ARAF_HUMAN - dbPTM
ARAF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARAF_HUMAN
UniProt AC P10398
Protein Name Serine/threonine-protein kinase A-Raf
Gene Name ARAF
Organism Homo sapiens (Human).
Sequence Length 606
Subcellular Localization
Protein Description Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade.; Isoform 2: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation..
Protein Sequence MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
15PhosphorylationPANGAEPSRAVGTVK
CCCCCCCCCCEEEEE		25.11-
20PhosphorylationEPSRAVGTVKVYLPN
CCCCCEEEEEEECCC		15.56-
24PhosphorylationAVGTVKVYLPNKQRT
CEEEEEEECCCCCCE		15.66-
28UbiquitinationVKVYLPNKQRTVVTV
EEEECCCCCCEEEEE		38.94-
40PhosphorylationVTVRDGMSVYDSLDK
EEEECCCCHHHCHHH		24.0528857561
42PhosphorylationVRDGMSVYDSLDKAL
EECCCCHHHCHHHHH		7.7828796482
44PhosphorylationDGMSVYDSLDKALKV
CCCCHHHCHHHHHHH		22.3028796482
155PhosphorylationSTNRQQFYHSVQDLS
CCCHHHHHHHHHCCC		6.7221945579
157PhosphorylationNRQQFYHSVQDLSGG
CHHHHHHHHHCCCCC		15.3023401153
162PhosphorylationYHSVQDLSGGSRQHE
HHHHHCCCCCCCCCC		49.7721945579
165PhosphorylationVQDLSGGSRQHEAPS
HHCCCCCCCCCCCCC		32.0921945579
172PhosphorylationSRQHEAPSNRPLNEL
CCCCCCCCCCCHHHH		53.1423401153
181PhosphorylationRPLNELLTPQGPSPR
CCHHHHCCCCCCCCC		26.6230266825
186PhosphorylationLLTPQGPSPRTQHCD
HCCCCCCCCCCCCCC		33.5625159151
189PhosphorylationPQGPSPRTQHCDPEH
CCCCCCCCCCCCHHH		26.5026074081
212PhosphorylationAPLQRIRSTSTPNVH
CCHHHHHCCCCCCEE		25.0823401153
213PhosphorylationPLQRIRSTSTPNVHM
CHHHHHCCCCCCEEE		27.1130278072
214PhosphorylationLQRIRSTSTPNVHMV
HHHHHCCCCCCEEEE		43.0130278072
215PhosphorylationQRIRSTSTPNVHMVS
HHHHCCCCCCEEEEE		20.9730278072
222PhosphorylationTPNVHMVSTTAPMDS
CCCEEEEEECCCCCC		16.6823401153
223PhosphorylationPNVHMVSTTAPMDSN
CCEEEEEECCCCCCC		18.6330278072
224PhosphorylationNVHMVSTTAPMDSNL
CEEEEEECCCCCCCC		22.6630278072
229PhosphorylationSTTAPMDSNLIQLTG
EECCCCCCCCEEHHC		27.5523927012
235PhosphorylationDSNLIQLTGQSFSTD
CCCCEEHHCCCEECC		19.4623663014
250PhosphorylationAAGSRGGSDGTPRGS
CCCCCCCCCCCCCCC		35.3722167270
253PhosphorylationSRGGSDGTPRGSPSP
CCCCCCCCCCCCCCC		18.1422167270
257PhosphorylationSDGTPRGSPSPASVS
CCCCCCCCCCCCCCC		24.3929255136
259PhosphorylationGTPRGSPSPASVSSG
CCCCCCCCCCCCCCC		34.4930266825
262PhosphorylationRGSPSPASVSSGRKS
CCCCCCCCCCCCCCC		26.3930266825
264PhosphorylationSPSPASVSSGRKSPH
CCCCCCCCCCCCCCC		25.2823401153
265PhosphorylationPSPASVSSGRKSPHS
CCCCCCCCCCCCCCC		40.2223927012
269PhosphorylationSVSSGRKSPHSKSPA
CCCCCCCCCCCCCHH		26.8726055452
272PhosphorylationSGRKSPHSKSPAEQR
CCCCCCCCCCHHHHH		37.9126055452
274PhosphorylationRKSPHSKSPAEQRER
CCCCCCCCHHHHHHH		32.1526055452
282UbiquitinationPAEQRERKSLADDKK
HHHHHHHHHHHHHHH		45.10-
283PhosphorylationAEQRERKSLADDKKK
HHHHHHHHHHHHHHH		34.7021815630
292UbiquitinationADDKKKVKNLGYRDS
HHHHHHHHHCCCCCC		56.16-
296PhosphorylationKKVKNLGYRDSGYYW
HHHHHCCCCCCCCEE		17.8922322096
299PhosphorylationKNLGYRDSGYYWEVP
HHCCCCCCCCEEECC		21.5021945579
301PhosphorylationLGYRDSGYYWEVPPS
CCCCCCCCEEECCHH		14.9021945579
302PhosphorylationGYRDSGYYWEVPPSE
CCCCCCCEEECCHHH		9.9121945579
308PhosphorylationYYWEVPPSEVQLLKR
CEEECCHHHHHHHHH		44.3123090842
314UbiquitinationPSEVQLLKRIGTGSF
HHHHHHHHHHCCCCC		51.03-
318PhosphorylationQLLKRIGTGSFGTVF
HHHHHHCCCCCCCEE		27.5520873877
320PhosphorylationLKRIGTGSFGTVFRG
HHHHCCCCCCCEECC		21.9729978859
323PhosphorylationIGTGSFGTVFRGRWH
HCCCCCCCEECCEEC		17.9220873877
339UbiquitinationDVAVKVLKVSQPTAE
EEEEEEEEECCCCHH		42.71-
341PhosphorylationAVKVLKVSQPTAEQA
EEEEEEECCCCHHHH		28.9324043423
344PhosphorylationVLKVSQPTAEQAQAF
EEEECCCCHHHHHHH		34.8824043423
352UbiquitinationAEQAQAFKNEMQVLR
HHHHHHHHHHHHHHH		55.82-
413PhosphorylationLIDVARQTAQGMDYL
HHHHHHHHHCCCHHH		18.52-
419PhosphorylationQTAQGMDYLHAKNII
HHHCCCHHHHHHCCC		7.47-
423UbiquitinationGMDYLHAKNIIHRDL
CCHHHHHHCCCCCCC		37.62-
431UbiquitinationNIIHRDLKSNNIFLH
CCCCCCCCCCCEEEE		56.26-
432PhosphorylationIIHRDLKSNNIFLHE
CCCCCCCCCCEEEEC		42.2616093354
442PhosphorylationIFLHEGLTVKIGDFG
EEEECCEEEEECCCE		30.5216093354
452PhosphorylationIGDFGLATVKTRWSG
ECCCEEEEEEECCCC		27.8128857561
454UbiquitinationDFGLATVKTRWSGAQ
CCEEEEEEECCCCCC		28.19-
455PhosphorylationFGLATVKTRWSGAQP
CEEEEEEECCCCCCC		32.7928450419
458PhosphorylationATVKTRWSGAQPLEQ
EEEEECCCCCCCCCC		22.4428450419
526PhosphorylationIFMVGRGYLSPDLSK
EEEECCCCCCCCHHH		11.5728796482
528PhosphorylationMVGRGYLSPDLSKIS
EECCCCCCCCHHHHH		14.10-
532PhosphorylationGYLSPDLSKISSNCP
CCCCCCHHHHHCCCH		35.01-
535PhosphorylationSPDLSKISSNCPKAM
CCCHHHHHCCCHHHH		21.1620873877
536PhosphorylationPDLSKISSNCPKAMR
CCHHHHHCCCHHHHH		46.0220873877
540UbiquitinationKISSNCPKAMRRLLS
HHHCCCHHHHHHHHH		57.95-
547PhosphorylationKAMRRLLSDCLKFQR
HHHHHHHHHHHHHHH		30.7628857561
551UbiquitinationRLLSDCLKFQREERP
HHHHHHHHHHHHHCC		45.87-
573PhosphorylationTIELLQRSLPKIERS
HHHHHHHHCHHHHHC		35.74-
576UbiquitinationLLQRSLPKIERSASE
HHHHHCHHHHHCCCC		63.59-
580PhosphorylationSLPKIERSASEPSLH
HCHHHHHCCCCCCCC		24.2926846344
582PhosphorylationPKIERSASEPSLHRT
HHHHHCCCCCCCCCC		51.8122167270
585PhosphorylationERSASEPSLHRTQAD
HHCCCCCCCCCCCHH		32.5330266825
589PhosphorylationSEPSLHRTQADELPA
CCCCCCCCCHHHHHH		19.8429496963
600PhosphorylationELPACLLSAARLVP-
HHHHHHHHHHHCCC-		13.6129396449
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
301YPhosphorylationKinaseSRCP12931
PSP
301YPhosphorylationKinaseSRC64-PhosphoELM
302YPhosphorylationKinaseSRCP12931
PSP
302YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARAF_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ARAF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASSY_HUMANASS1physical
12620389
CSN3_HUMANCOPS3physical
12620389
KLH12_HUMANKLHL12physical
16189514
NELFD_HUMANNELFCDphysical
12620389
PRP6_HUMANPRPF6physical
12620389
FBLN3_HUMANEFEMP1physical
12620389
TIM44_HUMANTIMM44physical
12620389
TOPK_HUMANPBKphysical
12620389
RRAS_HUMANRRASphysical
12620389
PGTB2_HUMANRABGGTBphysical
12620389
NELFD_HUMANNELFCDphysical
11952167
P85A_HUMANPIK3R1physical
11812000
RRAS_HUMANRRASphysical
10848612
TIM44_HUMANTIMM44physical
10848612
PRP6_HUMANPRPF6physical
10848612
MP2K2_HUMANMAP2K2physical
11909642
1433E_HUMANYWHAEphysical
20936779
1433Z_HUMANYWHAZphysical
20936779
CHD6_HUMANCHD6physical
20936779
MY18A_HUMANMYO18Aphysical
20936779
HS90A_HUMANHSP90AA1physical
22939624
BAD_HUMANBADphysical
19667065
DIDO1_HUMANDIDO1physical
21988832
NELFD_HUMANNELFCDphysical
21988832
E2F6_HUMANE2F6physical
21988832
MP2K2_HUMANMAP2K2physical
21988832
TESK1_HUMANTESK1physical
21988832
WNK1_HUMANWNK1physical
21988832
CPSM_HUMANCPS1physical
12620389
RRAS2_HUMANRRAS2physical
12620389
MP2K1_HUMANMAP2K1physical
24114843
GNA12_HUMANGNA12physical
24114843
RASK_HUMANKRASphysical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
ACTA_HUMANACTA2physical
25852190
AIFM1_HUMANAIFM1physical
25852190
ATPB_HUMANATP5Bphysical
25852190
BAG2_HUMANBAG2physical
25852190
CALU_HUMANCALUphysical
25852190
YBOX3_HUMANYBX3physical
25852190
CTNA1_HUMANCTNNA1physical
25852190
DDX5_HUMANDDX5physical
25852190
DNJA1_HUMANDNAJA1physical
25852190
DNJA2_HUMANDNAJA2physical
25852190
DPM1_HUMANDPM1physical
25852190
EF2_HUMANEEF2physical
25852190
EMD_HUMANEMDphysical
25852190
FKBP5_HUMANFKBP5physical
25852190
TECR_HUMANTECRphysical
25852190
ENPL_HUMANHSP90B1physical
25852190
HSPB1_HUMANHSPB1physical
25852190
KBP_HUMANKIAA1279physical
25852190
RASK_HUMANKRASphysical
25852190
LRC59_HUMANLRRC59physical
25852190
MP2K2_HUMANMAP2K2physical
25852190
PDIA1_HUMANP4HBphysical
25852190
PPP6_HUMANPPP6Cphysical
25852190
RCN1_HUMANRCN1physical
25852190
RCN2_HUMANRCN2physical
25852190
RL37_HUMANRPL37physical
25852190
RL39_HUMANRPL39physical
25852190
CAB45_HUMANSDF4physical
25852190
1433S_HUMANSFNphysical
25852190
TXTP_HUMANSLC25A1physical
25852190
CMC2_HUMANSLC25A13physical
25852190
GHC1_HUMANSLC25A22physical
25852190
CHIP_HUMANSTUB1physical
25852190
TCPA_HUMANTCP1physical
25852190
TIM50_HUMANTIMM50physical
25852190
TIF1B_HUMANTRIM28physical
25852190
TBA4A_HUMANTUBA4Aphysical
25852190
TBB6_HUMANTUBB6physical
25852190
USMG5_HUMANUSMG5physical
25852190
1433B_HUMANYWHABphysical
25852190
1433E_HUMANYWHAEphysical
25852190
1433G_HUMANYWHAGphysical
25852190
1433F_HUMANYWHAHphysical
25852190
1433T_HUMANYWHAQphysical
25852190
1433Z_HUMANYWHAZphysical
25852190
BRAF_HUMANBRAFphysical
25241761
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171Adenosine triphosphate
Regulatory Network of ARAF_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-257; SER-580AND SER-582, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213 AND THR-215, ANDMASS SPECTROMETRY.

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