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UniProtKB/Swiss-Prot entry P00563

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

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Entry information
Entry name KCRM_RABIT
Primary accession number P00563
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 69)
Name and origin of the protein
Protein name Creatine kinase M-type
Synonyms EC 2.7.3.2
Creatine kinase M chain
M-CK
Gene name
Name: CKM
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3857581 [NCBI, ExPASy, EBI, Israel, Japan]
Pickering L., Pang H., Biemann K., Munro H., Schimmel P.;
"Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences.";
Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6094551 [NCBI, ExPASy, EBI, Israel, Japan]
Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.;
"Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and detection of human homologues.";
J. Biol. Chem. 259:14317-14320(1984).
[3]
 ACTIVE SITE.
PubMed=5499971 [NCBI, ExPASy, EBI, Israel, Japan]
Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.;
"Brain adenosine 5'-triphosphate-creatine phosphotransferase.";
Biochem. J. 120:589-600(1970).
[4]
 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
TISSUE=Muscle;
DOI=10.1016/S0014-5793(98)01355-6; PubMed=9849893 [NCBI, ExPASy, EBI, Israel, Japan]
Rao J.K., Bujacz G., Wlodawer A.;
"Crystal structure of rabbit muscle creatine kinase.";
FEBS Lett. 439:133-137(1998).
[5]
 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.
DOI=10.1107/S0907444906056204; PubMed=17327675 [NCBI, ExPASy, EBI, Israel, Japan]
Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.;
"Structural asymmetry and intersubunit communication in muscle creatine kinase.";
Acta Crystallogr. D 63:381-389(2007).
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.
  • SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
  • WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/CRK/";.
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
K02831; AAA31205.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00673; KIRBCM.
RefSeq NP_001075708.1; -.
UniGene Ocu.6249
3D structure databases
PDB
1U6R; X-ray; 1.65 A; A/B=2-381.[ExPASy / RCSB / EBI]
2CRK; X-ray; 2.35 A; A=1-381.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1U6R; -.
2CRK; -.
ModBase P00563.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004111; Molecular function: creatine kinase activity (inferred from electronic annotation from EC).
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 P00563.
ProtoNet P00563.
Genome annotation databases
GeneID 100009056; -.
Phylogenomic databases
HOVERGEN P00563; -.
Other
LinkHub P00563; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   381  381     Creatine kinase M-type. PRO_0000211978
NP_BIND   128   132  5     ATP. 
NP_BIND   320   325  6     ATP. 
BINDING   191   191        ATP. 
BINDING   236   236        ATP. 
BINDING   292   292        ATP. 
HELIX   6    11  6      
HELIX   16    19  4      
HELIX   29    33  5      
HELIX   36    42  7      
HELIX   53    62  10      
HELIX   81    84  4      
HELIX   86    96  11      
TURN   97    99  3      
HELIX   112   114  3      
TURN   123   125  3      
STRAND   126   135  10      
TURN   143   145  3      
HELIX   148   163  16      
HELIX   167   169  3      
STRAND   171   175  5      
HELIX   176   178  3      
HELIX   181   189  9      
HELIX   200   203  4      
TURN   204   214  11      
STRAND   216   220  5      
STRAND   225   244  20      
HELIX   246   267  22      
TURN   275   277  3      
HELIX   284   286  3      
STRAND   292   298  7      
HELIX   300   303  4      
HELIX   308   315  8      
STRAND   317   320  4      
STRAND   322   324  3      
STRAND   333   338  6      
STRAND   342   344  3      
HELIX   346   369  24      
STRAND   374   376  3      
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 43112 Da [This is the MW of the unprocessed precursor] CRC64: 821447F395FE71CC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPHYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 

       190        200        210        220        230        240 
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 

       310        320        330        340        350        360 
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K
P00563 in FASTA format

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