Creatine kinase U-type, mitochondrial precursor

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P30275 (KCRU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:

Ckmt1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	418 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.
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
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Nitration Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853 PubMed 18614015. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LRRK2	Q5S007	2	EBI-773103,EBI-5323863	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

Mitochondrion By similarity

Chain

40 – 418

379

Creatine kinase U-type, mitochondrial

PRO_0000016591

Regions

Domain

46 – 132

Phosphagen kinase N-terminal

Domain

159 – 401

243

Phosphagen kinase C-terminal

Nucleotide binding

162 – 166

ATP By similarity

Nucleotide binding

354 – 359

ATP By similarity

Region

40 – 64

Cardiolipin-binding By similarity

Sites

Binding site

225

ATP By similarity

Binding site

270

ATP By similarity

Binding site

326

ATP By similarity

Binding site

369

ATP By similarity

Amino acid modifications

Modified residue

154

Phosphotyrosine Ref.5

Modified residue

313

Nitrated tyrosine Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P30275 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 993CD8C290C8BFB9
Show »

FASTA

418

47,004

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse ubiquitous mitochondrial creatine kinase: gene organization and consequences from inactivation in mouse embryonic stem cells." Steeghs K., Peters W., Brueckwilder M., Croes H., van Alewijk D., Wieringa B. DNA Cell Biol. 14:539-553(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[3]	Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 47-75; 105-130; 152-158; 173-182; 191-200; 250-270; 302-326 AND 355-375, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[4]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." 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. Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-313, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z13968 mRNA. Translation: CAA78371.1. Z13969 Genomic DNA. Translation: CAA78372.1. BC025976 mRNA. Translation: AAH25976.1.
IPI	IPI00128296.
PIR	S24612. I48308.
RefSeq	NP_034027.1. NM_009897.2.
UniGene	Mm.252145.
3D structure databases
ProteinModelPortal	P30275.
SMR	P30275. Positions 40-418.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30275. 4 interactions.
PTM databases
PhosphoSite	P30275.
Proteomic databases
PaxDb	P30275.
PRIDE	P30275.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000317; ENSMUSP00000000317; ENSMUSG00000000308. ENSMUST00000078222; ENSMUSP00000077349; ENSMUSG00000000308.
GeneID	12716.
KEGG	mmu:12716.
Organism-specific databases
CTD	12716.
MGI	MGI:99441. Ckmt1.
Phylogenomic databases
eggNOG	COG3869.
HOGENOM	HOG000232165.
HOVERGEN	HBG001339.
InParanoid	P30275.
KO	K00933.
OMA	ERHNGYN.
OrthoDB	EOG40VVPN.
Gene expression databases
ArrayExpress	P30275.
Bgee	P30275.
CleanEx	MM_CKMT1.
Genevestigator	P30275.
GermOnline	ENSMUSG00000000308. Mus musculus.
Family and domain databases
Gene3D	1.10.135.10. 1 hit. 3.30.590.10. 1 hit.
InterPro	IPR000749. ATP-guanido_PTrfase. IPR022415. ATP-guanido_PTrfase_AS. IPR022414. ATP-guanido_PTrfase_cat. IPR022413. ATP-guanido_PTrfase_N. IPR014746. Gln_synth/guanido_kin_cat_dom. [Graphical view]
PANTHER	PTHR11547. PTHR11547. 1 hit.
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
NextBio	281988.
SOURCE	Search...

Entry information

Entry name

KCRU_MOUSE

Accession

Primary (citable) accession number: P30275

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents