[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/12.18.6925; PubMed=6091045 [NCBI, ExPASy, EBI, Israel, Japan] Kwiatkowski R.W., Schweinfest C.W., Dottin R.P.; "Molecular cloning and the complete nucleotide sequence of the creatine kinase-M cDNA from chicken."; Nucleic Acids Res. 12:6925-6934(1984).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=6096363 [NCBI, ExPASy, EBI, Israel, Japan] Ordahl C.P., Evans G.L., Cooper T.A., Kunz G., Perriard J.-C.; "Complete cDNA-derived amino acid sequence of chick muscle creatine kinase."; J. Biol. Chem. 259:15224-15227(1984).

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.
TISSUE SPECIFICITY: Predominantly found in skeletal muscle, but not in the heart.
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

M10012; AAA48689.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00954; CAA25465.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00954; CAA25466.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A00675; KICHCM.

NP_990838.1; -.

3D structure databases

HSSP

P00563; 2CRK. [HSSP ENTRY / PDB]

SMR

P00565; 2-381.

ModBase

P00565.

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

P00565.

Genome annotation databases

GeneID

396507; -.

KEGG

gga:396507; -.

Phylogenomic databases

HOVERGEN

P00565; -.

Other

UniRef

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

Keywords

ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 381`	`381`	`Creatine kinase M-type.`	`PRO_0000211980`
`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).`

Sequence information

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

Molecular weight: 43328 Da [This is the MW of the unprocessed precursor]

CRC64: 192C236BB46E2531 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPFSSTHNKH KLKFSAEEEF PDLSKHNNHM AKVLTPELYK RLRDKETPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEVFKDLFD PVIQDRHGGY KPTDKHRTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPKYVLSSR VRTGRSIKGY SLPPHCSRGE RRAVEKLSVE ALNSLEGEFK GRYYPLKAMT 

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

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLKKI EEIFKKAGHP FMWTEHLGYI LTCPSNLGTG LRGGVHVKLP 

       310        320        330        340        350        360 
KLSQHPKFEE ILHRLRLQKR GTGGVDTAAV GAVFDISNAD RLGFSEVEQV QMVVDGVKLM 

       370        380 
VEMEKKLEQN QPIDDMIPAQ K

P00565 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