(data stored in ACNUC26462 zone)

HOGENOM: MOUSE2_PE61

ID   MOUSE2_PE61                          STANDARD;      PRT;   385 AA.
AC   MOUSE2_PE61; Q8BW96; Q3U450; Q80W64; Q8BWI7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1D;
DE   EC=2.7.11 17;AltName: Full=CaM kinase I delta; Short=CaM-KI delta;
DE   Short=CaMKI delta;AltName: Full=CaM kinase ID;AltName: Full=CaMKI-like
DE   protein kinase; Short=CKLiK; Short=mCKLiK; (MOUSE2.PE61).
GN   Name=Camk1d;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE2.PE61.
CC       Mus musculus chromosome 2 NCBIM37  sequence 1..181748087 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KCC1D_MOUSE
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that
CC       operates in the calcium-triggered CaMKK-CaMK1 signaling cascade
CC       and, upon calcium influx, activates CREB-dependent gene
CC       transcription, regulates calcium-mediated granulocyte function and
CC       respiratory burst and promotes basal dendritic growth of
CC       hippocampal neurons. In neutrophil cells, required for cytokine-
CC       induced proliferative responses and activation of the respiratory
CC       burst. Phosphorylates the transcription activator CREB1 on 'Ser-
CC       133' in hippocampal neuron nuclei. May play a role in apoptosis of
CC       erythroleukemia cells. In vitro, phosphorylates transcription
CC       factor CREM isoform Beta (By similarity). Isoform 1 but not
CC       isoform 2 activates CREB1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin results in conformational change that relieves
CC       intrasteric autoinhibition and allows phosphorylation of Thr-180
CC       within the activation loop by CaMKK1 or CaMKK2. Phosphorylation of
CC       Thr-180 results in several fold increase in total activity. Unlike
CC       CaMK4, may be unable to exhibit autonomous activity after
CC       Ca(2+)/calmodulin activation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic (By similarity).
CC       Nuclear upon activation (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q8BW96-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q8BW96-2; Sequence=VSP_012137;
CC         Note=Inactive. Does not activate CREB1;
CC       Name=3;
CC         IsoId=Q8BW96-3; Sequence=VSP_012136;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously with high levels in
CC       brain and low levels in kidney. Isoform 2 is highly expressed in
CC       brain compared to other tissues. In hematopoietic cell lines
CC       predominant expression was detected in T and EC cells.
CC   -!- DEVELOPMENTAL STAGE: In EML cell line differentiation, expression
CC       increases 4 to 8 hours after treatment with all-trans retinoic
CC       acid (ATRA) and then declines after 24 hours of ATRA induction.
CC   -!- INDUCTION: Down-regulated upon cholesterol-rich diet.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and interacts in the inactive folded state with the
CC       catalytic domain as a pseudosubstrate (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000039145;ENSMUST00000044009;ENSMUSP00000037028.
DR   EMBL; AK052401; - ;
DR   EMBL; AK053173; - ;
DR   EMBL; AK147616; - ;
DR   EMBL; AK147657; - ;
DR   EMBL; AK154434; - ;
DR   EMBL; AK170777; - ;
DR   EMBL; AL732403; - ;
DR   EMBL; AL928940; - ;
DR   EMBL; AL928958; - ;
DR   EMBL; AL929142; - ;
DR   EMBL; AY273822; - ;
DR   EMBL; BC141413; - ;
DR   EMBL; BC141414; - ;
DR   EMBL; CH466542; - ;
DR   UniProtKB/Swiss-Prot; Q8BW96; Q3U450; Q80W64; Q8BWI7; -.
DR   EMBL; AY273822; AAP31673.1; -; mRNA.
DR   EMBL; AK052401; BAC34975.1; -; mRNA.
DR   EMBL; AK053173; BAC35295.1; -; mRNA.
DR   EMBL; AK147616; BAE28027.1; -; mRNA.
DR   EMBL; AK154434; BAE32584.1; -; mRNA.
DR   EMBL; AK170777; BAE42022.1; -; mRNA.
DR   IPI; IPI00226188; -.
DR   IPI; IPI00403595; -.
DR   IPI; IPI00480395; -.
DR   RefSeq; NP_796317.2; NM_177343.3.
DR   UniGene; Mm.191949; -.
DR   ProteinModelPortal; Q8BW96; -.
DR   SMR; Q8BW96; 11-313.
DR   IntAct; Q8BW96; 1.
DR   STRING; Q8BW96; -.
DR   PhosphoSite; Q8BW96; -.
DR   PRIDE; Q8BW96; -.
DR   Ensembl; ENSMUST00000044009; ENSMUSP00000037028; ENSMUSG00000039145.
DR   Ensembl; ENSMUST00000114987; ENSMUSP00000110638; ENSMUSG00000039145.
DR   GeneID; 227541; -.
DR   KEGG; mmu:227541; -.
DR   NMPDR; fig|10090.3.peg.5372; -.
DR   CTD; 57118; -.
DR   MGI; MGI:2442190; Camk1d.
DR   GeneTree; ENSGT00600000084207; -.
DR   InParanoid; Q8BW96; -.
DR   OMA; VTTVHSG; -.
DR   PhylomeDB; Q8BW96; -.
DR   NextBio; 378629; -.
DR   ArrayExpress; Q8BW96; -.
DR   Bgee; Q8BW96; -.
DR   CleanEx; MM_CAMK1D; -.
DR   Genevestigator; Q8BW96; -.
DR   GermOnline; ENSMUSG00000039145; Mus musculus.
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; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0042981; P:regulation of apoptosis; IDA:MGI.
DR   InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   PANTHER; PTHR24347; PTHR24347; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; MOUSE2.PE61; -.
KW   ENSMUSG000000391455old_1320000031; ENSMUSP000000370281old_1320000031;
KW   B1AW58_MOUSE; Q3UH04_MOUSE; AK052401; AK053173; AK147616; AK147657;
KW   AK170777; AL732403; AL928940; AL928958; AL929142; AY273822; BC141413;
KW   CH466542;
KW   Allosteric enzyme; Alternative splicing; ATP-binding; Calcium;
KW   Calmodulin-binding; Complete proteome; Cytoplasm;
KW   Inflammatory response; Kinase; Neurogenesis; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   385 AA;  UNKNOWN MW;  UNKNOWN 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 GDTALSKNIH ESVSAQIRKN
     FAKSKWRQAF NATAVVRHMR RLQLGSSLDS SNASVSSNLS LASQKDCLAP STLCSFLSSS
     SGVAGVGAER RPRPTTVTTG HTGSK
//

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