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Q14012

- KCC1A_HUMAN

UniProt

Q14012 - KCC1A_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase type 1

Gene

CAMK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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-694', 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 By similarity. 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 similarity8 Publications

    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.2 Publications

    Sites

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

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. nucleocytoplasmic transport Source: Ensembl
    3. positive regulation of dendritic spine development Source: UniProtKB
    4. positive regulation of muscle cell differentiation Source: BHF-UCL
    5. positive regulation of neuron projection development Source: UniProtKB
    6. positive regulation of protein export from nucleus Source: Ensembl
    7. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    8. positive regulation of synapse structural plasticity Source: UniProtKB
    9. protein phosphorylation Source: UniProtKB
    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: ProtInc

    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

    Enzyme and pathway databases

    BRENDAi2.7.11.17. 2681.
    SignaLinkiQ14012.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:1459. CAMK1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491K → A: Catalytically inactive form; prevents CDK4 activation. 2 Publications
    Mutagenesisi177 – 1771T → A: Loss of activation by CaMKK1. 1 Publication
    Mutagenesisi177 – 1771T → D: Partial activation in absence of CaMKK1. 1 Publication

    Organism-specific databases

    PharmGKBiPA26048.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Calcium/calmodulin-dependent protein kinase type 1PRO_0000086076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei177 – 1771Phosphothreonine; by CaMKK1 and CaMKK21 Publication

    Post-translational modificationi

    Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.3 Publications
    Polybiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL12), leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14012.
    PaxDbiQ14012.
    PeptideAtlasiQ14012.
    PRIDEiQ14012.

    PTM databases

    PhosphoSiteiQ14012.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in cells of the zona glomerulosa of the adrenal cortex.2 Publications

    Gene expression databases

    ArrayExpressiQ14012.
    BgeeiQ14012.
    CleanExiHS_CAMK1.
    GenevestigatoriQ14012.

    Organism-specific databases

    HPAiCAB031904.
    HPA051409.

    Interactioni

    Subunit structurei

    Monomer. Interacts with XPO1 By similarity. Interacts with MARK2, ARHGEF7/BETAPIX and GIT1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi114106. 12 interactions.
    DIPiDIP-41906N.
    IntActiQ14012. 1 interaction.
    MINTiMINT-201810.
    STRINGi9606.ENSP00000256460.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 183
    Beta strandi20 – 2910
    Beta strandi32 – 398
    Turni40 – 423
    Beta strandi45 – 528
    Helixi66 – 705
    Beta strandi81 – 866
    Beta strandi88 – 958
    Beta strandi100 – 1023
    Helixi103 – 1097
    Helixi115 – 13420
    Helixi144 – 1463
    Beta strandi147 – 1526
    Beta strandi158 – 1603
    Helixi166 – 1683
    Helixi171 – 1799
    Turni182 – 1843
    Helixi187 – 1904
    Helixi198 – 21316
    Helixi223 – 23210
    Turni239 – 2446
    Helixi247 – 25610
    Turni261 – 2633
    Helixi267 – 2726
    Helixi274 – 2774
    Helixi287 – 29711
    Helixi301 – 31111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FG7X-ray2.70A1-293[»]
    4FG8X-ray2.20A/B1-315[»]
    4FG9X-ray2.40A/B1-320[»]
    4FGBX-ray2.60A1-320[»]
    ProteinModelPortaliQ14012.
    SMRiQ14012. 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 domainAdd
    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.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    InParanoidiQ14012.
    KOiK08794.
    OMAiARMYLMA.
    OrthoDBiEOG7WHH9K.
    PhylomeDBiQ14012.
    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.

    Q14012-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC    50
    IAKEALEGKE 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 TASHGELLTP VAGGPAAGCC 350
    CRDCCVEPGT ELSPTLPHQL 370
    Length:370
    Mass (Da):41,337
    Last modified:November 1, 1996 - v1
    Checksum:i57FA20ECE00FA76C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti217 – 2171P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040596
    Natural varianti361 – 3611E → K.1 Publication
    Corresponds to variant rs56033923 [ dbSNP | Ensembl ].
    VAR_040597

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41816 mRNA. Translation: AAA99458.1.
    BC106754 mRNA. Translation: AAI06755.1.
    BC106755 mRNA. Translation: AAI06756.1.
    CCDSiCCDS2582.1.
    PIRiS57347.
    RefSeqiNP_003647.1. NM_003656.4.
    UniGeneiHs.434875.

    Genome annotation databases

    EnsembliENST00000256460; ENSP00000256460; ENSG00000134072.
    GeneIDi8536.
    KEGGihsa:8536.
    UCSCiuc003bst.3. human.

    Polymorphism databases

    DMDMi3122301.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41816 mRNA. Translation: AAA99458.1 .
    BC106754 mRNA. Translation: AAI06755.1 .
    BC106755 mRNA. Translation: AAI06756.1 .
    CCDSi CCDS2582.1.
    PIRi S57347.
    RefSeqi NP_003647.1. NM_003656.4.
    UniGenei Hs.434875.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FG7 X-ray 2.70 A 1-293 [» ]
    4FG8 X-ray 2.20 A/B 1-315 [» ]
    4FG9 X-ray 2.40 A/B 1-320 [» ]
    4FGB X-ray 2.60 A 1-320 [» ]
    ProteinModelPortali Q14012.
    SMRi Q14012. Positions 10-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114106. 12 interactions.
    DIPi DIP-41906N.
    IntActi Q14012. 1 interaction.
    MINTi MINT-201810.
    STRINGi 9606.ENSP00000256460.

    Chemistry

    BindingDBi Q14012.
    ChEMBLi CHEMBL2493.
    GuidetoPHARMACOLOGYi 1952.

    PTM databases

    PhosphoSitei Q14012.

    Polymorphism databases

    DMDMi 3122301.

    Proteomic databases

    MaxQBi Q14012.
    PaxDbi Q14012.
    PeptideAtlasi Q14012.
    PRIDEi Q14012.

    Protocols and materials databases

    DNASUi 8536.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256460 ; ENSP00000256460 ; ENSG00000134072 .
    GeneIDi 8536.
    KEGGi hsa:8536.
    UCSCi uc003bst.3. human.

    Organism-specific databases

    CTDi 8536.
    GeneCardsi GC03M009774.
    HGNCi HGNC:1459. CAMK1.
    HPAi CAB031904.
    HPA051409.
    MIMi 604998. gene.
    neXtProti NX_Q14012.
    PharmGKBi PA26048.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    InParanoidi Q14012.
    KOi K08794.
    OMAi ARMYLMA.
    OrthoDBi EOG7WHH9K.
    PhylomeDBi Q14012.
    TreeFami TF314166.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 2681.
    SignaLinki Q14012.

    Miscellaneous databases

    GeneWikii CAMK1.
    GenomeRNAii 8536.
    NextBioi 31972.
    PROi Q14012.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14012.
    Bgeei Q14012.
    CleanExi HS_CAMK1.
    Genevestigatori Q14012.

    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. "Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase."
      Haribabu B., Hook S.S., Selbert M.A., Goldstein E.G., Tomhave E.D., Edelman A.M., Snyderman R., Means A.R.
      EMBO J. 14:3679-3686(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-177, MUTAGENESIS OF LYS-49 AND THR-177, ENZYME REGULATION.
    2. "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].
    3. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-9.
      Tissue: Platelet.
    4. "Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase."
      Hsu L.-S., Tsou A.-P., Chi C.-W., Lee C.-H., Chen J.-Y.
      J. Biomed. Sci. 5:141-149(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMKK1.
    5. "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."
      McKinsey T.A., Zhang C.-L., Olson E.N.
      Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5.
    6. "Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity."
      Hsu L.-S., Chen G.-D., Lee L.-S., Chi C.-W., Cheng J.-F., Chen J.-Y.
      J. Biol. Chem. 276:31113-31123(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMKK2.
    7. "Calmodulin-dependent kinase I regulates adrenal cell expression of aldosterone synthase."
      Condon J.C., Pezzi V., Drummond B.M., Yin S., Rainey W.E.
      Endocrinology 143:3651-3657(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I."
      Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.
      J. Biol. Chem. 278:48570-48579(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF EIF4G3.
    9. "Regulation of cyclin D1/Cdk4 complexes by calcium/calmodulin-dependent protein kinase I."
      Kahl C.R., Means A.R.
      J. Biol. Chem. 279:15411-15419(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYCLIN-D1/CDK4 COMPLEX, MUTAGENESIS OF LYS-49.
    10. "A calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowth."
      Uboha N.V., Flajolet M., Nairn A.C., Picciotto M.R.
      J. Neurosci. 27:4413-4423(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MARK2.
    11. "Spatiotemporal expression of four isoforms of Ca2+/calmodulin-dependent protein kinase I in brain and its possible roles in hippocampal dendritic growth."
      Kamata A., Sakagami H., Tokumitsu H., Owada Y., Fukunaga K., Kondo H.
      Neurosci. Res. 57:86-97(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIPPOCAMPAL DENDRITITE GROWTH, TISSUE SPECIFICITY.
    12. "Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-kinase I/betaPIX signaling complex."
      Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N., Natsume T., Soderling T.R.
      Neuron 57:94-107(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ARHGEF7/BETAPIX, INTERACTION WITH ARHGEF7/BETAPIX AND GIT1.
    13. "CaMKK-CaMKI signaling pathways differentially control axon and dendrite elongation in cortical neurons."
      Neal A.P., Molina-Campos E., Marrero-Rosado B., Bradford A.B., Fox S.M., Kovalova N., Hannon H.E.
      J. Neurosci. 30:2807-2809(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AXON ELONGATION.
    14. "Structure and regulation of calcium/calmodulin-dependent protein kinases."
      Soderling T.R., Stull J.T.
      Chem. Rev. 101:2341-2352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    15. "Calmodulin-kinases: modulators of neuronal development and plasticity."
      Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.
      Neuron 59:914-931(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Controlling the cell cycle: the role of calcium/calmodulin-stimulated protein kinases I and II."
      Skelding K.A., Rostas J.A., Verrills N.M.
      Cell Cycle 10:631-639(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON INVOLVEMENT IN CELL CYCLE.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Fbxl12 triggers G1 arrest by mediating degradation of calmodulin kinase I."
      Mallampalli R.K., Kaercher L., Snavely C., Pulijala R., Chen B.B., Coon T., Zhao J., Agassandian M.
      Cell. Signal. 25:2047-2059(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-59.
    20. "Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI."
      Zha M., Zhong C., Ou Y., Han L., Wang J., Ding J.
      PLoS ONE 7:E44828-E44828(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-315 IN COMPLEXES WITH ATP, DOMAIN, ENZYME REGULATION.
    21. "Patterns of somatic mutation in human cancer genomes."
      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.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-217 AND LYS-361.

    Entry informationi

    Entry nameiKCC1A_HUMAN
    AccessioniPrimary (citable) accession number: Q14012
    Secondary accession number(s): Q3KPF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3