Reviewed, UniProtKB/Swiss-Prot P06732 (KCRM_HUMAN)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	creatine metabolic process Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Ref.1 Traceable author statement. Source: ProtInc
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_0000211975

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

83

1

E → G: dbSNP rs11559024. Ref.4

VAR_018680

Natural variant

127

1

L → V: dbSNP rs17875653. Ref.4

VAR_018681

Natural variant

166

1

T → M: dbSNP rs17357122.

VAR_049675

Natural variant

243

1

G → A: dbSNP rs17875625. Ref.4

VAR_018682

Experimental info

Sequence conflict

47

1

T → I in AAA52025. Ref.1

Sequence conflict

130

1

R → P in AAA52025. Ref.1

Sequence conflict

193

1

L → Q in AAA52025. Ref.1

Sequence conflict

210

1

D → H in AAA52025. Ref.1

Sequence conflict

215

1

R → P in AAA52025. Ref.1

Sequence conflict

225

1

F → L in AAP35439. Ref.3

Sequence conflict

225

1

F → L in AAH07462. Ref.6

Sequence conflict

324

1

G → A in AAA52025. Ref.1

Secondary structure

1

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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

Beta strand

67 – 69

3

Helix

80 – 84

5

Helix

86 – 93

8

Turn

94 – 96

3

Beta strand

97 – 99

3

Turn

123 – 125

3

Beta strand

126 – 132

7

Turn

143 – 145

3

Helix

148 – 164

17

Helix

167 – 169

3

Beta strand

171 – 176

6

Turn

181 – 183

3

Helix

184 – 189

6

Turn

200 – 206

7

Turn

209 – 214

6

Beta strand

216 – 220

5

Beta strand

223 – 244

22

Helix

246 – 266

21

Turn

275 – 277

3

Helix

284 – 286

3

Beta strand

292 – 298

7

Turn

300 – 304

5

Helix

308 – 314

7

Beta strand

333 – 338

6

Beta strand

342 – 344

3

Helix

346 – 368

23

Sequences

	Sequence		Length	Mass (Da)
	P06732-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: 418FEAD0C2E138C8	FASTA	381	43,101
	10 20 30 40 50 60 MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG 70 80 90 100 110 120 VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD 130 140 150 160 170 180 LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 190 200 210 220 230 240 EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 250 260 270 280 290 300 EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV 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]	"Isolation and sequence analysis of a full-length cDNA for human M creatine kinase." Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R. Biochem. Biophys. Res. Commun. 140:981-989(1986) [PubMed: 3778496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene." Trask R.V., Strauss A.W., Billadello J.J. J. Biol. Chem. 263:17142-17149(1988) [PubMed: 2903158] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	SeattleSNPs variation discovery resource Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-83; VAL-127 AND ALA-243.
[5]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Liver.
[7]	"Muscle creatine kinase isoenzyme expression in adult human brain." Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D., Goodman C., Puleo P.R., Perryman M.B. J. Biol. Chem. 265:6403-6409(1990) [PubMed: 1690725] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-30. Tissue: Brain.
[8]	"cDNA cloning and mapping of the human creatine kinase M gene to 19q13." Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S., Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D., Martin-Deleon P. Am. J. Hum. Genet. 40:115-125(1987) [PubMed: 3031982] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-327.
[9]	"Crystallization and preliminary X-ray analysis of human muscle creatine kinase." Tang L., Zhou H.M., Lin Z.J. Acta Crystallogr. D 55:669-670(1999) [PubMed: 10089465] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Wikipedia

Creatine kinase entry

SeattleSNPs

Wikipedia

CKM entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14780 mRNA. Translation: AAA52025.1.
M21494 , M21488, M21489, M21490, M21491, M21492, M21493 Genomic DNA. Translation: AAA96609.1.
BT006793 mRNA. Translation: AAP35439.1.
AY585238 Genomic DNA. Translation: AAS79321.1.
AC005781 Genomic DNA. Translation: AAC62841.1.
BC007462 mRNA. Translation: AAH07462.1.
M16440 mRNA. Translation: AAA52026.1. Sequence problems.

IPI

IPI00027487.

PIR

KIHUCM. A31793.

RefSeq

NP_001815.2.

UniGene

Hs.334347

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I0E	X-ray	3.50	A/B/C/D	1-381	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P06732.

PTM databases

PhosphoSite

P06732.

2-D gel databases

HSC-2DPAGE

P06732.

Proteomic databases

PeptideAtlas

P06732.

PRIDE

P06732.

Genome annotation databases

Ensembl

ENST00000221476; ENSP00000221476; ENSG00000104879; Homo sapiens. [Genome view]
ENST00000417677; ENSP00000389063; ENSG00000104879; Homo sapiens. [Genome view]

GeneID

1158.

KEGG

hsa:1158.

UCSC

uc002pbd.1. human.

Organism-specific databases

CTD

1158.

GeneCards

GC19M050501.

H-InvDB

HIX0015228.

HGNC

HGNC:1994. CKM.

MIM

123310. gene.

PharmGKB

PA26532.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P06732.

HOVERGEN

P06732.

OMA

TVFKDLF.

Enzyme and pathway databases

BRENDA

2.7.3.2. 247.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

P06732.

Bgee

P06732.

CleanEx

HS_CKM.

Genevestigator

P06732.

GermOnline

ENSG00000104879. Homo sapiens.

Family and domain databases

InterPro

IPR000749. ATP-guanido_PTrfase.
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

DrugBank

DB00148. Creatine.

NextBio

4804.

SOURCE

Search...

Entry information

Entry name

KCRM_HUMAN

Accession

Primary (citable) accession number: P06732
Secondary accession number(s): Q96QL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1990
Last modified:	November 3, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.