Reviewed,
UniProtKB/Swiss-Prot P00564 (KCRM_RAT)
Last modified
November 4, 2008.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Creatine kinase M-type EC=2.7.3.2 Alternative name(s): Creatine kinase M chain M-CK | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 381 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 | Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. |
| Subcellular location | |
| Sequence similarities | Belongs to the ATP:guanido phosphotransferase family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 381 | 381 | Creatine kinase M-type | PRO_0000211979 | |||||
Regions | |||||||||
| Nucleotide binding | 128 – 132 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 320 – 325 | 6 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 191 | 1 | ATP By similarity | ||||||
| Binding site | 236 | 1 | ATP By similarity | ||||||
| Binding site | 292 | 1 | ATP By similarity | ||||||
| Binding site | 335 | 1 | ATP By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 16 | 1 | P → S in AAA40935. Ref.1 | ||||||
| Sequence conflict | 16 | 1 | P → S in AAA40936. Ref.3 | ||||||
| Sequence conflict | 87 | 1 | D → N in AAA40936. Ref.2 | ||||||
| Sequence conflict | 100 | 1 | Y → F in AAA40935. Ref.1 | ||||||
| Sequence conflict | 100 | 1 | Y → F in AAA40936. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and sequence analysis of cDNA clones coding for rat skeletal muscle creatine kinase." Benfield P.A., Zivin R.A., Miller L.S., Sowder R., Smythers G.W., Henderson L., Oroszlan S., Pearson M.L. J. Biol. Chem. 259:14979-14984(1984) [PubMed: 6209281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Fischer 344. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate. |
| [3] | "The nucleotide sequence of rat muscle creatine kinase cDNA and ckm transcription during myogenesis in an RNA polymerase II mutant of L6 myoblasts." Benfield P.A., Zivin R.A., Shearman C.W., Graf D., Henderson L., Oroszlan S., Pearson M.L. Exp. Biol. Med. 9:187-194(1984) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-381. |
| [4] | Lubec G., Afjehi-Sadat L. Submitted (DEC-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 87-96; 139-148; 157-170 AND 321-341, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| M10140 mRNA. Translation: AAA40935.1. BC062058 mRNA. Translation: AAH62058.1. M14864 mRNA. Translation: AAA40936.1. | |
| PIR | KIRTCM. A00674. |
| RefSeq | NP_036662.1. |
| UniGene | Rn.10756 |
3D structure databases | |
| HSSP | HSSP built from PDB template 2CRK based on UniProtKB P00563. |
| SMR | P00564. Positions 2-381. |
| ModBase | Search... |
2-D gel databases | |
| Rat-heart-2DPAGE | P00564. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000016837. Rattus norvegicus. [Contig view] |
| GeneID | 24265. |
| KEGG | rno:24265. |
Organism-specific databases | |
| RGD | 2358. Ckm. |
Phylogenomic databases | |
| HOVERGEN | P00564. |
Gene expression databases | |
| ArrayExpress | P00564. |
| GermOnline | ENSRNOG00000016837. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000749. ATP-gua_Ptrans. IPR014746. Gln_synth/guanido_kin_cat. [Graphical view] |
| Gene3D | G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit. G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit. |
| PANTHER | PTHR11547. ATP-gua_Ptrans. 1 hit. |
| Pfam | PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view] |
| PROSITE | PS00112. GUANIDO_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 602819. |
Entry information
| Entry name | KCRM_RAT | ||||||||
| Accession | Primary (citable) accession number: P00564 Secondary accession number(s): Q6P6R9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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