[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=Fischer 344; PubMed=6209281 [NCBI, ExPASy, EBI, Israel, Japan] Benfield P.A., Zivin R.A., Miller L.S., Sowder R., Smythers G.W., Henderson L., Oroszlan S., Pearson M.L.; "Isolation and sequence analysis of cDNA clones coding for rat skeletal muscle creatine kinase."; J. Biol. Chem. 259:14979-14984(1984).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; 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).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 87-381. Benfield P.A., Zivin R.A., Shearman C.W., Graf D., Henderson L., Oroszlan S., Pearson M.L.; "The nucleotide sequence of rat muscle creatine kinase cDNA and ckm transcription during myogenesis in an RNA polymerase II mutant of L6 myoblasts."; Exp. Biol. Med. 9:187-194(1984).
[4]	PROTEIN SEQUENCE OF 87-96; 139-148; 157-170 AND 321-341, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (DEC-2006) to UniProtKB.

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

M10140; AAA40935.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062058; AAH62058.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M14864; AAA40936.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A00674; KIRTCM.

NP_036662.1; -.

3D structure databases

HSSP

P00563; 2CRK. [HSSP ENTRY / PDB]

P00564; 2-381.

2D gel databases

P00564; -.

Organism-specific databases

RGD

2358; Ckm.

Gene expression databases

ArrayExpress

P00564; -.

GermOnline

ENSRNOG00000016837; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

P00564.

Genome annotation databases

Ensembl

ENSRNOG00000016837; Rattus norvegicus. [Contig view]

GeneID

24265; -.

KEGG

rno:24265; -.

Phylogenomic databases

HOVERGEN

P00564; -.

Other

NextBio

602819; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 381`	`381`	`Creatine kinase M-type.`	`PRO_0000211979`
`NP_BIND`	`128 132`	`5`	`ATP (By similarity).`
`NP_BIND`	`320 325`	`6`	`ATP (By similarity).`
`BINDING`	`191 191`		`ATP (By similarity).`
`BINDING`	`236 236`		`ATP (By similarity).`
`BINDING`	`292 292`		`ATP (By similarity).`
`BINDING`	`335 335`		`ATP (By similarity).`
`CONFLICT`	`16 16`		`P -> S (in Ref. 1; AAA40935 and 3; AAA40936).`
`CONFLICT`	`87 87`		`D -> N (in Ref. 2; AAA40936).`
`CONFLICT`	`100 100`		`Y -> F (in Ref. 1; AAA40935 and 3; AAA40936).`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 43045 Da [This is the MW of the unprocessed precursor]

CRC64: B573FEB1D2A41056 [This is a checksum on the sequence]

        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

P00564 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools