Reviewed,
UniProtKB/Swiss-Prot Q14004 (CDK13_HUMAN)
Last modified
February 9, 2010.
Version 99.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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Names and origin
| Protein names | Recommended name: Cell division protein kinase 13 EC=2.7.11.22 Alternative name(s): Cell division cycle 2-like protein kinase 5 CDC2-related protein kinase 5 Cholinesterase-related cell division controller | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1512 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May be a controller of the mitotic cell cycle. Involved in the blood cell development. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Tissue specificity | Expressed in fetal brain, liver, muscle and in adult brain. Also expressed in neuroblastoma and glioblastoma tumors. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 |
| Sequence similarities | Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain. |
| Sequence caution | The sequence AAA58424.1 differs from that shown. Reason: Frameshift at position 1006. The sequence AAS07490.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing Polymorphism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | multicellular organismal development Ref.4 Traceable author statement. Source: ProtInc positive regulation of cell proliferation Ref.4Traceable author statement. Source: ProtInc protein amino acid phosphorylationInferred from electronic annotation. Source: InterPro regulation of mitosis Ref.4Traceable author statement. Source: ProtInc |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q14004-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q14004-2) The sequence of this isoform differs from the canonical sequence as follows: 1079-1138: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1512 | 1512 | Cell division protein kinase 13 | PRO_0000085711 | |||||
Regions | |||||||||
| Domain | 705 – 998 | 294 | Protein kinase | ||||||
| Nucleotide binding | 711 – 719 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 837 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 734 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | Phosphoserine | ||||||
| Modified residue | 238 | 1 | Phosphoserine | ||||||
| Modified residue | 315 | 1 | Phosphoserine Ref.8 Ref.12 Ref.13 | ||||||
| Modified residue | 317 | 1 | Phosphoserine Ref.7 Ref.8 Ref.12 Ref.13 | ||||||
| Modified residue | 325 | 1 | Phosphoserine Ref.8 Ref.12 Ref.13 | ||||||
| Modified residue | 340 | 1 | Phosphoserine Ref.7 Ref.13 | ||||||
| Modified residue | 342 | 1 | Phosphoserine Ref.7 Ref.13 | ||||||
| Modified residue | 348 | 1 | Phosphoserine | ||||||
| Modified residue | 349 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 358 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 360 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 367 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 383 | 1 | Phosphoserine Ref.7 Ref.12 Ref.13 Ref.15 Ref.17 | ||||||
| Modified residue | 385 | 1 | Phosphoserine | ||||||
| Modified residue | 395 | 1 | Phosphoserine Ref.12 Ref.13 | ||||||
| Modified residue | 397 | 1 | Phosphoserine Ref.12 Ref.13 | ||||||
| Modified residue | 400 | 1 | Phosphoserine Ref.12 Ref.13 | ||||||
| Modified residue | 409 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 413 | 1 | Phosphoserine | ||||||
| Modified residue | 436 | 1 | Phosphoserine | ||||||
| Modified residue | 437 | 1 | Phosphoserine Ref.6 Ref.8 Ref.9 Ref.12 Ref.13 Ref.17 | ||||||
| Modified residue | 439 | 1 | Phosphoserine Ref.8 Ref.12 Ref.13 | ||||||
| Modified residue | 441 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 442 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 490 | 1 | Phosphoserine | ||||||
| Modified residue | 492 | 1 | Phosphothreonine | ||||||
| Modified residue | 494 | 1 | Phosphothreonine Ref.15 | ||||||
| Modified residue | 525 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 527 | 1 | Phosphoserine | ||||||
| Modified residue | 556 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 662 | 1 | Phosphoserine | ||||||
| Modified residue | 664 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 863 | 1 | Phosphoserine | ||||||
| Modified residue | 870 | 1 | Phosphotyrosine | ||||||
| Modified residue | 871 | 1 | Phosphothreonine Ref.12 Ref.13 | ||||||
| Modified residue | 1048 | 1 | Phosphoserine | ||||||
| Modified residue | 1054 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 1056 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 1058 | 1 | Phosphothreonine | ||||||
| Modified residue | 1066 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 1143 | 1 | Phosphothreonine | ||||||
| Modified residue | 1146 | 1 | Phosphoserine | ||||||
| Modified residue | 1147 | 1 | Phosphothreonine | ||||||
| Modified residue | 1246 | 1 | Phosphothreonine Ref.8 Ref.12 Ref.13 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1079 – 1138 | 60 | Missing in isoform 2. | VSP_013579 | |||||
| Natural variant | 340 | 1 | S → F: dbSNP rs13622. | VAR_053926 | |||||
| Natural variant | 356 | 1 | P → A: dbSNP rs17537669. Ref.2 | VAR_022381 | |||||
| Natural variant | 403 | 1 | L → F: dbSNP rs3735137. Ref.2 | VAR_022382 | |||||
| Natural variant | 410 | 1 | R → Q: dbSNP rs17496261. Ref.2 | VAR_022383 | |||||
| Natural variant | 494 | 1 | T → A: dbSNP rs34624759. Ref.19 | VAR_041965 | |||||
| Natural variant | 500 | 1 | T → A: dbSNP rs3735135. Ref.2 Ref.19 | VAR_022384 | |||||
| Natural variant | 624 | 1 | S → G: dbSNP rs17496275. Ref.2 | VAR_022385 | |||||
| Natural variant | 670 | 1 | T → R: dbSNP rs34775357. Ref.19 | VAR_041966 | |||||
| Natural variant | 700 | 1 | R → L: dbSNP rs1057000. Ref.1 Ref.4 | VAR_022386 | |||||
| Natural variant | 1062 | 1 | V → M: dbSNP rs17496712. Ref.2 | VAR_022387 | |||||
| Natural variant | 1170 | 1 | V → M: dbSNP rs3204309. Ref.19 Ref.1 | VAR_041967 | |||||
Experimental info | |||||||||
| Sequence conflict | 21 | 1 | K → R in CAC10400. Ref.1 | ||||||
| Sequence conflict | 21 | 1 | K → R in CAC10401. Ref.1 | ||||||
| Sequence conflict | 671 | 1 | A → T Ref.1 | ||||||
| Sequence conflict | 671 | 1 | A → T Ref.4 | ||||||
| Sequence conflict | 810 | 1 | N → Y in AAA58424. Ref.4 | ||||||
| Sequence conflict | 862 – 866 | 5 | YSSEE → FSVFF in BAB47420. Ref.5 | ||||||
| Sequence conflict | 1035 | 1 | Missing Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A new subfamily of high molecular mass CDC2-related kinases with PITAI/VRE." Marques F., Moreau J.L., Peaucellier G., Lozano J.C., Schatt P., Picard A., Callebaut I., Perre E., Geneviere A.M. Biochem. Biophys. Res. Commun. 279:832-837(2000) [PubMed: 11162436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS LEU-700 AND MET-1170. Tissue: Placenta. |
| [2] | NIEHS SNPs program Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-356; PHE-403; GLN-410; ALA-500; GLY-624 AND MET-1062. |
| [3] | "The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Cloning and antisense oligodeoxynucleotide inhibition of a human homolog of cdc2 required in hematopoiesis." Lapidot-Lifson Y., Patinkin D., Prody C.A., Ehrlich G., Seidman S., Ben-Aziz R., Benseler F., Eckstein F., Zakut H., Soreq H. Proc. Natl. Acad. Sci. U.S.A. 89:579-583(1992) [PubMed: 1731328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-1078, VARIANT LEU-700. Tissue: Glioblastoma. |
| [5] | "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed: 11347906] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1512 (ISOFORM 1). Tissue: Brain. |
| [6] | "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND THR-442, MASS SPECTROMETRY. Tissue: T-cell. |
| [7] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-340; SER-342; SER-367 AND SER-383, MASS SPECTROMETRY. Tissue: Epithelium. |
| [8] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-437; SER-439 AND THR-1246, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-441, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY. |
| [11] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY. |
| [12] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-358; SER-360; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439; SER-525; SER-664; THR-871; THR-1056 AND THR-1246, MASS SPECTROMETRY. |
| [13] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325; SER-340; SER-342; SER-349; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439; THR-871 AND THR-1246, MASS SPECTROMETRY. |
| [14] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [15] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND THR-494, MASS SPECTROMETRY. |
| [16] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-238; SER-315; SER-317; SER-325; SER-342; SER-348; SER-358; SER-360; SER-383; SER-385; SER-395; SER-397; SER-413; SER-436; SER-437; SER-439; SER-490; THR-492; SER-525; SER-527; SER-662; SER-664; SER-863; TYR-870; THR-871; SER-1048; SER-1054; THR-1058; THR-1143; SER-1146; THR-1147 AND THR-1246, MASS SPECTROMETRY. |
| [17] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-437, MASS SPECTROMETRY. Tissue: T-cell. |
| [18] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, MASS SPECTROMETRY. |
| [19] | "Patterns of somatic mutation in human cancer genomes." 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. Stratton M.R.Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND MET-1170. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ297709 mRNA. Translation: CAC10400.1. AJ297710 mRNA. Translation: CAC10401.1. AY679523 Genomic DNA. Translation: AAT74623.1. AC072061 Genomic DNA. Translation: AAS07490.1. Sequence problems. AC072061 Genomic DNA. Translation: AAS07491.1. AC006023 Genomic DNA. Translation: AAD54514.1. M80629 mRNA. Translation: AAA58424.1. Sequence problems. AB058694 mRNA. Translation: BAB47420.1. |
| IPI | IPI00029162. IPI00456970. |
| PIR | A38197. |
| RefSeq | NP_003709.3. NP_112557.2. |
| UniGene | Hs.233552 Hs.596235 |
3D structure databases | |
| SMR | Q14004. Positions 702-1001. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q14004. |
PTM databases | |
| PhosphoSite | Q14004. |
Proteomic databases | |
| PRIDE | Q14004. |
Genome annotation databases | |
| Ensembl | ENST00000181839; ENSP00000181839; ENSG00000065883; Homo sapiens. [Genome view] |
| GeneID | 8621. |
| KEGG | hsa:8621. |
| NMPDR | fig|9606.3.peg.28511. |
| UCSC | uc003thh.2. human. uc003thi.2. human. |
Organism-specific databases | |
| CTD | 8621. |
| GeneCards | GC07P039956. |
| HGNC | HGNC:1733. CDK13. |
| MIM | 603309. gene. |
| PharmGKB | PA26264. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG12381. |
| HOVERGEN | Q14004. |
| InParanoid | Q14004. |
| OMA | RHSHSGE. |
| OrthoDB | EOG9MGVSS. |
| PhylomeDB | Q14004. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 247. |
Gene expression databases | |
| ArrayExpress | Q14004. |
| Bgee | Q14004. |
| CleanEx | HS_CDC2L5. |
| Genevestigator | Q14004. |
| GermOnline | ENSG00000065883. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| SMART | SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 32303. |
| PMAP-CutDB | Q14004. |
| SOURCE | Search... |
Entry information
| Entry name | CDK13_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q14004 Secondary accession number(s): Q6DKQ9 Q9UDR4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| SIMILARITY comments Index of protein domains and families |

Clusters with


