Tag | Content |
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CPLM ID | CPLM-003790 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase A-Raf |
Protein Synonyms/Alias | Proto-oncogene A-Raf; Proto-oncogene A-Raf-1; Proto-oncogene Pks |
Gene Name | ARAF |
Gene Synonyms/Alias | ARAF1; PKS; PKS2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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423 | GMDYLHAKNIIHRDL | ubiquitination | [1] | 454 | DFGLATVKTRWSGAQ | ubiquitination | [1] | 551 | RLLSDCLKFQREERP | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. |
Sequence Annotation | DOMAIN 19 91 RBD. DOMAIN 310 570 Protein kinase. ZN_FING 98 144 Phorbol-ester/DAG-type. NP_BIND 316 324 ATP (By similarity). ACT_SITE 429 429 Proton acceptor (By similarity). METAL 99 99 Zinc 1 (By similarity). METAL 112 112 Zinc 2 (By similarity). METAL 115 115 Zinc 2 (By similarity). METAL 125 125 Zinc 1 (By similarity). METAL 128 128 Zinc 1 (By similarity). METAL 133 133 Zinc 2 (By similarity). METAL 136 136 Zinc 2 (By similarity). METAL 144 144 Zinc 1 (By similarity). BINDING 336 336 ATP (By similarity). MOD_RES 186 186 Phosphoserine. MOD_RES 257 257 Phosphoserine. MOD_RES 318 318 Phosphothreonine. |
Keyword | 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 606 AA |
Protein Sequence | MEPPRGPPAN GAEPSRAVGT VKVYLPNKQR TVVTVRDGMS VYDSLDKALK VRGLNQDCCV 60 VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN FVRKTFFSLA FCDFCLKFLF 120 HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN RQQFYHSVQD LSGGSRQHEA PSNRPLNELL 180 TPQGPSPRTQ HCDPEHFPFP APANAPLQRI RSTSTPNVHM VSTTAPMDSN LIQLTGQSFS 240 TDAAGSRGGS DGTPRGSPSP ASVSSGRKSP HSKSPAEQRE RKSLADDKKK VKNLGYRDSG 300 YYWEVPPSEV QLLKRIGTGS FGTVFRGRWH GDVAVKVLKV SQPTAEQAQA FKNEMQVLRK 360 TRHVNILLFM GFMTRPGFAI ITQWCEGSSL YHHLHVADTR FDMVQLIDVA RQTAQGMDYL 420 HAKNIIHRDL KSNNIFLHEG LTVKIGDFGL ATVKTRWSGA QPLEQPSGSV LWMAAEVIRM 480 QDPNPYSFQS DVYAYGVVLY ELMTGSLPYS HIGCRDQIIF MVGRGYLSPD LSKISSNCPK 540 AMRRLLSDCL KFQREERPLF PQILATIELL QRSLPKIERS ASEPSLHRTQ ADELPACLLS 600 AARLVP 606 |
Gene Ontology | GO:0005829; C:cytosol; IEA:Compara. GO:0005739; C:mitochondrion; IEA:Compara. GO:0005524; F:ATP binding; NAS:UniProtKB. GO:0004709; F:MAP kinase kinase kinase activity; IEA:Compara. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB. |
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