Reviewed,
UniProtKB/Swiss-Prot P05128 (KPCG_BOVIN)
Last modified
October 13, 2009.
Version 97.
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 gamma type Short name=PKC-gamma EC=2.7.11.13 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 682 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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 CDCP1 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
| Keywords | |
|---|---|
| Domain | Phorbol-ester binding Repeat Zinc-finger |
| Ligand | ATP-binding Calcium Metal-binding Nucleotide-binding Zinc |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylationInferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW diacylglycerol bindingInferred from electronic annotation. Source: UniProtKB-KW protein kinase C activityInferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 682 | ›682 | Protein kinase C gamma type | PRO_0000055688 | |||||
Regions | |||||||||
| Domain | 155 – 245 | 91 | C2 | ||||||
| Domain | 336 – 599 | 264 | Protein kinase | ||||||
| Domain | 600 – 670 | 71 | AGC-kinase C-terminal | ||||||
| Zinc finger | 20 – 70 | 51 | Phorbol-ester/DAG-type 1 | ||||||
| Zinc finger | 85 – 135 | 51 | Phorbol-ester/DAG-type 2 | ||||||
| Nucleotide binding | 342 – 350 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 465 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 171 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 172 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 172 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 178 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 231 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 231 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 232 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 233 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 233 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 233 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 236 | 1 | Calcium 3 By similarity | ||||||
| Metal binding | 237 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||
| Metal binding | 239 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 239 | 1 | Calcium 3 By similarity | ||||||
| Binding site | 365 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 180 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 182 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 297 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 307 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 315 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 499 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 503 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 633 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 640 | 1 | Phosphothreonine; by autocatalysis Potential | ||||||
| Modified residue | 672 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways." Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A. Science 233:859-866(1986) [PubMed: 3755548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The molecular heterogeneity of protein kinase C and its implications for cellular regulation." Nishizuka Y. Nature 334:661-665(1988) [PubMed: 3045562] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M13976 mRNA. Translation: AAA30704.1. | |
| IPI | IPI00685679. |
| PIR | KIBOGC. C24664. |
| UniGene | Bt.12762 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TBN based on UniProtKB P05697. |
| SMR | P05128. Positions 78-143, 333-668. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P05128. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000018020; ENSBTAP00000018020; ENSBTAG00000013550; Bos taurus. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | P05128. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.13. 251. |
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 | KPCG_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P05128 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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