wanglab/gogpt-training-data huggingface dataset:
Protein: Inducible lysine decarboxylase (LDCI) (EC 4.1.1.18) (P0A9H3)
Organism: Escherichia coli (strain K12)
Function: Inducible lysine decarboxylase that catalyzes the proton-dependent decarboxylation of L-lysine to produce the polyamine cadaverine and carbon dioxide. Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Regulatory ATPase RavA
- Cadaverine/lysine antiporter
- Constitutive lysine decarboxylase
- Putrescine aminotransferase
- Diaminopimelate decarboxylase
- Uncharacterized protein YaeR
- Regulatory protein ViaA
- Transcriptional activator CadC
- Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase
- Polyamine aminopropyltransferase
Sequence:
MNVIAILNHMGVYFKEEPIRELHRALERLNFQIVYPNDRDDLLKLIENNARLCGVIFDWDKYNLELCEEISKMNENLPLYAFANTYSTLDVSLNDLRLQISFFEYALGAAEDIANKIKQTTDEYINTILPPLTKALFKYVREGKYTFCTPGHMGGTAFQKSPVGSLFYDFFGPNTMKSDISISVSELGSLLDHSGPHKEAEQYIARVFNADRSYMVTNGTSTANKIVGMYSAPAGSTILIDRNCHKSLTHLMMMSDVTPIYFRPTRNAYGILGGIPQSEFQHATIAKRVKETPNATWPVHAVITNSTYDGLLYNTDFIKKTLDVKSIHFDSAWVPYTNFSPIYEGKCGMSGGRVEGKVIYETQSTHKLLAAFSQASMIHVKGDVNEETFNEAYMMHTTTSPHYGIVASTETAAAMMKGNAGKRLINGSIERAIKFRKEIKRLRTESDGWFFDVWQPDHIDTTECWPLRSDSTWHGFKNIDNEHMYLDPIKVTLLTPGMEKDGTMSDFGIPASIVAKYLDEHGIVVEKTGPYNLLFLFSIGIDKTKALSLLRALTDFKRAFDLNLRVKNMLPSLYREDPEFYENMRIQELAQNIHKLIVHHNLPDLMYRAFEVLPTMVMTPYAAFQKELHGMTEEVYLDEMVGRINANMILPYPPGVPLVMPGEMITEESRPVLEFLQMLCEIGAHYPGFETDIHGAYRQADGRYTVKVLKEESKK
Protein: Kinase (EC 2.7.-.-) (Q9VYE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVCALSQPQQPNKSNQNQKQKNGPARLPALATGNGSASASASGINLNGKAKGSVTPPTPPPSPQVRIYEDFDRMSAKEVYYNEAGKKVTVKLLHFPDVPPEEISKLKFDDDDDDEEEDGNGGENENGDDDNGEEADEDSDSGRRPTSADSEDAGHKSESSGGASNANALPSSSSKKIFRRKLSGNNMQPRKCSLAFAQAHGIRQRAEKKLSMPTISITANSGEHVAHNCGLRLNLGRKLSQQHSLPLGSPTSPASPTSPGPRRSHSPLGQSLCPGYIQYSKSLLEVPMPRDYGYASSDDLSSEWDSDVSTSAAGSATGSGSGAASQASTTGKKSSGWRKIRNIVQWTPFFQTYKKQRYPWVQLAGHQGNFKAGPEPGTVLKKLCPKEEECFQILMHDLLRPYVPVYKGQVTSEDGELYLQLQDLLSDYVQPCVMDCKVGVRTYLEEELSKAKEKPKLRKDMYDKMIQIDSHAPTAEEHAAKAVTKPRYMVWRETISSTATLGFRIEGIKKSDGTSSKDFKTTKSREQIKLAFLEFLSGHPHILPRYIQRLRAIRATLAVSEFFQTHEVIGSSLLFVHDQTHASIWLIDFAKTVELPPQLRIDHYSAWKVGNHEDGYLIGINNLIDIFVELQASMEAEAHAQAQAEAIQSPVSGSGGDQAEQTGEESKP
Protein: Histone RNA hairpin-binding protein RNA-binding domain-containing protein (Q57ZC0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small nuclear ribonucleoprotein SmD1
Sequence:
MSMTESSTRRALGSSGVWMNNSYSGANHPKFDTSLGTGSPKIDISTSQTPIRNGASSTTSVAATMSQQLRSPMVTVHQPYRSIPPSVFGVESELERYTRNPAETAVPVTSVYKSVVSRTPDSMARCGYIPSQCSSQRSPIAVLDGGDIGHAGDMCGGDVTHSATPHDTAVAGGGTTNGSSHIVSTRVLNNNGNKRMATIVHLGNDADCAGPGVYNASEPLQCPIALRMVEAEEKHLNYSGVELDPADLNRGDTTERARRLQQRLRQVQYGKETAGYENYIRAVPSRCDREFRNPMHPMTPRPEYDCSKRTFDRYLNVWRRQLHLWDDYDADNLAPQYTRIGIPTLGRLGLERVQNAADEQSCGFLSFTPTTAHGVVGTMAGTVACTPVVTRNQRRDVSVSMPSASHQRPGPYAVGGLSAVGGPHGPSMGMPNVCSSNVCGGGGGTCSIPNTPHTPYYGSTHSNSSHMPPFLSVLAQPTIYSPHWADSSRQGSPIQHGAQRSVGYSYNSTSGCSAPGNGCGTYMDNTNHCWNNVYAGGYHSPYGGHRATPHSSPNHHHYSYYNGVGVTNLAPPSPMCVGHEGWGNSLRQQRQ
Protein: ATP-dependent DNA helicase UvrD2 (EC 5.6.2.4) (DNA 3'-5' helicase UvrD2) (P9WMP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA-dependent ATPase, stimulated equally by ss- and dsDNA. Has both ATPase and helicase activities, and translocates along ssDNA displacing bound streptavidin. Its essentiality for growth does not depend on its helicase activity.
Interaction partners:
- DNA 3'-5' helicase
- ATP-dependent DNA helicase UvrD1
- UvrABC system protein B
- DNA 3'-5' helicase
- UvrABC system protein A
- Protein RecA
- ATP-dependent DNA helicase RecG
Sequence:
MSIASDPLIAGLDDQQREAVLAPRGPVCVLAGAGTGKTRTITHRIASLVASGHVAAGQVLAVTFTQRAAGEMRSRLRALDAAARTGSGVGAVQALTFHAAAYRQLRYFWSRVIADTGWQLLDSKFAVVARAASRTRLHASTDDVRDLAGEIEWAKASLIGPEEYVTAVAAARRDPPLDAAQIAAVYSEYEALKARGDGVTLLDFDDLLLHTAAAIENDAAVAEEFQDRYRCFVVDEYQDVTPLQQRVLSAWLGDRDDLTVVGDANQTIYSFTGASPRFLLDFSRRFPDAAVVRLERDYRSTPQVVSLANRVIAAARGRVAGSKLRLSGQREPGPVPSFHEHSDEPAEAATVAASIARLIASGTPPSEVAILYRVNAQSEVYEEALTQAGIAYQVRGGEGFFNRQEIKQALLALQRVSERDTDAALSDVVRAVLAPLGLTAQPPVGTRARERWEALTALAELVDDELAQRPALQLPGLLAELRRRAEARHPPVVQGVTLASLHAAKGLEWDAVFLVGLADGTLPISHALAHGPNSEPVEEERRLLYVGITRARVHLALSWALSRSPGGRQSRKPSRFLNGIAPQTRADPVPGTSRRNRGAAARCRICNNELNTSAAVMLRRCETCAADVDEELLLQLKSWRLSTAKEQNVPAYVVFTDNTLIAIAELLPTDDAALIAIPGIGARKLEQYGSDVLQLVRGRT
Protein: Lysine-specific demethylase JMJ27 (EC 1.14.11.65) (Jumonji domain-containing protein 27) (AtJMJ27) (Protein JUMONJI 27) (Lysine-specific histone demethylase JMJ27) ([histone H3]-dimethyl-L-lysine(9) monodemethylase JMJ27) (Q8VYB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone demethylase that demethylates 'Lys-9' (H3K9me) of histone H3 with a specific activity for H3K9me1 and H3K9me2. No activity on H3K4, H3K27, H3K36, H3R2 and H4R3 methyl marks, but weak activity on H3K9me3. Involved in regulation of gene expression. Regulates flowering time by repressing the major flowering regulator CONSTANS (CO) and promoting FLOWERING LOCUS C (FLC). Exhibits a positive impact on abscisic acid- (ABA), hydrogen peroxide- (H(2)O(2)) and calcium- (Ca(2+)) induced stomatal closure. Promotes stomatal-closure-dependent drought-stress responses through its histone demethylase activity toward at least GOLS2 and RD20 loci, thus protecting them from silencing by removing H3K9me2 marks in drought conditions. Required for plant defenses leading to resistance against the virulent bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst DC3000) via a negative regulation of WRKY25 (a repressor of defense) and by triggering the expression of several pathogenesis-related (PR) proteins (e.g. PR1, PR3, PR4 and PR5).
Subcellular location: Nucleus {ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643}. Cytoplasm {ECO:0000269|PubMed:28650521}. Note=Mainly observed in the nucleus, but also, to a lower extent, in the cytoplasm. {ECO:0000269|PubMed:28650521}.
Interaction partners:
- ATP-dependent RNA helicase DEAH12, chloroplastic
- Protein kinase superfamily protein
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH6
- Probable protein phosphatase 2C 51
- GLABRA2 expression modulator
Sequence:
MEKMRGKRIRPRDSGELVEDGRSESERKTRKKENDVVSKGRIGRGRGRGEVSKRSIEIDISNPEKDIKPDGSRKCLGSTCHHCKILTSESDLIFCSKCNKKCYCFDCIKRSYSERTHEEVRAACPFCMMTCICRACLRLPLVIKPPSEKDTDVKLKQLQYLLVKVLPVLKDIYTEQNRELEIESTIRGHPVTEANIKRCKLDPSERIYCDLCRTSIANFHRSCPNKNCSVDICLSCCKELSEGFHQERDGKKNAEGKGYECRIPAGQGKDSDAYVPLHFSTWKLNSDSSIPCPPKECGGCGTSTLELRRLWKRDWVEKLITNAEKCTLNFRPTDVDIVHECSSCSTNSDSIRRQAAFRKNAHDNFLYSPNAVDLAEDDIAHFQFHWMKAEPVIVRNVLEKTSGLSWEPMVMWRACREMDPKRKGTEEETTKVKALDCLDWCEVEINLHQFFEGYLEGRMHKNGWPEMLKLKDWPPSDLFEKRLPRHNAEFIAALPFFDYTDPKSGILNLATRFPEGSLKPDLGPKTYIAYGFHEELNRGDSVTKLHCDISDAVNVLTHTAKVEIPPVKYQNIKVHQKKYAEAMLQKQQYSGQVKEASELENKSMKEVDESKKDLKDKAANEEQSNNSSRPSGSGEAEKVIISKEDNPTQPAVSTSVESIQEQKLDAPKETDGNTNERSKAVHGGAVWDIFRREDVPKLIQFLKRHEHEFRHFNNEPLESVIHPIHDQTMFLSDSQKKQLKEEFDIEPWTFEQHLGEAVFIPAGCPHQVRNRQSCIKVALDFVAPESVEECLRLTQEFRRLPKDHSSSEDKLELKKIALYAASSAIREVKGLMQSSRRSDT
Protein: Retinoid-binding protein 7 (Cellular retinoic acid-binding protein 4) (CRABP4) (CRBP4) (Cellular retinoic acid-binding protein IV) (CRABP-IV) (Q96R05)
Organism: Homo sapiens (Human)
Function: Intracellular transport of retinol.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MPADLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRGLDNRKCKSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA
Protein: Prelamin-A/C [Cleaved into: Lamin-A/C] (P48678)
Organism: Mus musculus (Mouse)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis. Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis.
Subcellular location: Nucleus lamina {ECO:0000269|PubMed:28241138}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26436652}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. Also localizes to the micronuclear envelope in response to response to genome instability. {ECO:0000250|UniProtKB:P02545}.
Interaction partners:
- SUN domain-containing protein 1
- Emerin
- Lamin-B1
- Barrier-to-autointegration factor
- SUN domain-containing protein 2
- Lamin-B2
- Nesprin-2
- Nesprin-1
- Sterol regulatory element-binding protein 1
- Barrier-to-autointegration factor-like protein
Sequence:
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIRRQNGDDPLMTYRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGSSLRTALINSTGEEVAMRKLVRSLTMVEDNEDDDEDGEELLHHHRGSHCSGSGDPAEYNLRSRTVLCGTCGQPADKAAGGAGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGDNLVTRSYLLGNSSPRSQSSQNCSIM
Protein: Translocation protein SEC62 (Q9VL50)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MSEKKRARRRKDEYTEPGAQKVDKPSKDEKNVAKWLKKNVKTKKTKFLSHIVEYFTSSKAIDALLKSKFTEGSNPLFTTREQVIEFLDVMLEHKFFHRAKKVPVTLEEIRGKSGGDKKADKEKTQDKEKDKAKDEKKDTDPEGDNGQGDGGASGNEKEKEKKEKKKRKIRLDMHPEQIFVDGSEAYVWIYDPIPLHYWIFGFILLLGAVGICLFPLWPPLLRKGVYYLSIAAAGFLVFILALTIVRLIVFIIVWALTGGKLHFWIFPNLTEDVSFFASFWPLYESNYNSDPNNSSAKTDKKSKSKDKKKEKESDAEDTAVDADGDADGDVDAEVSTLEPEKIELIKEHDTDMEIRKRRKVGADDYEEDDVDEEETKAQPKDSKAGTPRNSGSDSESSSKDYEIISSSEVQNVAGN
Protein: Nuclear cap-binding protein subunit 2 (20 kDa nuclear cap-binding protein) (C9JQX9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364036}.
Interaction partners:
Sequence:
MGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYRQDYDAGRGGYGKLA
Protein: Glucomannan 4-beta-mannosyltransferase 9 (EC 2.4.1.32) (Cellulose synthase-like protein A9) (AtCslA9) (Glucomannan synthase) (Mannan synthase 9) (Protein RESISTANT TO AGROBACTERIUM TRANSFORMATION 4) (Q9LZR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses glucomannan synthase and mannan synthase activities in vitro. Mannan synthase consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall. Required for lateral root development.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cellulose synthase-like protein D2
- Cellulose synthase-like protein D5
- Cellulose synthase A catalytic subunit 4
- Cellulose synthase-like protein D3
- Cellulose synthase A catalytic subunit 1
- Cellulose synthase A catalytic subunit 8
- Cellulose synthase-like protein G1
- Cellulose synthase A catalytic subunit 7
- Transcription factor MYB46
- Cellulose synthase-like protein B6
Sequence:
MELGDTTSVIPDSFMGYRDDITMQMSMVLDQIRAPLIVPALRLGVYICLTMSVMLFVERVYMGIVISLVKLFGRKPDKRFKYEPIKDDIELGNSAYPMVLIQIPMFNEREVYQLSIGAACGLSWPSDRIVIQVLDDSTDPTIKDLVEMECSRWASKGVNIKYEIRDNRNGYKAGALKEGMKKSYVKSCDYVAIFDADFQPEADFLWRTVPYLLHNPKLALVQARWKFVNSDECLMTRMQEMSLDYHFTVEQEVGSSTYAFFGFNGTAGIWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFLYLGSLKVKNELPSTFKAYRYQQHRWSCGPANLFRKMAFEIMTNKNVTLWKKVHVIYSFFVVRKLVAHIVTFIFYCVILPATVLVPEVTVPKWGAVYIPSVITLLNAVGTPRSLHLMVFWILFENVMSLHRTKATFIGLLEGGRVNEWIVTEKLGDVKAKSATKTSKKVIRFRFGDRIHVLELGVGMYLLFVGCYDAFFGKNHYYLYLFAQAIAFFIAGFGQIGTIVPNH
Protein: LIM domain kinase 1 (LIMK-1) (EC 2.7.11.1) (dLIMK) (Q8IR79)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor tsr/cofilin, thereby stabilizing the actin cytoskeleton. Modulation of actin cytoskeleton dynamics may be essential for imaginal disk morphogenesis and axon guidance.
Subcellular location: Cytoplasm. Cleavage furrow. Midbody. Note=Localizes to the cleavage furrow and the midbody at cytokinesis.
Interaction partners:
- Cofilin/actin-depolymerizing factor homolog
- IP04855p
- Cdc42 homolog
- non-specific serine/threonine protein kinase
- Protein phosphatase Slingshot
- Ras-related protein Rac1
- non-specific serine/threonine protein kinase
- Rho-associated protein kinase
- Rho-related BTB domain containing, isoform B
- Heat shock protein 83
Sequence:
MHHQQRLRANGGRGGTGLGAGSGPVSGGHSPLCAHCRGQLLPHPEEPIVMALGQQWHCDCFRCSVCEGHLHNWYFEREGLLYCREDYYGRFGDACQQCMAVITGPVMVAGEHKFHPECFCCTACGSFIGEGESYALVERSKLYCGQCYGKRSCQPADAKARITTAGKPMHSIRLVEIPKDATPGLRVDGVALDDGCPTVRITDLFCNFFLWLTSMAEQCCGAPYRIDVNLTNLHIGDRILEVNGTPVSDSSVEQIDKLIRSNEKMLQLTVEHDPVQVCRSCSQADIQRAMSASTLILPLSTSASSVEVGRERLYKTPGEQGTKARKLRQATNASTTIPPAAGATAMTQLKEKERCSSLSKLLDEQHQAQQHSAHPQLYDLSRTQSCRVVQKPQRIFRATDLVIGEKLGEGFFGKVFKVTHRQSGEVMVLKELHRADEEAQRNFIKEVAVLRLLDHRHVLKFIGVLYKDKKLHMVTEYVAGGCLKELIHDPAQVLPWPQRVRLARDIACGMSYLHSMNIIHRDLNSMNCLVREDRSVIVADFGLARSVDAPRLPSGNMTPGGYGSGANSDAPMSPSGTLRRSKSRQRRQRYTVVGNPYWMAPEMMKGLKYDEKVDVFSFGIMLCEIIGRVEADPDFMPRNSDFSLNQQEFREKFCAQCPEPFVKVAFVCCDLNPDMRPCFETLHVWLQRLADDLAADRVPPERLLHEIETFQEWYASSEDALSPTSQRSLNNLDELVKSAVDSEISPVEKEKENMVIKPQDIPKSPHLGKDFSPSGERLRDSMRARRRQRFLGAQEERRNLTPDTESKERALKKALKKCRPFGERGYLVDLRAGAELQLEDVRDLNTYSDVDSSCDTSLNYHDVNNLPAAQEDENTVKPGKEELLEESTNKPSNQESQHHRLAIDDMRTRLNQCRSKFEHLEEASRRNFNQSQHSMKNFFKTPPVALKMFQRLEHEAAALNGGNNCPPPPPRTQRINQTPIFGRKNPPVAIVGQKLQHAESLEDLASSGVAKQLATPAPKRSKATATTKGGQSSNPPLFLPPSLNISVALNSNGNVTTTTNTNSSCPPSASDWLPKKHKLTLPLPSAQQQRTSSNHRLPMCNNKGKTLKPLPSRTGSQGIPASNCVSPTRSSRPGSPTKHLAQRHTAATAQRLTNAAATHQQQHQQQSSKTTRLNILSPEKVHRLGARLTDQKQKMREEAAATASSVGGAGCAAGTAAGSLNGHRTIGSSGTPNSAVGERRRRAAPSPPVRTHFNTRC
Protein: AT-rich interactive domain-containing protein 1B (A0A3F2YNW7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAARAAAAAAAAAARARARAGSGERRAPPGPRPAPGARDLEAGARGAAAAAAAPGPMLGGGGDGGGGLNSVHHHPLLPRHELNMAHNAGAAAAAGTHSAKSGGSEAALKEGGSAAALSSSSSSSAAAAAASSSSSSGPGSAMETGLLPNHKLKTVGEAPAAPPHQQHHHHHHAHHHHHHAHHLHHHHALQQQLNQFQQQQQQQQQQQQQQQQQQHPISNNNSLGGAGGGAPQPGPDMEQPQHGGAKDSAAGGQADPPGPPLLSKPGDEDDAPPKMGEPAGGRYEHPGLGALGTQQPPVAVPGGGGGPAAVPEFNNYYGSAAPASGGPGGRAGPCFDQHGGQQSPGMGMMHSASAAAAGAPGSMDPLQNSHEGYPNSQCNHYPGYSRPGAGGGGGGGGGGGGGSGGGGGGGGAGAGGAGAGAVAAAAAAAAAAAGGGGGGGYGGSSAGYGVLSSPRQQGGGMMMGPGGGGAASLSKAAAGSAAGGFQRFAGQNQHPSGATPTLNQLLTSPSPMMRSYGGSYPEYSSPSAPPPPPSQPQSQAAAAGAAAGGQQAAAGMGLGKDMGAQYAAASPAWAAAQQRSHPAMSPGTPGPTMGRSQGSPMDPMVMKRPQLYGMGSNPHSQPQQSSPYPGGSYGPPGPQRYPIGIQGRTPGAMAGMQYPQQQDSGDATWKETFWLMPPQYGQQGVSGYCQQGQQPYYSQQPQPPHLPPQAQYLPSQSQQRYQPQQDMSQEGYGTRSQPPLAPGKPNHEDLNLIQQERPSSLPDLSGSIDDLPTGTEATLSSAVSASGSTSSQGDQSNPAQSPFSPHASPHLSSIPGGPSPSPVGSPVGSNQSRSGPISPASIPGSQMPPQPPGSQSESSSHPALSQSPMPQERGFMAGTQRNPQMAQYGPQQTGPSMSPHPSPGGQMHAGISSFQQSNSSGTYGPQMSQYGPQGNYSRPPAYSGVPSASYSGPGPGMGISANNQMHGQGPSQPCGAVPLGRMPSAGMQNRPFPGNMSSMTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLMASSSPYSQPMNNSSSLMNTQAPPYSMAPAMVNSSAASVGLADMMSPGESKLPLPLKADGKEEGTPQPESKSKKSSSSTTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKIERGEEPPPEVFSTGDTKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTISVHDPFSDVSDSSFPKRNSMTPNAPYQQGMSMPDVMGRMPYEPNKDPFGGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGAMSNLGMGQRQQFPYGASYDRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYSSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMMGGPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQPSYQTPPSLPNHISRAPSPASFQRSLENRMSPSKSPFLPSMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPVLKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHNAARKDDSQSLADDSGKEEEDAECIDDDEEDEEDEEEDSEKTESDEKSSIALTAPDAAADPKEKPKQASKFDKLPIKIVKKNNLFVVDRSDKLGRVQEFNSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSAGRKKEQEGKGDSEEQQEKSIIATIDDVLSARPGALPEDANPGPQTESSKFPFGIQQAKSHRNIKLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
Protein: REST corepressor 2 (Q6NRZ0)
Organism: Xenopus laevis (African clawed frog)
Function: May act as a component of a corepressor complex that represses transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
Sequence:
MPSVMEKSHGSSAVISRNRAKSDSLGNSEEESSEDEAPRDSMIRVGSDYQAQIPECKPDNTSPSGNVELKGMLVWSPSQFVSDAKLNEYITMAKEKHGYNVEQSLGMLLWHKHDVERSLADLANFTPFPEEWSVEDKVLFEQAFSFHGKSFQRIQQMLPEKLIPSLVKYYYSWKKTRSRTSVMDRQARRLQAKREEGMEEVEDQIKMSDNETDVTETKKEAPVPQKVVSGAVSGKTGPVRKEPLISQYRHHPLRSRQRPPKGIHLNKSDVSAVCASSEMPAIALCQLETQLISLKRQVQNIKQMNSSLKESLEGGISEMRPPELNIKLNARWTTDEQLLAVQAVRKYGKDFQAISEVLGNKTPSQVKTFFISYRRRFNLEEVLQEWEAEQEPSPPPASTDMSNKTSGSSQTPNEEDDEVQITSVSSSSQPAPPAAAAAASLSLPPPLLRPAIPCAPTLHRQPPPLQPGRLLQPRPPPLVRPAPRQSPRAPPALVGSHAESTFS
Protein: Dual specificity phosphatase 29 (Dual specificity phosphatase DUPD1) (EC 3.1.3.16, EC 3.1.3.48) (Q8BK84)
Organism: Mus musculus (Mouse)
Function: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of intracellular signaling cascades. In skeletal muscle regulates systemic glucose homeostasis by activating, AMPK, an energy sensor protein kinase. Affects MAP kinase signaling though modulation of the MAPK1/2 cascade in skeletal muscle promoting muscle cell differentiation, development and atrophy.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30201684, ECO:0000269|PubMed:32639872}. Nucleus {ECO:0000269|PubMed:32639872}.
Interaction partners:
Sequence:
MASGDTKTSVKHAHLCAERLSVREEEGDAEDYCTPGAFELERLFWKGSPQYTHVNEVWPRLHIGDEATALDRYGLQKAGFTHVLNAAHGRWNVDTGPDYYRDMAIEYHGVEADDVPTFDLSIFFYSAAAFIDSALRDDHSKILVHCAMGRSRSATLVLAYLMIHKNMTLVDAIQQVAKNRCVLPNRGFLKQLRELDKQLVKQRRQAGPGDSDLGL
Protein: Carbonic anhydrase 6 (EC 4.2.1.1) (Carbonate dehydratase VI) (Carbonic anhydrase VI) (Q8N4G4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTDWQAELFLPSLSSPCGEGAKHKGQRQWLCSPSLDSWWEAIIDGGSLWATLAECGLRAEGPEEGRHMEEKSPASQGACSGSRLPISRGPCTFFL
Protein: Rab3 interacting molecule, isoform Q (Q9VEE5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDEMPDLSHLTPHERMQIENVLMRQKQEEEKQNEIMRRKQDEVVTLEMQIRQRSEQQKKAGVELDATCHICLKTKFADGVGHICHYCNIRCCARCGGKVTLRSNKVIWVCILCRKKQELLSKTGQWINKTAAQQDGFIRRIEPDGSSDISQHPIVDPHDTTDKRPKLERTRSAAEKENLPMQRAGSMLRRQYSQQEQPTNRRLSASDSGMDPVMSPGQQMQHHQQQQRARMQPMNPQQAQQGYGMQQQQQPRSGGAYPDDDPRYYQGELDGLMRQHPHLAHPSQVQPQHTPQSHSQQQQSQHQQQHLMPQQHRPSPQQHSQQQQQQQQHSQQFAARQQQHQQQQHQQQVQQSYHAQIHQQPQQHPHPHSQQQQHHQQMQHQHGQSVPQMGGYQKPPPLTRNLTISGGHAMDSSAYSQQQQQQQRRALAGSQYASQQQRSFSSSEEEFQHQLLAAQGAVTVTAGSDYDGGRLQVRTSLDPWRQQRSLNERDLLSSGGGGGGGVGGADFRHLSHATQRLYASADQRDRYELQLQHRERLEQYPLTRTARLDVQQRNSLNRSNHERQFSGGGAGVGPGGAGGGGAAGAYRRAPPLAAAGGGGSSSSSTTSSSYYPQSKPQIVIGPGSGYDRGSGSMASMASAAAATAADAQGQAARNSQRGGLLGATRGGGGSSSVSSTEAAYWDEPATSSSSSAAQDSRRFTERRIKKTVRFDAHDEEASILASSSLPPVTAILPSTAVDVGAATILSSGKSLDAVGVGGADWSRWEAERQGSQDSATKDSGIDTSSTFTSSEDSNRGDGPKNPVNWQTSADNTRLIGHMILRKYYDGEDILGLKVNGGQPLATGGSVSGAGTGAAIGAGGPCGAIVEKVKRGSVADLEGRIRPGDEILEWNGRGLHNKSADEVYDIIDESRLDAQVELIVSRPIGSGGGSGGSSANVSPISGASGGSANSVPARRSSANFPHSGLASSMAGSAVVSSGGRYLQRKAPAVEAIEIHRDKPSVLITSPGSPDIHTSVSGPGSVSGSGLRQRGGVGQTQRLGPSHSTHSHSSSGSGSGSGSSTSSVHAPASAHGPVHASASASGSAPGGLHGTTTAGHHHHPHPHHYHPHQHPLPHPHQHQGPPAAHLQGHGVGGGIGMGSGSGTTTQPIPIEGRLQLKLGYDQNTLQLIVTLVCATGLSLRQSGAGRNPYAKVFLLPDRSHKSKRRTKTVGTTCEPRWGQTFVYSGLRRCDLNGRLLEVTLWDYVRYGANDFIGEVVIDLAHHILDDEAEWYQLQPHQDTSYLLRDEGSDVDGLILTPTDHLSPPSTMSRLSDSDTTSDCDIDGMTPGASISSMGSSASPPPLLELDLNERRSRRDMSPQGRKRVAGMVARDYRTVSGIGQSYHNQASATGYYRRGGGNGVGSAIGPGGMSLSQRSHSAAPSDGYHSSGVGGAASGGPAYGYRSTSPRRGSLSPPDDRYIDYPVLPVHGSSPNAPSVYQGPGGVSSAAASASQQQRFQSRSATATPTGSPKKRQLPQVPQTSRSAMLRDRLGQDFDERLASGGRFGRHRTRQPHHQATYRSTGMGGWERHYTGLSDSDLHSMDARMRPRHSLSPDKDFMGEFGDSDMESVVSVTSSAFSTQSERPRTSRGLSEYDKDKNGAEEAGGSKSAEGAGAEDKVDGSLSDTANDRKKGGGVDQERSPKGGSGMGKKSNSTSQLSATEQEQYQAQFAIAGSSTSSAGHHHITLPPPHPYHQRQSRGSAGSIQRSVEVPPVPPVTRYSAGSIHSITSSEGSSFSPSLRNDGALNEFVDGLGPGQLVGRQVLGAPSLGDIQLSLCHQKGCLEVEVIRARGLQQKAQSKMLPAPYVKVYLVSGKRCVDKMKTSSARRTLDPLYQQQLVFKQSYTGCILQITVWGDYGRIEKKVFMGVAQIMLDDLNLSNIVIGWYKLFGTTSL
Protein: E3 ubiquitin-protein ligase TRAIP (EC 2.3.2.27) (TRAF-interacting protein) (Q6NRV0)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin ligase required to protect genome stability in response to replication stress. Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription. Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of mcm7 subunit of the CMG helicase complex. Short ubiquitin chains on mcm7 promote recruitment of DNA glycosylase neil3. If the interstrand cross-link cannot be cleaved by neil3, the ubiquitin chains continue to grow on mcm7, promoting the unloading of the CMG helicase complex by the vcp/p97 ATPase, enabling the Fanconi anemia DNA repair pathway. Only catalyzes ubiquitination of mcm7 when forks converge. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome. Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BWF2}. Chromosome {ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:30842657, ECO:0000269|PubMed:30979826}. Cytoplasm {ECO:0000250|UniProtKB:Q9BWF2}. Note=Localizes to DNA damage sites in response to replication stress. {ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:30842657}.
Interaction partners:
Sequence:
MPIRAYCTICSDFFDNARDVAAITCGHTFHQECLLQWFHSAPHRTCPQCRIQVSSRQIINKLFFDIGGEEETVLDAESLKNEVDRIKASLLVKEKEKRECQGLVDSLREMLDVRNVTIQSQQKELGDMEMLCSTLKKQIKFLDKQQSETKAAKDEARKLRNKLKTMESIEVLLQSQRSEVEEMIRDMGSGQAAVEQLAIYCVSLKKEYENLKEVRKSSAEMTEKLRKELFSSNHKAQKAELELTKVREELSASQKELHSADKEIMSLKKKVEFLQKTLTTPTASNEAISRLIFESPAPIGLERPKLRPPMMGNDINLDVTFDIDTPEHNTQKSVVAPFKKMKFDNKEHPLSSPTKNPLQESKGLMSWAGGRTGADEDDDLTLPSFIKNSLLHKKPVGSLLGLRQNTGAVRTGFDGLGGRTKFIQPSNLTEIRPLHQKMKRKKVSRPTACTSSLANQPRLEDFLK