Reviewed, UniProtKB/Swiss-Prot Q9XSC6 (KCRM_BOVIN)

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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
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 By similarity.
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 By similarity. Ref.4
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	phosphocreatine biosynthetic process Inferred from sequence or structural similarity. Source: AgBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from sequence or structural similarity. Source: AgBase
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_0000211973

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

Natural variations

Natural variant

377

1

I → M

Experimental info

Sequence conflict

376

1

M → L in AAD30974. Ref.1

Secondary structure

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381

Helix Strand Turn

Details...

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

Beta strand

126 – 135

10

Turn

143 – 145

3

Helix

148 – 162

15

Helix

167 – 169

3

Beta strand

171 – 175

5

Helix

176 – 178

3

Helix

181 – 190

10

Helix

200 – 203

4

Turn

204 – 214

11

Beta strand

216 – 220

5

Beta strand

225 – 244

20

Helix

246 – 266

21

Turn

275 – 277

3

Helix

284 – 286

3

Beta strand

292 – 298

7

Turn

300 – 303

4

Helix

308 – 315

8

Beta strand

317 – 320

4

Beta strand

332 – 338

7

Beta strand

342 – 344

3

Sequences

	Sequence		Length	Mass (Da)
	Q9XSC6-1 [UniParc]. Last modified June 27, 2006. Version 2. Checksum: C97EBBFB00BCF2FC	FASTA	381	42,989
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bovine creatine kinase M." Towler E.M. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-377. Tissue: Heart.
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." 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. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Heart ventricle.
[4]	"The three-dimensional structure of cytosolic bovine retinal creatine kinase." Tisi D., Bax B., Loew A. Acta Crystallogr. D 57:187-193(2001) [PubMed: 11173463] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-359, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF120106 mRNA. Translation: AAD30974.1.
BT020785 mRNA. Translation: AAX08802.1.
BT021173 mRNA. Translation: AAX31355.1.
BC102907 mRNA. Translation: AAI02908.1.

IPI

IPI00685709.

RefSeq

NP_777198.2.

UniGene

Bt.3651

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G0W	X-ray	2.30	A	2-381	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9XSC6.

Proteomic databases

PRIDE

Q9XSC6.

Genome annotation databases

Ensembl

ENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921; Bos taurus. [Genome view]

GeneID

286822.

KEGG

bta:286822.

Organism-specific databases

CTD

286822.

Phylogenomic databases

eggNOG

maNOG16451.

HOVERGEN

Q9XSC6.

InParanoid

Q9XSC6.

OMA

TVFKDLF.

OrthoDB

EOG986BZ7.

PhylomeDB

Q9XSC6.

Enzyme and pathway databases

BRENDA

2.7.3.2. 251.

Family and domain databases

InterPro

IPR000749. ATP-guanido_PTrfase.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[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...

Entry information

Entry name

KCRM_BOVIN

Accession

Primary (citable) accession number: Q9XSC6
Secondary accession number(s): Q5E9Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	June 27, 2006
Last modified:	January 19, 2010
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)