Creatine kinase, ubiquitous mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P12532 (KCRU_HUMAN)

Last modified November 25, 2008. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Creatine kinase, ubiquitous mitochondrial
    EC=2.7.3.2
Alternative name(s):
    U-MtCK
    Acidic-type mitochondrial creatine kinase
      Short name=Mia-CK

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

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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.

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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.
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.

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Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	creatine metabolic process Inferred from Experiment. Source: Reactome
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

Mitochondrion

Chain

40 – 417

378

Creatine kinase, ubiquitous mitochondrial

PRO_0000016590

Regions

Nucleotide binding

161 – 165

ATP By similarity

Nucleotide binding

353 – 358

ATP By similarity

Region

40 – 64

Cardiolipin-binding By similarity

Sites

Binding site

224

ATP By similarity

Binding site

269

ATP By similarity

Binding site

325

ATP By similarity

Binding site

368

ATP By similarity

Amino acid modifications

Modified residue

153

Phosphotyrosine

Experimental info

Sequence conflict

401

E → G in BAD97085. Ref.3

Secondary structure

417

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12532-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 274DAC2E9A8AD882
Show »

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

« Hide

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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].
[3]	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]. Tissue: Cerebellum.
[4]	"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: Lung and PNS.
[5]	"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. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, MASS SPECTROMETRY.
[6]	"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.

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Cross-references

Sequence databases

J04469 Genomic DNA. Translation: AAA98744.1.
BT006628 mRNA. Translation: AAP35274.1.
AK223365 mRNA. Translation: BAD97085.1.
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.

PIR

A30789. A31431.

RefSeq

NP_001015001.1.
NP_066270.1.

UniGene

Hs.425633
Hs.654988

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P12532.

PTM databases

PhosphoSite

P12532.

Proteomic databases

PeptideAtlas

P12532.

Genome annotation databases

Ensembl

ENSG00000166998. Homo sapiens. [Contig view]
ENSG00000168775. Homo sapiens. [Contig view]

GeneID

1159.
548596.

KEGG

hsa:1159.
hsa:548596.

Organism-specific databases

H-InvDB

HIX0012187.
HIX0023245.

HGNC

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

MIM

123290. gene.

PharmGKB

PA142672108.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P12532.

HOVERGEN

P12532.

Enzyme and pathway databases

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

CleanEx

HS_CKMT1A.
HS_CKMT1B.

GermOnline

ENSG00000166998. Homo sapiens.
ENSG00000168775. 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

4808.

SOURCE

Search...

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Entry information

Entry name

KCRU_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 25, 2008
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents