Reviewed,
UniProtKB/Swiss-Prot P05772 (KPCB_RABIT)
Last modified
October 13, 2009.
Version 105.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein kinase C beta type Short name=PKC-beta Short name=PKC-B EC=2.7.11.13 | ||||
| Gene names |
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| 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 | 671 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 | This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking By similarity. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Cofactor | Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity. |
| Subunit structure | Interacts with PDK1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosporylation By similarity. |
| Subcellular location | Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. |
| Post-translational modification | Phosphorylation on 'Thr-499' of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-640' and 'Ser-659', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on PKC activity By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Beta-I (identifier: P05772-1) 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 Beta-II (identifier: P05772-2) The sequence of this isoform differs from the canonical sequence as follows: 622-671: RDKRDTSNFD...YTNPEFVINV → CGRNAENFDR...SEFLKPEVKS |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 671 | 670 | Protein kinase C beta type | PRO_0000055686 | |||||
Regions | |||||||||
| Domain | 173 – 260 | 88 | C2 | ||||||
| Domain | 342 – 600 | 259 | Protein kinase | ||||||
| Domain | 601 – 671 | 71 | AGC-kinase C-terminal | ||||||
| Zinc finger | 36 – 86 | 51 | Phorbol-ester/DAG-type 1 | ||||||
| Zinc finger | 101 – 151 | 51 | Phorbol-ester/DAG-type 2 | ||||||
| Nucleotide binding | 348 – 356 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 466 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 186 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 187 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 187 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 193 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 246 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 246 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 247 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 248 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 251 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 252 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 254 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 254 | 1 | Calcium 3 By similarity | ||||||
| Binding site | 371 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 16 | 1 | Phosphoserine; by autocatalysis Potential | ||||||
| Modified residue | 17 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 195 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 314 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 324 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 500 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 504 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 635 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 642 | 1 | Phosphothreonine Potential | ||||||
| Modified residue | 661 | 1 | Phosphoserine; by autocatalysis By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 622 – 671 | 50 | RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. | VSP_004740 | |||||
Sequences
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References
| [1] | "Tissue-specific expression of three distinct types of rabbit protein kinase C." Ohno S., Kawasaki H., Imajoh S., Suzuki K., Inagaki M., Yokokura H., Sakoh T., Hidaka H. Nature 325:161-166(1987) [PubMed: 3808073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II). Tissue: Brain. |
Cross-references
Sequence databases | |
|---|---|
| X04795 mRNA. Translation: CAA28482.1. X04793 mRNA. Translation: CAA28480.1. | |
| PIR | KIRBC2. A26037. KIRBC1. B26037. |
| RefSeq | NP_001095193.1. NP_001095195.1. |
| UniGene | Ocu.3267 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A25 based on UniProtKB P04410. |
| SMR | P05772. Positions 94-158, 95-159, 156-287, 157-288, 339-668. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100037719. |
Organism-specific databases | |
| CTD | 100037719. |
Phylogenomic databases | |
| HOVERGEN | P05772. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.13. 255. |
Family and domain databases | |
| InterPro | IPR000961. AGC-kinase_C. IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR020477. C2_region. IPR020454. DAG/PE_bd. IPR015745. PKC. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR014375. Protein_kinase_C_a/b/g. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view] |
| PANTHER | PTHR22985:SF86. PKC. 1 hit. |
| Pfam | PF00130. C1_1. 2 hits. PF00168. C2. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF000550. PKC_alpha. 1 hit. |
| PRINTS | PR00360. C2DOMAIN. PR00008. DAGPEDOMAIN. |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS51285. AGC_KINASE_CTER. 1 hit. PS50004. C2. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 2 hits. PS50081. ZF_DAG_PE_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPCB_RABIT | ||||||||
| Accession | Primary (citable) accession number: P05772 Secondary accession number(s): P05773 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


