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UniProtKB/Swiss-Prot entry P17540


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

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Entry information
Entry name KCRS_HUMAN
Primary accession number P17540
Secondary accession numbers Q6ICS8 Q8N1E1
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Creatine kinase, sarcomeric mitochondrial [Precursor]
Synonyms EC 2.7.3.2
S-MtCK
Basic-type mitochondrial creatine kinase
Mib-CK
Gene name
Name: CKMT2
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 [MRNA].
TISSUE=Heart;
PubMed=2324105 [NCBI, ExPASy, EBI, Israel, Japan]
Haas R.C., Strauss A.W.;
"Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes.";
J. Biol. Chem. 265:6921-6927(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[4]
PROTEIN SEQUENCE OF 40-65.
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-416 IN COMPLEX WITH ADP.
Structural genomics consortium (SGC);
"Crystal structure of human sarcomeric mitochondrial creatine kinase.";
Submitted (APR-2006) to the PDB data bank.
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 CKMT2 homodimers.
  • SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
  • TISSUE SPECIFICITY: Sarcomere-specific. Found only in heart and skeletal muscles.
  • 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
J05401; AAA60561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450315; CAG29311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029140; AAH29140.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35756; A35756.
RefSeq NP_001093205.1; -.
NP_001093206.1; -.
NP_001816.2; -.
UniGene Hs.80691
3D structure databases
PDB
2GL6; X-ray; 2.30 A; A/B/C/D/E/F/G/H=27-416.[ExPASy / RCSB / EBI]
PDBsum 2GL6; -.
ModBase P17540.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
2D gel databases
HSC-2DPAGE P17540; -.
Organism-specific databases
H-InvDB HIX0004999; -.
HGNC HGNC:1996; CKMT2.
GenAtlas CKMT2.
MIM 123295; gene. [NCBI / EBI]
PharmGKB PA26534; -.
GeneCards P17540.
Gene expression databases
ArrayExpress P17540; -.
CleanEx HS_CKMT2; -.
GermOnline ENSG00000131730; 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).
GO:0006936; Biological process: muscle contraction (traceable author statement from ProtInc).
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 P17540.
Genome annotation databases
Ensembl ENSG00000131730; Homo sapiens. [Contig view]
GeneID 1160; -.
KEGG hsa:1160; -.
Phylogenomic databases
HOGENOM P17540; -.
HOVERGEN P17540; -.
Other
DrugBank DB00148; Creatine.
SOURCE CKMT2; Homo sapiens.
ProtoNet P17540.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; 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   419  380     Creatine kinase, sarcomeric mitochondrial. PRO_0000016594
NP_BIND   162   166  5     ATP. 
NP_BIND   354   359  6     ATP. 
REGION   40    64  25     Cardiolipin-binding (By similarity). 
ACT_SITE   317   317        By similarity. 
BINDING   225   225        ATP. 
BINDING   326   326        ATP. 
BINDING   369   369        ATP. 
CONFLICT   74    74        A -> S (in Ref. 1; AAA60561). 
HELIX   50    53  4      
HELIX   63    67  5      
HELIX   70    76  7      
HELIX   87    96  10      
HELIX   115   118  4      
HELIX   120   130  11      
TURN   131   133  3      
TURN   136   138  3      
STRAND   165   169  5      
TURN   177   179  3      
HELIX   182   197  16      
HELIX   201   203  3      
STRAND   205   210  6      
HELIX   215   223  9      
HELIX   234   237  4      
TURN   238   248  11      
STRAND   250   254  5      
STRAND   257   273  17      
HELIX   280   300  21      
TURN   309   311  3      
HELIX   318   320  3      
STRAND   326   332  7      
HELIX   334   338  5      
HELIX   342   348  7      
STRAND   351   355  5      
STRAND   367   373  7      
STRAND   376   378  3      
HELIX   380   388  9      
Sequence information
Length: 419 AA [This is the length of the unprocessed precursor] Molecular weight: 47504 Da [This is the MW of the unprocessed precursor] CRC64: 0CAF000074D99B6F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASIFSKLLT GRNASLLFAT MGTSVLTTGY LLNRQKVCAE VREQPRLFPP SADYPDLRKH 

        70         80         90        100        110        120 
NNCMAECLTP AIYAKLRNKV TPNGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA 

       130        140        150        160        170        180 
DLFDPVIKLR HNGYDPRVMK HTTDLDASKI TQGQFDEHYV LSSRVRTGRS IRGLSLPPAC 

       190        200        210        220        230        240 
TRAERREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG 

       250        260        270        280        290        300 
MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE 

       310        320        330        340        350        360 
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD 

       370        380        390        400        410 
TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK 

P17540 in FASTA format

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