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UniProtKB/Swiss-Prot entry P21127


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

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Entry information
Entry name CD2L1_HUMAN
Primary accession number P21127
Secondary accession numbers O95265 Q12817 Q12818 Q12819 Q12820 Q12822 Q8N530 Q9NZS5 Q9UBJ0 Q9UBQ1 Q9UBR0 Q9UNY2 Q9UP57 Q9UP58 Q9UP59
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on September 19, 2003 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 102)
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
CLK-1
p58 CLK-1
Galactosyltransferase-associated protein kinase p58/GTA
CDK11
Gene name
Name: CDC2L1
Synonyms: PITSLREA, PK58
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 7), AND FUNCTION.
TISSUE=Liver;
PubMed=2217177 [NCBI, ExPASy, EBI, Israel, Japan]
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.;
"Increased expression of a 58-kDa protein kinase leads to changes in the CHO cell cycle.";
Proc. Natl. Acad. Sci. U.S.A. 87:7467-7471(1990).
[2]
ERRATUM, AND SEQUENCE REVISION.
PubMed=2006197 [NCBI, ExPASy, EBI, Israel, Japan]
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.;
Proc. Natl. Acad. Sci. U.S.A. 88:2612-2612(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7), AND VARIANT GLN-601.
TISSUE=Hematopoietic;
DOI=10.1016/0888-7543(92)90132-C; PubMed=1639388 [NCBI, ExPASy, EBI, Israel, Japan]
Eipers P.G., Lahti J.M., Kidd V.J.;
"Structure and expression of the human p58clk-1 protein kinase chromosomal gene.";
Genomics 13:613-621(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; 2; 3; 8 AND SV11), VARIANT CYS-57, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=8195233 [NCBI, ExPASy, EBI, Israel, Japan]
Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.;
"Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms.";
J. Biol. Chem. 269:15786-15794(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SV1; SV4; SV5; SV9; SV10 AND SV11), AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9750192 [NCBI, ExPASy, EBI, Israel, Japan]
Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F., Kidd V.J.;
"Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2.";
Genome Res. 8:929-939(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV11).
TISSUE=Placenta;
Govindan M.V., Warriar N.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-795.
TISSUE=Uterus;
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).
[8]
INTERACTION WITH RNPS1.
PubMed=9580558 [NCBI, ExPASy, EBI, Israel, Japan]
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.;
"The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo.";
J. Cell Sci. 111:1495-1506(1998).
[9]
ALTERNATIVE INITIATION (ISOFORM 7), AND INDUCTION.
DOI=10.1016/S1097-2765(00)80239-7; PubMed=10882096 [NCBI, ExPASy, EBI, Israel, Japan]
Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S., Beyaert R.;
"Identification and characterization of a novel cell cycle-regulated internal ribosome entry site.";
Mol. Cell 5:597-605(2000).
[10]
INTERACTION WITH RANBP9, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.bbrc.2003.08.116; PubMed=14511641 [NCBI, ExPASy, EBI, Israel, Japan]
Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.;
"The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM.";
Biochem. Biophys. Res. Commun. 310:14-18(2003).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNL1 AND SFRS7.
DOI=10.1074/jbc.M210057200; PubMed=12501247 [NCBI, ExPASy, EBI, Israel, Japan]
Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.;
"CDK11 complexes promote pre-mRNA splicing.";
J. Biol. Chem. 278:8623-8629(2003).
[12]
FUNCTION, AND INTERACTION WITH PAK1.
DOI=10.1074/jbc.M300818200; PubMed=12624090 [NCBI, ExPASy, EBI, Israel, Japan]
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H., Hu Y., Yuan Z., Shen Z., Gu J.;
"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis.";
J. Biol. Chem. 278:20029-20036(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-589 AND THR-595, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND THR-595, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
VARIANTS [LARGE SCALE ANALYSIS] CYS-57; TRP-201; LEU-414; ALA-452; VAL-463; SER-506; GLN-601; ASN-641 AND VAL-670.
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
  • FUNCTION: Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • COFACTOR: Magnesium.
  • ENZYME REGULATION: Phosphorylation at Thr-448 or Tyr-449 inactivates the enzyme, while phosphorylation at Thr-595 activates it (By similarity).
  • SUBUNIT: The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1 and RANBP9. The cleaved p110 isoform interacts with RNPS1. The p58 isoform but not the p110 isoforms or p110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7.
  • INTERACTION:
    Q13153:PAK1; NbExp=2; IntAct=EBI-1298, EBI-1307;
    Q15287:RNPS1; NbExp=1; IntAct=EBI-1298, EBI-395959;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • ALTERNATIVE PRODUCTS: 10 named isoforms [FASTA] produced by alternative splicing and alternative initiation.
    NameSV9
    Synonymsp110
    Isoform IDP21127-1
    This is the isoform sequence displayed in this entry.
    NameSV1
    SynonymsAlpha 2-1
    Isoform IDP21127-2
    Features which should be applied to build the isoform sequence: VSP_008280.
    Name2
    SynonymsAlpha 2-2
    Isoform IDP21127-3
    Features which should be applied to build the isoform sequence: VSP_008278, VSP_008279, VSP_008280.
    Name3
    SynonymsAlpha 1
    Isoform IDP21127-4
    Features which should be applied to build the isoform sequence: VSP_008276.
    NameSV4
    Isoform IDP21127-5
    Features which should be applied to build the isoform sequence: VSP_008275.
    NameSV5
    Isoform IDP21127-6
    Features which should be applied to build the isoform sequence: VSP_008273, VSP_008277, VSP_008278, VSP_008280.
    Name8
    SynonymsAlpha 2-3
    Isoform IDP21127-8
    Features which should be applied to build the isoform sequence: VSP_008278, VSP_008280.
    NameSV10
    Isoform IDP21127-9
    Features which should be applied to build the isoform sequence: VSP_008273, VSP_008277, VSP_008280.
    NameSV11
    SynonymsAlpha 2-4
    Isoform IDP21127-10
    Features which should be applied to build the isoform sequence: VSP_008274, VSP_008280.
    Name7
    Synonymsp58
    Isoform IDP21127-12
    Note: Produced by alternative initiation at Met-357 of isoform SV9.
    Features which should be applied to build the isoform sequence: VSP_018834.
  • TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-specific tissue distribution.
  • INDUCTION: The p58 isoform is specifically induced in G2/M phase of the cell cycle.
  • PTM: During apoptosis, induced by Fas or tumor necrosis factor, specific PITSLRE p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the PITSLRE proteins.
  • PTM: P110C can be autophosphorylated.
  • MISCELLANEOUS: Duplicated gene. CDC2L1 and CDC2L2 encode almost identical protein kinases of 110 kDa that contain at their C termini the open reading frame of a smaller 58 kDa isoform which is expressed following IRES-mediated alternative initiation of translation.
  • SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
  • SIMILARITY: Contains 1 protein kinase domain.
  • CAUTION: Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDC2L1 and/or CDC2L2 or one/some of the isoforms of each.
  • SEQUENCE CAUTION:
    • Sequence=AAC83664.1; Type=Erroneous gene model prediction;
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
M37712; AAA36406.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88563; AAB59449.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88553; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88554; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88555; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88558; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88559; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88560; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88561; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M88562; AAB59449.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04815; AAA19581.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04816; AAA19582.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04817; AAA19583.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04818; AAA19584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04824; AAA19586.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067512; AAC72077.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067513; AAC72078.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067514; AAC72079.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067515; AAC72080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067516; AAC72081.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067517; AAC72082.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080683; AAC83662.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080685; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080686; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080687; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080688; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092429; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092430; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080678; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080679; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080680; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080681; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080682; AAC83662.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080683; AAC83663.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080685; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080686; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080687; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080688; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092429; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092430; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080678; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080679; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080680; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080681; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080682; AAC83663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080683; AAC83664.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080685; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080686; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080687; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080688; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092429; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092430; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080678; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080679; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080680; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080681; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080682; AAC83664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080683; AAC83665.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080685; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080686; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080687; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080688; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092429; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092430; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080678; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080679; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080680; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080681; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080682; AAC83665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080683; AAC83666.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092430; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080678; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080679; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080680; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080681; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF080682; AAC83666.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF174497; AAF36538.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033069; AAH33069.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38282; A38282.
B54024; B54024.
E54024; E54024.
F54024; F54024.
H54024; H54024.
T09568; T09568.
RefSeq NP_277021.1; -.
NP_277022.1; -.
NP_277023.1; -.
NP_277024.1; -.
NP_277027.1; -.
NP_277028.1; -.
UniGene Hs.651228
3D structure databases
HSSP P24941; 1H00. [HSSP ENTRY / PDB]
ModBase P21127.
Protein-protein interaction databases
DIP DIP:29015N; -.
IntAct P21127; -.
PTM databases
PhosphoSite P21127; -.
Organism-specific databases
H-InvDB HIX0000039; -.
HGNC HGNC:1729; CDC2L1.
GenAtlas CDC2L1.
HPA CAB010467; -.
MIM 176873; gene. [NCBI / EBI]
PharmGKB PA26262; -.
GeneCards P21127.
Gene expression databases
GermOnline ENSG00000008128; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from UniProtKB).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915; Biological process: apoptosis (non-traceable author statement from UniProtKB).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007067; Biological process: mitosis (non-traceable author statement from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0001558; Biological process: regulation of cell growth (inferred from expression pattern from UniProtKB).
GO:0050684; Biological process: regulation of mRNA processing (inferred from direct assay from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (non-traceable author statement from UniProtKB).
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 P21127.
Genome annotation databases
Ensembl ENSG00000008128; Homo sapiens. [Contig view]
GeneID 984; -.
KEGG hsa:984; -.
Phylogenomic databases
HOVERGEN P21127; -.
Other
LinkHub P21127; -.
NextBio 4128; -.
SOURCE CDC2L1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; Alternative splicing; Apoptosis; ATP-binding; Cell cycle; Cytoplasm; 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   795  795     PITSLRE serine/threonine-protein kinase CDC2L1. PRO_0000024311
DOMAIN   438   723  286     Protein kinase. 
NP_BIND   444   452  9     ATP (By similarity). 
COMPBIAS   126   393  268     Glu-rich. 
ACT_SITE   562   562        Proton acceptor (By similarity). 
BINDING   467   467        ATP (By similarity). 
MOD_RES   283   283        Phosphoserine. 
MOD_RES   448   448        Phosphothreonine (By similarity). 
MOD_RES   449   449        Phosphotyrosine (By similarity). 
MOD_RES   589   589        Phosphoserine. 
MOD_RES   595   595        Phosphothreonine. 
MOD_RES   751   751        Phosphothreonine (By similarity). 
MOD_RES   752   752        Phosphoserine (By similarity). 
VAR_SEQ   1   356        Missing (in isoform 7). VSP_018834
VAR_SEQ   1   269        Missing (in isoform SV4). VSP_008275
VAR_SEQ   1   217        Missing (in isoform SV11). VSP_008274
VAR_SEQ   1    34        Missing (in isoform SV5 and isoform SV10). VSP_008273
VAR_SEQ   2   335        Missing (in isoform 3). VSP_008276
VAR_SEQ   35    37        LKN -> MSQ (in isoform SV5 and isoform SV10). VSP_008277
VAR_SEQ   110   119        Missing (in isoform 2, isoform SV5 and isoform 8). VSP_008278
VAR_SEQ   165   165        R -> RGNDGVCLFR (in isoform 2). VSP_008279
VAR_SEQ   252   265        GEARPARAQKPAQL -> V (in isoform SV1, isoform 2, isoform SV5, isoform 8, isoform SV10 and isoform SV11). VSP_008280
VARIANT   57    57  1     R -> C.