BRAF_HUMAN - dbPTM
BRAF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRAF_HUMAN
UniProt AC P15056
Protein Name Serine/threonine-protein kinase B-raf
Gene Name BRAF
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Nucleus. Cytoplasm. Cell membrane. Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes..
Protein Description Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway..
Protein Sequence MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH
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
2Acetylation------MAALSGGGG
------CCCCCCCCC		19.67-
76PhosphorylationGGEHNPPSIYLEAYE
CCCCCCCCCHHHHHH		25.73-
78PhosphorylationEHNPPSIYLEAYEEY
CCCCCCCHHHHHHHH		11.6527642862
82PhosphorylationPSIYLEAYEEYTSKL
CCCHHHHHHHHHHHH		10.4227642862
88UbiquitinationAYEEYTSKLDALQQR
HHHHHHHHHHHHHHH		42.4522053931
112UbiquitinationNGTDFSVSSSASMDT
CCCCCCCCCCCCCCC		19.8532142685
119PhosphorylationSSSASMDTVTSSSSS
CCCCCCCCCCCCCCC		19.6216858395
130UbiquitinationSSSSSLSVLPSSLSV
CCCCCCEECCCCEEE		12.6632142685
147PhosphorylationNPTDVARSNPKSPQK
CHHHHHHCCCCCCCC		47.9823927012
151PhosphorylationVARSNPKSPQKPIVR
HHHCCCCCCCCCEEE		33.5423927012
154AcetylationSNPKSPQKPIVRVFL
CCCCCCCCCEEEEEC		39.8425953088
164UbiquitinationVRVFLPNKQRTVVPA
EEEECCCCCCCEEEC		38.9432142685
167PhosphorylationFLPNKQRTVVPARCG
ECCCCCCCEEECCCC		24.3027174698
244PhosphorylationFVRKTFFTLAFCDFC
HHHHHHHHHHHHHHH		17.00-
253AcetylationAFCDFCRKLLFQGFR
HHHHHHHHHHHCCCC		51.207709589
253UbiquitinationAFCDFCRKLLFQGFR
HHHHHHHHHHHCCCC		51.2023000965
277PhosphorylationQRCSTEVPLMCVNYD
CCCCCCCCEEEECHH		14.2432142685
285PhosphorylationLMCVNYDQLDLLFVS
EEEECHHHHHEEEEH		26.9032142685
310PhosphorylationEEASLAETALTSGSS
HHHHHHHHHHHCCCC		22.7428464451
313PhosphorylationSLAETALTSGSSPSA
HHHHHHHHCCCCCCC		28.6932142685
314PhosphorylationLAETALTSGSSPSAP
HHHHHHHCCCCCCCC		37.2130576142
316PhosphorylationETALTSGSSPSAPAS
HHHHHCCCCCCCCCC		38.5530576142
317PhosphorylationTALTSGSSPSAPASD
HHHHCCCCCCCCCCC		26.8030576142
319PhosphorylationLTSGSSPSAPASDSI
HHCCCCCCCCCCCCC		49.1629496963
321PhosphorylationSGSSPSAPASDSIGP
CCCCCCCCCCCCCCC		36.3132142685
323PhosphorylationSSPSAPASDSIGPQI
CCCCCCCCCCCCCCC		30.7230576142
325PhosphorylationPSAPASDSIGPQILT
CCCCCCCCCCCCCCC		27.2728464451
331PhosphorylationDSIGPQILTSPSPSK
CCCCCCCCCCCCCCC		3.0632142685
332PhosphorylationSIGPQILTSPSPSKS
CCCCCCCCCCCCCCC		39.9726074081
333PhosphorylationIGPQILTSPSPSKSI
CCCCCCCCCCCCCCC		21.6718669648
335PhosphorylationPQILTSPSPSKSIPI
CCCCCCCCCCCCCCC		41.3928464451
337PhosphorylationILTSPSPSKSIPIPQ
CCCCCCCCCCCCCCC		43.2930576142
339PhosphorylationTSPSPSKSIPIPQPF
CCCCCCCCCCCCCCC		37.6226074081
349PhosphorylationIPQPFRPADEDHRNQ
CCCCCCCCCHHHHHC		28.6832142685
358PhosphorylationEDHRNQFGQRDRSSS
HHHHHCCCCCCCCCC		16.3232645325
359PhosphorylationDHRNQFGQRDRSSSA
HHHHCCCCCCCCCCC		45.4432142685
363PhosphorylationQFGQRDRSSSAPNVH
CCCCCCCCCCCCCEE		32.6929255136
364PhosphorylationFGQRDRSSSAPNVHI
CCCCCCCCCCCCEEE		31.2629255136
365PhosphorylationGQRDRSSSAPNVHIN
CCCCCCCCCCCEEEE		49.3329255136
367PhosphorylationRDRSSSAPNVHINTI
CCCCCCCCCEEEECC		45.3732142685
368PhosphorylationDRSSSAPNVHINTIE
CCCCCCCCEEEECCC		37.4032142685
373PhosphorylationAPNVHINTIEPVNID
CCCEEEECCCCCCHH		26.5623927012
376PhosphorylationVHINTIEPVNIDDLI
EEEECCCCCCHHHHH		22.1732142685
394PhosphorylationGFRGDGGSTTGLSAT
CCCCCCCCCCCCCCC		28.4629255136
395PhosphorylationFRGDGGSTTGLSATP
CCCCCCCCCCCCCCC		28.3229255136
396PhosphorylationRGDGGSTTGLSATPP
CCCCCCCCCCCCCCC		37.5129255136
399PhosphorylationGGSTTGLSATPPASL
CCCCCCCCCCCCCCC		31.2930266825
401PhosphorylationSTTGLSATPPASLPG
CCCCCCCCCCCCCCC		26.8229255136
404PhosphorylationGLSATPPASLPGSLT
CCCCCCCCCCCCCCC		25.5532142685
405PhosphorylationLSATPPASLPGSLTN
CCCCCCCCCCCCCCC		40.6530266825
409PhosphorylationPPASLPGSLTNVKAL
CCCCCCCCCCCHHHH		30.0423403867
410PhosphorylationPASLPGSLTNVKALQ
CCCCCCCCCCHHHHH		5.1132142685
411PhosphorylationASLPGSLTNVKALQK
CCCCCCCCCHHHHHC		39.4028176443
412PhosphorylationSLPGSLTNVKALQKS
CCCCCCCCHHHHHCC		38.2932645325
413PhosphorylationLPGSLTNVKALQKSP
CCCCCCCHHHHHCCC		3.0232142685
418AcetylationTNVKALQKSPGPQRE
CCHHHHHCCCCCCCC		60.5119608861
419PhosphorylationNVKALQKSPGPQRER
CHHHHHCCCCCCCCC		23.3323401153
424PhosphorylationQKSPGPQRERKSSSS
HCCCCCCCCCCCCCC		49.1532645325
425PhosphorylationKSPGPQRERKSSSSS
CCCCCCCCCCCCCCH		60.2532142685
428PhosphorylationGPQRERKSSSSSEDR
CCCCCCCCCCCHHHH		41.4926074081
429PhosphorylationPQRERKSSSSSEDRN
CCCCCCCCCCHHHHH		36.9618451171
430PhosphorylationQRERKSSSSSEDRNR
CCCCCCCCCHHHHHH		45.0026074081
431PhosphorylationRERKSSSSSEDRNRM
CCCCCCCCHHHHHHH		39.4326699800
432PhosphorylationERKSSSSSEDRNRMK
CCCCCCCHHHHHHHH		45.5226074081
440PhosphorylationEDRNRMKTLGRRDSS
HHHHHHHHCCCCCCC		25.7127273156
441PhosphorylationDRNRMKTLGRRDSSD
HHHHHHHCCCCCCCC		4.1332142685
446PhosphorylationKTLGRRDSSDDWEIP
HHCCCCCCCCCCCCC		33.5822322096
447PhosphorylationTLGRRDSSDDWEIPD
HCCCCCCCCCCCCCC		43.8322322096
449PhosphorylationGRRDSSDDWEIPDGQ
CCCCCCCCCCCCCCE		47.0232645325
450PhosphorylationRRDSSDDWEIPDGQI
CCCCCCCCCCCCCEE		15.4832142685
458PhosphorylationEIPDGQITVGQRIGS
CCCCCEEEEEEEEEC		15.6523927012
465PhosphorylationTVGQRIGSGSFGTVY
EEEEEEECCCCCEEE		28.9727273156
467PhosphorylationGQRIGSGSFGTVYKG
EEEEECCCCCEEECC		23.3830108239
470PhosphorylationIGSGSFGTVYKGKWH
EECCCCCEEECCEEE		20.7428857561
473UbiquitinationGSFGTVYKGKWHGDV
CCCCEEECCEEECCE		50.07-
475UbiquitinationFGTVYKGKWHGDVAV
CCEEECCEEECCEEE		31.68-
486PhosphorylationDVAVKMLNVTAPTPQ
CEEEEEEEECCCCHH		26.1232645325
487PhosphorylationVAVKMLNVTAPTPQQ
EEEEEEEECCCCHHH		4.2032142685
566PhosphorylationQTAQGMDYLHAKSII
HHHCCCCHHHHHHHH		7.47-
578UbiquitinationSIIHRDLKSNNIFLH
HHHCCCCCCCCEEEE		56.26PubMed
579PhosphorylationIIHRDLKSNNIFLHE
HHCCCCCCCCEEEEC		42.2616093354
599PhosphorylationIGDFGLATVKSRWSG
ECCCEEEEEHHCCCC		33.2415710605
601UbiquitinationDFGLATVKSRWSGSH
CCEEEEEHHCCCCCC		29.92-
602PhosphorylationFGLATVKSRWSGSHQ
CEEEEEHHCCCCCCC		34.3515710605
605PhosphorylationATVKSRWSGSHQFEQ
EEEHHCCCCCCCHHH		29.3427422710
607PhosphorylationVKSRWSGSHQFEQLS
EHHCCCCCCCHHHHC		14.4828450419
614PhosphorylationSHQFEQLSGSILWMA
CCCHHHHCCCEEEEC		30.1328450419
616PhosphorylationQFEQLSGSILWMAPE
CHHHHCCCEEEECHH		15.9028634298
633PhosphorylationRMQDKNPYSFQSDVY
CCCCCCCCCCCCHHH		31.3530576142
656PhosphorylationLMTGQLPYSNINNRD
HHHCCCCCCCCCCCC		23.9630576142
657PhosphorylationMTGQLPYSNINNRDQ
HHCCCCCCCCCCCCE		29.3330576142
662PhosphorylationPYSNINNRDQIIFMV
CCCCCCCCCEEEEEE		32.4932142685
671MethylationQIIFMVGRGYLSPDL
EEEEEECCCCCCCCH		21.1221917714
673PhosphorylationIFMVGRGYLSPDLSK
EEEECCCCCCCCHHH		11.5728796482
675PhosphorylationMVGRGYLSPDLSKVR
EECCCCCCCCHHHHH		14.1028985074
680UbiquitinationYLSPDLSKVRSNCPK
CCCCCHHHHHHCCHH		49.3024816145
687UbiquitinationKVRSNCPKAMKRLMA
HHHHCCHHHHHHHHH		64.41-
698PhosphorylationRLMAECLKKKRDERP
HHHHHHHHHCCCCCC		68.8332142685
698UbiquitinationRLMAECLKKKRDERP
HHHHHHHHHCCCCCC		68.8324816145
713PhosphorylationLFPQILASIELLARS
CHHHHHHHHHHHHHC		17.1032142685
716PhosphorylationQILASIELLARSLPK
HHHHHHHHHHHCCHH		4.2832142685
720PhosphorylationSIELLARSLPKIHRS
HHHHHHHCCHHHHHC		43.3426074081
720UbiquitinationSIELLARSLPKIHRS
HHHHHHHCCHHHHHC		43.3424816145
727PhosphorylationSLPKIHRSASEPSLN
CCHHHHHCCCCCCCC		23.2230266825
728PhosphorylationLPKIHRSASEPSLNR
CHHHHHCCCCCCCCC		20.1932142685
729PhosphorylationPKIHRSASEPSLNRA
HHHHHCCCCCCCCCC		51.8129255136
732PhosphorylationHRSASEPSLNRAGFQ
HHCCCCCCCCCCCCC		33.9430266825
738UbiquitinationPSLNRAGFQTEDFSL
CCCCCCCCCCCCCEE		8.7324816145
740PhosphorylationLNRAGFQTEDFSLYA
CCCCCCCCCCCEEEE		34.9526074081
744PhosphorylationGFQTEDFSLYACASP
CCCCCCCEEEEECCC		32.5627080861
746PhosphorylationQTEDFSLYACASPKT
CCCCCEEEEECCCCC		9.8422817900
750PhosphorylationFSLYACASPKTPIQA
CEEEEECCCCCCCCC		27.1525159151
753PhosphorylationYACASPKTPIQAGGY
EEECCCCCCCCCCCC		29.0718042262
760PhosphorylationTPIQAGGYGAFPVH-
CCCCCCCCCCCCCC-		12.3623312004
790Phosphorylation-------------------------------
-------------------------------		32142685
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
151SPhosphorylationKinaseERK-SUBFAMILY-GPS
151SPhosphorylationKinaseERK1P27361
PSP
364SPhosphorylationKinaseSGK-FAMILY-GPS
364SPhosphorylationKinaseAKT-FAMILY-GPS
365SPhosphorylationKinaseAKT1P31749
PSP
365SPhosphorylationKinaseSGK_GROUP-PhosphoELM
365SPhosphorylationKinasePKB_GROUP-PhosphoELM
365SPhosphorylationKinaseSGK-FAMILY-GPS
365SPhosphorylationKinaseAKT-FAMILY-GPS
365SPhosphorylationKinaseSGK1O00141
Uniprot
365SPhosphorylationKinaseAKT3Q9Y243
PSP
373TPhosphorylationKinaseBRAFP15056
PSP
401TPhosphorylationKinaseMAPK1P28482
GPS
401TPhosphorylationKinaseMAPK3P27361
GPS
401TPhosphorylationKinaseERK-SUBFAMILY-GPS
428SPhosphorylationKinaseAKT-FAMILY-GPS
429SPhosphorylationKinasePKB_GROUP-PhosphoELM
429SPhosphorylationKinasePKA_GROUP-PhosphoELM
429SPhosphorylationKinaseAKT-FAMILY-GPS
429SPhosphorylationKinaseAKT1P31749
PSP
429SPhosphorylationKinasePKA-FAMILY-GPS
429SPhosphorylationKinaseAKT3Q9Y243
PSP
446SPhosphorylationKinasePAK1Q13153
PSP
614SPhosphorylationKinaseBRAFP15056
PSP
729SPhosphorylationKinasePRKAA1Q13131
GPS
750SPhosphorylationKinaseERK-SUBFAMILY-GPS
753TPhosphorylationKinaseERK-SUBFAMILY-GPS
753TPhosphorylationKinaseERK2P28482
PSP
753TPhosphorylationKinaseMAPK3P27361
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseRNF149Q8NC42
PMID:22628551
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:31015455
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
365SPhosphorylation


578Kubiquitylation

23907581
671RMethylation

21917714
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 BRAF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKT1_HUMANAKT1physical
10869359
RPGP1_HUMANRAP1GAPphysical
11278445
RAF1_HUMANRAF1physical
11325826
1433B_HUMANYWHABphysical
10931830
RAP1A_HUMANRAP1Aphysical
10454553
PAK2_HUMANPAK2physical
20936779
TERF1_HUMANTERF1physical
20936779
GRDN_HUMANCCDC88Aphysical
20936779
RN149_HUMANRNF149physical
22628551
MP2K1_HUMANMAP2K1physical
20212043
RAF1_HUMANRAF1physical
18332145
1433T_HUMANYWHAQphysical
18332145
MP2K1_HUMANMAP2K1physical
18332145
RAF1_HUMANRAF1physical
23153539
KPCE_HUMANPRKCEphysical
16810323
KS6B2_HUMANRPS6KB2physical
16810323
MP2K1_HUMANMAP2K1physical
16810323
BRAF_HUMANBRAFphysical
17979178
1433E_HUMANYWHAEphysical
17979178
GRP78_HUMANHSPA5physical
17979178
MP2K2_HUMANMAP2K2physical
17979178
MP2K1_HUMANMAP2K1physical
17979178
1433Z_HUMANYWHAZphysical
17979178
1433G_HUMANYWHAGphysical
17979178
HSP7C_HUMANHSPA8physical
17979178
1433F_HUMANYWHAHphysical
17979178
GRP75_HUMANHSPA9physical
17979178
1433T_HUMANYWHAQphysical
17979178
ARAF_HUMANARAFphysical
17979178
CDC37_HUMANCDC37physical
17979178
HS90B_HUMANHSP90AB1physical
17979178
KPBB_HUMANPHKBphysical
17979178
LIMK1_HUMANLIMK1physical
17979178
IQGA1_HUMANIQGAP1physical
18567582
MK01_HUMANMAPK1physical
18567582
BAD_HUMANBADphysical
19667065
FBXW7_HUMANFBXW7physical
26898828
MK01_HUMANMAPK1genetic
26627737
FGFR2_HUMANFGFR2genetic
28319113
BRCA2_HUMANBRCA2genetic
28319113
VHL_HUMANVHLgenetic
28319113
FNTA_HUMANFNTAgenetic
28319113
HDAC2_HUMANHDAC2genetic
28319113
PK3CA_HUMANPIK3CAgenetic
28319113
EGFR_HUMANEGFRgenetic
28319113
PTEN_HUMANPTENgenetic
28319113
MP2K1_HUMANMAP2K1physical
28514442
RB3GP_HUMANRAB3GAP1physical
28514442
MP2K2_HUMANMAP2K2physical
28514442
RASK_HUMANKRASphysical
28514442
1433Z_HUMANYWHAZphysical
28514442
RAF1_HUMANRAF1physical
28514442
DELE_HUMANKIAA0141physical
28514442
ARAF_HUMANARAFphysical
28514442
RASH_HUMANHRASphysical
28514442
1433G_HUMANYWHAGphysical
28514442
1433B_HUMANYWHABphysical
28514442
1433E_HUMANYWHAEphysical
28514442
1433T_HUMANYWHAQphysical
28514442
1433F_HUMANYWHAHphysical
28514442
ARMX3_HUMANARMCX3physical
28514442
RPTOR_HUMANRPTORphysical
28514442
MK01_HUMANMAPK1physical
26285778
MP2K1_HUMANMAP2K1physical
19371126
MP2K1_HUMANMAP2K1genetic
26627737
HSP74_HUMANHSPA4physical
27034005
DNJB6_HUMANDNAJB6physical
27034005
RASN_HUMANNRASphysical
27034005
RRP5_HUMANPDCD11physical
27034005
RASK_HUMANKRASphysical
27034005
PI51A_HUMANPIP5K1Aphysical
27034005
DJC15_HUMANDNAJC15physical
27034005
VANG1_HUMANVANGL1physical
27034005
DJC11_HUMANDNAJC11physical
27034005
FKBP5_HUMANFKBP5physical
27034005
HS74L_HUMANHSPA4Lphysical
27034005
ENPL_HUMANHSP90B1physical
27034005
IQGA1_HUMANIQGAP1physical
27034005
1433T_HUMANYWHAQphysical
27034005
1433B_HUMANYWHABphysical
27034005
1433E_HUMANYWHAEphysical
27034005
1433Z_HUMANYWHAZphysical
27034005
GNAI2_HUMANGNAI2physical
27034005
1433G_HUMANYWHAGphysical
27034005
CDC37_HUMANCDC37physical
27034005
HS90A_HUMANHSP90AA1physical
27034005
1433F_HUMANYWHAHphysical
27034005
DJC13_HUMANDNAJC13physical
27034005
MP2K2_HUMANMAP2K2physical
27034005
MP2K1_HUMANMAP2K1physical
27034005
GNAS3_HUMANGNASphysical
27034005
GNAS2_HUMANGNASphysical
27034005
ALEX_HUMANGNASphysical
27034005
GNAS1_HUMANGNASphysical
27034005
PP2AB_HUMANPPP2CBphysical
27034005
GRP78_HUMANHSPA5physical
27034005
DHI2_HUMANHSD11B2physical
27034005
DJB11_HUMANDNAJB11physical
27034005
PLD2_HUMANPLD2physical
27034005
RAP1B_HUMANRAP1Bphysical
27034005
WDR6_HUMANWDR6physical
27034005
CPNE3_HUMANCPNE3physical
27034005
MYOF_HUMANMYOFphysical
27034005
RASH_HUMANHRASphysical
27034005
COPA_HUMANCOPAphysical
27034005
UBCP1_HUMANUBLCP1physical
27034005
PP1A_HUMANPPP1CAphysical
27034005
RAD50_HUMANRAD50physical
27034005
PI42C_HUMANPIP4K2Cphysical
27034005
PHB_HUMANPHBphysical
27034005
VIME_HUMANVIMphysical
27034005
1433S_HUMANSFNphysical
27034005
PGAM1_HUMANPGAM1physical
27034005
DNJA1_HUMANDNAJA1physical
27034005
MP2K7_HUMANMAP2K7physical
27034005
SPY2_HUMANSPRY2physical
19690147
Drug and Disease Associations
Kegg Disease
H00032 Thyroid cancer
H00038 Malignant melanoma
H00523 Noonan syndrome and related disorders, including: Noonan syndrome (NS); Leopard syndrome (LS); Noona
OMIM Disease
0000269|PubMedNote=Defects in BRAF are found in a wide range of cancers. {ECO
114500
211980Lung cancer (LNCR)
605027Familial non-Hodgkin lymphoma (NHL)
115150Cardiofaciocutaneous syndrome 1 (CFC1)
613706Noonan syndrome 7 (NS7)
613707LEOPARD syndrome 3 (LPRD3)
Kegg Drug
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D08524 Sorafenib (USAN/INN)
D09996 Vemurafenib (USAN/INN); Zelboraf (TN)
D10064 Dabrafenib (USAN)
D10104 Dabrafenib mesylate (USAN); Tafinlar (TN)
DrugBank
DB08912Dabrafenib
DB08896Regorafenib
DB00398Sorafenib
DB08881Vemurafenib
Regulatory Network of BRAF_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Protein arginine methyltransferase 5 regulates ERK1/2 signaltransduction amplitude and cell fate through CRAF.";
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C.,Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R.,Canals F., Merlino G., Avila M.A., Recio J.A.;
Sci. Signal. 4:RA58-RA58(2011).
Cited for: INTERACTION WITH PRMT5, METHYLATION AT ARG-671, CHARACTERIZATION OFVARIANT GLU-600, AND MUTAGENESIS OF ARG-671.
Phosphorylation
ReferencePubMed
"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 SER-465 AND SER-614, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-729, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-446; SER-447AND SER-729, AND MASS SPECTROMETRY.
"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-729, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-365; THR-401;SER-419; SER-446; SER-729 AND SER-750, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-729, ANDMASS SPECTROMETRY.
"Serum- and glucocorticoid-inducible kinase SGK phosphorylates andnegatively regulates B-Raf.";
Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.;
J. Biol. Chem. 276:31620-31626(2001).
Cited for: PHOSPHORYLATION AT SER-365 BY SGK1.
"Diacylglycerol kinase eta augments C-Raf activity and B-Raf/C-Rafheterodimerization.";
Yasuda S., Kai M., Imai S., Takeishi K., Taketomi A., Toyota M.,Kanoh H., Sakane F.;
J. Biol. Chem. 284:29559-29570(2009).
Cited for: SUBUNIT, INTERACTION WITH DGKH, AND PHOSPHORYLATION AT THR-753 BYMAPK1.
"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-373, AND MASSSPECTROMETRY.
"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 THR-401, AND MASSSPECTROMETRY.
"95-kilodalton B-Raf serine/threonine kinase: identification of theprotein and its major autophosphorylation site.";
Stephens R.M., Sithanandam G., Copeland T.D., Kaplan D.R., Rapp U.R.,Morrison D.K.;
Mol. Cell. Biol. 12:3733-3742(1992).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ANDPHOSPHORYLATION AT THR-373.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory