Reviewed, UniProtKB/Swiss-Prot P00564 (KCRM_RAT)

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	Creatine kinase M-type		PRO_0000211979
Regions
	Nucleotide binding	128 – 132	5	ATP By similarity
	Nucleotide binding	320 – 325	6	ATP By similarity
Sites
	Binding site	191	1	ATP By similarity
	Binding site	236	1	ATP By similarity
	Binding site	292	1	ATP By similarity
	Binding site	335	1	ATP By similarity
Experimental info
	Sequence conflict	16	1	P → S in AAA40935. Ref.1
	Sequence conflict	16	1	P → S in AAA40936. Ref.3
	Sequence conflict	87	1	D → N in AAA40936. Ref.2
	Sequence conflict	100	1	Y → F in AAA40935. Ref.1
	Sequence conflict	100	1	Y → F in AAA40936. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P00564-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B573FEB1D2A41056	FASTA	381	43,045
	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

References

	« Hide 'large scale' referencesShow '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: 6209281] [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: 15489334] [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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M10140 mRNA. Translation: AAA40935.1. BC062058 mRNA. Translation: AAH62058.1. M14864 mRNA. Translation: AAA40936.1.
PIR	KIRTCM. A00674.
RefSeq	NP_036662.1.
UniGene	Rn.10756
3D structure databases
HSSP	HSSP built from PDB template 2CRK based on UniProtKB P00563.
SMR	P00564. Positions 2-381.
ModBase	Search...
2-D gel databases
Rat-heart-2DPAGE	P00564.
Genome annotation databases
Ensembl	ENSRNOG00000016837. Rattus norvegicus. [Contig view]
GeneID	24265.
KEGG	rno:24265.
Organism-specific databases
RGD	2358. Ckm.
Phylogenomic databases
HOVERGEN	P00564.
Gene expression databases
ArrayExpress	P00564.
GermOnline	ENSRNOG00000016837. Rattus norvegicus.
Family and domain databases
InterPro	IPR000749. ATP-gua_Ptrans. IPR014746. Gln_synth/guanido_kin_cat. [Graphical view]
Gene3D	G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit. G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PANTHER	PTHR11547. ATP-gua_Ptrans. 1 hit.
Pfam	PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view]
PROSITE	PS00112. GUANIDO_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	602819.

Entry information

Entry name

KCRM_RAT

Accession

Primary (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:	November 4, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)