UniProt Accession

 KCRB_HUMAN; P12277; A8K236; B2R5R4; Q2LE07; Q6FG40; Q9UC66 

Genbank Protein ID

 M16451; M21243; M21237; M21238; M21239; M21240; M21241; M21242; L47647; M16364; X15334; AK290101; AK312282; CR542268; DQ333313; CH471061; BC001190; BC004914; BC008323; BC010002; BC019259; BC019281; M22356; M22355 

Genbank Nucleotide ID

 AAA76851.1; AAC31758.1; AAC31758.1; AAC31758.1; AAC31758.1; AAC31758.1; AAC31758.1; AAC31758.1; AAA76852.1; AAA76850.1; CAA33389.1; BAF82790.1; BAG35211.1; CAG47064.1; ABC67465.1; EAW81822.1; AAH01190.1; AAH04914.1; AAH08323.1; AAH10002.1; AAH19259.1; AAH19281.1; AAA52024.1; AAA52024.1 

Protein Name

 Creatine kinase B-type 

Protein Synonyms/Alias

 B-CK; Creatine kinase B chain 

Gene Name

 CKB 

Gene Synonyms/Alias

 CKBB 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
11	SNSHNALKLRFPAED	ubiquitination	[1, 2]
156	GERRAIEKLAVEALS	ubiquitination	[3, 4]
196	DDHFLFDKPVSPLLL	ubiquitination	[4]
223	GIWHNDNKTFLVWVN	ubiquitination	[1, 2]
242	LRVISMQKGGNMKEV	ubiquitination	[1, 2, 4, 5, 6]
247	MQKGGNMKEVFTRFC	ubiquitination	[4, 7, 8]
265	TQIETLFKSKDYEFM	ubiquitination	[1, 2, 7]
298	LRAGVHIKLPNLGKH	ubiquitination	[1, 2]
304	IKLPNLGKHEKFSEV	ubiquitination	[1, 2, 5]
307	PNLGKHEKFSEVLKR	ubiquitination	[1, 2]
313	EKFSEVLKRLRLQKR	ubiquitination	[1, 2, 6]
381	DDLMPAQK*******	ubiquitination	[6, 8]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

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.
 NP_BIND 320 325 ATP.
 BINDING 72 72 Substrate; via amide nitrogen.
 BINDING 130 130 ATP.
 BINDING 132 132 ATP.
 BINDING 191 191 ATP.
 BINDING 232 232 Substrate.
 BINDING 236 236 ATP.
 BINDING 285 285 Substrate.
 BINDING 292 292 ATP.
 BINDING 320 320 ATP.
 BINDING 335 335 ATP (By similarity).
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 35 35 Phosphothreonine.
 MOD_RES 39 39 Phosphotyrosine (By similarity).
 MOD_RES 125 125 Phosphotyrosine (By similarity).
 MOD_RES 164 164 Phosphoserine (By similarity).
 MOD_RES 199 199 Phosphoserine.
 MOD_RES 269 269 Nitrated tyrosine (By similarity).  

Keyword

 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nitration; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 381 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004111; F:creatine kinase activity; TAS:ProtInc.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0030644; P:cellular chloride ion homeostasis; IEA:Compara.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006600; P:creatine metabolic process; TAS:Reactome. 

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