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Q91YS8

- KCC1A_MOUSE

UniProt

Q91YS8 - KCC1A_MOUSE

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Protein

Calcium/calmodulin-dependent protein kinase type 1

Gene
Camk1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca2+ elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-673', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation. Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K+ and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I By similarity.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-177 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-177 results in several fold increase in total activity. Unlike CaMK4, is unable to exhibit autonomous activity after Ca2+/calmodulin activation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATP By similarity
Active sitei141 – 1411Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: UniProtKB
  3. protein binding Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. nucleocytoplasmic transport Source: MGI
  3. positive regulation of dendritic spine development Source: UniProtKB
  4. positive regulation of muscle cell differentiation Source: Ensembl
  5. positive regulation of neuron projection development Source: UniProtKB
  6. positive regulation of protein export from nucleus Source: MGI
  7. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  8. positive regulation of synapse structural plasticity Source: UniProtKB
  9. protein phosphorylation Source: MGI
  10. regulation of muscle cell differentiation Source: UniProtKB
  11. regulation of protein binding Source: UniProtKB
  12. regulation of protein localization Source: UniProtKB
  13. signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type 1 (EC:2.7.11.17)
Alternative name(s):
CaM kinase I
Short name:
CaM-KI
CaM kinase I alpha
Short name:
CaMKI-alpha
Gene namesi
Name:Camk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1098535. Camk1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Predominantly cytoplasmic By similarity.

GO - Cellular componenti

  1. calcium- and calmodulin-dependent protein kinase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Calcium/calmodulin-dependent protein kinase type 1PRO_0000086077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei177 – 1771Phosphothreonine; by CaMKK1 and CaMKK2 By similarity

Post-translational modificationi

Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.
Polybiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL12), leading to proteasomal degradation By similarity.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ91YS8.
PaxDbiQ91YS8.
PRIDEiQ91YS8.

PTM databases

PhosphoSiteiQ91YS8.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ91YS8.
BgeeiQ91YS8.
CleanExiMM_CAMK1.
GenevestigatoriQ91YS8.

Interactioni

Subunit structurei

Monomer. Interacts with XPO1 By similarity.

Protein-protein interaction databases

BioGridi206419. 4 interactions.
IntActiQ91YS8. 2 interactions.
MINTiMINT-4099529.
STRINGi10090.ENSMUSP00000032409.

Structurei

3D structure databases

ProteinModelPortaliQ91YS8.
SMRiQ91YS8. Positions 10-299.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 276257Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 31641Autoinhibitory domain By similarityAdd
BLAST
Regioni296 – 31722Calmodulin-binding By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi315 – 3217Nuclear export signal By similarity

Domaini

The autoinhibitory domain overlaps with the calmodulin binding region and interacts in the inactive folded state with the catalytic domain as a pseudosubstrate By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000115341.
HOGENOMiHOG000233016.
HOVERGENiHBG108055.
InParanoidiQ91YS8.
KOiK08794.
OMAiGKENNIE.
OrthoDBiEOG7WHH9K.
PhylomeDBiQ91YS8.
TreeFamiTF314166.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91YS8-1 [UniParc]FASTAAdd to Basket

« Hide

MPGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC    50
IAKKALEGKE GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG 100
GELFDRIVEK GFYTERDASR LIFQVLDAVK YLHDLGIVHR DLKPENLLYY 150
SLDEDSKIMI SDFGLSKMED PGSVLSTACG TPGYVAPEVL AQKPYSKAVD 200
CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP YWDDISDSAK 250
DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK 300
SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TGSHGELLTP TAGGPAAGCC 350
CRDCCVEPGS ELPPAPPPSS RAMD 374
Length:374
Mass (Da):41,624
Last modified:December 1, 2001 - v1
Checksum:i37889CDA717D3AB2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC014825 mRNA. Translation: AAH14825.1.
CCDSiCCDS20415.1.
RefSeqiNP_598687.1. NM_133926.2.
UniGeneiMm.277373.

Genome annotation databases

EnsembliENSMUST00000032409; ENSMUSP00000032409; ENSMUSG00000030272.
GeneIDi52163.
KEGGimmu:52163.
UCSCiuc009dfk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC014825 mRNA. Translation: AAH14825.1 .
CCDSi CCDS20415.1.
RefSeqi NP_598687.1. NM_133926.2.
UniGenei Mm.277373.

3D structure databases

ProteinModelPortali Q91YS8.
SMRi Q91YS8. Positions 10-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206419. 4 interactions.
IntActi Q91YS8. 2 interactions.
MINTi MINT-4099529.
STRINGi 10090.ENSMUSP00000032409.

PTM databases

PhosphoSitei Q91YS8.

Proteomic databases

MaxQBi Q91YS8.
PaxDbi Q91YS8.
PRIDEi Q91YS8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032409 ; ENSMUSP00000032409 ; ENSMUSG00000030272 .
GeneIDi 52163.
KEGGi mmu:52163.
UCSCi uc009dfk.1. mouse.

Organism-specific databases

CTDi 8536.
MGIi MGI:1098535. Camk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000115341.
HOGENOMi HOG000233016.
HOVERGENi HBG108055.
InParanoidi Q91YS8.
KOi K08794.
OMAi GKENNIE.
OrthoDBi EOG7WHH9K.
PhylomeDBi Q91YS8.
TreeFami TF314166.

Miscellaneous databases

NextBioi 308578.
PROi Q91YS8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q91YS8.
Bgeei Q91YS8.
CleanExi MM_CAMK1.
Genevestigatori Q91YS8.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Calcium activation of ERK mediated by calmodulin kinase I."
    Schmitt J.M., Wayman G.A., Nozaki N., Soderling T.R.
    J. Biol. Chem. 279:24064-24072(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF MAPK1/ERK2.

Entry informationi

Entry nameiKCC1A_MOUSE
AccessioniPrimary (citable) accession number: Q91YS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi