLAFYDLQEADLDKEFRLPTTTFIGGSENTLSLREIIRRLESTYCQHIGLEFMFINDVEQCQWIRQKFETPGVMKFSIEEKRTLLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGVENVILGMPHRGRLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGMYHERINRVTNRNITLSLVANPSHLEAVDPVVQGKTKAEQFYRGDAQGRKVMSILVHGDAAFAGQGVVYETFHLSDLPSYTTNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEWRNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHKQVPVLKKYADKLIAEGTVTLQEFEEEIAKYDRICEEAYGRSKDKKILHIKHWLDSPWPGFFNVDGEPKSMTYPTTGIPEDTLSHIGNVASSVPLEDFKIHTGLSRILRGRADMTKKRTVDWALAEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQDVDRRTCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYAMASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLLPHGMEGMGPEHSSARPERFLQMSNDDSDAYPVFTEDFEVSQLYDCNWIVVNCSTPASYFHVLRRQVLLPFRKPLIVFTPKSLLRHPDAKSSFDQMVSGTSFQRMIPEDGPAAQSPERVERLIFCTGKVYYDLVKERSSQGLEKQVAITRLEQISPFPFDLIMREAEKYSGAELVWCQEEHKNMGYYDYISPRFMTLLGHSRPIWYVGREPAAAPATGNKNTHLVSLRKFLDTAFNLKAFEGKTF
Protein: Heat shock factor-binding protein 1 (Q9U3B7)
Organism: Caenorhabditis elegans
Interaction partners:
- WASH complex subunit homolog 3
- WASH complex subunit homolog 1
- Heat shock transcription factor hsf-1
Sequence:
MSDEKSTTPTAQLDAPADGNMNDLTSLIQGVLQQTQDRFQHMSDQIIRRIDDMTTRIDDLEKNINDLLQSNQVEHPPSAQ
Protein: BZIP domain-containing protein (H2L0F8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQQNIQYTYSSDPRSGGNQNQQLHGISQFQQNSYQPTTYSNSNANNFHSSNSATFIPNSVTQTPQRRMGEEKSLVNMLDAYFIDSTTPSTSTSWNNQQPVQMSSIQQSVGSYNQQIPQLKVGDVVNSLFFLCFFLGRISCYSVIFSRNFEFCSSKSAWIFAFERIFQKICSKSR
Protein: Tripartite terminase subunit 1 (P10212)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04014, ECO:0000269|PubMed:9882384}. Note=Found associated with the external surface of the viral capsid during assembly and DNA packaging, but seems absent in extracellular mature virions. {ECO:0000255|HAMAP-Rule:MF_04014}.
Interaction partners:
Sequence:
MAAPVSEPTVARQKLLALLGQVQTYVFQIELLRRCDPHIGRGKLPQLKLNALQVRALRRRLRPGLEAQAGAFLTPLSVTLELLLEYAWREGERLLGSLETFATAGDVAAFFTETMGLARPCPYHQRVRLDTYGGTVHMELCFLHDVENFLKQLNYCHLITPSRGATAALERVREFMVGAVGSGLIVPPELSDPSHPCAVCFEELCVTANQGATIARRLADRICNHVTQQAQVRLDANELRRYLPHAAGLSDADRARALSVLDHALARTAGGDGQPHPSPENDSVRKEADALLEAHDVFQATTPGLYAISELRFWLASGDRAGQTTMDAFASNLTALARRELQQETAAVAVELALFGRRAEHFDRAFGSHLAALDMVDALIIGGQATSPDDQIEALIRACYDHHLTTPLLRRLVSPEQCDEEALRRVLARMGAGGAADAPKGGAGPDDDGDRVAVEEGARGLGAPGGGGEDEDRRRGPGGQGPETWGDIATQAAADVRERRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSVHGEVLPATFAAVANGFAARARFCALTAGAGTVIDNRSAPGVFDAHRFMRASLLRHQVDPALLPSITHRFFELVNGPLFDHSTHSFAQPPNTALYYSVENVGLLPHLKEELARFIMGAGGSGADWAVSEFQRFYCFDGISGITPTQRAAWRYIRELIIATTLFASVYRCGELELRRPDCSRPTSEGRYRYPPGVYLTYDSDCPLVAIVESAPDGCIGPRSVVVYDRDVFSILYSVLQHLAPRLPDGGHDGPP
Protein: Holliday junction resolvase YEN1 (EC 3.1.-.-) (P40028)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Endonuclease which resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation. Involved in DNA-damage repair in vegetative cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19520826}. Nucleus {ECO:0000269|PubMed:19520826}. Note=Predominantly nuclear in G1-arrested cells, but cytoplasmically localized after release from G1 arrest.
Interaction partners:
- Crossover junction endonuclease MUS81
- Crossover junction endonuclease MMS4
- ATP-dependent helicase SGS1
- DNA replication ATP-dependent helicase/nuclease DNA2
- Structure-specific endonuclease subunit SLX1
- RecQ-mediated genome instability protein 1
- DNA mismatch repair protein MLH3
- DNA topoisomerase 3
- Exodeoxyribonuclease 1
- DNA repair protein RAD51
Sequence:
MGVSQIWEFLKPYLQDSRIPLRKFVIDFNKSQKRAPRIAIDAYGWLFECGFIQNIDISARSRSRSRSPTRSPRDSDIDSSQEYYGSRSYTTTGKAVINFISRLKELLSLNVEFLLVFDGVMKPSFKRKFNHEQNATTCDDEKEYYSSWEQHVKNHEVYGNCKGLLAPSDPEFISLVRKLLDLMNISYVIACGEGEAQCVWLQVSGAVDFILSNDSDTLVFGGEKILKNYSKFYDDFGPSSITSHSPSRHHDSKESFVTVIDLPKINKVAGKKFDRLSLLFFSVLLGADYNRGVKGLGKNKSLQLAQCEDPNFSMEFYDIFKDFNLEDLTSESLRKSRYRLFQKRLYLYCKDHSVELFGRNYPVLLNQGSFEGWPSTVAIMHYFHPIVQPYFDEEVLSDKYINMAGNGHYRNLNFNELKYFLQSLNLPQISSFDKWFHDSMHEMFLLREFLSIDESDNIGKGNMRITEEKIMNIDGGKFQIPCFKIRYTTFLPNIPISSQSPLKRSNSPSRSKSPTRRQMDIMEHPNSLWLPKYLIPQSHPLVIQYYETQQLIQKEKEKKGKKSNKSRLPQKNNLDEFLRKHTSPIKSIGKVGESRKEILEPVRKRLFVDTDEDTSLEEIPAPTRLTTVDEHSDNDDDSLIFVDEITNSQSVLDSSPGKRIRDLTQDEQVDVWKDVIEISPIKKSRTTNAEKNPPESGLKSRSSITINARLQGTKMLPPNLTAPRLEREHSSVLDQLVTDAQDTVDRFVACDSDSSSTIE
Protein: Tenascin R (H1A489)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Tenascin C
- Integrin beta
- Integrin beta
- Integrin subunit alpha 9
- Aggrecan core protein
- Integrin subunit alpha 8
- Integrin alpha-V
- Syndecan
- Syndecan
- Integrin beta
Sequence:
MGVDGENPVLRSVVISFSLLLLGAVLKPFECRLEMTAEPAERTAVDEAGGLANCSPPIKEQPMVFHHIYNINIPLDSCCSSMFKSSAEEVSSEDERLAEYTEQTSDSESQVTFTHRINMPKQACKCSTSLPSLQELLSRIEMLEREVSILRDQCTSNCCQENAATGQLDYIPQCSGHGNFSLESCSCVCMEGWAGSNCSEPRCPGGCSSRGVCLEGQCICDSDYGGEDCSQLRCPAGCGSRGLCVDGECVCEEGFTGEDCSQLRCPRDCSGRGRCVNGTCECPEGFGGEDCARPRCPGACGGRGLCRDGLCVCQPGYGGQDCSAVSPPENLRVTGISDSSIELAWDGSGAATEYVVSYQPAVPGGTQLQQRVPGDWSSITITDLEPGVAYNVSIYAVISDVFSIPVISKVMTNLATPQGLKFKTITETTAEVQWEPFSFPFDGWEISFIPKNNEGGVIAQLPSTVTTFNQTGLKPGEEYTVTVVALKEQARSPPTSDSVSTLIDGPTQILVRDVSDTVAFVEWTPPRAKVDAILLKYGLADGEGGRTTFRLQPPLSQYSLQALRPGARYHLAVSALRGANESRPAFAQFTTEIDAPKNLRVGSRSPASLELAWDNSEAEAHSYRVVYSTLAGEHYHEVLVPRDTGPTTRATLADLVPGTEYGIGISAVMDSQQSVPATMNARTELDSPRDLLVTASTETSISLAWTKATGPIDHYRITFTPASGMASEVTVSRDESQLTLSELEPGTEYTISIIAERGRQQSLEATVDAFTGVRPISQLHFSQLTSSSVNVTWSDPSPPADRLILTYSPRDEEEEAQQVTLDGTRRHTSLMGLQPSTEYLVSLVAVHGTISSEPVVGSITTGIDAPKDLRVDNVTQESMMVYWSAPIAAFDHYRISYRAAEGRTESMAISRDATEYTLQDLQPATKYEIGVKSVRGREESELASITAYTAMDVPLGVTATNITPTEALLQWNPPLSEVESYVLILTRRAVAGETILVDGDSQEYQLTNLLPSTTYTVSMYATSGPLTSQTISTNFTTLLDPPTNLTASEVTRRSALLSWVPPVGEIENYVMTYRSTDGSRKELIVDAEDTWIRLEGLSETTEYTVHLQAAQNAMRSGLISTTFTTGGRVFANPQDCAQHLMNGDTLSGVYTISINGDLSQRVPVYCDMTTDGGGWIVFQRRQNGLTDFFRKWADYRVGFGNLEDEFWLGLDNIHKITSQGRYELRIDMRDGQEAAYAYYDKFSIGDSRSLYKLRIGDYNGTSGDSLTYHQGRPFSTKDRDNDVAVTNCAMSYKGAWWYKNCHRTNLNGKYGESRHSQGINWYHWKGHEFSIPFVEMKMRPYNHRNISGRKRRSLQL
Protein: Uncharacterized HTH-type transcriptional regulator Rv2912c (P9WMC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv2913c
- Uncharacterized protein Rv2915c
- Transcriptional regulatory protein
- Possible transcriptional regulatory protein
- HTH-type transcriptional regulator RipA
- HTH-type transcriptional regulator VirS
- NAD-dependent protein deacylase
- Transcriptional regulatory protein
- HTH-type transcriptional regulator Rv0792c
- Probable transcriptional regulatory protein
Sequence:
MARTQQQRREETVARLLQASIDTIIEVGYARASAAVITKRAGVSVGALFRHFETMGDFMAATAYEVLRRQLETFTKQVAEIPADRPALPAALTILRDITAGSTNAVLYELMVAARTDEKLKETLQNVLGQYSAKIHDAARALPGAESFPEETFPVIVALMTNVFDGAAIVRGVLPQPELEEQRIPMLTALLTAGL
Protein: Repetin (P97347)
Organism: Mus musculus (Mouse)
Function: Involved in the cornified cell envelope formation. Multifunctional epidermal matrix protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Trichohyalin
- Loricrin
- Small proline-rich protein 2D
- Periplakin
- Protein-glutamine gamma-glutamyltransferase K
- Envoplakin
Sequence:
MPQLLNSILNVSKVFQDYAEYHGVGASLSKKELKQLLLTEFGDILRRPNDPETVETILEHLDRDRNGYVDFHEYLLLVFQLVQACHHKLDSKFYGSRTSSQKEHDQEGTRSHKFSESTGRQHRQRYEGERRNSHHNQSEGQHQNVQHDQSQRQDKDSERHDTDPHCGQSETFHGDSHYGHSERQDTDYSSDQSESDNESSSSSQRLGYKSSHEQPKGQGYVFALSQSKNPEQAFHYGQSKTSGQQSSHGQSGRFRKDSYSSQTSQQESDSYEQYGSQHQKSGNSQTERQGQNSQYGQTNKKGHSSYHEQTEGQGQSFHYGQKGRKDQSFQQGQKGRKDQSPHLGQKGRQDQSPHRGQKGRQDQSPHQGQKGRQDQSPHRGQKGRQDQSPHQGQKGRQDQSPHLGQKGRQDQSPHQGQKGRQDQSPHQGQKGRQDQSSHQGQKGRQDQSSHQGQKGRQDQSSHQGQKGRQDQSSHQGQREGQDQNSQWHRTDSQGQSFHYGQTGGHSLSSHQGQTDSQGQNSNWHRTDSQGQSFHYGQTGGQGLSSHQGQTDSQGQNSNWHRTDSQGQSFHFDQAGREVQGSHHGQTDRQSQNSNWHRTDSQGQSFHFDQAGKEVQGSHQGQTDSQGQSSHWHQTDRQGQSSQQGHKDRQGQNTHQGQKGRQDLSPHQGQKGRQDQSPHLGQKGRHDQSPHQGQKGRHDQSPHQGQKGRQDLSSHQGQKGRQDQSPHLGQKGRHDQSPHRGQKGRQDQSPHQGQKGRQDQSSHQGQREGQDQNSHWHRTDRQGQSFHYGQTGGQGLSSHQGQTDSQGQNSQWHRTDSQGQSFHFDQAGREGQSSHHGQTDRQSQSSHCGQSEIGKTENQGQNRHSLGTDRTRRDSYVEQSGRSVKLSQQNSREEVRQTQSQRSHDRREQQIQQQTWKPKEDNQHKLLAQVQQEPYSYEEYDWQSQSSEQDHCGEEEYQDWDRHSVEDQENLYEMQNWQTHEEEQSHQTSDRQTHVDEQNQQRQHRQTHEENHDHQHGRHHEDEHNHRRQDHHQQRERQTHEEKEKYQGGQDQSRSFPNREKSHMSEDDQCEGPQGRRFHPTHGGGKSQRREKSGNHPTKPANYSSPLYDYVQEQAAYQY
Protein: Ras-specific guanine nucleotide-releasing factor 1 (Ras-GRF1) (Guanine nucleotide-releasing protein) (GNRP) (Ras-specific nucleotide exchange factor CDC25) (Q13972)
Organism: Homo sapiens (Human)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
- GTPase HRas
- Glutamate receptor ionotropic, NMDA 2B
- Calmodulin-1
- Calmodulin-like protein 5
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Transforming protein RhoA
- GTPase KRas
- Ras-specific guanine nucleotide-releasing factor 2
Sequence:
MQKGIRLNDGHVASLGLLARKDGTRKGYLSKRSSDNTKWQTKWFALLQNLLFYFESDSSSRPSGLYLLEGCVCDRAPSPKPALSAKEPLEKQHYFTVNFSHENQKALELRTEDAKDCDEWVAAIAHASYRTLATEHEALMQKYLHLLQIVETEKTVAKQLRQQIEDGEIEIERLKAEITSLLKDNERIQSTQTVAPNDEDSDIKKIKKVQSFLRGWLCRRKWKTIIQDYIRSPHADSMRKRNQVVFSMLEAEAEYVQQLHILVNNFLRPLRMAASSKKPPITHDDVSSIFLNSETIMFLHQIFYQGLKARISSWPTLVLADLFDILLPMLNIYQEFVRNHQYSLQILAHCKQNRDFDKLLKHYEAKPDCEERTLETFLTYPMFQIPRYILTLHELLAHTPHEHVERNSLDYAKSKLEELSRIMHDEVSETENIRKNLAIERMIIEGCEILLDTSQTFVRQGSLIQVPMSEKGKITRGRLGSLSLKKEGERQCFLFSKHLIICTRGSGGKLHLTKNGVISLIDCTLLEEPESTEEEAKGSGQDIDHLDFKIGVEPKDSPPFTVILVASSRQEKAAWTSDISQCVDNIRCNGLMMNAFEENSKVTVPQMIKRTREGTREAEMSRSDASLYCDDVDIRFSKTMNSCKVLQIRYASVERLLERLTDLRFLSIDFLNTFLHSYRVFTTAIVVLDKLITIYKKPISAIPARWLRSLELLFASGQNNKLLYGEPPKSPRATRKFSSPPPLSITKTSSPSRRRKLSLNIPIITGGKALDLAALSCNSNGYTSMYSAMSPFSKATLDTSKLYVSSSFTNKIPDEGDTTPEKPEDPSALSKQSSEVSMREESDIDQNQSDDGDTETSPTKSPTTPKSVKNKNSSEFPLFSYNNGVVMTSCRELDNNRSALSAASAFAIATAGANEGTPNKEKYRRMSLASAGFPPDQRNGDKEFVIRRAATNRVLNVLRHWVSKHSQDFETNDELKCKVIGFLEEVMHDPELLTQERKAAANIIRTLTQEDPGDNQITLEEITQMAEGVKAEPFENHSALEIAEQLTLLDHLVFKKIPYEEFFGQGWMKLEKNERTPYIMKTTKHFNDISNLIASEIIRNEDINARVSAIEKWVAVADICRCLHNYNAVLEITSSMNRSAIFRLKKTWLKVSKQTKALIDKLQKLVSSEGRFKNLREALKNCDPPCVPYLGMYLTDLAFIEEGTPNYTEDGLVNFSKMRMISHIIREIRQFQQTAYKIEHQAKVTQYLLDQSFVMDEESLYESSLRIEPKLPT