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P00563 (KCRM_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase M-type

EC=2.7.3.2
Alternative name(s):
Creatine kinase M chain
M-CK
Gene names
Name:CKM
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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. Ref.3

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.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKMP119742EBI-2750756,EBI-7133357

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380Creatine kinase M-type
PRO_0000211978

Regions

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

Sites

Binding site1911ATP
Binding site2361ATP
Binding site2921ATP

Secondary structure

................................................................. 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00563 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 821447F395FE71CC

FASTA38143,112
        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 

« Hide

References

[1]"Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences."
Pickering L., Pang H., Biemann K., Munro H., Schimmel P.
Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and detection of human homologues."
Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.
J. Biol. Chem. 259:14317-14320(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Brain adenosine 5'-triphosphate-creatine phosphotransferase."
Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.
Biochem. J. 120:589-600(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION.
[4]"Crystal structure of rabbit muscle creatine kinase."
Rao J.K., Bujacz G., Wlodawer A.
FEBS Lett. 439:133-137(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
Tissue: Muscle.
[5]"Structural asymmetry and intersubunit communication in muscle creatine kinase."
Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.
Acta Crystallogr. D 63:381-389(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02831 mRNA. Translation: AAA31205.1.
PIRKIRBCM. A00673.
RefSeqNP_001075708.1. NM_001082239.1.
UniGeneOcu.6249.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U6RX-ray1.65A/B2-381[»]
2CRKX-ray2.35A1-381[»]
ProteinModelPortalP00563.
SMRP00563. Positions 2-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00563. 1 interaction.
MINTMINT-6824935.
STRING9986.ENSOCUP00000020805.

Chemistry

ChEMBLCHEMBL1075201.

Proteomic databases

PRIDEP00563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009056.

Organism-specific databases

CTD1158.

Phylogenomic databases

eggNOGCOG3869.
HOVERGENHBG001339.

Enzyme and pathway databases

SABIO-RKP00563.

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

EvolutionaryTraceP00563.
PMAP-CutDBP00563.

Entry information

Entry nameKCRM_RABIT
AccessionPrimary (citable) accession number: P00563
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 99 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references