Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12532 (KCRU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.7

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion
Chain40 – 417378Creatine kinase U-type, mitochondrial
PRO_0000016590

Regions

Domain45 – 13187Phosphagen kinase N-terminal
Domain158 – 400243Phosphagen kinase C-terminal
Nucleotide binding161 – 1655ATP By similarity
Nucleotide binding353 – 3586ATP By similarity
Region40 – 6425Cardiolipin-binding By similarity

Sites

Binding site2241ATP By similarity
Binding site2691ATP By similarity
Binding site3251ATP By similarity
Binding site3681ATP By similarity

Natural variations

Alternative sequence501S → SQTWPTGQLPGNCTRSRRLC PPSMVTGYPLPS in isoform 2.
VSP_038045

Experimental info

Sequence conflict1761P → L in BAG58600. Ref.3
Sequence conflict4011E → G in BAD97085. Ref.4

Secondary structure

................................................................. 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA41747,037
        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

Isoform 2 [UniParc].

Checksum: 460CD2E9E9D6A0E2
Show »

FASTA44850,421

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung and PNS.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [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.
PIRA30789. A31431.
RefSeqNP_001015001.1. NM_001015001.1.
NP_066270.1. NM_020990.3.
UniGeneHs.654988.
Hs.741420.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QK1X-ray2.70A/B/C/D/E/F/G/H39-417[»]
ProteinModelPortalP12532.
SMRP12532. Positions 39-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107579. 9 interactions.
139227. 4 interactions.
IntActP12532. 4 interactions.
MINTMINT-3304503.
STRING9606.ENSP00000300283.

Chemistry

DrugBankDB00148. Creatine.

PTM databases

PhosphoSiteP12532.

Polymorphism databases

DMDM125315.

2D gel databases

UCD-2DPAGEP12532.

Proteomic databases

PaxDbP12532.
PeptideAtlasP12532.
PRIDEP12532.

Protocols and materials databases

DNASU1159.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300283; ENSP00000300283; ENSG00000237289. [P12532-1]
ENST00000413453; ENSP00000406577; ENSG00000223572. [P12532-1]
ENST00000434505; ENSP00000413165; ENSG00000223572. [P12532-1]
ENST00000441322; ENSP00000413255; ENSG00000237289. [P12532-1]
GeneID1159.
548596.
KEGGhsa:1159.
hsa:548596.
UCSCuc001zsc.3. human. [P12532-1]
uc010uds.2. human. [P12532-2]

Organism-specific databases

CTD1159.
548596.
GeneCardsGC15P043885.
GC15P043985.
HGNCHGNC:31736. CKMT1A.
HGNC:1995. CKMT1B.
HPAHPA043491.
MIM123290. gene.
613415. gene.
neXtProtNX_P12532.
PharmGKBPA142672108.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP12532.
KOK00933.
OMAERHNGYN.
PhylomeDBP12532.
TreeFamTF314214.

Enzyme and pathway databases

BioCycMetaCyc:HS09820-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP12532.
CleanExHS_CKMT1A.
HS_CKMT1B.
GenevestigatorP12532.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCKMT1B. human.
EvolutionaryTraceP12532.
GeneWikiCKMT1B.
NextBio4808.
PROP12532.
SOURCESearch...

Entry information

Entry nameKCRU_HUMAN
AccessionPrimary (citable) accession number: P12532
Secondary accession number(s): B4DIT8 expand/collapse secondary AC list , B7ZA09, Q0VAM3, Q32NF6, Q53FC4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 15

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