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UniProtKB/Swiss-Prot entry Q9NYV4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CD2L7_HUMAN
Primary accession number Q9NYV4
Secondary accession numbers A7E2B2 O94978
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 72)
Name and origin of the protein
Protein name Cell division cycle 2-related protein kinase 7
Synonyms CDC2-related protein kinase 7
EC 2.7.11.22
Cdc2-related kinase, arginine/serine-rich
CrkRS
Gene name
Name: CRKRS
Synonyms: CRK7, KIAA0904
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11683387 [NCBI, ExPASy, EBI, Israel, Japan]
Ko T.K., Kelly E., Pines J.;
"CrkRS: a novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles.";
J. Cell Sci. 114:2591-2603(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1093/dnares/5.6.355; PubMed=10048485 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[3]
SEQUENCE REVISION.
DOI=10.1093/dnares/9.3.99; PubMed=12168954 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-249; SER-265; SER-293; SER-303; SER-423; THR-692 AND SER-1083, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-80; SER-84; SER-274; SER-276; SER-423; SER-681 AND SER-685, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND THR-692, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-276; SER-383; SER-385; SER-423; SER-681; SER-685 AND THR-893, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-301; SER-303; SER-318; SER-320; SER-323; SER-325; SER-332; SER-333; SER-334; SER-343; SER-345; SER-382; SER-383; SER-385; SER-400; SER-423; SER-681; SER-685 AND THR-692, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
VARIANTS [LARGE SCALE ANALYSIS] ALA-530; HIS-912; GLN-1189 AND LEU-1275.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF227198; AAF36401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020711; BAA74927.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC150265; AAI50266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_055898.1; -.
NP_057591.2; -.
UniGene Hs.416108
3D structure databases
HSSP P24941; 1P2A. [HSSP ENTRY / PDB]
ModBase Q9NYV4.
Protein-protein interaction databases
IntAct Q9NYV4; -.
PTM databases
PhosphoSite Q9NYV4; -.
Organism-specific databases
H-InvDB HIX0013777; -.
HGNC HGNC:24224; CRKRS.
GenAtlas CRKRS.
HPA HPA008038; -.
PharmGKB PA142672078; -.
GeneCards Q9NYV4.
HUGE KIAA0904.
Gene expression databases
ArrayExpress Q9NYV4; -.
CleanEx HS_CRKRS; -.
Ontologies
GO
GO:0016607; Cellular component: nuclear speck (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0003702; Molecular function: RNA polymerase II transcription factor activity (non-traceable author statement from HGNC).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NYV4.
Genome annotation databases
Ensembl ENSG00000167258; Homo sapiens. [Contig view]
GeneID 51755; -.
KEGG hsa:51755; -.
Phylogenomic databases
HOGENOM Q9NYV4; -.
HOVERGEN Q9NYV4; -.
Other
NextBio 55858; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1490  1490     Cell division cycle 2-related protein kinase 7. PRO_0000085715
DOMAIN   727   1020  294     Protein kinase. 
NP_BIND   733    741  9     ATP (By similarity). 
COMPBIAS   407    413  7     Poly-Ala. 
COMPBIAS   535    540  6     Poly-Pro. 
COMPBIAS   1266   1280  15     Poly-Pro. 
ACT_SITE   859    859        Proton acceptor (By similarity). 
BINDING   756    756        ATP (By similarity). 
MOD_RES   77     77        Phosphoserine. 
MOD_RES   78     78        Phosphoserine. 
MOD_RES   80     80        Phosphoserine. 
MOD_RES   84     84        Phosphoserine. 
MOD_RES   215    215        Phosphoserine. 
MOD_RES   249    249        Phosphoserine. 
MOD_RES   265    265        Phosphoserine. 
MOD_RES   274    274        Phosphoserine. 
MOD_RES   276    276        Phosphoserine. 
MOD_RES   279    279        Phosphotyrosine (By similarity). 
MOD_RES   293    293        Phosphoserine. 
MOD_RES   301    301        Phosphoserine. 
MOD_RES   303    303        Phosphoserine. 
MOD_RES   318    318        Phosphoserine. 
MOD_RES   319    319        Phosphotyrosine (By similarity). 
MOD_RES   320    320        Phosphoserine. 
MOD_RES   323    323        Phosphoserine. 
MOD_RES   325    325        Phosphoserine. 
MOD_RES   332    332        Phosphoserine. 
MOD_RES   333    333        Phosphoserine. 
MOD_RES   334    334        Phosphoserine. 
MOD_RES   343    343        Phosphoserine. 
MOD_RES   345    345        Phosphoserine. 
MOD_RES   382    382        Phosphoserine. 
MOD_RES   383    383        Phosphoserine. 
MOD_RES   385    385        Phosphoserine. 
MOD_RES   400    400        Phosphoserine. 
MOD_RES   423    423        Phosphoserine. 
MOD_RES   681    681        Phosphoserine. 
MOD_RES   685    685        Phosphoserine. 
MOD_RES   692    692        Phosphothreonine. 
MOD_RES   893    893        Phosphothreonine. 
MOD_RES   1083   1083        Phosphoserine. 
VAR_SEQ   1254   1262        Missing (in isoform 2). VSP_030284
VARIANT   530    530  1     P -> A. VAR_041968 
VARIANT   912    912  1     R -> H (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041969 
VARIANT   1189   1189  1     L -> Q. VAR_041970 
VARIANT   1275   1275  1     P -> L. VAR_041971 
CONFLICT   639    639        G -> D (in Ref. 2; BAA74927 and 4; AAI50266). 
CONFLICT   745    745        R -> K (in Ref. 2; BAA74927 and 4; AAI50266). 
Sequence information
Length: 1490 AA [This is the length of the unprocessed precursor] Molecular weight: 164155 Da [This is the MW of the unprocessed precursor] CRC64: 851E18DF3BD2B1A1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 

        70         80         90        100        110        120 
ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 

       130        140        150        160        170        180 
DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 

       190        200        210        220        230        240 
KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 

       250        260        270        280        290        300 
SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 

       310        320        330        340        350        360 
SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP 

       370        380        390        400        410        420 
AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES 

       430        440        450        460        470        480 
KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK 

       490        500        510        520        530        540 
VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP 

       550        560        570        580        590        600 
TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 

       610        620        630        640        650        660 
SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGGD DMDSPKETLP SKPVKKEKEQ 

       670        680        690        700        710        720 
RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG 

       730        740        750        760        770        780 
KRCVDKFDII GIIGEGTYGQ VYKARDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ 

       790        800        810        820        830        840 
LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM 

       850        860        870        880        890        900 
KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 

       910        920        930        940        950        960 
YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW 

       970        980        990       1000       1010       1020 
PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL 

      1030       1040       1050       1060       1070       1080 
KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK 

      1090       1100       1110       1120       1130       1140 
NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI 

      1150       1160       1170       1180       1190       1200 
HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQMTLEAS 

      1210       1220       1230       1240       1250       1260 
STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAACPPHIL 

      1270       1280       1290       1300       1310       1320 
PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA LLQLLSQPEA EPPGHLPHEH 

      1330       1340       1350       1360       1370       1380 
QALRPMEYST RPRPNRTYGN TDGPETGFSA IDTDERNSGP ALTESLVQTL VKNRTFSGSL 

      1390       1400       1410       1420       1430       1440 
SHLGESSSYQ GTGSVQFPGD QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY 

      1450       1460       1470       1480       1490 
GELGPGTTGA SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY 

Q9NYV4 in FASTA format

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