Creatine kinase B-type - Mus musculus (Mouse)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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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
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Nitration Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed By similarity

Chain

2 – 381

380

Creatine kinase B-type

PRO_0000211967

Regions

Nucleotide binding

128 – 132

5

ATP By similarity

Nucleotide binding

320 – 325

6

ATP By similarity

Sites

Binding site

191

1

ATP By similarity

Binding site

236

1

ATP By similarity

Binding site

292

1

ATP By similarity

Binding site

335

1

ATP By similarity

Amino acid modifications

Modified residue

39

1

Phosphotyrosine

Modified residue

125

1

Phosphotyrosine

Modified residue

164

1

Phosphoserine

Modified residue

269

1

Nitrated tyrosine

Experimental info

Sequence conflict

143

1

P → H in BAE28690. Ref.3

Sequence conflict

217

1

I → M in BAE39162. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

Q04447-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: D901C5653054A490
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FASTA

381

42,713

        10         20         30         40         50         60 
MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG 

        70         80         90        100        110        120 
VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY QPSDEHKTDL NPDNLQGGDD 

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

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

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

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

       370        380 
IEMEQRLEQG QAIDDLMPAQ K

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic variability of the murine creatine kinase B gene locus and related pseudogenes in different inbred strains of mice." van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G., Hendriks W., Wieringa B. Genomics 12:340-349(1992) [PubMed: 1740343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Pentecost B.T. Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic head, Kidney, Sympathetic ganglion and Wolffian duct.
[4]	"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]. Strain: FVB/N. Tissue: Colon.
[5]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 108-130; 157-172; 224-236; 253-265; 268-292 AND 321-358, MASS SPECTROMETRY. Tissue: Hippocampus.
[6]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 139-148; 157-172; 178-209; 224-236; 253-265 AND 320-381, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[7]	"The 3' non-coding region of the mouse brain B creatine kinase mRNA: a sequence with exceptional homology among species." Papenbrock T., Wille W. Nucleic Acids Res. 14:8690-8690(1986) [PubMed: 3641191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 354-381. Strain: C57BL/6J. Tissue: Cerebellum.
[8]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed: 15648052] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed: 16800626] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 AND TYR-125, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M74149 Genomic DNA. Translation: AAA37462.1. L09069 Genomic DNA. Translation: AAA37455.1. AK002467 mRNA. Translation: BAB22121.1. AK014299 mRNA. Translation: BAB29254.1. AK148885 mRNA. Translation: BAE28690.1. AK152388 mRNA. Translation: BAE31176.1. AK153484 mRNA. Translation: BAE32032.1. AK166980 mRNA. Translation: BAE39162.1. AK161990 mRNA. Translation: BAE36669.1. AK167034 mRNA. Translation: BAE39205.1. BC015271 mRNA. Translation: AAH15271.1. BC106109 mRNA. Translation: AAI06110.2. X04591 mRNA. Translation: CAA28259.1.
PIR	A42078.
RefSeq	NP_067248.1.
UniGene	Mm.16831
3D structure databases
HSSP	HSSP built from PDB template 1QH4 based on UniProtKB P05122.
SMR	Q04447. Positions 2-381.
ModBase	Search...
PTM databases
PhosphoSite	Q04447.
2-D gel databases
REPRODUCTION-2DPAGE	Q04447.
Genome annotation databases
Ensembl	ENSMUSG00000001270. Mus musculus. [Contig view]
GeneID	12709.
KEGG	mmu:12709.
Organism-specific databases
MGI	MGI:88407. Ckb.
Phylogenomic databases
HOGENOM	Q04447.
HOVERGEN	Q04447.
Gene expression databases
ArrayExpress	Q04447.
CleanEx	MM_CKB.
GermOnline	ENSMUSG00000001270. Mus musculus.
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
NextBio	281980.
SOURCE	Search...

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Entry information

Entry name

KCRB_MOUSE

Accession

Primary (citable) accession number: Q04447
Secondary accession number(s): Q3KQP4

Q9CXK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 25, 2008
This is version 75 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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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents