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P07335 (KCRB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase B-type

EC=2.7.3.2
Alternative name(s):
B-CK
Creatine kinase B chain
Gene names
Name:Ckb
Synonyms:Ckbb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Sequence caution

The sequence AAH87656.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380Creatine kinase B-type
PRO_0000211970

Regions

Domain11 – 9888Phosphagen kinase N-terminal
Domain125 – 367243Phosphagen kinase C-terminal
Nucleotide binding128 – 1325ATP By similarity
Nucleotide binding320 – 3256ATP By similarity

Sites

Binding site1301ATP By similarity
Binding site1321ATP By similarity
Binding site1911ATP By similarity
Binding site2321Substrate By similarity
Binding site2361ATP By similarity
Binding site2851Substrate By similarity
Binding site2921ATP By similarity
Binding site3201ATP By similarity
Binding site3351ATP By similarity

Amino acid modifications

Modified residue41Phosphoserine By similarity
Modified residue351Phosphothreonine By similarity
Modified residue1251Phosphotyrosine By similarity
Modified residue1991Phosphoserine By similarity
Modified residue2691Nitrated tyrosine By similarity

Experimental info

Sequence conflict181D → A in AAA40931. Ref.3
Sequence conflict181D → A in AAA40933. Ref.3
Sequence conflict183 – 1842EQ → DE in AAA40930. Ref.1
Sequence conflict183 – 1842EQ → DE in AAA40932. Ref.2
Sequence conflict2061G → A in AAA40932. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P07335 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: A8C8A09F6FF1A4D1

FASTA38142,725
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKIRTCB. A23980.
RefSeqNP_036661.3. NM_012529.3.
UniGeneRn.1472.

3D structure databases

ProteinModelPortalP07335.
SMRP07335. Positions 2-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246448. 1 interaction.
IntActP07335. 1 interaction.
MINTMINT-4586357.

Chemistry

ChEMBLCHEMBL2176812.

PTM databases

PhosphoSiteP07335.

2D gel databases

World-2DPAGE0004:P07335.

Proteomic databases

PaxDbP07335.
PRIDEP07335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015122; ENSRNOP00000015122; ENSRNOG00000010872.
GeneID24264.
KEGGrno:24264.
UCSCRGD:2357. rat.

Organism-specific databases

CTD1152.
RGD2357. Ckb.

Phylogenomic databases

eggNOGCOG3869.
GeneTreeENSGT00550000074561.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP07335.
KOK00933.
OMAYMAKILT.
OrthoDBEOG7XM2XW.
PhylomeDBP07335.
TreeFamTF314214.

Gene expression databases

GenevestigatorP07335.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio602815.

Entry information

Entry nameKCRB_RAT
AccessionPrimary (citable) accession number: P07335
Secondary accession number(s): A0JPK7 expand/collapse secondary AC list , Q499P7, Q5PPJ5, Q6IRE0, Q6P139
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families