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Q8IU85

- KCC1D_HUMAN

UniProt

Q8IU85 - KCC1D_HUMAN

Protein

Calcium/calmodulin-dependent protein kinase type 1D

Gene

CAMK1D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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, activates CREB-dependent gene transcription, regulates calcium-mediated granulocyte function and respiratory burst and promotes basal dendritic growth of hippocampal neurons. In neutrophil cells, required for cytokine-induced proliferative responses and activation of the respiratory burst. Activates the transcription factor CREB1 in hippocampal neuron nuclei. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows phosphorylation of Thr-180 within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-180 results in several fold increase in total activity. Unlike CaMK4, may be unable to exhibit autonomous activity after Ca2+/calmodulin activation.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521ATPPROSITE-ProRule annotation
    Active sitei144 – 1441Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 379ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. inflammatory response Source: UniProtKB-KW
    2. negative regulation of apoptotic process Source: Ensembl
    3. positive regulation of apoptotic process Source: Ensembl
    4. positive regulation of CREB transcription factor activity Source: UniProtKB
    5. positive regulation of neuron projection development Source: UniProtKB
    6. positive regulation of neutrophil chemotaxis Source: UniProtKB
    7. positive regulation of phagocytosis Source: UniProtKB
    8. positive regulation of respiratory burst Source: UniProtKB
    9. regulation of dendrite development Source: UniProtKB
    10. regulation of granulocyte chemotaxis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Inflammatory response, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.17. 2681.
    SignaLinkiQ8IU85.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent protein kinase type 1D (EC:2.7.11.17)
    Alternative name(s):
    CaM kinase I delta
    Short name:
    CaM kinase ID
    Short name:
    CaM-KI delta
    Short name:
    CaMKI delta
    Short name:
    CaMKID
    CaMKI-like protein kinase
    Short name:
    CKLiK
    Gene namesi
    Name:CAMK1D
    Synonyms:CAMKID
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:19341. CAMK1D.

    Subcellular locationi

    Cytoplasm Curated. Nucleus Curated
    Note: Predominantly cytoplasmic. Nuclear localization increases upon activation by KCl treatment in hippocampal neurons.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521K → A: Catalytically inactive form. 1 Publication
    Mutagenesisi180 – 1801T → A: Loss of ionomycin-induced activation. 2 Publications

    Organism-specific databases

    PharmGKBiPA134992438.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 385385Calcium/calmodulin-dependent protein kinase type 1DPRO_0000086082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221Phosphoserine2 Publications
    Modified residuei180 – 1801Phosphothreonine; by CaMKK1 and CaMKK22 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IU85.
    PaxDbiQ8IU85.
    PRIDEiQ8IU85.

    PTM databases

    PhosphoSiteiQ8IU85.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes.3 Publications

    Developmental stagei

    Expressed during hippocampal formation with high expression in the pyramidal cell layers.2 Publications

    Inductioni

    Expression increases upon treatment of EC cells with DMSO and retinoic acid. Induced by KCL in PC12 cells.1 Publication

    Gene expression databases

    ArrayExpressiQ8IU85.
    BgeeiQ8IU85.
    CleanExiHS_CAMK1D.
    GenevestigatoriQ8IU85.

    Organism-specific databases

    HPAiHPA007266.

    Interactioni

    Protein-protein interaction databases

    BioGridi121382. 21 interactions.
    IntActiQ8IU85. 7 interactions.
    STRINGi9606.ENSP00000368124.

    Structurei

    Secondary structure

    1
    385
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 153
    Helixi19 – 224
    Beta strandi23 – 319
    Beta strandi36 – 427
    Turni43 – 453
    Beta strandi48 – 558
    Helixi66 – 7510
    Beta strandi84 – 896
    Beta strandi91 – 999
    Helixi106 – 1127
    Helixi118 – 13720
    Helixi147 – 1493
    Beta strandi150 – 1567
    Beta strandi161 – 1633
    Helixi190 – 1934
    Helixi201 – 21616
    Helixi226 – 23510
    Turni242 – 2476
    Helixi250 – 25910
    Turni264 – 2663
    Helixi270 – 2734
    Helixi277 – 2804
    Helixi290 – 30011
    Helixi305 – 3117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JC6X-ray2.30A/C1-333[»]
    ProteinModelPortaliQ8IU85.
    SMRiQ8IU85. Positions 11-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IU85.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 279257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni279 – 31941Autoinhibitory domainBy similarityAdd
    BLAST
    Regioni299 – 32022Calmodulin-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi318 – 3247Nuclear export signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi326 – 36439Ser-richAdd
    BLAST

    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.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108055.
    InParanoidiQ8IU85.
    KOiK08794.
    OMAiPYWDQIS.
    OrthoDBiEOG7WHH9K.
    PhylomeDBiQ8IU85.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IU85-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MARENGESSS SWKKQAEDIK KIFEFKETLG TGAFSEVVLA EEKATGKLFA    50
    VKCIPKKALK GKESSIENEI AVLRKIKHEN IVALEDIYES PNHLYLVMQL 100
    VSGGELFDRI VEKGFYTEKD ASTLIRQVLD AVYYLHRMGI VHRDLKPENL 150
    LYYSQDEESK IMISDFGLSK MEGKGDVMST ACGTPGYVAP EVLAQKPYSK 200
    AVDCWSIGVI AYILLCGYPP FYDENDSKLF EQILKAEYEF DSPYWDDISD 250
    SAKDFIRNLM EKDPNKRYTC EQAARHPWIA GDTALNKNIH ESVSAQIRKN 300
    FAKSKWRQAF NATAVVRHMR KLHLGSSLDS SNASVSSSLS LASQKDCLAP 350
    STLCSFISSS SGVSGVGAER RPRPTTVTAV HSGSK 385
    Length:385
    Mass (Da):42,914
    Last modified:March 1, 2003 - v1
    Checksum:i717467D019E30FC9
    GO
    Isoform 2 (identifier: Q8IU85-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         348-385: LAPSTLCSFISSSSGVSGVGAERRPRPTTVTAVHSGSK → AYVAKPESLS

    Show »
    Length:357
    Mass (Da):40,190
    Checksum:i1FA184EEFA976FB4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661I → M.1 Publication
    Corresponds to variant rs34194224 [ dbSNP | Ensembl ].
    VAR_040599

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei348 – 38538LAPST…HSGSK → AYVAKPESLS in isoform 2. 1 PublicationVSP_012135Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF286366 mRNA. Translation: AAG00534.1.
    AB081726 mRNA. Translation: BAC19846.1.
    EF444962 Genomic DNA. Translation: ACA05959.1.
    AL391314
    , AL512284, AL512783, AL731559 Genomic DNA. Translation: CAI14410.1.
    AL512284
    , AL391314, AL512783, AL731559 Genomic DNA. Translation: CAH71693.1.
    AL512284
    , AL391314, AL512783, AL731559 Genomic DNA. Translation: CAH71694.1.
    AL512783
    , AL391314, AL512284, AL731559 Genomic DNA. Translation: CAH74035.1.
    AL512783
    , AL391314, AL512284, AL731559 Genomic DNA. Translation: CAH74036.1.
    AL731559
    , AL391314, AL512284, AL512783 Genomic DNA. Translation: CAI14675.1.
    CH471072 Genomic DNA. Translation: EAW86314.1.
    BC035745 mRNA. Translation: AAH35745.1.
    CCDSiCCDS7091.1. [Q8IU85-1]
    CCDS7092.1. [Q8IU85-2]
    RefSeqiNP_065130.1. NM_020397.2. [Q8IU85-2]
    NP_705718.1. NM_153498.2. [Q8IU85-1]
    UniGeneiHs.659517.

    Genome annotation databases

    EnsembliENST00000378845; ENSP00000368122; ENSG00000183049. [Q8IU85-2]
    GeneIDi57118.
    KEGGihsa:57118.
    UCSCiuc001ilo.3. human. [Q8IU85-1]

    Polymorphism databases

    DMDMi56404610.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF286366 mRNA. Translation: AAG00534.1 .
    AB081726 mRNA. Translation: BAC19846.1 .
    EF444962 Genomic DNA. Translation: ACA05959.1 .
    AL391314
    , AL512284 , AL512783 , AL731559 Genomic DNA. Translation: CAI14410.1 .
    AL512284
    , AL391314 , AL512783 , AL731559 Genomic DNA. Translation: CAH71693.1 .
    AL512284
    , AL391314 , AL512783 , AL731559 Genomic DNA. Translation: CAH71694.1 .
    AL512783
    , AL391314 , AL512284 , AL731559 Genomic DNA. Translation: CAH74035.1 .
    AL512783
    , AL391314 , AL512284 , AL731559 Genomic DNA. Translation: CAH74036.1 .
    AL731559
    , AL391314 , AL512284 , AL512783 Genomic DNA. Translation: CAI14675.1 .
    CH471072 Genomic DNA. Translation: EAW86314.1 .
    BC035745 mRNA. Translation: AAH35745.1 .
    CCDSi CCDS7091.1. [Q8IU85-1 ]
    CCDS7092.1. [Q8IU85-2 ]
    RefSeqi NP_065130.1. NM_020397.2. [Q8IU85-2 ]
    NP_705718.1. NM_153498.2. [Q8IU85-1 ]
    UniGenei Hs.659517.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JC6 X-ray 2.30 A/C 1-333 [» ]
    ProteinModelPortali Q8IU85.
    SMRi Q8IU85. Positions 11-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121382. 21 interactions.
    IntActi Q8IU85. 7 interactions.
    STRINGi 9606.ENSP00000368124.

    Chemistry

    BindingDBi Q8IU85.
    ChEMBLi CHEMBL5073.
    GuidetoPHARMACOLOGYi 1953.

    PTM databases

    PhosphoSitei Q8IU85.

    Polymorphism databases

    DMDMi 56404610.

    Proteomic databases

    MaxQBi Q8IU85.
    PaxDbi Q8IU85.
    PRIDEi Q8IU85.

    Protocols and materials databases

    DNASUi 57118.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378845 ; ENSP00000368122 ; ENSG00000183049 . [Q8IU85-2 ]
    GeneIDi 57118.
    KEGGi hsa:57118.
    UCSCi uc001ilo.3. human. [Q8IU85-1 ]

    Organism-specific databases

    CTDi 57118.
    GeneCardsi GC10P012391.
    HGNCi HGNC:19341. CAMK1D.
    HPAi HPA007266.
    MIMi 607957. gene.
    neXtProti NX_Q8IU85.
    PharmGKBi PA134992438.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108055.
    InParanoidi Q8IU85.
    KOi K08794.
    OMAi PYWDQIS.
    OrthoDBi EOG7WHH9K.
    PhylomeDBi Q8IU85.
    TreeFami TF314166.

    Enzyme and pathway databases

    BRENDAi 2.7.11.17. 2681.
    SignaLinki Q8IU85.

    Miscellaneous databases

    ChiTaRSi CAMK1D. human.
    EvolutionaryTracei Q8IU85.
    GenomeRNAii 57118.
    NextBioi 62987.
    PROi Q8IU85.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IU85.
    Bgeei Q8IU85.
    CleanExi HS_CAMK1D.
    Genevestigatori Q8IU85.

    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. "Identification and characterization of CKLiK, a novel granulocyte Ca++/calmodulin-dependent protein kinase."
      Verploegen S., Lammers J.-W.L., Koenderman L., Coffer P.J.
      Blood 96:3215-3223(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CREM AND ACTIVATION OF CREB1, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells."
      Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H., Kobayashi R.
      FEBS Lett. 550:57-63(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT THR-180, PHOSPHORYLATION BY CAMKK1 AND CAMKK2, MUTAGENESIS OF THR-180, TISSUE SPECIFICITY.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Pancreas.
    7. "Characterization of the role of CaMKI-like kinase (CKLiK) in human granulocyte function."
      Verploegen S., Ulfman L., van Deutekom H.W., van Aalst C., Honing H., Lammers J.W., Koenderman L., Coffer P.J.
      Blood 106:1076-1083(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Prominent expression and activity-dependent nuclear translocation of Ca2+/calmodulin-dependent protein kinase Idelta in hippocampal neurons."
      Sakagami H., Kamata A., Nishimura H., Kasahara J., Owada Y., Takeuchi Y., Watanabe M., Fukunaga K., Kondo H.
      Eur. J. Neurosci. 22:2697-2707(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CREB1 ACTIVATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION BY KCL, MUTAGENESIS OF LYS-52 AND THR-180.
    9. "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 DENDTRITIC GROWTH, DEVELOPMENTAL STAGE.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND THR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Crystal structure of human calmodulin-dependent protein kinase 1D."
      Debreczeni J.E., Rellos P., Fedorov O., Niesen F.H., Bhatia C., Shrestha L., Salah E., Smee C., Colebrook S., Berridge G., Gileadi O., Bunkoczi G., Ugochukwu E., Pike A.C.W., Von Delft F., Knapp S., Sundstrom M., Weigelt J., Arrowsmith C.H., Edwards A.
      Submitted (DEC-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 IN COMPLEX WITH INHIBITOR.
    13. "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: VARIANT [LARGE SCALE ANALYSIS] MET-66.

    Entry informationi

    Entry nameiKCC1D_HUMAN
    AccessioniPrimary (citable) accession number: Q8IU85
    Secondary accession number(s): B0YIY0, Q9HD31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 123 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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