RAF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAF1_HUMAN
• UniProt AC: P04049
• Protein Name: RAF proto-oncogene serine/threonine-protein kinase
• Gene Name: RAF1
• Organism: Homo sapiens (Human).
• Sequence Length: 648
• Subcellular Localization: Cytoplasm. Cell membrane. Mitochondrion. Nucleus. Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphoryla
• Protein Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation..
• Protein Sequence: MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF

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
10	Phosphorylation	HIQGAWKTISNGFGF CCCCHHHHHHCCCCC	20.95	28555341
12	Phosphorylation	QGAWKTISNGFGFKD CCHHHHHHCCCCCCC	35.81	23312004
18	Methylation	ISNGFGFKDAVFDGS HHCCCCCCCEEECCC	45.19	115976085
25	Phosphorylation	KDAVFDGSSCISPTI CCEEECCCCCCCHHH	24.71	23401153
26	Phosphorylation	DAVFDGSSCISPTIV CEEECCCCCCCHHHH	22.47	23882029
29	Phosphorylation	FDGSSCISPTIVQQF ECCCCCCCHHHHHHH	21.96	25159151
31	Phosphorylation	GSSCISPTIVQQFGY CCCCCCHHHHHHHCC	27.30	23882029
38	Phosphorylation	TIVQQFGYQRRASDD HHHHHHCCCCCCCCC	10.51	-
43	Phosphorylation	FGYQRRASDDGKLTD HCCCCCCCCCCCCCC	34.13	23927012
49	Phosphorylation	ASDDGKLTDPSKTSN CCCCCCCCCCCCCCC	49.72	23927012
52	Phosphorylation	DGKLTDPSKTSNTIR CCCCCCCCCCCCEEE	51.91	23403867
53	Ubiquitination	GKLTDPSKTSNTIRV CCCCCCCCCCCEEEE	62.45	-
54	Phosphorylation	KLTDPSKTSNTIRVF CCCCCCCCCCEEEEE	31.39	29759185
55	Phosphorylation	LTDPSKTSNTIRVFL CCCCCCCCCEEEEEC	35.39	29759185
57	Phosphorylation	DPSKTSNTIRVFLPN CCCCCCCEEEEECCC	15.21	29759185
65	Ubiquitination	IRVFLPNKQRTVVNV EEEECCCCCCEEEEC	38.94	-
144	Acetylation	TTHNFARKTFLKLAF CCCHHHHHHHHHHHH	39.95	25953088
148	Acetylation	FARKTFLKLAFCDIC HHHHHHHHHHHHHHH	33.31	25953088
182	Phosphorylation	HCSTKVPTMCVDWSN CCCCCCCEEEECHHH	26.62	26552605
188	Phosphorylation	PTMCVDWSNIRQLLL CEEEECHHHHCHHHC	20.23	26552605
199	Phosphorylation	QLLLFPNSTIGDSGV HHHCCCCCCCCCCCC	22.95	26552605
200	Phosphorylation	LLLFPNSTIGDSGVP HHCCCCCCCCCCCCC	35.30	26552605
204	Phosphorylation	PNSTIGDSGVPALPS CCCCCCCCCCCCCCH	36.16	26552605
211	Phosphorylation	SGVPALPSLTMRRMR CCCCCCCHHHHHHHH	37.00	26552605
213	Phosphorylation	VPALPSLTMRRMRES CCCCCHHHHHHHHHH	16.99	27050516
220	Phosphorylation	TMRRMRESVSRMPVS HHHHHHHHHHCCCCC	18.28	30576142
222	Phosphorylation	RRMRESVSRMPVSSQ HHHHHHHHCCCCCCC	31.94	28102081
223	Methylation	RMRESVSRMPVSSQH HHHHHHHCCCCCCCC	31.13	115490173
227	O-linked_Glycosylation	SVSRMPVSSQHRYST HHHCCCCCCCCCCCC	20.57	31521821
227	Phosphorylation	SVSRMPVSSQHRYST HHHCCCCCCCCCCCC	20.57	23401153
228	Phosphorylation	VSRMPVSSQHRYSTP HHCCCCCCCCCCCCC	30.18	23927012
231	Methylation	MPVSSQHRYSTPHAF CCCCCCCCCCCCCEE	21.33	115490183
232	Phosphorylation	PVSSQHRYSTPHAFT CCCCCCCCCCCCEEE	18.12	23927012
233	Phosphorylation	VSSQHRYSTPHAFTF CCCCCCCCCCCEEEE	35.10	11997508
234	Phosphorylation	SSQHRYSTPHAFTFN CCCCCCCCCCEEEEE	15.34	23927012
239	Phosphorylation	YSTPHAFTFNTSSPS CCCCCEEEEECCCCC	19.43	23927012
242	Phosphorylation	PHAFTFNTSSPSSEG CCEEEEECCCCCCCC	26.79	23927012
243	Phosphorylation	HAFTFNTSSPSSEGS CEEEEECCCCCCCCC	41.16	23927012
244	Phosphorylation	AFTFNTSSPSSEGSL EEEEECCCCCCCCCC	27.11	25159151
246	Phosphorylation	TFNTSSPSSEGSLSQ EEECCCCCCCCCCCH	42.86	22199227
247	Phosphorylation	FNTSSPSSEGSLSQR EECCCCCCCCCCCHH	49.73	22199227
250	Phosphorylation	SSPSSEGSLSQRQRS CCCCCCCCCCHHHHC	22.31	22199227
252	Phosphorylation	PSSEGSLSQRQRSTS CCCCCCCCHHHHCCC	25.64	17525332
257	Phosphorylation	SLSQRQRSTSTPNVH CCCHHHHCCCCCCEE	20.55	29255136
258	Phosphorylation	LSQRQRSTSTPNVHM CCHHHHCCCCCCEEE	38.52	29255136
259	Phosphorylation	SQRQRSTSTPNVHMV CHHHHCCCCCCEEEE	43.01	29255136
260	Phosphorylation	QRQRSTSTPNVHMVS HHHHCCCCCCEEEEE	20.97	29255136
267	Phosphorylation	TPNVHMVSTTLPVDS CCCEEEEECEECCCC	14.22	30278072
268	Phosphorylation	PNVHMVSTTLPVDSR CCEEEEECEECCCCH	22.42	30278072
269	Phosphorylation	NVHMVSTTLPVDSRM CEEEEECEECCCCHH	22.89	30278072
274	Phosphorylation	STTLPVDSRMIEDAI ECEECCCCHHHHHHH	24.79	23927012
283	Phosphorylation	MIEDAIRSHSESASP HHHHHHHHCCCCCCH	25.83	23401153
285	Phosphorylation	EDAIRSHSESASPSA HHHHHHCCCCCCHHH	34.20	23927012
287	Phosphorylation	AIRSHSESASPSALS HHHHCCCCCCHHHHC	36.74	23927012
289	Phosphorylation	RSHSESASPSALSSS HHCCCCCCHHHHCCC	28.77	25159151
291	Phosphorylation	HSESASPSALSSSPN CCCCCCHHHHCCCCC	39.07	23927012
294	Phosphorylation	SASPSALSSSPNNLS CCCHHHHCCCCCCCC	28.61	23927012
295	Phosphorylation	ASPSALSSSPNNLSP CCHHHHCCCCCCCCC	51.14	23401153
296	Phosphorylation	SPSALSSSPNNLSPT CHHHHCCCCCCCCCC	28.42	25159151
301	Phosphorylation	SSSPNNLSPTGWSQP CCCCCCCCCCCCCCC	23.65	23927012
303	Phosphorylation	SPNNLSPTGWSQPKT CCCCCCCCCCCCCCC	48.16	23927012
306	Phosphorylation	NLSPTGWSQPKTPVP CCCCCCCCCCCCCCC	37.64	23927012
310	Phosphorylation	TGWSQPKTPVPAQRE CCCCCCCCCCCCCCC	35.88	30576142
322	Phosphorylation	QRERAPVSGTQEKNK CCCCCCCCCCCCCCC	34.76	29396449
324	Phosphorylation	ERAPVSGTQEKNKIR CCCCCCCCCCCCCCC	26.50	29496963
338	Phosphorylation	RPRGQRDSSYYWEIE CCCCCCCCCEEEEEE	23.56	22322096
339	Phosphorylation	PRGQRDSSYYWEIEA CCCCCCCCEEEEEEE	26.91	22322096
340	Dephosphorylation	RGQRDSSYYWEIEAS CCCCCCCEEEEEEEE	19.29	10373531
340	Phosphorylation	RGQRDSSYYWEIEAS CCCCCCCEEEEEEEE	19.29	14688280
341	Phosphorylation	GQRDSSYYWEIEASE CCCCCCEEEEEEEEE	9.86	22322096
352	Phosphorylation	EASEVMLSTRIGSGS EEEEEEEEEEECCCC	9.50	24719451
353	Phosphorylation	ASEVMLSTRIGSGSF EEEEEEEEEECCCCC	23.50	-
357	Phosphorylation	MLSTRIGSGSFGTVY EEEEEECCCCCCCEE	28.97	27273156
359	Phosphorylation	STRIGSGSFGTVYKG EEEECCCCCCCEECC	23.38	30108239
362	Phosphorylation	IGSGSFGTVYKGKWH ECCCCCCCEECCEEE	20.74	28857561
365	Ubiquitination	GSFGTVYKGKWHGDV CCCCCEECCEEECCE	50.07	-
367	Ubiquitination	FGTVYKGKWHGDVAV CCCEECCEEECCEEE	31.68	-
378	Ubiquitination	DVAVKILKVVDPTPE CEEEEEEEECCCCHH	43.62	-
452	Phosphorylation	LIDIARQTAQGMDYL HHHHHHHHHCCCHHH	18.52	-
458	Phosphorylation	QTAQGMDYLHAKNII HHHCCCHHHHHHHCC	7.47	-
462	Ubiquitination	GMDYLHAKNIIHRDM CCHHHHHHHCCCCCC	37.62	-
470	Ubiquitination	NIIHRDMKSNNIFLH HCCCCCCCCCCEEEE	55.08	-
471	Phosphorylation	IIHRDMKSNNIFLHE CCCCCCCCCCEEEEC	28.59	18775988
481	Phosphorylation	IFLHEGLTVKIGDFG EEEECCEEEEECCEE	30.52	16093354
490 (in isoform 2)	Ubiquitination	-	15.66	-
491	Phosphorylation	IGDFGLATVKSRWSG ECCEEEEEECCCCCC	33.24	28857561
493	Ubiquitination	DFGLATVKSRWSGSQ CEEEEEECCCCCCCC	29.92	-
494	Phosphorylation	FGLATVKSRWSGSQQ EEEEEECCCCCCCCC	34.35	22617229
497	Phosphorylation	ATVKSRWSGSQQVEQ EEECCCCCCCCCEEC	27.70	8288587
499	Phosphorylation	VKSRWSGSQQVEQPT ECCCCCCCCCEECCC	16.36	21082442
506	Phosphorylation	SQQVEQPTGSVLWMA CCCEECCCCCEEEEC	41.61	27732954
508	Phosphorylation	QVEQPTGSVLWMAPE CEECCCCCEEEECCE	19.26	23090842
563	Symmetric dimethylarginine	QIIFMVGRGYASPDL EEEEEECCCCCCCCH	24.44	-
563	Methylation	QIIFMVGRGYASPDL EEEEEECCCCCCCCH	24.44	21917714
574	Phosphorylation	SPDLSKLYKNCPKAM CCCHHHHHHHCHHHH	12.14	29496907
575	Ubiquitination	PDLSKLYKNCPKAMK CCHHHHHHHCHHHHH	63.61	-
604	Phosphorylation	PLFPQILSSIELLQH CCHHHHHHHHHHHHC	30.79	28634298
605	Phosphorylation	LFPQILSSIELLQHS CHHHHHHHHHHHHCC	19.35	28634298
611 (in isoform 2)	Ubiquitination	-	31.13	-
612	Phosphorylation	SIELLQHSLPKINRS HHHHHHCCCCCCCCC	33.15	25159151
619	Phosphorylation	SLPKINRSASEPSLH CCCCCCCCCCCCCHH	31.49	8288587
621	Phosphorylation	PKINRSASEPSLHRA CCCCCCCCCCCHHHH	51.81	22167270
624	Phosphorylation	NRSASEPSLHRAAHT CCCCCCCCHHHHHCC	32.53	30266825
631	Phosphorylation	SLHRAAHTEDINACT CHHHHHCCCCCCCCC	30.54	23927012
638	Phosphorylation	TEDINACTLTTSPRL CCCCCCCCCCCCCCC	25.40	23927012
640	Phosphorylation	DINACTLTTSPRLPV CCCCCCCCCCCCCCC	13.69	23401153
641	Phosphorylation	INACTLTTSPRLPVF CCCCCCCCCCCCCCC	39.59	30266825
642	Phosphorylation	NACTLTTSPRLPVF- CCCCCCCCCCCCCC-	11.64	29255136

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
29	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
43	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
43	S	Phosphorylation	Kinase	PKACA	P00517	PSP
43	S	Phosphorylation	Kinase	PKACA	P17612	PSP
43	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
43	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
43	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
43	S	Phosphorylation	Kinase	PKA	-	Uniprot
43	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
233	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
259	S	Phosphorylation	Kinase	RAF1	P04049	PSP
259	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
259	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
259	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
259	S	Phosphorylation	Kinase	LATS1	O95835	PSP
259	S	Phosphorylation	Kinase	PKC	-	Uniprot
259	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
259	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
259	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS
259	S	Phosphorylation	Kinase	PKA	-	Uniprot
259	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
259	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
259	S	Phosphorylation	Kinase	PKACA	P17612	PSP
268	T	Phosphorylation	Kinase	RAF1	P04049	GPS
269	T	Phosphorylation	Kinase	KSR1	Q8IVT5	PhosphoELM
269	T	Phosphorylation	Kinase	PKA	-	Uniprot
269	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
289	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
289	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
296	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
301	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
301	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
338	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM
338	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
338	S	Phosphorylation	Kinase	RAF1	P04049	PSP
338	S	Phosphorylation	Kinase	PAK3	Q62829	PSP
338	S	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
338	S	Phosphorylation	Kinase	PAK7	Q9P286	GPS
338	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
338	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
338	S	Phosphorylation	Kinase	PAK3	O75914	Uniprot
339	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
339	S	Phosphorylation	Kinase	PAK3	O75914	Uniprot
339	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
340	Y	Phosphorylation	Kinase	SRC	P00523	PSP
340	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
341	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
341	Y	Phosphorylation	Kinase	SRC	P00523	PSP
341	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
359	S	Phosphorylation	Kinase	RAF1	P04049	PSP
497	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
497	S	Phosphorylation	Kinase	PKCA	P05696	PSP
497	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
499	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
499	S	Phosphorylation	Kinase	PKC	-	Uniprot
499	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
499	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
619	S	Phosphorylation	Kinase	PKCA	P05696	PSP
619	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
621	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
621	S	Phosphorylation	Kinase	RAF1	P04049	PSP
621	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
621	S	Phosphorylation	Kinase	PKACA	P17612	PSP
621	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
621	S	Phosphorylation	Kinase	PRKAA1	Q5EG47	GPS
642	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:18922468
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:19011619
-	K	Ubiquitination	E3 ubiquitin ligase	HECTD3	Q5T447	PMID:28636940

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
29	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	21917714
43	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	8349614
259	S	Phosphorylation	Dephosphorylation of Ser-259 by the complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading to stimulate RAF1 activity.	8349614
259	S	Phosphorylation	Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity.	8349614
269	T	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	7477354
289	S	Methylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
289	S	Phosphorylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
289	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	21917714
296	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	21917714
296	S	Phosphorylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
296	S	Phosphorylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
296	S	Methylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
296	S	Methylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
301	S	Methylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
301	S	Methylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
301	S	Phosphorylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
301	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	21917714
301	S	Phosphorylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
338	S	Methylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
338	S	Phosphorylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
338	S	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	21917714
338	S	Phosphorylation	Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization.	21917714
338	S	Phosphorylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
338	S	Phosphorylation	Dephosphorylation at Ser-338 by PPP5C results in an activity decrease.	21917714
338	S	Methylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
339	S	Phosphorylation	Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization.	15849194
491	T	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	11447113
494	S	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	11447113
563	R	Methylation	Methylated at Arg-563 in response to EGF treatment.	21917714
621	S	Methylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
621	S	Methylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
621	S	Phosphorylation	Phosphorylation at Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation potential of cells.	21917714
621	S	Phosphorylation	Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation.	21917714
621	S	Phosphorylation	Treatment of cells with HGF in the presence of the methylation inhibitor 5'-methylthioadenosine (MTA) results in increased phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-301 and Ser-338.	21917714
642	S	Phosphorylation	Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.	18669648

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RASH_HUMAN	HRAS	physical	14654780
VDAC1_HUMAN	VDAC1	physical	12079506
RASH_HUMAN	HRAS	physical	15031288
RASH_HUMAN	HRAS	physical	14724584
RHES_HUMAN	RASD2	physical	14724584
CNKR2_HUMAN	CNKSR2	physical	14597674
1433B_HUMAN	YWHAB	physical	12620389
RASH_HUMAN	HRAS	physical	12620389
MS18B_HUMAN	OIP5	physical	12620389
KPB2_HUMAN	PHKA2	physical	12620389
TCPG_HUMAN	CCT3	physical	12620389
RASM_HUMAN	MRAS	physical	10498616
SHOC2_HUMAN	SHOC2	physical	10783161
T22D3_HUMAN	TSC22D3	physical	12391160
STK26_HUMAN	STK26	physical	11306563
KPCE_HUMAN	PRKCE	physical	11350735
BCL2_HUMAN	BCL2	physical	8929532
B2CL1_HUMAN	BCL2L1	physical	8929532
MP2K1_HUMAN	MAP2K1	physical	10757792
PEBP1_HUMAN	PEBP1	physical	10757792
GRB10_HUMAN	GRB10	physical	10585452
RASH_HUMAN	HRAS	physical	10882715
RASK_HUMAN	KRAS	physical	10882715
RASN_HUMAN	NRAS	physical	10882715
AKT1_HUMAN	AKT1	physical	10576742
HS90A_HUMAN	HSP90AA1	physical	8408024
GBG4_HUMAN	GNG4	physical	7782277
RHEB_HUMAN	RHEB	physical	15150271
1433Z_HUMAN	YWHAZ	physical	7628630
RB_HUMAN	RB1	physical	9819434
RBL2_HUMAN	RBL2	physical	9819434
KGP1_HUMAN	PRKG1	physical	12237340
JAK2_HUMAN	JAK2	physical	8876196
CFLAR_HUMAN	CFLAR	physical	10837247
MPIP1_HUMAN	CDC25A	physical	7744247
BRAF_HUMAN	BRAF	physical	11325826
M3K1_HUMAN	MAP3K1	physical	10969079
PGFRB_HUMAN	PDGFRB	physical	2475255
M3K5_HUMAN	MAP3K5	physical	11427728
PHB_HUMAN	PHB	physical	10523633
RAP1A_HUMAN	RAP1A	physical	10454553
GRB10_HUMAN	GRB10	physical	9553107
RASH_HUMAN	HRAS	physical	8530446
BAG1_HUMAN	BAG1	physical	8692945
1433B_HUMAN	YWHAB	physical	10620507
1433G_HUMAN	YWHAG	physical	10620507
1433T_HUMAN	YWHAQ	physical	10620507
1433F_HUMAN	YWHAH	physical	10620507
1433Z_HUMAN	YWHAZ	physical	10620507
KPCZ_HUMAN	PRKCZ	physical	10620507
RRAS_HUMAN	RRAS	physical	10848612
PRP6_HUMAN	PRPF6	physical	10848612
1433B_HUMAN	YWHAB	physical	10848612
RASH_HUMAN	HRAS	physical	9150145
1433B_HUMAN	YWHAB	physical	8702721
1433F_HUMAN	YWHAH	physical	8702721
1433E_HUMAN	YWHAE	physical	8702721
MPIP1_HUMAN	CDC25A	physical	9230211
1433B_HUMAN	YWHAB	physical	7644510
1433E_HUMAN	YWHAE	physical	7644510
LCK_HUMAN	LCK	physical	8939988
LTK_HUMAN	LTK	physical	8084603
XIAP_HUMAN	XIAP	physical	19011619
HS90A_HUMAN	HSP90AA1	physical	19011619
CHIP_HUMAN	STUB1	physical	19011619
EF1A1_HUMAN	EEF1A1	physical	17332776
RRAS_HUMAN	RRAS	physical	19805522
CFLAR_HUMAN	CFLAR	physical	16537561
HS90A_HUMAN	HSP90AA1	physical	16504566
RB_HUMAN	RB1	physical	15485920
MP2K1_HUMAN	MAP2K1	physical	15485920
HS90A_HUMAN	HSP90AA1	physical	20039095
HSP7C_HUMAN	HSPA8	physical	20039095
GRP78_HUMAN	HSPA5	physical	18064632
PEBP4_HUMAN	PEBP4	physical	19197339
MP2K1_HUMAN	MAP2K1	physical	9311917
SCNNB_HUMAN	SCNN1B	physical	19380724
NED4L_HUMAN	NEDD4L	physical	19380724
SGK1_HUMAN	SGK1	physical	19380724
T22D3_HUMAN	TSC22D3	physical	19380724
STK3_HUMAN	STK3	physical	20212043
BRAF_HUMAN	BRAF	physical	20212043
MP2K1_HUMAN	MAP2K1	physical	20212043
BRAF_HUMAN	BRAF	physical	18332145
BRAP_HUMAN	BRAP	physical	18332145
MP2K1_HUMAN	MAP2K1	physical	21336309
RASK_HUMAN	KRAS	physical	19029954
MP2K1_HUMAN	MAP2K1	physical	18556463
MP2K1_HUMAN	MAP2K1	physical	15866172
XIAP_HUMAN	XIAP	physical	16964381
WDR83_HUMAN	WDR83	physical	15118098
RFXK_MOUSE	Rfxank	physical	10329666
RFXK_HUMAN	RFXANK	physical	10329666
PP1G_HUMAN	PPP1CC	physical	12374792
RASK_HUMAN	KRAS	physical	23153539
1433T_HUMAN	YWHAQ	physical	15618521
CH60_HUMAN	HSPD1	physical	15618521
HS90A_HUMAN	HSP90AA1	physical	15618521
STK3_HUMAN	STK3	physical	15618521
BAD_HUMAN	BAD	physical	15849194
BCL6_HUMAN	BCL6	physical	15849194
BCL2_HUMAN	BCL2	physical	15849194
BIRC7_HUMAN	BIRC7	physical	22711539
PIN1_HUMAN	PIN1	physical	15664191
2AAA_HUMAN	PPP2R1A	physical	16041367
2ABB_HUMAN	PPP2R2B	physical	16041367
PP2AA_HUMAN	PPP2CA	physical	16041367
PHB_HUMAN	PHB	physical	16041367
1433B_HUMAN	YWHAB	physical	16041367
1433E_HUMAN	YWHAE	physical	16041367
1433F_HUMAN	YWHAH	physical	16041367
1433G_HUMAN	YWHAG	physical	16041367
1433T_HUMAN	YWHAQ	physical	16041367
1433Z_HUMAN	YWHAZ	physical	16041367
1433S_HUMAN	SFN	physical	16041367
STK3_HUMAN	STK3	physical	20086174
RB_HUMAN	RB1	physical	21139044
MP2K1_HUMAN	MAP2K1	physical	16093354
MK01_HUMAN	MAPK1	physical	16093354
HSP74_HUMAN	HSPA4	physical	16093354
HSP7C_HUMAN	HSPA8	physical	16093354
HS90A_HUMAN	HSP90AA1	physical	16093354
RAF1_HUMAN	RAF1	physical	16093354
BAD_HUMAN	BAD	physical	19667065
HS90A_HUMAN	HSP90AA1	physical	8962087
CTIP_HUMAN	RBBP8	physical	21988832
TYY1_HUMAN	YY1	physical	21988832
RASK_HUMAN	KRAS	physical	10958680
MP2K1_HUMAN	MAP2K1	physical	10958680
KPYM_HUMAN	PKM	physical	12620389
SHOC2_HUMAN	SHOC2	physical	25022756
HUWE1_HUMAN	HUWE1	physical	25022756
MP2K1_HUMAN	MAP2K1	physical	19058874
MP2K2_HUMAN	MAP2K2	physical	19058874
MK03_HUMAN	MAPK3	physical	19058874
MK01_HUMAN	MAPK1	physical	19058874
AKT1_HUMAN	AKT1	physical	19058874
RB_HUMAN	RB1	physical	19058874
RANB9_HUMAN	RANBP9	physical	16364241
MP2K2_HUMAN	MAP2K2	physical	16364241
TMM70_HUMAN	TMEM70	physical	16364241
PACN3_HUMAN	PACSIN3	physical	16364241
NPL4_HUMAN	NPLOC4	physical	16364241
KAP0_HUMAN	PRKAR1A	physical	16364241
DCAF8_HUMAN	DCAF8	physical	16364241
PURA_HUMAN	PURA	physical	16364241
FYCO1_HUMAN	FYCO1	physical	16364241
MYPC1_HUMAN	MYBPC1	physical	16364241
CSN7A_HUMAN	COPS7A	physical	16364241
CALU_HUMAN	CALU	physical	25852190
TCPQ_HUMAN	CCT8	physical	25852190
DNJA1_HUMAN	DNAJA1	physical	25852190
EMD_HUMAN	EMD	physical	25852190
RASK_HUMAN	KRAS	physical	25852190
1433S_HUMAN	SFN	physical	25852190
TIM50_HUMAN	TIMM50	physical	25852190
1433B_HUMAN	YWHAB	physical	25852190
1433E_HUMAN	YWHAE	physical	25852190
1433G_HUMAN	YWHAG	physical	25852190
1433F_HUMAN	YWHAH	physical	25852190
1433T_HUMAN	YWHAQ	physical	25852190
1433Z_HUMAN	YWHAZ	physical	25852190
RANB9_HUMAN	RANBP9	physical	23118896
HS90A_HUMAN	HSP90AA1	physical	23118896
CASZ1_HUMAN	CASZ1	physical	25640309
MRC2_HUMAN	MRC2	physical	25640309
PDLI2_HUMAN	PDLIM2	physical	25640309
1433S_HUMAN	SFN	physical	26578655
ACOX1_HUMAN	ACOX1	physical	26496610
CALU_HUMAN	CALU	physical	26496610
PCDH7_HUMAN	PCDH7	physical	26496610
1433F_HUMAN	YWHAH	physical	26496610
MCA3_HUMAN	EEF1E1	physical	26496610
CSN5_HUMAN	COPS5	physical	26496610
S18L2_HUMAN	SS18L2	physical	26496610
PEBP1_HUMAN	PEBP1	physical	21831839
RASH_HUMAN	HRAS	physical	26721396
RASK_HUMAN	KRAS	physical	26721396
SPAT7_HUMAN	SPATA7	physical	27173435
HSP74_HUMAN	HSPA4	physical	16322212
RASK_HUMAN	KRAS	physical	15192046
RASH_HUMAN	HRAS	physical	10887184

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 611553: Noonan syndrome 5 (NS5)
• 611554: LEOPARD syndrome 2 (LPRD2)
• 615916: Cardiomyopathy, dilated 1NN (CMD1NN)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB08912: Dabrafenib
• DB08896: Regorafenib
• DB00398: Sorafenib

Related Literatures of Post-Translational Modification

Methylation

"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: PROTEIN SEQUENCE OF 42-53; 60-65; 310-316 AND 564-572, INTERACTIONWITH PRMT5, METHYLATION AT ARG-563, PHOSPHORYLATION AT SER-289;SER-296; SER-301; SER-338 AND SER-621, AND MUTAGENESIS OF ARG-563.
PubMed: 21917714

Phosphorylation

"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-289; SER-301 ANDSER-612, AND MASS SPECTROMETRY.
PubMed: 19690332

"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-257, AND MASSSPECTROMETRY.
PubMed: 19369195

"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 SER-642, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-43; SER-244 AND SER-259,AND MASS SPECTROMETRY.
PubMed: 18691976

"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 SER-257 AND THR-258, ANDMASS SPECTROMETRY.
PubMed: 18220336

"p21 activated kinase 5 activates Raf-1 and targets it tomitochondria.";
Wu X., Carr H.S., Dan I., Ruvolo P.P., Frost J.A.;
J. Cell. Biochem. 105:167-175(2008).
Cited for: PHOSPHORYLATION AT SER-338 BY PAK5.
PubMed: 18465753

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASSSPECTROMETRY.
PubMed: 19007248

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASSSPECTROMETRY.
PubMed: 17525332

"A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalyticsubunit of PP1 functions as an M-Ras effector to modulate Rafactivity.";
Rodriguez-Viciana P., Oses-Prieto J., Burlingame A., Fried M.,McCormick F.;
Mol. Cell 22:217-230(2006).
Cited for: IDENTIFICATION IN A COMPLEX WITH PP1CA; PPP1CB; PPP1CC; SHOC2 ANDMRAS, PHOSPHORYLATION AT SER-259, AND CHARACTERIZATION OF VARIANTALA-259.
PubMed: 16630891

"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-294 AND SER-301, ANDMASS SPECTROMETRY.
PubMed: 17081983

"Identification of Raf-1 S471 as a novel phosphorylation site criticalfor Raf-1 and B-Raf kinase activities and for MEK binding.";
Zhu J., Balan V., Bronisz A., Balan K., Sun H., Leicht D.T., Luo Z.,Qin J., Avruch J., Tzivion G.;
Mol. Biol. Cell 16:4733-4744(2005).
Cited for: PHOSPHORYLATION AT SER-471.
PubMed: 16093354

"p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1regulates its mitochondrial localization, phosphorylation of BAD, andBcl-2 association.";
Jin S., Zhuo Y., Guo W., Field J.;
J. Biol. Chem. 280:24698-24705(2005).
Cited for: FUNCTION IN THE PHOSPHORYLATION OF BAD, PHOSPHORYLATION AT SER-338 ANDSER-339 BY PAK1, SUBCELLULAR LOCATION, AND INTERACTION WITH BCL2.
PubMed: 15849194

"LGI1, a putative tumor metastasis suppressor gene, controls in vitroinvasiveness and expression of matrix metalloproteinases in gliomacells through the ERK1/2 pathway.";
Kunapuli P., Kasyapa C.S., Hawthorn L., Cowell J.K.;
J. Biol. Chem. 279:23151-23157(2004).
Cited for: PHOSPHORYLATION AT SER-259.
PubMed: 15047712

"Dephosphorylation of Ser-259 regulates Raf-1 membrane association.";
Kubicek M., Pacher M., Abraham D., Podar K., Eulitz M., Baccarini M.;
J. Biol. Chem. 277:7913-7919(2002).
Cited for: PHOSPHORYLATION AT SER-259, DEPHOSPHORYLATION AT SER-259, ANDSUBCELLULAR LOCATION.
PubMed: 11756411

"Interaction between active Pak1 and Raf-1 is necessary forphosphorylation and activation of Raf-1.";
Zang M., Hayne C., Luo Z.;
J. Biol. Chem. 277:4395-4405(2002).
Cited for: PHOSPHORYLATION AT SER-338 BY PAK1, ENZYME REGULATION, AND INTERACTIONWITH PAK1.
PubMed: 11733498

"Raf-1-associated protein phosphatase 2A as a positive regulator ofkinase activation.";
Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A.,Dilworth S.M., Mischak H., Kolch W., Baccarini M.;
J. Biol. Chem. 275:22300-22304(2000).
Cited for: PHOSPHORYLATION AT SER-259 AND SER-621, DEPHOSPHORYLATION AT SER-43;SER-259 AND SER-621, ENZYME REGULATION, AND INTERACTION WITH PPP2CAAND PPP2R1B.
PubMed: 10801873

"Phosphorylation and regulation of Raf by Akt (protein kinase B).";
Zimmermann S., Moelling K.;
Science 286:1741-1744(1999).
Cited for: PHOSPHORYLATION AT SER-259 BY PKB/AKT1, ENZYME REGULATION, ANDINTERACTION WITH PKB/AKT1.
PubMed: 10576742

"Identification of the major phosphorylation sites of the Raf-1kinase.";
Morrison D.K., Heidecker G., Rapp U.R., Copeland T.D.;
J. Biol. Chem. 268:17309-17316(1993).
Cited for: PHOSPHORYLATION AT SER-43; SER-259; THR-268; SER-499 AND SER-621.
PubMed: 8349614

"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: PROTEIN SEQUENCE OF 42-53; 60-65; 310-316 AND 564-572, INTERACTIONWITH PRMT5, METHYLATION AT ARG-563, PHOSPHORYLATION AT SER-289;SER-296; SER-301; SER-338 AND SER-621, AND MUTAGENESIS OF ARG-563.
PubMed: 21917714

"Phosphorylation of Raf by ceramide-activated protein kinase.";
Yao B., Zhang Y., Delikat S., Mathias S., Basu S., Kolesnick R.;
Nature 378:307-310(1995).
Cited for: PROTEIN SEQUENCE OF 254-278, AND PHOSPHORYLATION AT THR-269.
PubMed: 7477354