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Q63450

- KCC1A_RAT

UniProt

Q63450 - KCC1A_RAT

Protein

Calcium/calmodulin-dependent protein kinase type 1

Gene

Camk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      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-516', 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 By similarity. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-275' and 'Ser-294'. 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 – 491ATPPROSITE-ProRule annotation
    Active sitei141 – 1411Proton acceptor

    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: 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: Ensembl
    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: Ensembl

    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. 5301.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi629473. Camk1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi177 – 1771T → A: Loss of activation by CaMKK1 and CaMKK2. 2 Publications
    Mutagenesisi263 – 2642KR → AA: Partially excluded from the nucleus; when associated with 319-AQA-321. 1 Publication
    Mutagenesisi319 – 3213LQL → AQA: Retention in the nucleus. Partially excluded from the nucleus; when associated with 263-AA-264. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 374374Calcium/calmodulin-dependent protein kinase type 1PRO_0000086078Add
    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 CaMKK21 Publication

    Post-translational modificationi

    Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.1 Publication
    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

    PRIDEiQ63450.

    PTM databases

    PhosphoSiteiQ63450.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    GenevestigatoriQ63450.

    Interactioni

    Subunit structurei

    Monomer. Interacts with XPO1.2 Publications

    Protein-protein interaction databases

    BioGridi251279. 1 interaction.
    IntActiQ63450. 5 interactions.
    MINTiMINT-3375300.
    STRINGi10116.ENSRNOP00000033456.

    Structurei

    Secondary structure

    1
    374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 183
    Beta strandi20 – 289
    Helixi29 – 335
    Beta strandi34 – 396
    Turni40 – 423
    Beta strandi45 – 528
    Helixi65 – 717
    Beta strandi81 – 866
    Beta strandi88 – 958
    Helixi103 – 1086
    Helixi115 – 13420
    Helixi144 – 1463
    Beta strandi147 – 1537
    Beta strandi158 – 1603
    Helixi187 – 1904
    Helixi198 – 21316
    Helixi223 – 2319
    Turni239 – 2446
    Helixi247 – 25610
    Helixi261 – 2633
    Helixi267 – 2726
    Turni274 – 2763
    Beta strandi277 – 2793
    Helixi287 – 29711
    Helixi298 – 31720

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A06X-ray2.50A1-329[»]
    1MXEX-ray1.70E/F294-318[»]
    2L7LNMR-B299-320[»]
    ProteinModelPortaliQ63450.
    SMRiQ63450. Positions 10-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63450.

    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-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi263 – 2642Involved in nuclear importCurated
    Motifi315 – 3217Nuclear export signal

    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.
    GeneTreeiENSGT00740000115341.
    HOVERGENiHBG108055.
    KOiK08794.
    OMAiGKENNIE.
    OrthoDBiEOG7WHH9K.
    PhylomeDBiQ63450.

    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.

    Q63450-1 [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 TASHGELLTP TAGGPAAGCC 350
    CRDCCVEPGS ELPPAPPPSS RAMD 374
    Length:374
    Mass (Da):41,638
    Last modified:July 15, 1998 - v2
    Checksum:i37889B3DEF033AB2
    GO

    Sequence cautioni

    The sequence AAA19670.1 differs from that shown. Reason: Frameshift at positions 321 and 363.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371A → T AA sequence (PubMed:8386178)Curated
    Sequence conflicti112 – 1121F → G in AAA19670. (PubMed:8253780)Curated
    Sequence conflicti118 – 1181A → R in AAA19670. (PubMed:8253780)Curated
    Sequence conflicti239 – 2391S → V AA sequence (PubMed:8386178)Curated
    Sequence conflicti309 – 3091A → R in AAA19670. (PubMed:8253780)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24907 mRNA. Translation: AAA19670.1. Frameshift.
    L26288 mRNA. Translation: AAA66944.1.
    BC071177 mRNA. Translation: AAH71177.1.
    PIRiS50193.
    RefSeqiNP_604463.1. NM_134468.1.
    XP_006237065.1. XM_006237003.1.
    UniGeneiRn.11018.

    Genome annotation databases

    EnsembliENSRNOT00000029728; ENSRNOP00000033456; ENSRNOG00000021781.
    GeneIDi171503.
    KEGGirno:171503.
    UCSCiRGD:629473. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24907 mRNA. Translation: AAA19670.1 . Frameshift.
    L26288 mRNA. Translation: AAA66944.1 .
    BC071177 mRNA. Translation: AAH71177.1 .
    PIRi S50193.
    RefSeqi NP_604463.1. NM_134468.1.
    XP_006237065.1. XM_006237003.1.
    UniGenei Rn.11018.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A06 X-ray 2.50 A 1-329 [» ]
    1MXE X-ray 1.70 E/F 294-318 [» ]
    2L7L NMR - B 299-320 [» ]
    ProteinModelPortali Q63450.
    SMRi Q63450. Positions 10-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 251279. 1 interaction.
    IntActi Q63450. 5 interactions.
    MINTi MINT-3375300.
    STRINGi 10116.ENSRNOP00000033456.

    PTM databases

    PhosphoSitei Q63450.

    Proteomic databases

    PRIDEi Q63450.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000029728 ; ENSRNOP00000033456 ; ENSRNOG00000021781 .
    GeneIDi 171503.
    KEGGi rno:171503.
    UCSCi RGD:629473. rat.

    Organism-specific databases

    CTDi 8536.
    RGDi 629473. Camk1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115341.
    HOVERGENi HBG108055.
    KOi K08794.
    OMAi GKENNIE.
    OrthoDBi EOG7WHH9K.
    PhylomeDBi Q63450.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 5301.

    Miscellaneous databases

    EvolutionaryTracei Q63450.
    NextBioi 622477.

    Gene expression databases

    Genevestigatori Q63450.

    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. "Calcium/calmodulin-dependent protein kinase I. cDNA cloning and identification of autophosphorylation site."
      Picciotto M.R., Czernik A.J., Nairn A.C.
      J. Biol. Chem. 268:26512-26521(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Erratum
      Picciotto M.R., Czernik A.J., Nairn A.C.
      J. Biol. Chem. 270:10358-10358(1995)
    3. "Characterization of a rat cDNA clone encoding calcium/calmodulin-dependent protein kinase I."
      Cho F.S., Phillips K.S., Bogucki B., Weaver T.E.
      Biochim. Biophys. Acta 1224:156-160(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Lung.
    4. "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].
      Tissue: Lung.
    5. "Purification and characterization of Ca2+/calmodulin-dependent protein kinase V from rat cerebrum."
      Mochizuki H., Ito T., Hidaka H.
      J. Biol. Chem. 268:9143-9147(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 12-37; 158-167; 233-241 AND 285-295.
    6. "CREB: a Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases."
      Sheng M., Thompson M.A., Greenberg M.E.
      Science 252:1427-1430(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1.
    7. "Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I."
      Dale S., Wilson W.A., Edelman A.M., Hardie D.G.
      FEBS Lett. 361:191-195(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE RECOGNITION MOTIF.
    8. "Immunochemical localization of calcium/calmodulin-dependent protein kinase I."
      Picciotto M.R., Zoli M., Bertuzzi G., Nairn A.C.
      Synapse 20:75-84(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    9. "Regulation of activating transcription factor-1 and the cAMP response element-binding protein by Ca2+/calmodulin-dependent protein kinases type I, II, and IV."
      Sun P., Lou L., Maurer R.A.
      J. Biol. Chem. 271:3066-3073(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ATF1 AND CREB1.
    10. "Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence."
      Edelman A.M., Mitchelhill K.I., Selbert M.A., Anderson K.A., Hook S.S., Stapleton D., Goldstein E.G., Means A.R., Kemp B.E.
      J. Biol. Chem. 271:10806-10810(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-177 BY CAMKK1 AND CAMKK2, MUTAGENESIS OF THR-177.
    11. "Activation of a calcium-calmodulin-dependent protein kinase I cascade in PC12 cells."
      Aletta J.M., Selbert M.A., Nairn A.C., Edelman A.M.
      J. Biol. Chem. 271:20930-20934(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Expression and subcellular localization of multifunctional calmodulin-dependent protein kinases-I, -II and -IV are altered in rat hippocampal CA1 neurons after induction of long-term potentiation."
      Ahmed B.Y., Yamaguchi F., Tsumura T., Gotoh T., Sugimoto K., Tai Y., Konishi R., Kobayashi R., Tokuda M.
      Neurosci. Lett. 290:149-153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Characterization of Ca2+/calmodulin-dependent protein kinase I as a myosin II regulatory light chain kinase in vitro and in vivo."
      Suizu F., Fukuta Y., Ueda K., Iwasaki T., Tokumitsu H., Hosoya H.
      Biochem. J. 367:335-345(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION IN PHOSPHORYLATION OF MYL9.
    14. "Cytoplasmic localization of calcium/calmodulin-dependent protein kinase I-alpha depends on a nuclear export signal in its regulatory domain."
      Stedman D.R., Uboha N.V., Stedman T.T., Nairn A.C., Picciotto M.R.
      FEBS Lett. 566:275-280(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF 319-LEU--LEU-321 AND 263-LYS-ARG-264, INTERACTION WITH XPO1.
    15. "Regulation of axonal extension and growth cone motility by calmodulin-dependent protein kinase I."
      Wayman G.A., Kaech S., Grant W.F., Davare M., Impey S., Tokumitsu H., Nozaki N., Banker G., Soderling T.R.
      J. Neurosci. 24:3786-3794(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AXONAL OUTGROWTH.
    16. "Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation."
      Schmitt J.M., Guire E.S., Saneyoshi T., Soderling T.R.
      J. Neurosci. 25:1281-1290(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LONG-TERM POTENTIATION.
    17. "Phosphorylation of Numb regulates its interaction with the clathrin-associated adaptor AP-2."
      Tokumitsu H., Hatano N., Yokokura S., Sueyoshi Y., Nozaki N., Kobayashi R.
      FEBS Lett. 580:5797-5801(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NUMB.
    18. "Activity-dependent dendritic arborization mediated by CaM-kinase I activation and enhanced CREB-dependent transcription of Wnt-2."
      Wayman G.A., Impey S., Marks D., Saneyoshi T., Grant W.F., Derkach V., Soderling T.R.
      Neuron 50:897-909(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DENDTRITIC GROWTH.
    19. "Calmodulin-kinases regulate basal and estrogen stimulated medulloblastoma migration via Rac1."
      Davare M.A., Saneyoshi T., Soderling T.R.
      J. Neurooncol. 104:65-82(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEDULLOBLASTOMA CELLS MIGRATION.
    20. "Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I."
      Goldberg J., Nairn A.C., Kuriyan J.
      Cell 84:875-887(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Tissue: Brain.
    21. "Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism."
      Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M.
      Biochemistry 41:14669-14679(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 294-318 IN COMPLEX WITH CALMODULIN, DOMAIN.

    Entry informationi

    Entry nameiKCC1A_RAT
    AccessioniPrimary (citable) accession number: Q63450
    Secondary accession number(s): Q63084
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Dendrite development is blocked in hippocampal neurons silencing CAKM1.

    Keywords - Technical termi

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3