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CHK2 checkpoint homolog (S. pombe), isoform CRA_a (Checkpoint kinase 2) (Checkpoint kinase Chk2)

 Q9R019_RAT              Unreviewed;       545 AA.
Q9R019;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 137.
SubName: Full=CHK2 checkpoint homolog (S. pombe), isoform CRA_a {ECO:0000313|EMBL:EDM14023.1};
SubName: Full=Checkpoint kinase 2 {ECO:0000313|Ensembl:ENSRNOP00000053643};
SubName: Full=Checkpoint kinase Chk2 {ECO:0000313|EMBL:AAD55890.1};
Name=Chek2 {ECO:0000313|EMBL:EDM14023.1,
ECO:0000313|Ensembl:ENSRNOP00000053643, ECO:0000313|RGD:621543};
ORFNames=rCG_21791 {ECO:0000313|EMBL:EDM14023.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|EMBL:AAD55890.1};
[1] {ECO:0000313|EMBL:AAD55890.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Thymus {ECO:0000313|EMBL:AAD55890.1};
PubMed=10435585; DOI=10.1038/sj.onc.1202925;
Chaturvedi P., Eng W.K., Zhu Y., Mattern M.R., Mishra R., Hurle M.R.,
Zhang X., Annan R.S., Lu Q., Faucette L.F., Scott G.F., Li X.,
Carr S.A., Johnson R.K., Winkler J.D., Zhou B.B.;
"Mammalian Chk2 is a downstream effector of the ATM-dependent DNA
damage checkpoint pathway.";
Oncogene 18:4047-4054(1999).
[2] {ECO:0000313|Ensembl:ENSRNOP00000053643, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053643,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3] {ECO:0000313|EMBL:EDM14023.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM14023.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[4] {ECO:0000313|EMBL:EDM14023.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM14023.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|Ensembl:ENSRNOP00000053643}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053643};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[6] {ECO:0000313|Ensembl:ENSRNOP00000074651}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000074651};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
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EMBL; AC095390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF134054; AAD55890.1; -; mRNA.
EMBL; CH473973; EDM14023.1; -; Genomic_DNA.
RefSeq; NP_446129.1; NM_053677.1.
RefSeq; XP_006249580.1; XM_006249518.3.
RefSeq; XP_006249581.1; XM_006249519.2.
RefSeq; XP_006249582.1; XM_006249520.3.
RefSeq; XP_006249583.1; XM_006249521.3.
UniGene; Rn.163213; -.
STRING; 10116.ENSRNOP00000053643; -.
Ensembl; ENSRNOT00000056800; ENSRNOP00000053643; ENSRNOG00000037509.
Ensembl; ENSRNOT00000085591; ENSRNOP00000074651; ENSRNOG00000037509.
GeneID; 114212; -.
KEGG; rno:114212; -.
CTD; 11200; -.
RGD; 621543; Chek2.
eggNOG; KOG0615; Eukaryota.
eggNOG; ENOG410YA63; LUCA.
GeneTree; ENSGT00800000124190; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG108055; -.
KO; K06641; -.
OMA; SRAVDCW; -.
OrthoDB; EOG091G0DVW; -.
TreeFam; TF101082; -.
Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-RNO-6804757; Regulation of TP53 Degradation.
Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
Reactome; R-RNO-69541; Stabilization of p53.
Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000037509; -.
GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0016301; F:kinase activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0044257; P:cellular protein catabolic process; IEA:Ensembl.
GO; GO:1903926; P:cellular response to bisphenol A; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IMP:RGD.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IEA:Ensembl.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
GO; GO:0044773; P:mitotic DNA damage checkpoint; IBA:GO_Central.
GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
GO; GO:0071157; P:negative regulation of cell cycle arrest; IGI:RGD.
GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:2000210; P:positive regulation of anoikis; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0001302; P:replicative cell aging; IEA:Ensembl.
GO; GO:1903416; P:response to glycoside; IEP:RGD.
GO; GO:0042770; P:signal transduction in response to DNA damage; IBA:GO_Central.
GO; GO:0072428; P:signal transduction involved in intra-S DNA damage checkpoint; IEA:Ensembl.
CDD; cd00060; FHA; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00240; FHA; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Kinase {ECO:0000313|EMBL:AAD55890.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Transferase {ECO:0000313|EMBL:AAD55890.1}.
DOMAIN 116 178 FHA. {ECO:0000259|PROSITE:PS50006}.
DOMAIN 223 489 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 545 AA; 60930 MW; CE532BAD08608873 CRC64;
MKSHQSHGST SSKAHDSASC SQSQGGFSQS QGTPSQLHDL SQYQGASSSS TSTVPSSSQS
SHSSSGTLSS LETVSTQELC SIPEDQEPEE PGPTPWARLW ALQDGFSNLD CVNDNYWFGR
DKSCEYCFDG PLLKRTDKYR TYSKKHFRIF REMGPKNCYI VYLEDHSGNG TFVNTELIGK
GKRCPLSNNS EIALSLCRNK VFVFFDLTVD DQSVYPKELR DEYIMSKTLG SGACGEVKMA
FERKTCKKVA IKIISKRRFA LGSSREADTA PSVETEIEIL KKLNHPCIIK IKDVFDVEDY
YIVLELMEGG ELFDRVVGNK RLKEATCKLY FYQMLLAVQY LHENGIIHRD LKPENVLLSS
QEEDCLIKIT DFGQSKILGE TSLMRTLCGT PTYLAPEVLI SNGTAGYSRA VDCWSLGVIL
FICLSGYPPF SEHKTQVSLK DQITSGKYNL IPEVWTDVSE KALDLVKKLL VVDPKARLTT
EEALSHPWLQ DEHMKKKFQD LLVQEKNLVP LPLAPAQTSG QKRPLELEAE DAESSKRLAV
CKAVL


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