ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P07335


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KCRB_RAT
Primary accession number P07335
Secondary accession numbers A0JPK7 Q499P7 Q5PPJ5 Q6IRE0 Q6P139
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 9, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 76)
Name and origin of the protein
Protein name Creatine kinase B-type
Synonyms EC 2.7.3.2
Creatine kinase B chain
B-CK
Gene name
Name: Ckb
Synonyms: Ckbb
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(85)90321-X; PubMed=3005113 [NCBI, ExPASy, EBI, Israel, Japan]
Benfield P.A., Henderson L., Pearson M.L.;
"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.";
Gene 39:263-267(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(88)90527-6; PubMed=2838389 [NCBI, ExPASy, EBI, Israel, Japan]
Benfield P.A., Graf D., Korolkoff P.N., Hobson G., Pearson M.L.;
"Isolation of four rat creatine kinase genes and identification of multiple potential promoter sequences within the rat brain creatine kinase promoter region.";
Gene 63:227-243(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Uterus;
PubMed=2284002 [NCBI, ExPASy, EBI, Israel, Japan]
Pentecost B.T., Mattheiss L., Dickerman H.W., Kumar S.A.;
"Estrogen regulation of creatine kinase-B in the rat uterus.";
Mol. Endocrinol. 4:1000-1010(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Embryonic brain, Heart, and Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 138-148; 157-172; 224-236; 253-265 AND 320-341, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[6]
PHOSPHORYLATION.
PubMed=6477506 [NCBI, ExPASy, EBI, Israel, Japan]
Mahadevan L.C., Whatley S.A., Leung T.K.C., Lim L.;
"The brain isoform of a key ATP-regulating enzyme, creatine kinase, is a phosphoprotein.";
Biochem. J. 222:139-144(1984).
[7]
TISSUE SPECIFICITY.
PubMed=1939264 [NCBI, ExPASy, EBI, Israel, Japan]
Friedman D.L., Perryman M.B.;
"Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney.";
J. Biol. Chem. 266:22404-22410(1991).
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: 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.
  • SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M14400; AAA40930.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18668; AAA40932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M57664; AAA40933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M57665; AAA40931.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065307; AAH65307.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070955; AAH70955.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC087656; AAH87656.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099814; AAH99814.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127477; AAI27478.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23980; KIRTCB.
RefSeq NP_036661.2; -.
UniGene Rn.1472
3D structure databases
HSSP P05122; 1QH4. [HSSP ENTRY / PDB]
SMR P07335; 2-381.
ModBase P07335.
PTM databases
PhosphoSite P07335; -.
Organism-specific databases
RGD 2357; Ckb.
Gene expression databases
ArrayExpress P07335; -.
GermOnline ENSRNOG00000010872; Rattus norvegicus.
Family and domain databases
InterPro IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.
Gene3D G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
PANTHER PTHR11547; ATP-gua_Ptrans; 1.
Pfam PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.
PROSITE PS00112; GUANIDO_KINASE; 1.
BLOCKS P07335.
Genome annotation databases
Ensembl ENSRNOG00000010872; Rattus norvegicus. [Contig view]
GeneID 24264; -.
KEGG rno:24264; -.
Phylogenomic databases
HOVERGEN P07335; -.
Other
ProtoNet P07335.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   381  380     Creatine kinase B-type. PRO_0000211970
NP_BIND   128   132  5     ATP (By similarity). 
NP_BIND   320   325  6     ATP (By similarity). 
ACT_SITE   283   283         
BINDING   191   191        ATP (By similarity). 
BINDING   292   292        ATP (By similarity). 
BINDING   335   335        ATP (By similarity). 
MOD_RES   39    39        Phosphotyrosine (By similarity). 
MOD_RES   125   125        Phosphotyrosine (By similarity). 
MOD_RES   164   164        Phosphoserine (By similarity). 
CONFLICT   18    18        D -> A (in Ref. 3; AAA40931/AAA40933). 
CONFLICT   183   184        EQ -> DE (in Ref. 1; AAA40930 and 2; AAA40932). 
CONFLICT   206   206        G -> A (in Ref. 2; AAA40932). 
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 42725 Da [This is the MW of the unprocessed precursor] CRC64: A8C8A09F6FF1A4D1 [This is a checksum on the sequence]
        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 

P07335 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!