Creatine kinase B-type - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P12277 (KCRB_HUMAN)

Last modified November 25, 2008. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Creatine kinase B-type
    EC=2.7.3.2
Alternative name(s):
    Creatine kinase B chain
    B-CK

Gene names

Name:	CKB
Synonyms:	CKBB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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.
Catalytic activity	ATP + creatine = ADP + phosphocreatine.
Subunit structure	Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	creatine metabolic process Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 381

380

Creatine kinase B-type

PRO_0000211966

Regions

Nucleotide binding

128 – 132

ATP By similarity

Nucleotide binding

320 – 325

ATP By similarity

Sites

Binding site

191

ATP By similarity

Binding site

236

ATP By similarity

Binding site

292

ATP By similarity

Binding site

335

ATP By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

125

Phosphotyrosine By similarity

Modified residue

164

Phosphoserine By similarity

Natural variations

Natural variant

177

K → R

VAR_025838

Natural variant

309

S → L

VAR_025839

Experimental info

Mutagenesis

283

C → S or Y: Complete loss of activity

Mutagenesis

292

R → H, L or Q: Complete loss of activity

Mutagenesis

292

R → K: 42% of wild-type activity

Mutagenesis

340

D → E: No change in activity

Sequence conflict

41 – 42

EL → DV in AAA76851. Ref.1

Sequence conflict

D → G Ref.3 Ref.7

Sequence conflict

98 – 99

GG → RR in AAA76851. Ref.1

Sequence conflict

105 – 106

EH → DD in AAA76851. Ref.1

Sequence conflict

130

R → G in AAA76850. Ref.3

Sequence conflict

132

R → A in AAA76851. Ref.1

Sequence conflict

203

L → S in AAC31758. Ref.2

Sequence conflict

215 – 216

RG → AR in AAA76851. Ref.1

Sequence conflict

296

H → D in AAA76851. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P12277-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 637AA67A86AE3059
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FASTA

381

42,644

        10         20         30         40         50         60 
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT 

       190        200        210        220        230        240 
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM 

       250        260        270        280        290        300 
QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 

       310        320        330        340        350        360 
NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 

       370        380 
IEMEQRLEQG QAIDDLMPAQ K

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number." Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B. Biochem. Biophys. Res. Commun. 144:1116-1127(1987) [PubMed: 3034271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and expression of the human creatine kinase B gene." Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I., Wieringa B. Genomics 1:126-137(1987) [PubMed: 3692484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci." Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A. J. Clin. Invest. 79:1412-1420(1987) [PubMed: 2883200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete nucleotide sequence of the human creatine kinase B gene." Mariman E.C.M., Schepens J.T.G., Wieringa B. Nucleic Acids Res. 17:6385-6385(1989) [PubMed: 2771648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[5]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-177 AND LEU-309.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Eye and Lung.
[7]	"Isolation of a functional human gene for brain creatine kinase." Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P. J. Biol. Chem. 263:2442-2446(1988) [PubMed: 2828370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[8]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314 AND 342-366, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[9]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 108-130; 157-172; 224-236 AND 253-265, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[10]	"Determination of the catalytic site of creatine kinase by site-directed mutagenesis." Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S. Biochim. Biophys. Acta 1206:97-104(1994) [PubMed: 8186255] [Abstract] Cited for: MUTAGENESIS OF CYS-283; ARG-292 AND ASP-340.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Creatine kinase entry

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Cross-references

Sequence databases
	M16451 mRNA. Translation: AAA76851.1. M21243 M21242 Genomic DNA. Translation: AAC31758.1. L47647 mRNA. Translation: AAA76852.1. M16364 mRNA. Translation: AAA76850.1. X15334 Genomic DNA. Translation: CAA33389.1. DQ333313 Genomic DNA. Translation: ABC67465.1. BC001190 mRNA. Translation: AAH01190.1. BC004914 mRNA. Translation: AAH04914.1. BC008323 mRNA. Translation: AAH08323.1. BC010002 mRNA. Translation: AAH10002.1. BC019259 mRNA. Translation: AAH19259.1. BC019281 mRNA. Translation: AAH19281.1. M22356, M22355 Genomic DNA. Translation: AAA52024.1.
PIR	KIHUCB. S15935.
RefSeq	NP_001814.2.
UniGene	Hs.173724
3D structure databases
HSSP	HSSP built from PDB template 1QH4 based on UniProtKB P05122.
SMR	P12277. Positions 2-381.
ModBase	Search...
Protein-protein interaction databases
IntAct	P12277.
PTM databases
PhosphoSite	P12277.
Polymorphism databases
NIEHS-SNPs	Search...
2-D gel databases
HSC-2DPAGE	P12277.
PHCI-2DPAGE	P12277.
REPRODUCTION-2DPAGE	IPI00022977. P12277.
Proteomic databases
PeptideAtlas	P12277.
Genome annotation databases
Ensembl	ENSG00000166165. Homo sapiens. [Contig view]
GeneID	1152.
KEGG	hsa:1152.
Organism-specific databases
H-InvDB	HIX0012001.
HGNC	HGNC:1991. CKB.
HPA	HPA001254.
MIM	123280. gene.
PharmGKB	PA26528.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P12277.
HOVERGEN	P12277.
Enzyme and pathway databases
Reactome	REACT_13. Metabolism of amino acids.
Gene expression databases
ArrayExpress	P12277.
CleanEx	HS_CKB.
Family and domain databases
InterPro	IPR000749. ATP-gua_Ptrans. IPR014746. Gln_synth/guanido_kin_cat. [Graphical view]
Gene3D	G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit. G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PANTHER	PTHR11547. ATP-gua_Ptrans. 1 hit.
Pfam	PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view]
PROSITE	PS00112. GUANIDO_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00148. Creatine.
NextBio	4784.
SOURCE	Search...

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Entry information

Entry name

KCRB_HUMAN

Accession

Primary (citable) accession number: P12277
Secondary accession number(s): Q2LE07

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 25, 2008
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Human chromosome 14: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents