CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
423GMDYLHAKNIIHRDLubiquitination[1]
454DFGLATVKTRWSGAQubiquitination[1]
551RLLSDCLKFQREERPubiquitination[1]
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. 
Interpro
 IPR020454; DAG/PE-bd.
 IPR011009; Kinase-like_dom.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR003116; Raf-like_ras-bd.
 IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00130; C1_1
 PF07714; Pkinase_Tyr
 PF02196; RBD 
SMART
 SM00109; C1
 SM00455; RBD 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS50898; RBD
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00008; DAGPEDOMAIN.