Reviewed, UniProtKB/Swiss-Prot P07335 (KCRB_RAT)

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
Tissue specificity	In the kidney localized primarily in the outer medulla in the thick ascending limb and distal convoluted tubule. Ref.7
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 expression pattern. Source: RGD cellular chloride ion homeostasis Inferred from mutant phenotype. Source: RGD phosphocreatine metabolic process Traceable author statement. Source: RGD
Cellular component	plasma membrane Traceable author statement. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Traceable author statement. Source: RGD protein binding Inferred from direct assay. Source: RGD
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_0000211970
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
Experimental info
	Sequence conflict	18	1	D → A in AAA40931. Ref.3
	Sequence conflict	18	1	D → A in AAA40933. Ref.3
	Sequence conflict	183 – 184	2	EQ → DE in AAA40930. Ref.1
	Sequence conflict	183 – 184	2	EQ → DE in AAA40932. Ref.2
	Sequence conflict	206	1	G → A in AAA40932. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P07335-1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: A8C8A09F6FF1A4D1	FASTA	381	42,725
	10 20 30 40 50 60 MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG 70 80 90 100 110 120 VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEDRHGGY 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 QPIDDLMPAQ K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a rat brain creatine kinase-beta-galactosidase fusion protein in Escherichia coli and derivation of the complete amino acid sequence of rat brain creatine kinase." Benfield P.A., Henderson L., Pearson M.L. Gene 39:263-267(1985) [PubMed: 3005113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation of four rat creatine kinase genes and identification of multiple potential promoter sequences within the rat brain creatine kinase promoter region." Benfield P.A., Graf D., Korolkoff P.N., Hobson G., Pearson M.L. Gene 63:227-243(1988) [PubMed: 2838389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Estrogen regulation of creatine kinase-B in the rat uterus." Pentecost B.T., Mattheiss L., Dickerman H.W., Kumar S.A. Mol. Endocrinol. 4:1000-1010(1990) [PubMed: 2284002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Uterus.
[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]. Tissue: Brain, Embryonic brain, Heart and Prostate.
[5]	Lubec G., Afjehi-Sadat L., Diao W., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 138-148; 157-172; 224-236; 253-265 AND 320-341, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[6]	"The brain isoform of a key ATP-regulating enzyme, creatine kinase, is a phosphoprotein." Mahadevan L.C., Whatley S.A., Leung T.K.C., Lim L. Biochem. J. 222:139-144(1984) [PubMed: 6477506] [Abstract] Cited for: PHOSPHORYLATION.
[7]	"Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney." Friedman D.L., Perryman M.B. J. Biol. Chem. 266:22404-22410(1991) [PubMed: 1939264] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M14400 mRNA. Translation: AAA40930.1. M18668 Genomic DNA. Translation: AAA40932.1. M57664 mRNA. Translation: AAA40933.1. M57665 Genomic DNA. Translation: AAA40931.1. BC065307 mRNA. Translation: AAH65307.2. BC070955 mRNA. Translation: AAH70955.2. BC087656 mRNA. Translation: AAH87656.1. Different initiation. BC099814 mRNA. Translation: AAH99814.2. BC127477 mRNA. Translation: AAI27478.2.
IPI	IPI00470288.
PIR	KIRTCB. A23980.
RefSeq	NP_036661.2.
UniGene	Rn.1472
3D structure databases
HSSP	HSSP built from PDB template 1QH4 based on UniProtKB P05122.
SMR	P07335. Positions 2-381.
ModBase	Search...
PTM databases
PhosphoSite	P07335.
Proteomic databases
PRIDE	P07335.
Genome annotation databases
Ensembl	ENSRNOG00000010872. Rattus norvegicus. [Contig view]
GeneID	24264.
KEGG	rno:24264.
Organism-specific databases
RGD	2357. Ckb.
Phylogenomic databases
HOVERGEN	P07335.
Enzyme and pathway databases
BRENDA	2.7.3.2. 248.
Gene expression databases
ArrayExpress	P07335.
GermOnline	ENSRNOG00000010872. Rattus norvegicus.
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...
Other Resources
NextBio	602815.

Entry information

Entry name

KCRB_RAT

Accession

Primary (citable) accession number: P07335
Secondary accession number(s): A0JPK7 , Q499P7, Q5PPJ5, Q6IRE0, Q6P139

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 9, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)