P12532 (KCRU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Creatine kinase U-type, mitochondrial
EC=2.7.3.2

Alternative name(s):
Acidic-type mitochondrial creatine kinase
Short name=Mia-CK
Ubiquitous mitochondrial creatine kinase
Short name=U-MtCK

Gene names

Name:	CKMT1A
Synonyms:	CKMT
AND
Name:	CKMT1B
Synonyms:	CKMT

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	417 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 MTCK homodimers. Ref.9
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Miscellaneous	Mitochondrial creatine kinase binds cardiolipin.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family. Contains 1 phosphagen kinase C-terminal domain. Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	creatine metabolic process Traceable author statement. Source: Reactome
Cellular component	mitochondrial inner membrane Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P12532-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P12532-2)

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: S → SQTWPTGQLPGNCTRSRRLCPPSMVTGYPLPS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

39

Mitochondrion

Chain

40 – 417

378

Creatine kinase U-type, mitochondrial

PRO_0000016590

Regions

Domain

45 – 131

87

Phosphagen kinase N-terminal

Domain

158 – 400

243

Phosphagen kinase C-terminal

Nucleotide binding

161 – 165

5

ATP By similarity

Nucleotide binding

353 – 358

6

ATP By similarity

Region

40 – 64

25

Cardiolipin-binding By similarity

Sites

Binding site

224

1

ATP By similarity

Binding site

269

1

ATP By similarity

Binding site

325

1

ATP By similarity

Binding site

368

1

ATP By similarity

Amino acid modifications

Modified residue

153

1

Phosphotyrosine Ref.6 Ref.7

Natural variations

Alternative sequence

50

1

S → SQTWPTGQLPGNCTRSRRLC PPSMVTGYPLPS in isoform 2.

VSP_038045

Experimental info

Sequence conflict

176

1

P → L in BAG58600. Ref.3

Sequence conflict

401

1

E → G in BAD97085. Ref.4

Secondary structure

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417

Helix Strand Turn

Details...

Helix

49 – 52

4

Helix

62 – 66

5

Helix

69 – 75

7

Helix

86 – 95

10

Beta strand

100 – 102

3

Helix

114 – 117

4

Helix

119 – 129

11

Turn

130 – 132

3

Turn

135 – 137

3

Helix

146 – 148

3

Turn

156 – 158

3

Beta strand

159 – 168

10

Turn

176 – 178

3

Helix

181 – 195

15

Helix

200 – 202

3

Beta strand

204 – 208

5

Helix

209 – 211

3

Helix

214 – 222

9

Helix

233 – 236

4

Turn

237 – 247

11

Beta strand

249 – 253

5

Beta strand

258 – 277

20

Helix

279 – 298

20

Turn

299 – 301

3

Turn

308 – 310

3

Helix

317 – 319

3

Beta strand

325 – 331

7

Helix

333 – 337

5

Helix

341 – 348

8

Beta strand

350 – 353

4

Turn

359 – 361

3

Beta strand

364 – 372

9

Beta strand

375 – 377

3

Helix

379 – 400

22

Turn

401 – 403

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 274DAC2E9A8AD882	FASTA	417	47,037
	10 20 30 40 50 60 MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS AEYPDLRKHN 70 80 90 100 110 120 NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAD 130 140 150 160 170 180 LFDPVIQERH NGYDPRTMKH TTDLDASKIR SGYFDERYVL SSRVRTGRSI RGLSLPPACT 190 200 210 220 230 240 RAERREVERV VVDALSGLKG DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM 250 260 270 280 290 300 ARDWPDARGI WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER 310 320 330 340 350 360 GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT 370 380 390 400 410 AATGGVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL ERGQDIRIPT PVIHTKH
	Isoform 2 [UniParc]. Checksum: 460CD2E9E9D6A0E2	FASTA	448	50,421
	10 20 30 40 50 60 MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS QTWPTGQLPG 70 80 90 100 110 120 NCTRSRRLCP PSMVTGYPLP SAEYPDLRKH NNCMASHLTP AVYARLCDKT TPTGWTLDQC 130 140 150 160 170 180 IQTGVDNPGH PFIKTVGMVA GDEETYEVFA DLFDPVIQER HNGYDPRTMK HTTDLDASKI 190 200 210 220 230 240 RSGYFDERYV LSSRVRTGRS IRGLSLPPAC TRAERREVER VVVDALSGLK GDLAGRYYRL 250 260 270 280 290 300 SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG MARDWPDARG IWHNNEKSFL IWVNEEDHTR 310 320 330 340 350 360 VISMEKGGNM KRVFERFCRG LKEVERLIQE RGWEFMWNER LGYILTCPSN LGTGLRAGVH 370 380 390 400 410 420 IKLPLLSKDS RFPKILENLR LQKRGTGGVD TAATGGVFDI SNLDRLGKSE VELVQLVIDG 430 440 VNYLIDCERR LERGQDIRIP TPVIHTKH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Colon and Hippocampus.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cerebellum.
[5]	"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] (ISOFORM 1). Tissue: Lung and PNS.
[6]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[7]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Crystal structure of human ubiquitous mitochondrial creatine kinase." Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., Schlattner U. Proteins 39:216-225(2000) [PubMed: 10737943] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-417, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04469 Genomic DNA. Translation: AAA98744.1.
BT006628 mRNA. Translation: AAP35274.1.
AK295776 mRNA. Translation: BAG58600.1.
AK223365 mRNA. Translation: BAD97085.1.
AK316124 mRNA. Translation: BAH14495.1.
AK316319 mRNA. Translation: BAH14690.1.
BC001926 mRNA. Translation: AAH01926.1.
BC006467 mRNA. Translation: AAH06467.1.
BC108652 mRNA. Translation: AAI08653.1.
BC121001 mRNA. Translation: AAI21002.1.
BC121002 mRNA. Translation: AAI21003.1.

IPI

IPI00658109.
IPI00877726.

PIR

A30789. A31431.

RefSeq

NP_001015001.1. NM_001015001.1.
NP_066270.1. NM_020990.3.

UniGene

Hs.425633.
Hs.654988.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QK1	X-ray	2.70	A/B/C/D/E/F/G/H	39-417	[»]

ProteinModelPortal

P12532.

SMR

P12532. Positions 39-417.

ModBase

Search...

Protein-protein interaction databases

IntAct

P12532. 1 interaction.

MINT

MINT-3304503.

STRING

P12532.

PTM databases

PhosphoSite

P12532.

2D gel databases

UCD-2DPAGE

P12532.

Proteomic databases

PeptideAtlas

P12532.

PRIDE

P12532.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300283; ENSP00000300283; ENSG00000237289.
ENST00000381694; ENSP00000371113; ENSG00000223572.
ENST00000413453; ENSP00000406577; ENSG00000223572.
ENST00000413657; ENSP00000390428; ENSG00000237289.
ENST00000424065; ENSP00000392779; ENSG00000223572.
ENST00000434505; ENSP00000413165; ENSG00000223572.
ENST00000441322; ENSP00000413255; ENSG00000237289.

GeneID

1159.
548596.

KEGG

hsa:1159.
hsa:548596.

UCSC

uc001zsc.1. human.

Organism-specific databases

CTD

1159.
548596.

GeneCards

GC15P043885.
GC15P043886.

H-InvDB

HIX0012187.
HIX0023245.

HGNC

HGNC:31736. CKMT1A.
HGNC:1995. CKMT1B.

MIM

123290. gene.
613415. gene.

neXtProt

NX_P12532.

PharmGKB

PA142672108.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10393.

GeneTree

ENSGT00550000074561.

HOVERGEN

HBG001339.

InParanoid

P12532.

OMA

ERHNGYN.

OrthoDB

EOG40VVPN.

PhylomeDB

P12532.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14593.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P12532.

Bgee

P12532.

CleanEx

HS_CKMT1A.
HS_CKMT1B.

Genevestigator

P12532.

GermOnline

ENSG00000166998. Homo sapiens.
ENSG00000168775. Homo sapiens.

Family and domain databases

InterPro

IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
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.

KO

K00933.

Pfam

PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]

SUPFAM

SSF48034. ATP-gua_Ptrans. 1 hit.

PROSITE

PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00148. Creatine.

NextBio

4808.

SOURCE

Search...

Entry information

Entry name

KCRU_HUMAN

Accession

Primary (citable) accession number: P12532
Secondary accession number(s): B4DIT8 , B7ZA09, Q0VAM3, Q32NF6, Q53FC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.