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Q91YS8

- KCC1A_MOUSE

UniProt

Q91YS8 - KCC1A_MOUSE

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
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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.By similarity

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei141 – 1411Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    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

    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

    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 CaMKK2By 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.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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 276257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni276 – 31641Autoinhibitory domainBy similarityAdd
    BLAST
    Regioni296 – 31722Calmodulin-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi315 – 3217Nuclear export signalBy 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

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 119 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