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UniProtKB/Swiss-Prot entry Q04447


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

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Entry information
Entry name KCRB_MOUSE
Primary accession number Q04447
Secondary accession numbers Q3KQP4 Q3TKI3 Q3U5P5 Q3UF71 Q9CXK6
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 73)
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
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(92)90383-4; PubMed=1740343 [NCBI, ExPASy, EBI, Israel, Japan]
van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G., Hendriks W., Wieringa B.;
"Genetic variability of the murine creatine kinase B gene locus and related pseudogenes in different inbred strains of mice.";
Genomics 12:340-349(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Pentecost B.T.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryonic head, Kidney, Sympathetic ganglion, and Wolffian duct;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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; 108-130; 157-172; 224-236; 253-265; 268-292 AND 321-358, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 139-148; 157-172; 178-209; 224-236; 253-265 AND 320-381, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
STRAIN=C57BL/6J;
TISSUE=Cerebellum;
DOI=10.1093/nar/14.21.8690; PubMed=3641191 [NCBI, ExPASy, EBI, Israel, Japan]
Papenbrock T., Wille W.;
"The 3' non-coding region of the mouse brain B creatine kinase mRNA: a sequence with exceptional homology among species.";
Nucleic Acids Res. 14:8690-8690(1986).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1002/pmic.200401066; PubMed=15648052 [NCBI, ExPASy, EBI, Israel, Japan]
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.;
"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol.";
Proteomics 5:388-398(2005).
[9]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/bi060474w; PubMed=16800626 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 AND TYR-125, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
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.
  • 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
M74149; AAA37462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L09069; AAA37455.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002467; BAB22121.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK014299; BAB29254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK148885; BAE28690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK152388; BAE31176.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153484; BAE32032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166980; BAE39162.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK161990; BAE36669.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK167034; BAE39205.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015271; AAH15271.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106109; AAI06110.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04591; CAA28259.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42078; A42078.
RefSeq NP_067248.1; -.
UniGene Mm.16831
3D structure databases
HSSP P05122; 1QH4. [HSSP ENTRY / PDB]
SMR Q04447; 2-381.
ModBase Q04447.
PTM databases
PhosphoSite Q04447; -.
2D gel databases
REPRODUCTION-2DPAGE Q04447; -.
Organism-specific databases
MGI MGI:88407; Ckb.
Gene expression databases
ArrayExpress Q04447; -.
CleanEx MM_CKB; -.
GermOnline ENSMUSG00000001270; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
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 Q04447.
Genome annotation databases
Ensembl ENSMUSG00000001270; Mus musculus. [Contig view]
GeneID 12709; -.
KEGG mmu:12709; -.
Phylogenomic databases
HOGENOM Q04447; -.
HOVERGEN Q04447; -.
Other
SOURCE Ckb; Mus musculus.
ProtoNet Q04447.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nitration; 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_0000211967
NP_BIND   128   132  5     ATP (By similarity). 
NP_BIND   320   325  6     ATP (By similarity). 
ACT_SITE   283   283        By similarity. 
BINDING   191   191        ATP (By similarity). 
BINDING   292   292        ATP (By similarity). 
BINDING   335   335        ATP (By similarity). 
MOD_RES   39    39        Phosphotyrosine. 
MOD_RES   125   125        Phosphotyrosine. 
MOD_RES   164   164        Phosphoserine. 
MOD_RES   269   269        Nitrated tyrosine. 
CONFLICT   143   143        P -> H (in Ref. 3; BAE28690). 
CONFLICT   217   217        I -> M (in Ref. 3; BAE39162). 
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 42713 Da [This is the MW of the unprocessed precursor] CRC64: D901C5653054A490 [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 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 

Q04447 in FASTA format

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