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UniProtKB/Swiss-Prot entry Q00535


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

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Entry information
Entry name CDK5_HUMAN
Primary accession number Q00535
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on December 15, 1998 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 96)
Name and origin of the protein
Protein name Cell division protein kinase 5
Synonyms EC 2.7.11.22
Cyclin-dependent kinase 5
Tau protein kinase II catalytic subunit
TPKII catalytic subunit
Serine/threonine-protein kinase PSSALRE
Gene name
Name: CDK5
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].
TISSUE=Fetal brain;
PubMed=1639063 [NCBI, ExPASy, EBI, Israel, Japan]
Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H.;
"A family of human cdc2-related protein kinases.";
EMBO J. 11:2909-2917(1992).
[2]
SEQUENCE REVISION.
Meyerson M.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Hu X., Xu Y., Zhang B., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[6]
INTERACTION WITH AATK.
DOI=10.1016/j.bbrc.2003.08.143; PubMed=14521924 [NCBI, ExPASy, EBI, Israel, Japan]
Honma N., Asada A., Takeshita S., Enomoto M., Yamakawa E., Tsutsumi K., Saito T., Satoh T., Itoh H., Kaziro Y., Kishimoto T., Hisanaga S.;
"Apoptosis-associated tyrosine kinase is a Cdk5 activator p35 binding protein.";
Biochem. Biophys. Res. Commun. 310:398-404(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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 J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[8]
VARIANT [LARGE SCALE ANALYSIS] ASP-225.
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
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
X66364; CAA47007.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY049778; AAL15435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006680; AAP35326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005115; AAH05115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23386; S23386.
RefSeq NP_004926.1; -.
UniGene Hs.647078
3D structure databases
PDB
1H4L; X-ray; 2.65 A; A/B=1-292.[ExPASy / RCSB / EBI]
1LFR; Model; -; A=1-292.[ExPASy / RCSB / EBI]
1UNG; X-ray; 2.30 A; A/B=1-292.[ExPASy / RCSB / EBI]
1UNH; X-ray; 2.35 A; A/B=1-292.[ExPASy / RCSB / EBI]
1UNL; X-ray; 2.20 A; A/B=1-292.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H4L; -.
1LFR; -.
1UNG; -.
1UNH; -.
1UNL; -.
ModBase Q00535.
Protein-protein interaction databases
DIP DIP:24221N; -.
IntAct Q00535; -.
PTM databases
PhosphoSite Q00535; -.
Organism-specific databases
H-InvDB HIX0019667; -.
HGNC HGNC:1774; CDK5.
GenAtlas CDK5.
HPA CAB008909; -.
MIM 123831; gene. [NCBI / EBI]
PharmGKB PA26310; -.
GeneCards Q00535.
Gene expression databases
ArrayExpress Q00535; -.
CleanEx HS_CDK5; -.
GermOnline ENSG00000164885; Homo sapiens.
Ontologies
GO
GO:0030424; Cellular component: axon (inferred from sequence or structural similarity from UniProtKB).
GO:0043025; Cellular component: cell soma (inferred from sequence or structural similarity from UniProtKB).
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0030425; Cellular component: dendrite (inferred from sequence or structural similarity from UniProtKB).
GO:0030426; Cellular component: growth cone (inferred from sequence or structural similarity from UniProtKB).
GO:0016020; Cellular component: membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0031594; Cellular component: neuromuscular junction (inferred from sequence or structural similarity from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0030549; Molecular function: acetylcholine receptor activator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (traceable author statement from ProtInc).
GO:0005176; Molecular function: ErbB-2 class receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0043125; Molecular function: ErbB-3 class receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0050321; Molecular function: tau-protein kinase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0009790; Biological process: embryonic development (inferred from sequence or structural similarity from UniProtKB).
GO:0031175; Biological process: neurite development (inferred from sequence or structural similarity from UniProtKB).
GO:0043525; Biological process: positive regulation of neuron apoptosis (inferred from sequence or structural similarity 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; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q00535.
Genome annotation databases
Ensembl ENSG00000164885; Homo sapiens. [Contig view]
GeneID 1020; -.
KEGG hsa:1020; -.
Phylogenomic databases
HOGENOM Q00535; -.
HOVERGEN Q00535; -.
Other
BindingDB Q00535; -.
LinkHub Q00535; -.
SOURCE CDK5; Homo sapiens.
ProtoNet Q00535.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; Cell division; Cell projection; Cytoplasm; Kinase; Nucleotide-binding; 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   292  292     Cell division protein kinase 5. PRO_0000085784
DOMAIN   4   286  283     Protein kinase. 
NP_BIND   10    18  9     ATP (By similarity). 
ACT_SITE   126   126        Proton acceptor (By similarity). 
BINDING   33    33        ATP (By similarity). 
MOD_RES   14    14        Phosphothreonine (By similarity). 
MOD_RES   15    15        Phosphotyrosine; by ABL1. 
MOD_RES   159   159        Phosphoserine (By similarity). 
VARIANT   225   225  1     E -> D. VAR_041977 [3D]
STRAND   4     9  6      
STRAND   17    23  7      
TURN   24    26  3      
STRAND   29    38  10      
STRAND   40    42  3      
HELIX   45    55  11      
STRAND   66    72  7      
STRAND   75    81  7      
STRAND   84    86  3      
HELIX   87    93  7      
TURN   94    96  3      
HELIX   100   119  20      
HELIX   129   131  3      
STRAND   132   134  3      
STRAND   140   142  3      
HELIX   145   147  3      
HELIX   165   167  3      
HELIX   170   173  4      
HELIX   182   195  14      
TURN   196   198  3      
HELIX   208   219  12      
TURN   224   226  3      
HELIX   230   232  3      
TURN   249   251  3      
HELIX   257   266  10      
HELIX   271   273  3      
HELIX   277   280  4      
HELIX   284   286  3      
Sequence information
Length: 292 AA [This is the length of the unprocessed precursor] Molecular weight: 33304 Da [This is the MW of the unprocessed precursor] CRC64: 54D10495F017D527 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH 

        70         80         90        100        110        120 
KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR 

       130        140        150        160        170        180 
NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS 

       190        200        210        220        230        240 
TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPSM TKLPDYKPYP 

       250        260        270        280        290 
MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP 

Q00535 in FASTA format

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