KCC1D_HUMAN
ID KCC1D_HUMAN Reviewed; 385 AA.
AC Q8IU85; B0YIY0; Q9HD31;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1D;
DE EC=2.7.11.17;
DE AltName: Full=CaM kinase I delta;
DE Short=CaM kinase ID;
DE Short=CaM-KI delta;
DE Short=CaMKI delta;
DE Short=CaMKID;
DE AltName: Full=CaMKI-like protein kinase;
DE Short=CKLiK;
GN Name=CAMK1D; Synonyms=CAMKID;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CREM
RP AND ACTIVATION OF CREB1, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11050006;
RA Verploegen S., Lammers J.-W.L., Koenderman L., Coffer P.J.;
RT "Identification and characterization of CKLiK, a novel granulocyte
RT Ca++/calmodulin-dependent protein kinase.";
RL Blood 96:3215-3223(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PHOSPHORYLATION AT THR-180, PHOSPHORYLATION BY CAMKK1 AND
RP CAMKK2, MUTAGENESIS OF THR-180, AND TISSUE SPECIFICITY.
RX PubMed=12935886; DOI=10.1016/s0014-5793(03)00817-2;
RA Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H.,
RA Kobayashi R.;
RT "Identification and characterization of novel components of a
RT Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells.";
RL FEBS Lett. 550:57-63(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15840691; DOI=10.1182/blood-2004-09-3755;
RA Verploegen S., Ulfman L., van Deutekom H.W., van Aalst C., Honing H.,
RA Lammers J.W., Koenderman L., Coffer P.J.;
RT "Characterization of the role of CaMKI-like kinase (CKLiK) in human
RT granulocyte function.";
RL Blood 106:1076-1083(2005).
RN [8]
RP FUNCTION IN CREB1 ACTIVATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP INDUCTION BY KCL, AND MUTAGENESIS OF LYS-52 AND THR-180.
RX PubMed=16324104; DOI=10.1111/j.1460-9568.2005.04463.x;
RA Sakagami H., Kamata A., Nishimura H., Kasahara J., Owada Y., Takeuchi Y.,
RA Watanabe M., Fukunaga K., Kondo H.;
RT "Prominent expression and activity-dependent nuclear translocation of
RT Ca2+/calmodulin-dependent protein kinase Idelta in hippocampal neurons.";
RL Eur. J. Neurosci. 22:2697-2707(2005).
RN [9]
RP FUNCTION IN DENDRITIC GROWTH, AND DEVELOPMENTAL STAGE.
RX PubMed=17056143; DOI=10.1016/j.neures.2006.09.013;
RA Kamata A., Sakagami H., Tokumitsu H., Owada Y., Fukunaga K., Kondo H.;
RT "Spatiotemporal expression of four isoforms of Ca2+/calmodulin-dependent
RT protein kinase I in brain and its possible roles in hippocampal dendritic
RT growth.";
RL Neurosci. Res. 57:86-97(2007).
RN [10]
RP REVIEW ON FUNCTION IN NEURONAL PLASTICITY.
RX PubMed=18817731; DOI=10.1016/j.neuron.2008.08.021;
RA Wayman G.A., Lee Y.S., Tokumitsu H., Silva A.J., Silva A., Soderling T.R.;
RT "Calmodulin-kinases: modulators of neuronal development and plasticity.";
RL Neuron 59:914-931(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND THR-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 IN COMPLEX WITH INHIBITOR.
RA Debreczeni J.E., Rellos P., Fedorov O., Niesen F.H., Bhatia C.,
RA Shrestha L., Salah E., Smee C., Colebrook S., Berridge G., Gileadi O.,
RA Bunkoczi G., Ugochukwu E., Pike A.C.W., Von Delft F., Knapp S.,
RA Sundstrom M., Weigelt J., Arrowsmith C.H., Edwards A.;
RT "Crystal structure of human calmodulin-dependent protein kinase 1D.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] MET-66.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in
CC the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium
CC influx, activates CREB-dependent gene transcription, regulates calcium-
CC mediated granulocyte function and respiratory burst and promotes basal
CC dendritic growth of hippocampal neurons. In neutrophil cells, required
CC for cytokine-induced proliferative responses and activation of the
CC respiratory burst. Activates the transcription factor CREB1 in
CC hippocampal neuron nuclei. May play a role in apoptosis of
CC erythroleukemia cells. In vitro, phosphorylates transcription factor
CC CREM isoform Beta. {ECO:0000269|PubMed:11050006,
CC ECO:0000269|PubMed:15840691, ECO:0000269|PubMed:16324104,
CC ECO:0000269|PubMed:17056143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17;
CC Evidence={ECO:0000269|PubMed:12935886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.17; Evidence={ECO:0000269|PubMed:12935886};
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC calmodulin results in conformational change that relieves intrasteric
CC autoinhibition and allows phosphorylation of Thr-180 within the
CC activation loop by CaMKK1 or CaMKK2. Phosphorylation of Thr-180 results
CC in several fold increase in total activity. Unlike CaMK4, may be unable
CC to exhibit autonomous activity after Ca(2+)/calmodulin activation.
CC {ECO:0000269|PubMed:11050006, ECO:0000269|PubMed:12935886}.
CC -!- INTERACTION:
CC Q8IU85; Q14012: CAMK1; NbExp=2; IntAct=EBI-3911453, EBI-6380130;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC Note=Predominantly cytoplasmic. Nuclear localization increases upon
CC activation by KCl treatment in hippocampal neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IU85-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IU85-2; Sequence=VSP_012135;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly and mostly expressed in
CC polymorphonuclear leukocytes (neutrophilic and eosinophilic
CC granulocytes) while little or no expression is observed in monocytes
CC and lymphocytes. {ECO:0000269|PubMed:11050006,
CC ECO:0000269|PubMed:12935886, ECO:0000269|PubMed:15840691}.
CC -!- DEVELOPMENTAL STAGE: Expressed during hippocampal formation with high
CC expression in the pyramidal cell layers. {ECO:0000269|PubMed:16324104,
CC ECO:0000269|PubMed:17056143}.
CC -!- INDUCTION: Expression increases upon treatment of EC cells with DMSO
CC and retinoic acid. Induced by KCL in PC12 cells.
CC {ECO:0000269|PubMed:16324104}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AF286366; AAG00534.1; -; mRNA.
DR EMBL; AB081726; BAC19846.1; -; mRNA.
DR EMBL; EF444962; ACA05959.1; -; Genomic_DNA.
DR EMBL; AL391314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86314.1; -; Genomic_DNA.
DR EMBL; BC035745; AAH35745.1; -; mRNA.
DR CCDS; CCDS7091.1; -. [Q8IU85-1]
DR CCDS; CCDS7092.1; -. [Q8IU85-2]
DR RefSeq; NP_065130.1; NM_020397.3. [Q8IU85-2]
DR RefSeq; NP_705718.1; NM_153498.3. [Q8IU85-1]
DR PDB; 2JC6; X-ray; 2.30 A; A/C=1-333.
DR PDB; 6QP5; X-ray; 1.90 A; A=10-329.
DR PDB; 6T28; X-ray; 1.55 A; AAA=1-385.
DR PDB; 6T29; X-ray; 1.48 A; AAA=1-385.
DR PDB; 6T6F; X-ray; 1.97 A; A/B=10-329.
DR PDBsum; 2JC6; -.
DR PDBsum; 6QP5; -.
DR PDBsum; 6T28; -.
DR PDBsum; 6T29; -.
DR PDBsum; 6T6F; -.
DR AlphaFoldDB; Q8IU85; -.
DR SMR; Q8IU85; -.
DR BioGRID; 121382; 50.
DR IntAct; Q8IU85; 22.
DR STRING; 9606.ENSP00000478874; -.
DR BindingDB; Q8IU85; -.
DR ChEMBL; CHEMBL5073; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB08454; N-(5-METHYL-1H-PYRAZOL-3-YL)-2-PHENYLQUINAZOLIN-4-AMINE.
DR DrugCentral; Q8IU85; -.
DR GuidetoPHARMACOLOGY; 1953; -.
DR GlyGen; Q8IU85; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IU85; -.
DR PhosphoSitePlus; Q8IU85; -.
DR BioMuta; CAMK1D; -.
DR DMDM; 56404610; -.
DR EPD; Q8IU85; -.
DR jPOST; Q8IU85; -.
DR MassIVE; Q8IU85; -.
DR MaxQB; Q8IU85; -.
DR PaxDb; Q8IU85; -.
DR PeptideAtlas; Q8IU85; -.
DR PRIDE; Q8IU85; -.
DR ProteomicsDB; 70522; -. [Q8IU85-1]
DR ProteomicsDB; 70523; -. [Q8IU85-2]
DR Antibodypedia; 1550; 449 antibodies from 37 providers.
DR DNASU; 57118; -.
DR Ensembl; ENST00000378845.5; ENSP00000368122.1; ENSG00000183049.14. [Q8IU85-2]
DR Ensembl; ENST00000619168.5; ENSP00000478874.1; ENSG00000183049.14. [Q8IU85-1]
DR GeneID; 57118; -.
DR KEGG; hsa:57118; -.
DR MANE-Select; ENST00000619168.5; ENSP00000478874.1; NM_153498.4; NP_705718.1.
DR UCSC; uc001iln.4; human. [Q8IU85-1]
DR CTD; 57118; -.
DR DisGeNET; 57118; -.
DR GeneCards; CAMK1D; -.
DR HGNC; HGNC:19341; CAMK1D.
DR HPA; ENSG00000183049; Tissue enhanced (retina).
DR MIM; 607957; gene.
DR neXtProt; NX_Q8IU85; -.
DR OpenTargets; ENSG00000183049; -.
DR PharmGKB; PA134992438; -.
DR VEuPathDB; HostDB:ENSG00000183049; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000156776; -.
DR InParanoid; Q8IU85; -.
DR OMA; ADCPEGK; -.
DR OrthoDB; 25795at2759; -.
DR PhylomeDB; Q8IU85; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.17; 2681.
DR PathwayCommons; Q8IU85; -.
DR SignaLink; Q8IU85; -.
DR SIGNOR; Q8IU85; -.
DR BioGRID-ORCS; 57118; 8 hits in 1108 CRISPR screens.
DR ChiTaRS; CAMK1D; human.
DR EvolutionaryTrace; Q8IU85; -.
DR GenomeRNAi; 57118; -.
DR Pharos; Q8IU85; Tchem.
DR PRO; PR:Q8IU85; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IU85; protein.
DR Bgee; ENSG00000183049; Expressed in middle temporal gyrus and 181 other tissues.
DR ExpressionAtlas; Q8IU85; baseline and differential.
DR Genevisible; Q8IU85; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0060267; P:positive regulation of respiratory burst; IMP:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:0071622; P:regulation of granulocyte chemotaxis; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Calcium; Calmodulin-binding; Cytoplasm; Inflammatory response;
KW Isopeptide bond; Kinase; Neurogenesis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..385
FT /note="Calcium/calmodulin-dependent protein kinase type 1D"
FT /id="PRO_0000086082"
FT DOMAIN 23..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 279..319
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT REGION 299..320
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 360..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 318..324
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 180
FT /note="Phosphothreonine; by CaMKK1 and CaMKK2"
FT /evidence="ECO:0000269|PubMed:12935886,
FT ECO:0007744|PubMed:18669648"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 348..385
FT /note="LAPSTLCSFISSSSGVSGVGAERRPRPTTVTAVHSGSK -> AYVAKPESLS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11050006"
FT /id="VSP_012135"
FT VARIANT 66
FT /note="I -> M (in dbSNP:rs34194224)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040599"
FT MUTAGEN 52
FT /note="K->A: Catalytically inactive form."
FT /evidence="ECO:0000269|PubMed:16324104"
FT MUTAGEN 180
FT /note="T->A: Loss of ionomycin-induced activation."
FT /evidence="ECO:0000269|PubMed:12935886,
FT ECO:0000269|PubMed:16324104"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2JC6"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:6QP5"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6T6F"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6T6F"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6QP5"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:6QP5"
FT TURN 242..247
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:6QP5"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:6QP5"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:2JC6"
FT TURN 323..327
FT /evidence="ECO:0007829|PDB:6T6F"
SQ SEQUENCE 385 AA; 42914 MW; 717467D019E30FC9 CRC64;
MARENGESSS SWKKQAEDIK KIFEFKETLG TGAFSEVVLA EEKATGKLFA VKCIPKKALK
GKESSIENEI AVLRKIKHEN IVALEDIYES PNHLYLVMQL VSGGELFDRI VEKGFYTEKD
ASTLIRQVLD AVYYLHRMGI VHRDLKPENL LYYSQDEESK IMISDFGLSK MEGKGDVMST
ACGTPGYVAP EVLAQKPYSK AVDCWSIGVI AYILLCGYPP FYDENDSKLF EQILKAEYEF
DSPYWDDISD SAKDFIRNLM EKDPNKRYTC EQAARHPWIA GDTALNKNIH ESVSAQIRKN
FAKSKWRQAF NATAVVRHMR KLHLGSSLDS SNASVSSSLS LASQKDCLAP STLCSFISSS
SGVSGVGAER RPRPTTVTAV HSGSK
