Reviewed,
UniProtKB/Swiss-Prot P14056 (ARAF_RAT)
Last modified
June 16, 2009.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: A-Raf proto-oncogene serine/threonine-protein kinase EC=2.7.11.1 | ||||
| Gene names |
| ||||
| 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 | 604 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subunit structure | Interacts with TH1L/NELFD By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain. Contains 1 RBD (Ras-binding) domain. |
Ontologies
| Keywords | |
|---|---|
| Disease | Proto-oncogene |
| Domain | Phorbol-ester binding Zinc-finger |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | protein amino acid phosphorylation Inferred from direct assay. Source: RGD protein kinase cascadeTraceable author statement. Source: RGD |
| Cellular component | cytosol Inferred from direct assay. Source: RGD insoluble fractionInferred from direct assay. Source: RGD |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase kinase activityInferred from direct assay. Source: RGD diacylglycerol bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 604 | 604 | A-Raf proto-oncogene serine/threonine-protein kinase | PRO_0000085625 | |||||
Regions | |||||||||
| Domain | 19 – 91 | 73 | RBD | ||||||
| Domain | 308 – 568 | 261 | Protein kinase | ||||||
| Zinc finger | 98 – 144 | 47 | Phorbol-ester/DAG-type | ||||||
| Nucleotide binding | 314 – 322 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 427 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 99 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 112 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 115 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 125 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 128 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 133 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 136 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 144 | 1 | Zinc 1 By similarity | ||||||
| Binding site | 334 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 186 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 213 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 215 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 255 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 578 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 580 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "The complete primary structure of the rat A-raf cDNA coding region: conservation of the putative regulatory regions present in rat c-raf." Ishikawa F., Takaku F., Nagao M., Sugimura T. Oncogene Res. 1:243-253(1987) [PubMed: 3449797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| X06942 mRNA. Translation: CAA30023.1. | |
| IPI | IPI00563950. |
| PIR | S00726. |
| RefSeq | NP_071977.1. |
| UniGene | Rn.1714 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FAR based on UniProtKB P04049. |
| SMR | P14056. Positions 20-91, 96-146, 301-574. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P14056. |
Proteomic databases | |
| PRIDE | P14056. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000010838. Rattus norvegicus. [Contig view] |
| GeneID | 64363. |
Organism-specific databases | |
| RGD | 2148. Araf. |
Phylogenomic databases | |
| HOVERGEN | P14056. |
Enzyme and pathway databases | |
| BRENDA | 2.7.10.2. 248. 2.7.11.1. 248. |
Gene expression databases | |
| ArrayExpress | P14056. |
| GermOnline | ENSRNOG00000010838. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR002219. DAG_PE_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR003116. Raf-like_ras_bd. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view] |
| Pfam | PF00130. C1_1. 1 hit. PF00069. Pkinase. 1 hit. PF02196. RBD. 1 hit. [Graphical view] |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00109. C1. 1 hit. SM00455. RBD. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS50898. RBD. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 613074. |
Entry information
| Entry name | ARAF_RAT | ||||||||
| Accession | Primary (citable) accession number: P14056 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


