[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. PubMed=7598809 [NCBI, ExPASy, EBI, Israel, Japan] Steeghs K., Peters W., Brueckwilder M., Croes H., van Alewijk D., Wieringa B.; "Mouse ubiquitous mitochondrial creatine kinase: gene organization and consequences from inactivation in mouse embryonic stem cells."; DNA Cell Biol. 14:539-553(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Colon; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 47-75; 105-130; 152-158; 173-182; 191-200; 250-270; 302-326 AND 355-375, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Brain; Lubec G., Kang S.U.; Submitted (APR-2007) to UniProtKB.
[4]	PROTEIN SEQUENCE OF 47-58; 258-270; 302-326 AND 355-375, AND MASS SPECTROMETRY. TISSUE=Hippocampus; Lubec G., Klug S.; Submitted (MAR-2007) to UniProtKB.
[5]	NITRATION [LARGE SCALE ANALYSIS] AT TYR-313, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1021/bi060474w; PubMed=16800626 [NCBI, ExPASy, EBI, Israel, Japan] Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.; "Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."; Biochemistry 45:8009-8022(2006).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan] Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."; J. Proteome Res. 7:311-318(2008).

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: 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.
SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z13968; CAA78371.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z13969; CAA78372.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025976; AAH25976.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I48308; S24612.

NP_034027.1; -.

3D structure databases

HSSP

P12532; 1QK1. [HSSP ENTRY / PDB]

P30275; 47-413.

PTM databases

P30275; -.

Organism-specific databases

MGI

MGI:99441; Ckmt1.

Gene expression databases

ArrayExpress

P30275; -.

CleanEx

MM_CKMT1; -.

GermOnline

ENSMUSG00000000308; Mus musculus.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004111;	Molecular function: creatine kinase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.

PANTHER

PTHR11547; ATP-gua_Ptrans; 1.

Pfam

PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.

PROSITE

PS00112; GUANIDO_KINASE; 1.

Proteomics databases

PRIDE

P30275; -.

Genome annotation databases

Ensembl

ENSMUSG00000000308; Mus musculus. [Contig view]

GeneID

12716; -.

KEGG

mmu:12716; -.

Phylogenomic databases

HOGENOM

P30275; -.

HOVERGEN

P30275; -.

Other

281988; -.

Ckmt1; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nitration; Nucleotide-binding; Phosphoprotein; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion (By similarity).`
`CHAIN`	`40 418`	`379`	`Creatine kinase, ubiquitous mitochondrial.`	`PRO_0000016591`
`NP_BIND`	`162 166`	`5`	`ATP (By similarity).`
`NP_BIND`	`354 359`	`6`	`ATP (By similarity).`
`REGION`	`40 64`	`25`	`Cardiolipin-binding (By similarity).`
`BINDING`	`225 225`		`ATP (By similarity).`
`BINDING`	`270 270`		`ATP (By similarity).`
`BINDING`	`326 326`		`ATP (By similarity).`
`BINDING`	`369 369`		`ATP (By similarity).`
`MOD_RES`	`154 154`		`Phosphotyrosine.`
`MOD_RES`	`313 313`		`Nitrated tyrosine.`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47004 Da [This is the MW of the unprocessed precursor]

CRC64: 993CD8C290C8BFB9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGPFSRLLS ARPGLRLLAL AGAGSLTAGI LLRPESVGAA AAERRRLYPP SAEYPDLRKH 

        70         80         90        100        110        120 
NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA 

       130        140        150        160        170        180 
ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC 

       190        200        210        220        230        240 
TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG 

       250        260        270        280        290        300 
MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKEVEKLIQE 

       310        320        330        340        350        360 
RGWEFMWNER LGYILTCPSN LGTGLRAGVH IKLPLLSKDN RFPKILENLR LQKRGTGGVD 

       370        380        390        400        410 
TAATGSVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LERGQDIRIP PPLVHSKH

P30275 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools