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UniProtKB/Swiss-Prot entry P12532


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCRU_HUMAN
Primary accession number P12532
Secondary accession numbers Q0VAM3 Q32NF6 Q53FC4
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 96)
Name and origin of the protein
Protein name Creatine kinase, ubiquitous mitochondrial [Precursor]
Synonyms EC 2.7.3.2
U-MtCK
Acidic-type mitochondrial creatine kinase
Mia-CK
Gene names
Name: CKMT1A
Synonyms: CKMT
and
Name: CKMT1B
Synonyms: CKMT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2914937 [NCBI, ExPASy, EBI, Israel, Japan]
Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D., Strauss A.W.;
"Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase.";
J. Biol. Chem. 264:2890-2897(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and PNS;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[6]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-417, AND SUBUNIT.
DOI=10.1002/(SICI)1097-0134(20000515)39:3<216::AID-PROT40>3.0.CO;2-#; PubMed=10737943 [NCBI, ExPASy, EBI, Israel, Japan]
Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., Schlattner U.;
"Crystal structure of human ubiquitous mitochondrial creatine kinase.";
Proteins 39:216-225(2000).
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
J04469; AAA98744.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006628; AAP35274.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223365; BAD97085.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001926; AAH01926.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006467; AAH06467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108652; AAI08653.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC121001; AAI21002.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC121002; AAI21003.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31431; A30789.
RefSeq NP_001015001.1; -.
NP_066270.1; -.
UniGene Hs.425633
3D structure databases
PDB
1QK1; X-ray; 2.70 A; A/B/C/D/E/F/G/H=39-417.[ExPASy / RCSB / EBI]
PDBsum 1QK1; -.
ModBase P12532.
PTM databases
PhosphoSite P12532; -.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
Organism-specific databases
H-InvDB HIX0012187; -.
HIX0023245; -.
HGNC HGNC:31736; CKMT1A.
HGNC:1995; CKMT1B.
GenAtlas CKMT1A.
MIM 123290; gene. [NCBI / EBI]
PharmGKB PA142672108; -.
GeneCards P12532.
Gene expression databases
CleanEx HS_CKMT1A; -.
HS_CKMT1B; -.
GermOnline ENSG00000166998; Homo sapiens.
ENSG00000168775; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (traceable author statement from ProtInc).
GO:0004111; Molecular function: creatine kinase activity (traceable author statement from ProtInc).
GO:0006600; Biological process: creatine metabolic process (inferred from experiment from Reactome).
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.
BLOCKS 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; -.
Phylogenomic databases
HOGENOM P12532; -.
HOVERGEN P12532; -.
Other
DrugBank DB00148; Creatine.
SOURCE CKMT1A; Homo sapiens.
ProtoNet P12532.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    39  39     Mitochondrion. 
CHAIN   40   417  378     Creatine kinase, ubiquitous mitochondrial. PRO_0000016590
NP_BIND   161   165  5     ATP (By similarity). 
NP_BIND   353   358  6     ATP (By similarity). 
REGION   40    64  25     Cardiolipin-binding (By similarity). 
ACT_SITE   316   316        By similarity. 
BINDING   224   224        ATP (By similarity). 
BINDING   325   325        ATP (By similarity). 
BINDING   368   368        ATP (By similarity). 
MOD_RES   153   153        Phosphotyrosine. 
CONFLICT   401   401        E -> G (in Ref. 3; BAD97085). 
HELIX   49    52  4      
HELIX   62    66  5      
HELIX   69    75  7      
HELIX   86    95  10      
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      
STRAND   159   168  10      
TURN   176   178  3      
HELIX   181   195  15      
HELIX   200   202  3      
STRAND   204   208  5      
HELIX   209   211  3      
HELIX   214   222  9      
HELIX   233   236  4      
TURN   237   247  11      
STRAND   249   253  5      
STRAND   258   277  20      
HELIX   279   298  20      
TURN   299   301  3      
TURN   308   310  3      
HELIX   317   319  3      
STRAND   325   331  7      
HELIX   333   337  5      
HELIX   341   348  8      
STRAND   350   353  4      
TURN   359   361  3      
STRAND   364   372  9      
STRAND   375   377  3      
HELIX   379   400  22      
TURN   401   403  3      
Sequence information
Length: 417 AA [This is the length of the unprocessed precursor] Molecular weight: 47037 Da [This is the MW of the unprocessed precursor] CRC64: 274DAC2E9A8AD882 [This is a checksum on the sequence]
        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 

P12532 in FASTA format

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