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Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (CR6 protein kinase) (CRK6) (Cell division protein kinase 5) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit)

 CDK5_MOUSE              Reviewed;         292 AA.
P49615;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 177.
RecName: Full=Cyclin-dependent-like kinase 5;
EC=2.7.11.1;
AltName: Full=CR6 protein kinase;
Short=CRK6;
AltName: Full=Cell division protein kinase 5;
AltName: Full=Serine/threonine-protein kinase PSSALRE;
AltName: Full=Tau protein kinase II catalytic subunit;
Short=TPKII catalytic subunit;
Name=Cdk5; Synonyms=Cdkn5, Crk6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7834371; DOI=10.1016/0006-8993(94)91197-5;
Ino H., Ishizuka T., Chiba T., Tatibana M.;
"Expression of CDK5 (PSSALRE kinase), a neural cdc2-related protein
kinase, in the mature and developing mouse central and peripheral
nervous systems.";
Brain Res. 661:196-206(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 130-165.
STRAIN=CBA/J; TISSUE=Bone marrow;
PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
"Novel CDC2-related protein kinases produced in murine hematopoietic
stem cells.";
Gene 124:305-306(1993).
[4]
NUCLEOTIDE SEQUENCE OF 1-12.
PubMed=7490100; DOI=10.1006/geno.1995.1194;
Ohshima T., Nagle J.W., Pant H.C., Joshi J.B., Kozak C.A., Brady R.O.,
Kulkarni A.B.;
"Molecular cloning and chromosomal mapping of the mouse cyclin-
dependent kinase 5 gene.";
Genomics 28:585-588(1995).
[5]
IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CABLES1 AND ABL1,
INTERACTION WITH CABLES1, PHOSPHORYLATION AT TYR-15, AND MUTAGENESIS
OF TYR-15.
PubMed=10896159; DOI=10.1016/S0896-6273(00)81200-3;
Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L.,
Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
"Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine
phosphorylation, kinase upregulation, and neurite outgrowth.";
Neuron 26:633-646(2000).
[6]
SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND ENZYME REGULATION.
PubMed=11517264;
Ko J., Humbert S., Bronson R.T., Takahashi S., Kulkarni A.B., Li E.,
Tsai L.H.;
"p35 and p39 are essential for cyclin-dependent kinase 5 function
during neurodevelopment.";
J. Neurosci. 21:6758-6771(2001).
[7]
DISRUPTION PHENOTYPE.
PubMed=11226314; DOI=10.1073/pnas.051628498;
Ohshima T., Ogawa M., Veeranna A., Hirasawa M., Longenecker G.,
Ishiguro K., Pant H.C., Brady R.O., Kulkarni A.B., Mikoshiba K.;
"Synergistic contributions of cyclin-dependant kinase 5/p35 and
Reelin/Dab1 to the positioning of cortical neurons in the developing
mouse brain.";
Proc. Natl. Acad. Sci. U.S.A. 98:2764-2769(2001).
[8]
INTERACTION WITH CABLES2.
PubMed=11955625; DOI=10.1016/S0167-4781(01)00367-0;
Sato H., Nishimoto I., Matsuoka M.;
"Ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and
c-abl.";
Biochim. Biophys. Acta 1574:157-163(2002).
[9]
FUNCTION, AND INTERACTION WITH PTK2/FAK1.
PubMed=12941275; DOI=10.1016/S0092-8674(03)00605-6;
Xie Z., Sanada K., Samuels B.A., Shih H., Tsai L.H.;
"Serine 732 phosphorylation of FAK by Cdk5 is important for
microtubule organization, nuclear movement, and neuronal migration.";
Cell 114:469-482(2003).
[10]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=16203963; DOI=10.1073/pnas.0507678102;
Fu A.K.Y., Ip F.C.F., Fu W.-Y., Cheung J., Wang J.H., Yung W.-H.,
Ip N.Y.;
"Aberrant motor axon projection, acetylcholine receptor clustering,
and neurotransmission in cyclin-dependent kinase 5 null mice.";
Proc. Natl. Acad. Sci. U.S.A. 102:15224-15229(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[12]
FUNCTION IN DENDRITIC SPINE MORPHOGENESIS.
PubMed=17143272; DOI=10.1038/nn1811;
Fu W.Y., Chen Y., Sahin M., Zhao X.S., Shi L., Bikoff J.B., Lai K.O.,
Yung W.H., Fu A.K., Greenberg M.E., Ip N.Y.;
"Cdk5 regulates EphA4-mediated dendritic spine retraction through an
ephexin1-dependent mechanism.";
Nat. Neurosci. 10:67-76(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION AS APEX1 KINASE, AND INTERACTION WITH APEX1.
PubMed=20473298; DOI=10.1038/ncb2058;
Huang E., Qu D., Zhang Y., Venderova K., Haque M.E., Rousseaux M.W.C.,
Slack R.S., Woulfe J.M., Park D.S.;
"The role of Cdk5-mediated apurinic/apyrimidinic endonuclease 1
phosphorylation in neuronal death.";
Nat. Cell Biol. 12:563-571(2010).
[15]
DISRUPTION PHENOTYPE, AND FUNCTION IN OLIGODENDROCYTE DIFFERENTIATION.
PubMed=21210220; DOI=10.1007/s11064-010-0391-0;
He X., Takahashi S., Suzuki H., Hashikawa T., Kulkarni A.B.,
Mikoshiba K., Ohshima T.;
"Hypomyelination Phenotype caused by impaired differentiation of
oligodendrocytes in Emx1-cre mediated Cdk5 conditional knockout
mice.";
Neurochem. Res. 36:1293-1303(2011).
[16]
FUNCTION, AND INTERACTION WITH CLOCK.
PubMed=24235147; DOI=10.1074/jbc.M113.494856;
Kwak Y., Jeong J., Lee S., Park Y.U., Lee S.A., Han D.H., Kim J.H.,
Ohshima T., Mikoshiba K., Suh Y.H., Cho S., Park S.K.;
"Cyclin-dependent kinase 5 (Cdk5) regulates the function of CLOCK
protein by direct phosphorylation.";
J. Biol. Chem. 288:36878-36889(2013).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[18]
INTERACTION WITH HTR6.
PubMed=25078650; DOI=10.1242/dev.108043;
Jacobshagen M., Niquille M., Chaumont-Dubel S., Marin P., Dayer A.;
"The serotonin 6 receptor controls neuronal migration during
corticogenesis via a ligand-independent Cdk5-dependent mechanism.";
Development 141:3370-3377(2014).
-!- FUNCTION: Proline-directed serine/threonine-protein kinase
essential for neuronal cell cycle arrest and differentiation and
may be involved in apoptotic cell death in neuronal diseases by
triggering abortive cell cycle re-entry. Interacts with D1 and D3-
type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin,
p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5,
SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5,
MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1,
huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several
neuronal development and physiological processes including
neuronal survival, migration and differentiation, axonal and
neurite growth, synaptogenesis, oligodendrocyte differentiation,
synaptic plasticity and neurotransmission, by phosphorylating key
proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2
(p39), especially in post-mitotic neurons, and promotes CDK5R1
(p35) expression in an autostimulation loop. Phosphorylates many
downstream substrates such as Rho and Ras family small GTPases
(e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins
(e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to
regulate neurite growth and/or spine morphogenesis. Phosphorylates
also exocytosis associated proteins such as MCAM/MUC18, SEPT5,
SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated
proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In
the mature central nervous system (CNS), regulates
neurotransmitter movements by phosphorylating substrates
associated with neurotransmitter release and synapse plasticity;
synaptic vesicle exocytosis, vesicles fusion with the presynaptic
membrane, and endocytosis. Promotes cell survival by activating
anti-apoptotic proteins BCL2 and STAT3, and negatively regulating
of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response
to genotoxic and oxidative stresses enhances its stabilization by
preventing ubiquitin ligase-mediated proteasomal degradation, and
induces transactivation of p53/TP53 target genes, thus regulating
apoptosis. Phosphorylation of p35/CDK5R1 enhances its
stabilization by preventing calpain-mediated proteolysis producing
p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal
degradation. During aberrant cell-cycle activity and DNA damage,
p25/CDK5 activity elicits cell-cycle activity and double-strand
DNA breaks that precedes neuronal death by deregulating HDAC1. DNA
damage triggered phosphorylation of huntingtin/HTT in nuclei of
neurons protects neurons against polyglutamine expansion as well
as DNA damage mediated toxicity. Phosphorylation of PXN reduces
its interaction with PTK2/FAK1 in matrix-cell focal adhesions
(MCFA) during oligodendrocytes (OLs) differentiation. Negative
regulator of Wnt/beta-catenin signaling pathway. Activator of the
GAIT (IFN-gamma-activated inhibitor of translation) pathway, which
suppresses expression of a post-transcriptional regulon of
proinflammatory genes in myeloid cells; phosphorylates the linker
domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-
dependent manner, the initial event in assembly of the GAIT
complex. Phosphorylation of SH3GLB1 is required for autophagy
induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in
response to osmotic stress mediates its rapid nuclear
localization. MEF2 is inactivated by phosphorylation in nucleus in
response to neurotoxin, thus leading to neuronal apoptosis. APEX1
AP-endodeoxyribonuclease is repressed by phosphorylation,
resulting in accumulation of DNA damage and contributing to
neuronal death. NOS3 phosphorylation down regulates NOS3-derived
nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-
dependent degradation and thus leads to cytoskeletal
reorganization. May regulate endothelial cell migration and
angiogenesis via the modulation of lamellipodia formation.
Involved in dendritic spine morphogenesis by mediating the EFNA1-
EPHA4 signaling. The complex p35/CDK5 participates in the
regulation of the circadian clock by modulating the function of
CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and
regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1
heterodimer in association with altered stability and subcellular
distribution. {ECO:0000269|PubMed:12941275,
ECO:0000269|PubMed:17143272, ECO:0000269|PubMed:20473298,
ECO:0000269|PubMed:21210220, ECO:0000269|PubMed:24235147}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Inhibited by 2-(1-ethyl-2-hydroxyethylamino)-6-
benzylamino-9-isopropylpurine (roscovitine), 1-isopropyl-4-
aminobenzyl-6-ether-linked benzimidazoles, resveratrol, AT-7519
and olomoucine. Activated by CDK5R1 (p35) and CDK5R2 (p39) during
the development of the nervous system; degradation of CDK5R1 (p35)
and CDK5R2 (p39) by proteasome result in down regulation of kinase
activity, during this process, CDK5 phosphorylates p35 and induces
its ubiquitination and subsequent degradation. Kinase activity is
mainly determined by the amount of p35 available and subcellular
location; reversible association to plasma membrane inhibits
activity. Long-term inactivation as well as CDK5R1 (p25)-mediated
hyperactivation of CDK5 triggers cell death. The pro-death
activity of hyperactivated CDK5 is suppressed by membrane
association of CDK5, via myristoylation of p35. Brain-derived
neurotrophic factor, glial-derived neurotrophic factor, nerve
growth factor (NGF), retinoic acid, laminin and neuregulin promote
activity. Neurotoxicity enhances nuclear activity, thus leading to
MEF2 phosphorylation and inhibition prior to apoptosis of cortical
neurons. Repression by GSTP1 via p25/p35 translocation prevents
neurodegeneration (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer composed of a catalytic subunit CDK5 and a
regulatory subunit CDK5R1 (p25) and macromolecular complex
composed of at least CDK5, CDK5R1 (p35) and CDK5RAP1 or CDK5RAP2
or CDK5RAP3. Only the heterodimer shows kinase activity. Under
neurotoxic stress and neuronal injury conditions, p35 is cleaved
by calpain to generate p25 that hyperactivates CDK5, that becomes
functionally disabled and often toxic. Found in a trimolecular
complex with CABLES1 and ABL1. Interacts with CABLES1 and CABLES2.
Interacts with AATK and GSTP1. Binds to HDAC1 when in complex with
p25. Interaction with myristoylation p35 promotes CDK5 association
with membranes. Both isoforms 1 and 2 interacts with beta-
catenin/CTNNB1. Interacts with delta-catenin/CTNND2 and APEX1.
Interacts with P53/TP53 in neurons (By similarity). Interacts with
EPHA4; may mediate the activation of NGEF by EPHA4M. Interacts
with PTK2/FAK1. The complex p35/CDK5 interacts with CLOCK (By
similarity). Interacts with HTR6 (PubMed:25078650). {ECO:0000250,
ECO:0000269|PubMed:25078650}.
-!- INTERACTION:
P61809:Cdk5r1; NbExp=4; IntAct=EBI-6510052, EBI-7840438;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:11517264}. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Perikaryon
{ECO:0000250}. Cell projection, lamellipodium
{ECO:0000269|PubMed:11517264}. Cell projection, growth cone
{ECO:0000269|PubMed:11517264}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Note=In axonal growth cone with extension to the peripheral
lamellipodia. Under neurotoxic stress and neuronal injury
conditions, CDK5R1 (p35) is cleaved by calpain to generate CDK5R1
(p25) in response to increased intracellular calcium. The elevated
level of p25, when in complex with CDK5, leads to its subcellular
misallocation as well as its hyperactivation. Colocalizes with
CTNND2 in the cell body of neuronal cells, and with CTNNB1 in the
cell-cell contacts and plasma membrane of undifferentiated and
differentiated neuroblastoma cells. Reversibly attached to the
plasma membrane in an inactive form when complexed to
dephosphorylated p35 or CDK5R2 (p39), p35 phosphorylation releases
this attachment and activates CDK5 (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Specifically expressed in post-mitotic neurons
and postsynaptic muscle. {ECO:0000269|PubMed:16203963}.
-!- PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by
casein kinase 1 promotes kinase activity. By contrast,
phosphorylation at Thr-14 inhibits activity (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylation at Ser-159 is essential for maximal catalytic
activity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Perinatal mortality associated with severe
disruption of the cytoarchitecture of the brain cortex as a result
of defects in neuronal migration and cohesiveness, and
degenerative changes in large neurons of the brain stem, such as
motor neurons in the lower cranial nerve nuclei and spinal cord.
Disruption of lamination in the cerebral cortex, hippocampus, and
cerebellum. Hypomyelination caused by impaired differentiation of
oligodendrocytes. {ECO:0000269|PubMed:11226314,
ECO:0000269|PubMed:11517264, ECO:0000269|PubMed:16203963,
ECO:0000269|PubMed:21210220}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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EMBL; D29678; BAA06148.1; -; mRNA.
EMBL; BC052007; AAH52007.1; -; mRNA.
EMBL; X64604; CAA45888.1; -; mRNA.
EMBL; S80121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS51434.1; -.
PIR; I49592; I49592.
RefSeq; NP_031694.1; NM_007668.3.
UniGene; Mm.298798; -.
UniGene; Mm.445256; -.
ProteinModelPortal; P49615; -.
SMR; P49615; -.
BioGrid; 198646; 9.
CORUM; P49615; -.
DIP; DIP-29353N; -.
ELM; P49615; -.
IntAct; P49615; 10.
MINT; MINT-4090424; -.
STRING; 10090.ENSMUSP00000030814; -.
iPTMnet; P49615; -.
PhosphoSitePlus; P49615; -.
EPD; P49615; -.
PaxDb; P49615; -.
PeptideAtlas; P49615; -.
PRIDE; P49615; -.
Ensembl; ENSMUST00000030814; ENSMUSP00000030814; ENSMUSG00000028969.
GeneID; 12568; -.
KEGG; mmu:12568; -.
UCSC; uc008wrl.1; mouse.
CTD; 1020; -.
MGI; MGI:101765; Cdk5.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00900000140869; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P49615; -.
KO; K02090; -.
OMA; IGTPDDR; -.
OrthoDB; EOG091G0CH0; -.
PhylomeDB; P49615; -.
TreeFam; TF101023; -.
BRENDA; 2.7.11.22; 3474.
Reactome; R-MMU-180024; DARPP-32 events.
Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
ChiTaRS; Cdk5; mouse.
PRO; PR:P49615; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000028969; -.
CleanEx; MM_CDK5; -.
ExpressionAtlas; P49615; baseline and differential.
Genevisible; P49615; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0016533; C:cyclin-dependent protein kinase 5 holoenzyme complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:MGI.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030549; F:acetylcholine receptor activator activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
GO; GO:0005176; F:ErbB-2 class receptor binding; IDA:UniProtKB.
GO; GO:0043125; F:ErbB-3 class receptor binding; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0070509; P:calcium ion import; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IDA:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
GO; GO:0021695; P:cerebellar cortex development; IMP:MGI.
GO; GO:0021697; P:cerebellar cortex formation; IMP:MGI.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0022038; P:corpus callosum development; IMP:MGI.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
GO; GO:0030517; P:negative regulation of axon extension; IGI:MGI.
GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:MGI.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0035418; P:protein localization to synapse; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0032801; P:receptor catabolic process; IMP:MGI.
GO; GO:0043113; P:receptor clustering; IMP:MGI.
GO; GO:0045055; P:regulated exocytosis; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0042220; P:response to cocaine; IMP:MGI.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0014044; P:Schwann cell development; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
GO; GO:0042501; P:serine phosphorylation of STAT protein; IDA:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
GO; GO:0007416; P:synapse assembly; IMP:MGI.
GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
GO; GO:0021537; P:telencephalon development; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; ATP-binding; Biological rhythms; Cell cycle;
Cell division; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Kinase; Membrane; Neurodegeneration;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome;
Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1 292 Cyclin-dependent-like kinase 5.
/FTId=PRO_0000085785.
DOMAIN 4 286 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 126 126 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 15 15 Phosphotyrosine; by ABL1, EPHA4 and FYN.
{ECO:0000269|PubMed:10896159}.
MOD_RES 17 17 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00535}.
MOD_RES 56 56 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:Q00535}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:Q00535}.
MUTAGEN 15 15 Y->F: Loss of tyrosine phosphorylations
by CABLES1 and ABL1; decreased activity.
{ECO:0000269|PubMed:10896159}.
SEQUENCE 292 AA; 33288 MW; 4CB11CED9017D535 CRC64;
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH
KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR
NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS
TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP
MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP


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