Reviewed,
UniProtKB/Swiss-Prot P00567 (KCRB_RABIT)
Last modified
May 5, 2009.
Version 64.
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 B-type EC=2.7.3.2 Alternative name(s): Creatine kinase B chain B-CK | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 381 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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 |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | brain development Inferred from sequence or structural similarity. Source: AgBase cellular chloride ion homeostasisInferred from sequence or structural similarity. Source: AgBase |
| Cellular component | mitochondrion Inferred from sequence or structural similarity. Source: AgBase |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activityInferred from electronic annotation. Source: EC protein bindingInferred from sequence or structural similarity. Source: AgBase |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 381 | 380 | Creatine kinase B-type | PRO_0000211969 | |||||
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 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 35 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 125 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 164 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 199 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences." Pickering L., Pang H., Biemann K., Munro H., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed: 3857581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| M11306 mRNA. Translation: AAA31201.1. | |
| PIR | KIRBCB. A00678. |
| RefSeq | NP_001075730.1. |
| UniGene | Ocu.3366 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QH4 based on UniProtKB P05122. |
| SMR | P00567. Positions 2-381. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSOCUG00000008818. Oryctolagus cuniculus. [Contig view] |
| GeneID | 100009085. |
Phylogenomic databases | |
| HOVERGEN | P00567. |
Enzyme and pathway databases | |
| BRENDA | 2.7.3.2. 255. |
Family and domain databases | |
| InterPro | IPR000749. ATP-guanido_PTrfase. 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... |
Entry information
| Entry name | KCRB_RABIT | ||||||||
| Accession | Primary (citable) accession number: P00567 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


