KCC1B_MOUSE
ID KCC1B_MOUSE Reviewed; 343 AA.
AC Q9QYK9; Q80W07;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase type 1B;
DE EC=2.7.11.17;
DE AltName: Full=CaM kinase I beta;
DE Short=CaM kinase IB;
DE Short=CaM-KI beta;
DE Short=CaMKI-beta;
DE AltName: Full=Pregnancy up-regulated non-ubiquitously-expressed CaM kinase homolog;
GN Name=Pnck;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10537072;
RA Ueda T., Sakagami H., Abe K., Oishi I., Maruo A., Kondo H., Terashima T.,
RA Ichihashi M., Yamamura H., Minami Y.;
RT "Distribution and intracellular localization of a mouse homologue of
RT Ca2+/calmodulin-dependent protein kinase Ibeta2 in the nervous system.";
RL J. Neurochem. 73:2119-2129(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10673339; DOI=10.1006/geno.1999.6091;
RA Gardner H.P., Rajan J.V., Ha S.I., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Marquis S.T., Chodosh L.A.;
RT "Cloning, characterization, and chromosomal localization of Pnck, a
RT Ca2+/calmodulin-pependent protein kinase.";
RL Genomics 63:279-288(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a
CC proposed calcium-triggered signaling cascade. In vitro phosphorylates
CC CREB1 and SYN1/synapsin I. Phosphorylates and activates CAMK1 (By
CC similarity). {ECO:0000250}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10537072}. Nucleus
CC {ECO:0000269|PubMed:10537072}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in adult brain, and
CC expressed in embryo. In the adult brain detected at high levels in the
CC anterior olfactory nuclei, piriform cortex, septal nuclei, bed nuclei
CC of the stria terminalis, hippocampal pyramidal cells, dentate granule
CC cells, amygdala, hypothalamic nuclei, parabrachial nucleus, and nucleus
CC of the solitary tract. Expressed at lower levels in adult ovary and
CC heart and at very low levels in testis, lung and muscle.
CC {ECO:0000269|PubMed:10537072, ECO:0000269|PubMed:10673339}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis detected at 10 dpc and
CC expression gradually increases thereafter. Expressed mainly in the
CC nervous system, including brain, spinal cord, trigeminal ganglion, and
CC retina. Within the CNS detected in the mantle zone, but not in the
CC ventricular zone. Detected at postnatal day 23 with highest levels in
CC mesencephalon. Also expressed in developing bone and gut.
CC {ECO:0000269|PubMed:10537072, ECO:0000269|PubMed:10673339}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023027; BAA87926.1; -; mRNA.
DR EMBL; AF181984; AAF29157.1; -; mRNA.
DR EMBL; BC051996; AAH51996.1; ALT_INIT; mRNA.
DR EMBL; BC055891; AAH55891.1; -; mRNA.
DR CCDS; CCDS30207.1; -.
DR RefSeq; NP_001186280.1; NM_001199351.1.
DR RefSeq; NP_001186281.1; NM_001199352.1.
DR RefSeq; NP_036170.1; NM_012040.3.
DR RefSeq; XP_006528407.1; XM_006528344.3.
DR RefSeq; XP_011245994.1; XM_011247692.2.
DR AlphaFoldDB; Q9QYK9; -.
DR SMR; Q9QYK9; -.
DR STRING; 10090.ENSMUSP00000002087; -.
DR iPTMnet; Q9QYK9; -.
DR PhosphoSitePlus; Q9QYK9; -.
DR PaxDb; Q9QYK9; -.
DR PRIDE; Q9QYK9; -.
DR ProteomicsDB; 263485; -.
DR Antibodypedia; 2076; 216 antibodies from 26 providers.
DR DNASU; 93843; -.
DR Ensembl; ENSMUST00000002087; ENSMUSP00000002087; ENSMUSG00000002012.
DR Ensembl; ENSMUST00000114472; ENSMUSP00000110116; ENSMUSG00000002012.
DR Ensembl; ENSMUST00000114473; ENSMUSP00000110117; ENSMUSG00000002012.
DR GeneID; 93843; -.
DR KEGG; mmu:93843; -.
DR UCSC; uc009tmc.2; mouse.
DR CTD; 139728; -.
DR MGI; MGI:1347357; Pnck.
DR VEuPathDB; HostDB:ENSMUSG00000002012; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162187; -.
DR InParanoid; Q9QYK9; -.
DR OMA; EFVWARQ; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q9QYK9; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 93843; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Pnck; mouse.
DR PRO; PR:Q9QYK9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QYK9; protein.
DR Bgee; ENSMUSG00000002012; Expressed in ventromedial nucleus of hypothalamus and 199 other tissues.
DR ExpressionAtlas; Q9QYK9; baseline and differential.
DR Genevisible; Q9QYK9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd14169; STKc_CaMKI_beta; 1.
DR InterPro; IPR042696; CaMKI_beta_STKc.
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 ATP-binding; Calcium; Calmodulin-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..343
FT /note="Calcium/calmodulin-dependent protein kinase type 1B"
FT /id="PRO_0000086080"
FT DOMAIN 15..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 290..311
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 314..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 343 AA; 38519 MW; 1B4A28D36E7A936E CRC64;
MLLLKKQTED ISSVYEIREK LGSGAFSEVM LAQERGSAHL VALKCIPKKA LRGKEALVEN
EIAVLRRISH PNIVALEDVH ESPSHLYLAM ELVTGGELFD RIMERGSYTE KDASHLVGQV
LGAVSYLHSL GIVHRDLKPE NLLYATPFED SKIMVSDFGL SKIQAGNMLG TACGTPGYVA
PELLEQKPYG KAVDVWALGV ISYILLCGYP PFYDESDPEL FSQILRASYE FDSPFWDDIS
ESAKDFIRHL LERDPQKRFT CQQALQHLWI SGDAAFDRDI LGSVSEQIQK NFARTHWKRA
FNATSFLRHI RKLGQSPEGE EASRQCMTRH SHPGLGTSQS PKW
