[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-377. TISSUE=Heart; Towler E.M.; "Bovine creatine kinase M."; Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-359, AND SUBUNIT. DOI=10.1107/S0907444900015614; PubMed=11173463 [NCBI, ExPASy, EBI, Israel, Japan] Tisi D., Bax B., Loew A.; "The three-dimensional structure of cytosolic bovine retinal creatine kinase."; Acta Crystallogr. D 57:187-193(2001).

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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

AF120106; AAD30974.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020785; AAX08802.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT021173; AAX31355.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102907; AAI02908.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777198.2; -.

UniGene

Bt.3651

3D structure databases

PDB

1G0W; X-ray; 2.30 A; A=11-359.

[ExPASy / RCSB / EBI]

1G0W; -.

Q9XSC6; 2-381.

Ontologies

GO:0004111;	Molecular function: creatine kinase activity (inferred from sequence or structural similarity from AgBase).
GO:0046314;	Biological process: phosphocreatine biosynthetic process (inferred from sequence or structural similarity from AgBase).
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.

BLOCKS

Q9XSC6.

Genome annotation databases

Ensembl

ENSBTAG00000013921; Bos taurus. [Contig view]

GeneID

286822; -.

KEGG

bta:286822; -.

Phylogenomic databases

HOVERGEN

Q9XSC6; -.

Other

Q9XSC6; -.

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

Keywords

3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Polymorphism; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 381`	`381`	`Creatine kinase M-type.`	`PRO_0000211973`
`NP_BIND`	`128 132`	`5`	`ATP (By similarity).`
`NP_BIND`	`320 325`	`6`	`ATP (By similarity).`
`ACT_SITE`	`283 283`		`By similarity.`
`BINDING`	`191 191`		`ATP (By similarity).`
`BINDING`	`292 292`		`ATP (By similarity).`
`BINDING`	`335 335`		`ATP (By similarity).`
`VARIANT`	`377 377`	`1`	`I -> M.`
`CONFLICT`	`376 376`		`M -> L (in Ref. 1; AAD30974).`
`HELIX`	`16 19`	`4`
`HELIX`	`29 33`	`5`
`HELIX`	`36 42`	`7`
`HELIX`	`53 62`	`10`
`HELIX`	`81 84`	`4`
`HELIX`	`86 96`	`11`
`TURN`	`97 99`	`3`
`HELIX`	`112 114`	`3`
`TURN`	`123 125`	`3`
`STRAND`	`126 135`	`10`
`TURN`	`143 145`	`3`
`HELIX`	`148 162`	`15`
`HELIX`	`167 169`	`3`
`STRAND`	`171 175`	`5`
`HELIX`	`176 178`	`3`
`HELIX`	`181 190`	`10`
`HELIX`	`200 203`	`4`
`TURN`	`204 214`	`11`
`STRAND`	`216 220`	`5`
`STRAND`	`225 244`	`20`
`HELIX`	`246 266`	`21`
`TURN`	`275 277`	`3`
`HELIX`	`284 286`	`3`
`STRAND`	`292 298`	`7`
`TURN`	`300 303`	`4`
`HELIX`	`308 315`	`8`
`STRAND`	`317 320`	`4`
`STRAND`	`332 338`	`7`
`STRAND`	`342 344`	`3`

Sequence information

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

Molecular weight: 42989 Da [This is the MW of the unprocessed precursor]

CRC64: C97EBBFB00BCF2FC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG 

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

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE 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 GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K

Q9XSC6 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