CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038195
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Calcium/calmodulin-dependent protein kinase type II subunit beta 
Protein Synonyms/Alias
  
Gene Name
 Camk2d 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
138GIVHRDLKPENLLLAacetylation[1]
138GIVHRDLKPENLLLAubiquitination[2]
227HRLYQQIKAGAYDFPacetylation[3]
227HRLYQQIKAGAYDFPubiquitination[2]
246DTVTPEAKDLINKMLubiquitination[2]
251EAKDLINKMLTINPAubiquitination[2]
259MLTINPAKRITASEAubiquitination[2]
268ITASEALKHPWICQRacetylation[4]
268ITASEALKHPWICQRubiquitination[2]
292QETVDCLKKFNARRKubiquitination[2]
301FNARRKLKGAILTTMubiquitination[2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 488 AA 
Protein Sequence
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER 60
EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI 120
LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY 180
LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT 240
VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL 300
KGAILTTMLA TRNFSAKSLL KKPDGVKKRK SSSSVQMMES TESSNTTIED EDVKARKQEI 360
IKVTEQLIEA INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE NALSKSNKPI 420
HTIILNPHVH LVGDDAACIA YIRLTQYMDG SGMPKTMQSE ETRVWHRRDG KWQNVHFHRS 480
GSPTVPIN 488 
Gene Ontology
 GO:0043194; C:axon initial segment; IDA:MGI.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0014704; C:intercalated disc; IDA:MGI.
 GO:0031594; C:neuromuscular junction; IDA:MGI.
 GO:0043025; C:neuronal cell body; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0030315; C:T-tubule; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:InterPro.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
 GO:0006816; P:calcium ion transport; IDA:MGI.
 GO:0060048; P:cardiac muscle contraction; IDA:MGI.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
 GO:0046777; P:protein autophosphorylation; IMP:MGI.
 GO:0002028; P:regulation of sodium ion transport; IDA:MGI. 
Interpro
 IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
 IPR013543; Ca/CaM-dep_prot_kinase-assoc.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF08332; CaMKII_AD
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS