Reviewed, UniProtKB/Swiss-Prot P05124 (KCRB_CANFA)

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

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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.

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	brain development Inferred from sequence or structural similarity. Source: AgBase cellular chloride ion homeostasis Inferred from sequence or structural similarity. Source: AgBase
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: AgBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from sequence or structural similarity. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 381	380	Creatine kinase B-type		PRO_0000211965
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	35	1	Phosphothreonine By similarity
	Modified residue	39	1	Phosphotyrosine By similarity
	Modified residue	125	1	Phosphotyrosine By similarity
	Modified residue	164	1	Phosphoserine By similarity
	Modified residue	199	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P05124-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 2C2F925C78F16364	FASTA	381	42,701
	10 20 30 40 50 60 MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG 70 80 90 100 110 120 VDNPGHPYIM TVGCVAGDEE SYDVFKELFD 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 DNKTFLVWIN EEDHLRVISM 250 260 270 280 290 300 QKGGNMKEVF TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 310 320 330 340 350 360 HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 370 380 IEMEQRLEQG QAIDDLVPAQ K

References

[1]

"The complete nucleotide sequence of canine brain B creatine kinase mRNA: homology in the coding and 3' noncoding regions among species." Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W. Biochem. Biophys. Res. Commun. 138:392-398(1986) [PubMed: 3755597] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.

[2]

"Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species." Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W. Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985) [PubMed: 3866230] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208; 224-236; 247-261; 268-287; 321-357 AND 364-381. Tissue: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M13453 mRNA. Translation: AAA30837.1.
PIR	B24686. A24227.
3D structure databases
HSSP	HSSP built from PDB template 1QH4 based on UniProtKB P05122.
SMR	P05124. Positions 2-381.
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFG00000018277. Canis familiaris. [Contig view]
Phylogenomic databases
HOVERGEN	P05124.
Enzyme and pathway databases
BRENDA	2.7.3.2. 463.
Family and domain databases
InterPro	IPR000749. ATP-guanido_PTrfase. 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...

Entry information

Entry name

KCRB_CANFA

Accession

Primary (citable) accession number: P05124

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 5, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)