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Identification
HMDB Protein ID HMDBP01398
Secondary Accession Numbers
  • 6694
Name Cell division protein kinase 5
Synonyms
  1. Cyclin-dependent kinase 5
  2. Serine/threonine-protein kinase PSSALRE
  3. TPKII catalytic subunit
  4. Tau protein kinase II catalytic subunit
Gene Name CDK5
Protein Type Enzyme
Biological Properties
General Function Involved in protein kinase activity
Specific Function Probably involved in the control of the cell cycle. Interacts with D1 and D3-type G1 cyclins. Can phosphorylate histone H1, tau, MAP2 and NF-H and NF-M. Also interacts with p35 which activates the kinase
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
protein kinase activity
protein serine/threonine kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
metabolic process
cellular metabolic process
protein amino acid phosphorylation
phosphorylation
Cellular Location
  1. Cytoplasm
  2. Cell projection
  3. Cell projection
  4. lamellipodium
  5. growth cone
Gene Properties
Chromosome Location Chromosome:7
Locus 7q36
SNPs CDK5
Gene Sequence
>879 bp
ATGCAGAAATACGAGAAACTGGAAAAGATTGGGGAAGGCACCTACGGAACTGTGTTCAAG
GCCAAAAACCGGGAGACTCATGAGATCGTGGCTCTGAAACGGGTGAGGCTGGATGACGAT
GATGAGGGTGTGCCGAGTTCCGCCCTCCGGGAGATCTGCCTACTCAAGGAGCTGAAGCAC
AAGAACATCGTCAGGCTTCATGACGTCCTGCACAGCGACAAGAAGCTGACTTTGGTTTTT
GAATTCTGTGACCAGGACCTGAAGAAGTATTTTGACAGTTGCAATGGTGACCTCGATCCT
GAGATTGTAAAGTCATTCCTCTTCCAGCTACTAAAAGGGCTGGGATTCTGTCATAGCCGC
AATGTGCTACACAGGGACCTGAAGCCCCAGAACCTGCTAATAAACAGGAATGGGGAGCTG
AAATTGGCTGATTTTGGCCTGGCTCGAGCCTTTGGGATTCCCGTCCGCTGTTACTCAGCT
GAGGTGGTCACACTGTGGTACCGCCCACCGGATGTCCTCTTTGGGGCCAAGCTGTACTCC
ACGTCCATCGACATGTGGTCAGCCGGCTGCATCTTTGCAGAGCTGGCCAATGCTGGGCGG
CCTCTTTTTCCCGGCAATGATGTCGATGACCAGTTGAAGAGGATCTTCCGACTGCTGGGG
ACGCCCACCGAGGAGCAGTGGCCCTCTATGACCAAGCTGCCAGACTATAAGCCCTATCCG
ATGTACCCGGCCACAACATCCCTGGTGAACGTCGTGCCCAAACTCAATGCCACAGGGAGG
GATCTGCTGCAGAACCTTCTGAAGTGTAACCCTGTCCAGCGTATCTCAGCAGAAGAGGCC
CTGCAGCACCCCTACTTCTCCGACTTCTGTCCGCCCTAG
Protein Properties
Number of Residues 292
Molecular Weight 33304.1
Theoretical pI 7.75
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Cell division protein kinase 5
MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKH
KNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSR
NVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYS
TSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYP
MYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP
GenBank ID Protein 36621
UniProtKB/Swiss-Prot ID Q00535
UniProtKB/Swiss-Prot Entry Name CDK5_HUMAN
PDB IDs
GenBank Gene ID X66364
GeneCard ID CDK5
GenAtlas ID CDK5
HGNC ID HGNC:1774
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  5. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  8. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
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  10. Meyerson M, Enders GH, Wu CL, Su LK, Gorka C, Nelson C, Harlow E, Tsai LH: A family of human cdc2-related protein kinases. EMBO J. 1992 Aug;11(8):2909-17. [PubMed:1639063 ]
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