CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002485
UniProt Accession
Genbank Protein ID
 X03233 
Genbank Nucleotide ID
Protein Name
 Creatine kinase M-type 
Protein Synonyms/Alias
 Creatine kinase M chain; M-CK 
Gene Name
 Ckm 
Gene Synonyms/Alias
 Ckmm 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
9PFGNTHNKFKLNYKPacetylation[1]
9PFGNTHNKFKLNYKPubiquitination[2]
11GNTHNKFKLNYKPQEacetylation[1]
11GNTHNKFKLNYKPQEubiquitination[2]
15NKFKLNYKPQEEYPDacetylation[1]
15NKFKLNYKPQEEYPDubiquitination[2]
25EEYPDLSKHNNHMAKubiquitination[2]
32KHNNHMAKVLTPDLYacetylation[1]
32KHNNHMAKVLTPDLYubiquitination[2]
41LTPDLYNKLRDKETPacetylation[1]
41LTPDLYNKLRDKETPubiquitination[2]
101QDRHGGYKPTDKHKTacetylation[1]
105GGYKPTDKHKTDLNHubiquitination[2]
107YKPTDKHKTDLNHENubiquitination[2]
116DLNHENLKGGDDLDPacetylation[1]
116DLNHENLKGGDDLDPubiquitination[2]
138VRTGRSIKGYTLPPHubiquitination[2]
156GERRAVEKLSVEALNacetylation[1]
156GERRAVEKLSVEALNubiquitination[2]
170NSLTGEFKGKYYPLKacetylation[1]
170NSLTGEFKGKYYPLKubiquitination[2]
172LTGEFKGKYYPLKSMacetylation[1]
196DDHFLFDKPVSPLLLacetylation[1]
196DDHFLFDKPVSPLLLubiquitination[2]
223GIWHNDNKSFLVWVNubiquitination[2]
242LRVISMEKGGNMKEVacetylation[1]
242LRVISMEKGGNMKEVubiquitination[2]
247MEKGGNMKEVFRRFCubiquitination[2]
259RFCVGLQKIEEIFKKacetylation[1]
259RFCVGLQKIEEIFKKubiquitination[2]
265QKIEEIFKKAGHPFMacetylation[1]
265QKIEEIFKKAGHPFMubiquitination[2]
266KIEEIFKKAGHPFMWubiquitination[2]
298LRGGVHVKLANLSKHacetylation[1]
298LRGGVHVKLANLSKHubiquitination[2]
304VKLANLSKHPKFEEIacetylation[1]
304VKLANLSKHPKFEEIubiquitination[2]
307ANLSKHPKFEEILTRacetylation[1]
307ANLSKHPKFEEILTRubiquitination[2]
365KLMVEMEKKLEKGQSacetylation[1]
369EMEKKLEKGQSIDDMubiquitination[2]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [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
Functional Description
 Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. 
Sequence Annotation
 DOMAIN 11 98 Phosphagen kinase N-terminal.
 DOMAIN 125 367 Phosphagen kinase C-terminal.
 NP_BIND 128 132 ATP (By similarity).
 NP_BIND 320 325 ATP (By similarity).
 BINDING 191 191 ATP (By similarity).
 BINDING 236 236 ATP (By similarity).
 BINDING 292 292 ATP (By similarity).
 BINDING 335 335 ATP (By similarity).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 381 AA 
Protein Sequence
MPFGNTHNKF KLNYKPQEEY PDLSKHNNHM AKVLTPDLYN KLRDKETPSG FTLDDVIQTG 60
VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGY KPTDKHKTDL NHENLKGGDD 120
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 180
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 240
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 300
NLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GAVFDISNAD RLGSSEVEQV QLVVDGVKLM 360
VEMEKKLEKG QSIDDMIPAQ K 381 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004111; F:creatine kinase activity; IDA:MGI.
 GO:0046314; P:phosphocreatine biosynthetic process; IDA:MGI. 
Interpro
 IPR000749; ATP-guanido_PTrfase.
 IPR022415; ATP-guanido_PTrfase_AS.
 IPR022414; ATP-guanido_PTrfase_cat.
 IPR022413; ATP-guanido_PTrfase_N.
 IPR014746; Gln_synth/guanido_kin_cat_dom. 
Pfam
 PF00217; ATP-gua_Ptrans
 PF02807; ATP-gua_PtransN 
SMART
  
PROSITE
 PS00112; PHOSPHAGEN_KINASE
 PS51510; PHOSPHAGEN_KINASE_C
 PS51509; PHOSPHAGEN_KINASE_N 
PRINTS