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P00564 (KCRM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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 M-type

EC=2.7.3.2
Alternative name(s):
Creatine kinase M chain
M-CK
Gene names
Name:Ckm
Synonyms:Ckmm
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.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processphosphocreatine biosynthetic process

Inferred from direct assay PubMed 12069495. Source: RGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

creatine kinase activity

Inferred from direct assay PubMed 12069495. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380Creatine kinase M-type
PRO_0000211979

Regions

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

Sites

Binding site1911ATP By similarity
Binding site2361ATP By similarity
Binding site2921ATP By similarity
Binding site3351ATP By similarity

Experimental info

Sequence conflict161P → S in AAA40935. Ref.1
Sequence conflict871D → N in AAA40936. Ref.3
Sequence conflict1001Y → F in AAA40935. Ref.1
Sequence conflict1001Y → F in AAA40936. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P00564 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B573FEB1D2A41056

FASTA38143,045
        10         20         30         40         50         60 
MPFGNTHNKF KLNYKPQEEY PDLSKHNNHM AKVLTPDLYN KLRDKETPSG FTLDDVIQTG 

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

       130        140        150        160        170        180 
LDPNYVLSSR 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 
NLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GAVFDISNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence analysis of cDNA clones coding for rat skeletal muscle creatine kinase."
Benfield P.A., Zivin R.A., Miller L.S., Sowder R., Smythers G.W., Henderson L., Oroszlan S., Pearson M.L.
J. Biol. Chem. 259:14979-14984(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Fischer 344.
[2]"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: Prostate.
[3]"The nucleotide sequence of rat muscle creatine kinase cDNA and ckm transcription during myogenesis in an RNA polymerase II mutant of L6 myoblasts."
Benfield P.A., Zivin R.A., Shearman C.W., Graf D., Henderson L., Oroszlan S., Pearson M.L.
Exp. Biol. Med. 9:187-194(1984)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-381.
[4]Lubec G., Afjehi-Sadat L.
Submitted (DEC-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 87-96; 139-148; 157-170 AND 321-341, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10140 mRNA. Translation: AAA40935.1.
BC062058 mRNA. Translation: AAH62058.1.
M14864 mRNA. Translation: AAA40936.1.
PIRKIRTCM. A00674.
RefSeqNP_036662.1. NM_012530.2.
UniGeneRn.10756.

3D structure databases

ProteinModelPortalP00564.
SMRP00564. Positions 2-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246449. 1 interaction.
STRING10116.ENSRNOP00000022895.

Chemistry

ChEMBLCHEMBL2176800.

PTM databases

PhosphoSiteP00564.

Proteomic databases

PaxDbP00564.
PRIDEP00564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022895; ENSRNOP00000022895; ENSRNOG00000016837.
GeneID24265.
KEGGrno:24265.
UCSCRGD:2358. rat.

Organism-specific databases

CTD1158.
RGD2358. Ckm.

Phylogenomic databases

eggNOGCOG3869.
GeneTreeENSGT00550000074561.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP00564.
KOK00933.
OrthoDBEOG7XM2XW.
PhylomeDBP00564.
TreeFamTF314214.

Gene expression databases

GenevestigatorP00564.

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

NextBio602819.

Entry information

Entry nameKCRM_RAT
AccessionPrimary (citable) accession number: P00564
Secondary accession number(s): Q6P6R9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 110 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