Reviewed, UniProtKB/Swiss-Prot P17540 (KCRS_HUMAN)

Names and origin

Protein names

Recommended name:
    Creatine kinase, sarcomeric mitochondrial
    EC=2.7.3.2
Alternative name(s):
    S-MtCK
    Basic-type mitochondrial creatine kinase
    Mib-CK

Gene names

Name:

CKMT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Exists as an octamer composed of four CKMT2 homodimers.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Tissue specificity	Sarcomere-specific. Found only in heart and skeletal muscles.
Miscellaneous	Mitochondrial creatine kinase binds cardiolipin.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	creatine metabolic process Inferred from Experiment. Source: Reactome muscle contraction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
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

Transit peptide

1 – 39

39

Mitochondrion

Chain

40 – 419

380

Creatine kinase, sarcomeric mitochondrial

PRO_0000016594

Regions

Nucleotide binding

162 – 166

5

ATP

Nucleotide binding

354 – 359

6

ATP

Region

40 – 64

25

Cardiolipin-binding By similarity

Sites

Binding site

225

1

ATP

Binding site

270

1

ATP By similarity

Binding site

326

1

ATP

Binding site

369

1

ATP

Experimental info

Sequence conflict

74

1

A → S in AAA60561. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

419

Helix Strand Turn

Details...

Helix

50 – 53

4

Helix

63 – 67

5

Helix

70 – 76

7

Helix

87 – 96

10

Helix

115 – 118

4

Helix

120 – 130

11

Turn

131 – 133

3

Turn

136 – 138

3

Beta strand

165 – 169

5

Turn

177 – 179

3

Helix

182 – 197

16

Helix

201 – 203

3

Beta strand

205 – 210

6

Helix

215 – 223

9

Helix

234 – 237

4

Turn

238 – 248

11

Beta strand

250 – 254

5

Beta strand

257 – 273

17

Helix

280 – 300

21

Turn

309 – 311

3

Helix

318 – 320

3

Beta strand

326 – 332

7

Helix

334 – 338

5

Helix

342 – 348

7

Beta strand

351 – 355

5

Beta strand

367 – 373

7

Beta strand

376 – 378

3

Helix

380 – 388

9

Helix

394 – 399

6

Sequences

	Sequence		Length	Mass (Da)
	P17540-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 0CAF000074D99B6F	FASTA	419	47,504
	10 20 30 40 50 60 MASIFSKLLT GRNASLLFAT MGTSVLTTGY LLNRQKVCAE VREQPRLFPP SADYPDLRKH 70 80 90 100 110 120 NNCMAECLTP AIYAKLRNKV TPNGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA 130 140 150 160 170 180 DLFDPVIKLR HNGYDPRVMK HTTDLDASKI TQGQFDEHYV LSSRVRTGRS IRGLSLPPAC 190 200 210 220 230 240 TRAERREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG 250 260 270 280 290 300 MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE 310 320 330 340 350 360 RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD 370 380 390 400 410 TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes." Haas R.C., Strauss A.W. J. Biol. Chem. 265:6921-6927(1990) [PubMed: 2324105] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: Brain.
[4]	"Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase." Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D., Strauss A.W. J. Biol. Chem. 264:2890-2897(1989) [PubMed: 2914937] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-65.
[5]	"Crystal structure of human sarcomeric mitochondrial creatine kinase." Structural genomics consortium (SGC) Submitted (APR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-416 IN COMPLEX WITH ADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05401 mRNA. Translation: AAA60561.1.
CR450315 mRNA. Translation: CAG29311.1.
BC029140 mRNA. Translation: AAH29140.1.

PIR

A35756.

RefSeq

NP_001093205.1.
NP_001093206.1.
NP_001816.2.

UniGene

Hs.80691

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GL6	X-ray	2.30	A/B/C/D/E/F/G/H	27-416	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P17540.

PTM databases

PhosphoSite

P17540.

2-D gel databases

HSC-2DPAGE

P17540.

Genome annotation databases

Ensembl

ENSG00000131730. Homo sapiens. [Contig view]

GeneID

1160.

KEGG

hsa:1160.

Organism-specific databases

H-InvDB

HIX0004999.

HGNC

HGNC:1996. CKMT2.

MIM

123295. gene.

PharmGKB

PA26534.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P17540.

HOVERGEN

P17540.

Enzyme and pathway databases

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

P17540.

CleanEx

HS_CKMT2.

GermOnline

ENSG00000131730. Homo sapiens.

Family and domain databases

InterPro

IPR000749. ATP-gua_Ptrans.
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

4814.

SOURCE

Search...

Entry information

Entry name

KCRS_HUMAN

Accession

Primary (citable) accession number: P17540
Secondary accession number(s): Q6ICS8, Q8N1E1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	October 17, 2006
Last modified:	November 25, 2008
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)