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 27-MAR-2024, entry version 186. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8BFM; X-ray; 1.70 A; A=1-385. DR PDB; 8BFS; X-ray; 1.95 A; A=1-385. DR PDBsum; 2JC6; -. DR PDBsum; 6QP5; -. DR PDBsum; 6T28; -. DR PDBsum; 6T29; -. DR PDBsum; 6T6F; -. DR PDBsum; 8BFM; -. DR PDBsum; 8BFS; -. DR AlphaFoldDB; Q8IU85; -. DR SMR; Q8IU85; -. DR BioGRID; 121382; 53. DR IntAct; Q8IU85; 24. DR MINT; Q8IU85; -. 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; 9606-ENSP00000478874; -. DR PeptideAtlas; Q8IU85; -. DR ProteomicsDB; 70522; -. [Q8IU85-1] DR ProteomicsDB; 70523; -. [Q8IU85-2] DR Pumba; Q8IU85; -. DR Antibodypedia; 1550; 494 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 AGR; HGNC:19341; -. DR CTD; 57118; -. DR DisGeNET; 57118; -. DR GeneCards; CAMK1D; -. DR HGNC; HGNC:19341; CAMK1D. DR HPA; ENSG00000183049; Tissue enhanced (brain, 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; RPKVQPC; -. DR OrthoDB; 1121238at2759; -. 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; 9 hits in 1188 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 183 other cell types or tissues. DR ExpressionAtlas; Q8IU85; baseline and differential. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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 CDD; cd14168; STKc_CaMKI_delta; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24347:SF252; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 1D; 1. DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q8IU85; HS. 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:8BFM" FT STRAND 23..31 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:8BFM" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 48..55 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:6T6F" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 118..137 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:8BFM" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:8BFM" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 201..216 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 227..234 FT /evidence="ECO:0007829|PDB:8BFM" FT TURN 242..247 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:8BFM" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 270..275 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:8BFM" FT HELIX 290..300 FT /evidence="ECO:0007829|PDB:8BFM" 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 //