RAF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAF1_MOUSE
• UniProt AC: Q99N57
• Protein Name: RAF proto-oncogene serine/threonine-protein kinase
• Gene Name: Raf1
• Organism: Mus musculus (Mouse).
• 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. Phosphoryl
• 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. 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 (By similarity). Regulates Rho signaling and migration, and is required for normal wound healing..
• Protein Sequence: MEHIQGAWKTISNGFGLKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDSSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLQEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTVGDSGVPAPPSFPMRRMRESVSRMPASSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLHVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPGSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF

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
12	Phosphorylation	QGAWKTISNGFGLKD CCHHHHHHCCCCCCC	35.81	29514104
25	Phosphorylation	KDAVFDGSSCISPTI CCCEECCCCCCCHHH	24.71	25619855
26	Phosphorylation	DAVFDGSSCISPTIV CCEECCCCCCCHHHH	22.47	25619855
29	Phosphorylation	FDGSSCISPTIVQQF ECCCCCCCHHHHHHH	21.96	27087446
31	Phosphorylation	GSSCISPTIVQQFGY CCCCCCHHHHHHHCC	27.30	25619855
38	Phosphorylation	TIVQQFGYQRRASDD HHHHHHCCCCCCCCC	10.51	23375375
43	Phosphorylation	FGYQRRASDDGKLTD HCCCCCCCCCCCCCC	34.13	11782426
49	Phosphorylation	ASDDGKLTDSSKTSN CCCCCCCCCCCCCCC	37.00	28833060
51	Phosphorylation	DDGKLTDSSKTSNTI CCCCCCCCCCCCCEE	28.62	28833060
52	Phosphorylation	DGKLTDSSKTSNTIR CCCCCCCCCCCCEEE	42.64	28833060
57	Phosphorylation	DSSKTSNTIRVFLPN CCCCCCCEEEEECCC	15.21	21454597
65	Ubiquitination	IRVFLPNKQRTVVNV EEEECCCCCCEEEEC	38.94	-
68	Phosphorylation	FLPNKQRTVVNVRNG ECCCCCCEEEECCCC	26.72	29514104
220	Phosphorylation	PMRRMRESVSRMPAS CHHHHHHHHHCCCCC	18.28	25338131
227	Phosphorylation	SVSRMPASSQHRYST HHHCCCCCCCCCCCC	25.35	26643407
228	Phosphorylation	VSRMPASSQHRYSTP HHCCCCCCCCCCCCC	31.92	26643407
232	Phosphorylation	PASSQHRYSTPHAFT CCCCCCCCCCCCEEE	18.12	28833060
233	Phosphorylation	ASSQHRYSTPHAFTF CCCCCCCCCCCEEEE	35.10	11997508
234	Phosphorylation	SSQHRYSTPHAFTFN CCCCCCCCCCEEEEE	15.34	21082442
239	Phosphorylation	YSTPHAFTFNTSSPS CCCCCEEEEECCCCC	19.43	28833060
242	Phosphorylation	PHAFTFNTSSPSSEG CCEEEEECCCCCCCC	26.79	28833060
243	Phosphorylation	HAFTFNTSSPSSEGS CEEEEECCCCCCCCC	41.16	28833060
244	Phosphorylation	AFTFNTSSPSSEGSL EEEEECCCCCCCCCC	27.11	28833060
246	Phosphorylation	TFNTSSPSSEGSLSQ EEECCCCCCCCCCCH	42.86	28833060
247	Phosphorylation	FNTSSPSSEGSLSQR EECCCCCCCCCCCHH	49.73	28833060
250	Phosphorylation	SSPSSEGSLSQRQRS CCCCCCCCCCHHHHC	22.31	28833060
252	Phosphorylation	PSSEGSLSQRQRSTS CCCCCCCCHHHHCCC	25.64	23984901
257	Phosphorylation	SLSQRQRSTSTPNVH CCCHHHHCCCCCCEE	20.55	27742792
258	Phosphorylation	LSQRQRSTSTPNVHM CCHHHHCCCCCCEEE	38.52	27742792
259	Phosphorylation	SQRQRSTSTPNVHMV CHHHHCCCCCCEEEE	43.01	11782426
260	Phosphorylation	QRQRSTSTPNVHMVS HHHHCCCCCCEEEEE	20.97	27742792
267	Phosphorylation	TPNVHMVSTTLHVDS CCCEEEEEEEEECCH	14.22	28833060
268	Phosphorylation	PNVHMVSTTLHVDSR CCEEEEEEEEECCHH	23.20	28833060
269	Phosphorylation	NVHMVSTTLHVDSRM CEEEEEEEEECCHHH	13.83	28833060
274	Phosphorylation	STTLHVDSRMIEDAI EEEEECCHHHHHHHH	23.74	28833060
283	Phosphorylation	MIEDAIRSHSESASP HHHHHHHHCCCCCCH	25.83	27087446
285 (in isoform 2)	Phosphorylation	-	34.20	23737553
285	Phosphorylation	EDAIRSHSESASPSA HHHHHHCCCCCCHHH	34.20	26643407
287	Phosphorylation	AIRSHSESASPSALS HHHHCCCCCCHHHHC	36.74	26643407
289	Phosphorylation	RSHSESASPSALSSS HHCCCCCCHHHHCCC	28.77	27087446
291	Phosphorylation	HSESASPSALSSSPN CCCCCCHHHHCCCCC	39.07	27087446
294	Phosphorylation	SASPSALSSSPNNLS CCCHHHHCCCCCCCC	28.61	27087446
295	Phosphorylation	ASPSALSSSPNNLSP CCHHHHCCCCCCCCC	51.14	27087446
296	Phosphorylation	SPSALSSSPNNLSPT CHHHHCCCCCCCCCC	28.42	27087446
301	Phosphorylation	SSSPNNLSPTGWSQP CCCCCCCCCCCCCCC	23.65	27087446
303	Phosphorylation	SPNNLSPTGWSQPKT CCCCCCCCCCCCCCC	48.16	25168779
306	Phosphorylation	NLSPTGWSQPKTPVP CCCCCCCCCCCCCCC	37.64	22942356
309 (in isoform 2)	Phosphorylation	-	58.80	25266776
310	Phosphorylation	TGWSQPKTPVPAQRE CCCCCCCCCCCCCCC	35.88	23684622
338	Phosphorylation	RPRGQRDSSYYWEIE CCCCCCCCCEEEEEE	23.56	11782426
339	Phosphorylation	PRGQRDSSYYWEIEA CCCCCCCCEEEEEEE	26.91	-
340	Phosphorylation	RGQRDSSYYWEIEAS CCCCCCCEEEEEEEE	19.29	11296227
341	Phosphorylation	GQRDSSYYWEIEASE CCCCCCEEEEEEEEE	9.86	11296227
357	Phosphorylation	MLSTRIGSGSFGTVY EEEEEECCCCCCCEE	28.97	26745281
359	Phosphorylation	STRIGSGSFGTVYKG EEEECCCCCCCEECC	23.38	28066266
362	Phosphorylation	IGSGSFGTVYKGKWH ECCCCCCCEECCEEE	20.74	28066266
471	Phosphorylation	IIHRDMKSNNIFLHE CCCCCCCCCCEEEEC	28.59	-
491	Phosphorylation	IGDFGLATVKSRWSG ECCEEEEEECCCCCC	33.24	-
494	Phosphorylation	FGLATVKSRWSGSQQ EEEEEECCCCCCCCC	34.35	26643407
497	Phosphorylation	ATVKSRWSGSQQVEQ EEECCCCCCCCCEEC	27.70	26643407
499	Phosphorylation	VKSRWSGSQQVEQPT ECCCCCCCCCEECCC	16.36	25266776
506	Phosphorylation	SQQVEQPTGSVLWMA CCCEECCCCCEEEEC	41.61	20531401
508	Phosphorylation	QVEQPTGSVLWMAPE CEECCCCCEEEECCE	19.26	26643407
563	Methylation	QIIFMVGRGYASPDL EEEEEECCCCCCCHH	24.44	-
563	Symmetric dimethylarginine	QIIFMVGRGYASPDL EEEEEECCCCCCCHH	24.44	-
604	Phosphorylation	PLFPQILSSIELLQH CCHHHHHHHHHHHHC	30.79	26643407
605	Phosphorylation	LFPQILSSIELLQHS CHHHHHHHHHHHHCC	19.35	26643407
612	Phosphorylation	SIELLQHSLPKINRS HHHHHHCCCCCCCCC	33.15	29514104
619	Phosphorylation	SLPKINRSASEPSLH CCCCCCCCCCCCCHH	31.49	27742792
621	Phosphorylation	PKINRSASEPSLHRA CCCCCCCCCCCHHHH	51.81	26824392
624	Phosphorylation	NRSASEPSLHRAAHT CCCCCCCCHHHHHCC	32.53	20469934
631	Phosphorylation	SLHRAAHTEDINACT CHHHHHCCCCCCCCC	30.54	25619855
638	Phosphorylation	TEDINACTLTTSPRL CCCCCCCCCCCCCCC	25.40	25619855
640	Phosphorylation	DINACTLTTSPRLPV CCCCCCCCCCCCCCC	13.69	25619855
641	Phosphorylation	INACTLTTSPRLPVF CCCCCCCCCCCCCCC	39.59	25521595
642	Phosphorylation	NACTLTTSPRLPVF- CCCCCCCCCCCCCC-	11.64	26824392

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	P63085	Uniprot
43	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
43	S	Phosphorylation	Kinase	PKA	-	Uniprot
43	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
233	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
233	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
233	S	Phosphorylation	Kinase	PKA	-	Uniprot
259	S	Phosphorylation	Kinase	PKA	-	Uniprot
259	S	Phosphorylation	Kinase	AKT1	P31750	Uniprot
259	S	Phosphorylation	Kinase	PKC	-	Uniprot
269	T	Phosphorylation	Kinase	PKA	-	Uniprot
289	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
296	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
301	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
338	S	Phosphorylation	Kinase	MEK1	Q02750	PSP
338	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
338	S	Phosphorylation	Kinase	PAK1	O88643	Uniprot
338	S	Phosphorylation	Kinase	PAK2	Q8CIN4	Uniprot
338	S	Phosphorylation	Kinase	PAK3	Q61036	Uniprot
338	S	Phosphorylation	Kinase	PAK5	Q8C015	Uniprot
339	S	Phosphorylation	Kinase	PAK2	Q8CIN4	Uniprot
339	S	Phosphorylation	Kinase	PAK3	Q61036	Uniprot
339	S	Phosphorylation	Kinase	PAK1	O88643	Uniprot
340	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
341	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
341	Y	Phosphorylation	Kinase	LYN	P25911	PSP
497	S	Phosphorylation	Kinase	PKC	-	Uniprot
499	S	Phosphorylation	Kinase	PRKCA	P20444	GPS
499	S	Phosphorylation	Kinase	PKC	-	Uniprot
621	S	Phosphorylation	Kinase	RAF1	Q99N57	PSP
642	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Stub1	Q9WUD1	PMID:22199232

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.	15664191
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.	15664191
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.	15664191
259	S	Phosphorylation	Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity.	15664191
269	T	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	-
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
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.	15664191
338	S	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	15664191
338	S	Phosphorylation	Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization (By similarity).	15664191
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.	15664191
338	S	Phosphorylation	Dephosphorylation at SER-338 by PPP5C results in a decreased of activity (By similarity).	15664191
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.	15664191
339	S	Phosphorylation	Phosphorylation at Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its mitochondrial localization (By similarity).	-
491	T	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	-
494	S	Phosphorylation	Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation.	-
563	R	Methylation	Methylated at Arg-563 in response to EGF treatment.	-
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.	15664191
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.	15664191
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.	15664191
621	S	Phosphorylation	Phosphorylation at Ser-621 in response to growth factor treatment stabilizes the protein, possibly by preventing proteasomal degradation.	15664191
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.	15664191
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.	15664191

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RASH_MOUSE	Hras	physical	16803888
MP2K1_MOUSE	Map2k1	physical	20956560
NEK10_MOUSE	Nek10	physical	20956560
BRAF_MOUSE	Braf	physical	18332145
KSR1_MOUSE	Ksr1	physical	18332145
BRAP_MOUSE	Brap	physical	18332145
RFXK_MOUSE	Rfxank	physical	10329666
RASH_MOUSE	Hras	physical	16405865
ROCK2_MOUSE	Rock2	physical	16365167
RASH_MOUSE	Hras	physical	17984326
VKIND_MOUSE	Kndc1	physical	17984326
RABX5_MOUSE	Rabgef1	physical	15235600
RASH_MOUSE	Hras	physical	15235600
RASH_MOUSE	Hras	physical	24470255
PAXI_MOUSE	Pxn	physical	14636584
MP2K1_MOUSE	Map2k1	physical	14636584
MP2K1_MOUSE	Map2k1	physical	11435472
RASH_MOUSE	Hras	physical	11435472
PEBP1_MOUSE	Pebp1	physical	23055494
MP2K1_MOUSE	Map2k1	physical	23055494
RASH_MOUSE	Hras	physical	28053233

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASSSPECTROMETRY.
PubMed: 19367708

"Regulation of Raf-1 by direct feedback phosphorylation.";
Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z.,Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K.;
Mol. Cell 17:215-224(2005).
Cited for: PHOSPHORYLATION AT SER-29; SER-43; SER-259; SER-289; SER-296; SER-301;SER-338; SER-621 AND SER-642, ENZYME REGULATION, AND INTERACTION WITHPIN1; PPP2CA AND PPP2R1B.
PubMed: 15664191