ID   CD2L7_HUMAN             Reviewed;        1490 AA.
AC   Q9NYV4; A7E2B2; O94978;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 78.
DE   RecName: Full=Cell division cycle 2-related protein kinase 7;
DE            Short=CDC2-related protein kinase 7;
DE            EC=2.7.11.22;
DE   AltName: Full=Cdc2-related kinase, arginine/serine-rich;
DE            Short=CrkRS;
GN   Name=CRKRS; Synonyms=CRK7, KIAA0904;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   MEDLINE=21539573; PubMed=11683387;
RA   Ko T.K., Kelly E., Pines J.;
RT   "CrkRS: a novel conserved Cdc2-related protein kinase that colocalises
RT   with SC35 speckles.";
RL   J. Cell Sci. 114:2591-2603(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=99156230; PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [3]
RP   SEQUENCE REVISION.
RX   MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-249; SER-265;
RP   SER-293; SER-303; SER-423; THR-692 AND SER-1083, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-80;
RP   SER-84; SER-274; SER-276; SER-423; SER-681 AND SER-685, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND THR-692, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-276; SER-383;
RP   SER-385; SER-423; SER-681; SER-685 AND THR-893, AND MASS SPECTROMETRY.
RX   PubMed=17192257; DOI=10.1074/mcp.T600062-MCP200;
RA   Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,
RA   Keri G., Wehland J., Daub H.;
RT   "Proteomics analysis of protein kinases by target class-selective
RT   prefractionation and tandem mass spectrometry.";
RL   Mol. Cell. Proteomics 6:537-547(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-25; SER-32;
RP   THR-57; TYR-73; SER-77; SER-78; SER-80; SER-84; SER-236; SER-238;
RP   SER-249; SER-274; SER-276; SER-291; SER-293; SER-301; SER-303;
RP   SER-341; SER-343; SER-383; SER-385; SER-400; SER-423; THR-514;
RP   SER-681; SER-685; THR-692; THR-893; SER-1083 AND THR-1244, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-301; SER-303;
RP   SER-318; SER-320; SER-323; SER-325; SER-332; SER-333; SER-334;
RP   SER-343; SER-345; SER-382; SER-383; SER-385; SER-400; SER-423;
RP   SER-681; SER-685 AND THR-692, AND MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [12]
RP   VARIANTS [LARGE SCALE ANALYSIS] ALA-530; HIS-912; GLN-1189 AND
RP   LEU-1275.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Involved in RNA splicing.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Colocalized
CC       with nuclear speckles throughout interphase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NYV4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NYV4-2; Sequence=VSP_030284;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF227198; AAF36401.1; -; mRNA.
DR   EMBL; AB020711; BAA74927.2; ALT_INIT; mRNA.
DR   EMBL; BC150265; AAI50266.1; -; mRNA.
DR   IPI; IPI00021175; -.
DR   IPI; IPI00868781; -.
DR   RefSeq; NP_055898.1; -.
DR   RefSeq; NP_057591.2; -.
DR   UniGene; Hs.416108; -.
DR   HSSP; P24941; 1P2A.
DR   IntAct; Q9NYV4; 6.
DR   PhosphoSite; Q9NYV4; -.
DR   PRIDE; Q9NYV4; -.
DR   Ensembl; ENSG00000167258; Homo sapiens.
DR   GeneID; 51755; -.
DR   KEGG; hsa:51755; -.
DR   GeneCards; GC17P034872; -.
DR   H-InvDB; HIX0013777; -.
DR   HGNC; HGNC:24224; CRKRS.
DR   HPA; HPA008038; -.
DR   PharmGKB; PA142672078; -.
DR   HOGENOM; Q9NYV4; -.
DR   HOVERGEN; Q9NYV4; -.
DR   BRENDA; 2.7.11.22; 247.
DR   NextBio; 55858; -.
DR   ArrayExpress; Q9NYV4; -.
DR   Bgee; Q9NYV4; -.
DR   CleanEx; HS_CRKRS; -.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor acti...; NAS:HGNC.
DR   GO; GO:0046777; P:protein amino acid autophosphorylation; IDA:HGNC.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1490       Cell division cycle 2-related protein
FT                                kinase 7.
FT                                /FTId=PRO_0000085715.
FT   DOMAIN      727   1020       Protein kinase.
FT   NP_BIND     733    741       ATP (By similarity).
FT   COMPBIAS    407    413       Poly-Ala.
FT   COMPBIAS    535    540       Poly-Pro.
FT   COMPBIAS   1266   1280       Poly-Pro.
FT   ACT_SITE    859    859       Proton acceptor (By similarity).
FT   BINDING     756    756       ATP (By similarity).
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES      57     57       Phosphothreonine.
FT   MOD_RES      73     73       Phosphotyrosine.
FT   MOD_RES      77     77       Phosphoserine.
FT   MOD_RES      78     78       Phosphoserine.
FT   MOD_RES      80     80       Phosphoserine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     236    236       Phosphoserine.
FT   MOD_RES     238    238       Phosphoserine.
FT   MOD_RES     249    249       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     274    274       Phosphoserine.
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     279    279       Phosphotyrosine (By similarity).
FT   MOD_RES     291    291       Phosphoserine.
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     301    301       Phosphoserine.
FT   MOD_RES     303    303       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine.
FT   MOD_RES     319    319       Phosphotyrosine (By similarity).
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES     325    325       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine.
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     341    341       Phosphoserine.
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     385    385       Phosphoserine.
FT   MOD_RES     400    400       Phosphoserine.
FT   MOD_RES     423    423       Phosphoserine.
FT   MOD_RES     514    514       Phosphothreonine.
FT   MOD_RES     681    681       Phosphoserine.
FT   MOD_RES     685    685       Phosphoserine.
FT   MOD_RES     692    692       Phosphothreonine.
FT   MOD_RES     893    893       Phosphothreonine.
FT   MOD_RES    1083   1083       Phosphoserine.
FT   MOD_RES    1244   1244       Phosphothreonine.
FT   VAR_SEQ    1254   1262       Missing (in isoform 2).
FT                                /FTId=VSP_030284.
FT   VARIANT     530    530       P -> A.
FT                                /FTId=VAR_041968.
FT   VARIANT     912    912       R -> H (in a colorectal adenocarcinoma
FT                                sample; somatic mutation).
FT                                /FTId=VAR_041969.
FT   VARIANT    1189   1189       L -> Q.
FT                                /FTId=VAR_041970.
FT   VARIANT    1275   1275       P -> L.
FT                                /FTId=VAR_041971.
FT   CONFLICT    639    639       G -> D (in Ref. 2; BAA74927 and 4;
FT                                AAI50266).
FT   CONFLICT    745    745       R -> K (in Ref. 2; BAA74927 and 4;
FT                                AAI50266).
SQ   SEQUENCE   1490 AA;  164155 MW;  851E18DF3BD2B1A1 CRC64;
     MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA
     ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR
     DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH
     KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA
     SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR
     SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP
     AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES
     KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK
     VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP
     TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN
     SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGGD DMDSPKETLP SKPVKKEKEQ
     RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG
     KRCVDKFDII GIIGEGTYGQ VYKARDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ
     LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM
     KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW
     YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW
     PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL
     KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK
     NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI
     HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQMTLEAS
     STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAACPPHIL
     PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA LLQLLSQPEA EPPGHLPHEH
     QALRPMEYST RPRPNRTYGN TDGPETGFSA IDTDERNSGP ALTESLVQTL VKNRTFSGSL
     SHLGESSSYQ GTGSVQFPGD QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY
     GELGPGTTGA SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY
//