ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P24788


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CD2L1_MOUSE
Primary accession number P24788
Secondary accession numbers Q3UI03 Q61399 Q7TST4 Q8BP53
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on January 4, 2005 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name PITSLRE serine/threonine-protein kinase CDC2L1
Synonyms EC 2.7.11.22
Cell division cycle 2-like protein kinase 1
Galactosyltransferase-associated protein kinase p58/GTA
Gene name
Name: Cdc2l1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=2069872 [NCBI, ExPASy, EBI, Israel, Japan]
Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S., Snead M.L.;
"Regulated expression of a cell division control-related protein kinase during development.";
Cell Growth Differ. 2:85-93(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7528743 [NCBI, ExPASy, EBI, Israel, Japan]
Malek S.N., Desiderio S.;
"A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand.";
J. Biol. Chem. 269:33009-33020(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Stomach;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-784 (ISOFORM 1).
TISSUE=Eye;
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-270, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-740 AND SER-741, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(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
M58633; AAA03518.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L37092; AAA66169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK077668; BAC36942.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK147133; BAE27703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052920; AAH52920.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A55817; A55817.
RefSeq NP_031687.2; -.
UniGene Mm.267410
3D structure databases
HSSP P24941; 1H00. [HSSP ENTRY / PDB]
ModBase P24788.
PTM databases
PhosphoSite P24788; -.
Organism-specific databases
MGI MGI:88353; Cdc2l1.
Gene expression databases
CleanEx MM_CDC2L1; -.
GermOnline ENSMUSG00000029062; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
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:0006915; Biological process: apoptosis (inferred from mutant phenotype from MGI).
GO:0001824; Biological process: blastocyst development (inferred from mutant phenotype from MGI).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007088; Biological process: regulation of mitosis (inferred from mutant phenotype from MGI).
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; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P24788.
Genome annotation databases
Ensembl ENSMUSG00000029062; Mus musculus. [Contig view]
GeneID 12537; -.
KEGG mmu:12537; -.
Phylogenomic databases
HOGENOM P24788; -.
HOVERGEN P24788; -.
Other
NextBio 281574; -.
SOURCE Cdc2l1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   784  784     PITSLRE serine/threonine-protein kinase CDC2L1. PRO_0000024313
DOMAIN   427   712  286     Protein kinase. 
NP_BIND   433   441  9     ATP (By similarity). 
COMPBIAS   291   304  14     Poly-Glu. 
COMPBIAS   309   325  17     Poly-Glu. 
ACT_SITE   551   551        Proton acceptor (By similarity). 
BINDING   456   456        ATP (By similarity). 
MOD_RES   270   270        Phosphoserine. 
MOD_RES   437   437        Phosphothreonine (By similarity). 
MOD_RES   438   438        Phosphotyrosine (By similarity). 
MOD_RES   578   578        Phosphoserine (By similarity). 
MOD_RES   584   584        Phosphothreonine (By similarity). 
MOD_RES   740   740        Phosphothreonine. 
MOD_RES   741   741        Phosphoserine. 
VAR_SEQ   1   345        Missing (in isoform 2). VSP_018835
CONFLICT   35    37        LKN -> MSQ (in Ref. 4; AAH52920). 
CONFLICT   284   284        Missing (in Ref. 2; AAA66169). 
CONFLICT   560   560        S -> T (in Ref. 1; AAA03518). 
CONFLICT   608   608        V -> C (in Ref. 1; AAA03518). 
CONFLICT   645   645        T -> S (in Ref. 1; AAA03518). 
CONFLICT   668   668        Y -> I (in Ref. 1; AAA03518). 
Sequence information
Length: 784 AA [This is the length of the unprocessed precursor] Molecular weight: 91513 Da [This is the MW of the unprocessed precursor] CRC64: CDF03AC3957FA351 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI 

        70         80         90        100        110        120 
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK 

       130        140        150        160        170        180 
HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK 

       190        200        210        220        230        240 
LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR 

       250        260        270        280        290        300 
ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE 

       310        320        330        340        350        360 
EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV 

       370        380        390        400        410        420 
VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG 

       430        440        450        460        470        480 
CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK 

       490        500        510        520        530        540 
AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK 

       550        560        570        580        590        600 
HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG 

       610        620        630        640        650        660 
AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV 

       670        680        690        700        710        720 
KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID 

       730        740        750        760        770        780 
PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF 


SLKF 

P24788 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!