dbPTM

SHC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SHC1_HUMAN
UniProt AC	P29353
Protein Name	SHC-transforming protein 1
Gene Name	SHC1
Organism	Homo sapiens (Human).
Sequence Length	583
Subcellular Localization	Cytoplasm. Isoform p46Shc: Mitochondrion matrix . Localized to the mitochondria matrix. Targeting of isoform p46Shc to mitochondria is mediated by its first 32 amino acids, which behave as a bona fide mitochondrial targeting sequence. Isoform p52Shc
Protein Description	Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis..
Protein Sequence	MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDLLPPKP -------CCCCCCCC	8.06	22814378
1 (in isoform 2)	Acetylation	-	8.06	22814378
1 (in isoform 7)	Acetylation	-	8.06	22814378
17	Phosphorylation	YNPLRNESLSSLEEG CCCCCCCCHHHHHCC	36.78	28348404
19	Phosphorylation	PLRNESLSSLEEGAS CCCCCCHHHHHCCCC	42.00	28348404
20	Phosphorylation	LRNESLSSLEEGASG CCCCCHHHHHCCCCC	45.13	28348404
26	Phosphorylation	SSLEEGASGSTPPEE HHHHCCCCCCCCCHH	44.10	28348404
28	Phosphorylation	LEEGASGSTPPEELP HHCCCCCCCCCHHCC	34.93	28348404
29	Phosphorylation	EEGASGSTPPEELPS HCCCCCCCCCHHCCC	46.52	33259812
33	Ubiquitination	SGSTPPEELPSPSAS CCCCCCHHCCCCCHH	72.29	29967540
36	Phosphorylation	TPPEELPSPSASSLG CCCHHCCCCCHHHCC	44.08	16699171
54	Phosphorylation	PPLPGDDSPTTLCSF CCCCCCCCCCCHHHH	28.96	16251354
80	Phosphorylation	PAGGRPGSKGEPGRA CCCCCCCCCCCCCCC	39.92	28674419
115	Phosphorylation	LQDMNKLSGGGGRRT HHCHHHHCCCCCCCC	36.68	25394399
139	Phosphorylation	EEWTRHGSFVNKPTR CCCCCCCCCCCCCCC	21.64	29255136
143	Ubiquitination	RHGSFVNKPTRGWLH CCCCCCCCCCCCCCC	42.33	29967540
145	Phosphorylation	GSFVNKPTRGWLHPN CCCCCCCCCCCCCCC	43.34	20201521
154	Ubiquitination	GWLHPNDKVMGPGVS CCCCCCCCCCCCCHH	40.54	-
154	Acetylation	GWLHPNDKVMGPGVS CCCCCCCCCCCCCHH	40.54	-
161	Phosphorylation	KVMGPGVSYLVRYMG CCCCCCHHHHHHHHH	20.75	23663014
162	Phosphorylation	VMGPGVSYLVRYMGC CCCCCHHHHHHHHHH	13.55	23663014
166	Ubiquitination	GVSYLVRYMGCVEVL CHHHHHHHHHHHHHH	7.15	29967540
203	Ubiquitination	CEAVPGAKGATRRRK HHHCCCCCCCCCCCC	55.80	-
203 (in isoform 6)	Ubiquitination	-	55.80	-
206	Phosphorylation	VPGAKGATRRRKPCS CCCCCCCCCCCCCCC	33.12	-
211	Ubiquitination	GATRRRKPCSRPLSS CCCCCCCCCCCCHHH	21.36	29967540
213	Phosphorylation	TRRRKPCSRPLSSIL CCCCCCCCCCHHHHH	45.52	-
226	Ubiquitination	ILGRSNLKFAGMPIT HHCCCCCEECCCEEE	37.10	-
237	Phosphorylation	MPITLTVSTSSLNLM CEEEEEEECHHHHHH	19.82	27251275
238	Phosphorylation	PITLTVSTSSLNLMA EEEEEEECHHHHHHH	20.28	27251275
239	Phosphorylation	ITLTVSTSSLNLMAA EEEEEECHHHHHHHH	25.89	27251275
240	Phosphorylation	TLTVSTSSLNLMAAD EEEEECHHHHHHHHH	22.74	27251275
280	Ubiquitination	YVAYVAKDPVNQRAC HHHHHHCCCCCCCEE	42.51	29967540
296	Ubiquitination	ILECPEGLAQDVIST EECCCCHHHHHHHHH	3.54	24816145
307	Ubiquitination	VISTIGQAFELRFKQ HHHHHHHHHHHHHHH	8.48	24816145
313	Ubiquitination	QAFELRFKQYLRNPP HHHHHHHHHHHHCCC	31.44	-
313 (in isoform 6)	Ubiquitination	-	31.44	-
315	Phosphorylation	FELRFKQYLRNPPKL HHHHHHHHHHCCCCC	14.28	28152594
317 (in isoform 7)	Phosphorylation	-	48.99	25627689
318 (in isoform 7)	Phosphorylation	-	55.41	25849741
321	Ubiquitination	QYLRNPPKLVTPHDR HHHHCCCCCCCCCHH	57.77	29967540
324	Phosphorylation	RNPPKLVTPHDRMAG HCCCCCCCCCHHHCC	25.91	21722762
325	Ubiquitination	NPPKLVTPHDRMAGF CCCCCCCCCHHHCCC	21.65	29967540
326	Ubiquitination	PPKLVTPHDRMAGFD CCCCCCCCHHHCCCC	26.41	29967540
334	Ubiquitination	DRMAGFDGSAWDEEE HHHCCCCCCCCCCCC	19.59	24816145
335	Phosphorylation	RMAGFDGSAWDEEEE HHCCCCCCCCCCCCC	28.20	21945579
344	Ubiquitination	WDEEEEEPPDHQYYN CCCCCCCCCCCCCCC	42.79	24816145
349	Phosphorylation	EEPPDHQYYNDFPGK CCCCCCCCCCCCCCC	10.79	21945579
350	Phosphorylation	EPPDHQYYNDFPGKE CCCCCCCCCCCCCCC	11.16	21945579
352	Ubiquitination	PDHQYYNDFPGKEPP CCCCCCCCCCCCCCC	34.69	24816145
352 (in isoform 2)	Ubiquitination	-	34.69	21906983
353	Ubiquitination	DHQYYNDFPGKEPPL CCCCCCCCCCCCCCC	8.38	24816145
380	Phosphorylation	APGAARPTAPNAQTP CCCCCCCCCCCCCCC	49.55	27050516
386	Phosphorylation	PTAPNAQTPSHLGAT CCCCCCCCCCCCCCC	25.09	25159151
388	Phosphorylation	APNAQTPSHLGATLP CCCCCCCCCCCCCCC	34.43	25159151
393	Phosphorylation	TPSHLGATLPVGQPV CCCCCCCCCCCCCCC	29.78	23312004
399 (in isoform 3)	Ubiquitination	-	22.31	21906983
426	Phosphorylation	RELFDDPSYVNVQNL CCCCCCCCCCCCCCH	49.02	22167270
427 (in isoform 6)	Phosphorylation	-	11.05	25627689
427	Phosphorylation	ELFDDPSYVNVQNLD CCCCCCCCCCCCCHH	11.05	19664994
428 (in isoform 6)	Phosphorylation	-	7.12	25849741
435	Ubiquitination	VNVQNLDKARQAVGG CCCCCHHHHHHHHCC	48.94	29967540
436	Ubiquitination	NVQNLDKARQAVGGA CCCCHHHHHHHHCCC	14.42	29967540
444	Ubiquitination	RQAVGGAGPPNPAIN HHHHCCCCCCCCCCC	41.28	24816145
445	Ubiquitination	QAVGGAGPPNPAING HHHCCCCCCCCCCCC	25.59	24816145
453	Phosphorylation	PNPAINGSAPRDLFD CCCCCCCCCCHHHCC	30.52	9488479
454	Ubiquitination	NPAINGSAPRDLFDM CCCCCCCCCHHHCCC	12.44	24816145
462 (in isoform 1)	Ubiquitination	-	48.69	21906983
462	Ubiquitination	PRDLFDMKPFEDALR CHHHCCCCCHHHHHC	48.69	21906983
463	Ubiquitination	RDLFDMKPFEDALRV HHHCCCCCHHHHHCC	31.08	24816145
471	Ubiquitination	FEDALRVPPPPQSVS HHHHHCCCCCCCCCC	29.28	24816145
472	Ubiquitination	EDALRVPPPPQSVSM HHHHCCCCCCCCCCH	50.80	24816145
494	Phosphorylation	PWFHGKLSRREAEAL CCCCCCCCHHHHHHH	32.55	-
513	Phosphorylation	GDFLVRESTTTPGQY CCEEEEECCCCCCEE	22.08	25159151
514	Phosphorylation	DFLVRESTTTPGQYV CEEEEECCCCCCEEE	29.90	25159151
515	Phosphorylation	FLVRESTTTPGQYVL EEEEECCCCCCEEEE	40.03	25159151
516	Phosphorylation	LVRESTTTPGQYVLT EEEECCCCCCEEEEE	26.05	25159151
520	Phosphorylation	STTTPGQYVLTGLQS CCCCCCEEEEEECCC	11.89	28152594
558	Phosphorylation	SVSHLISYHMDNHLP CHHHHHHHHHCCCCC	8.31	-

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	PRKCD	Q05655	GPS
54	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
139	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
194	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
194	Y	Phosphorylation	Kinase	SRC	P12931	PSP
195	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
195	Y	Phosphorylation	Kinase	SRC	P12931	PSP
206	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
213	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
239	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
239	Y	Phosphorylation	Kinase	SYK	P43405	PSP
239	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
239	Y	Phosphorylation	Kinase	LCK	P06239	PSP
240	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
240	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
240	Y	Phosphorylation	Kinase	SYK	P43405	PSP
240	Y	Phosphorylation	Kinase	LCK	P06239	PSP
272	Y	Phosphorylation	Kinase	SRC	P12931	PSP
272	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
317	Y	Phosphorylation	Kinase	LCK	P06239	PSP
317	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
317	Y	Phosphorylation	Kinase	NTRK1	P04629	GPS
317	Y	Phosphorylation	Kinase	SYK	P43405	PSP
317	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
317	Y	Phosphorylation	Kinase	CSK	P41240	GPS
317	Y	Phosphorylation	Kinase	PTK2	P34152-2	GPS
349	Y	Phosphorylation	Kinase	ZAP70	P43403	PhosphoELM
349	Y	Phosphorylation	Kinase	SYK	P43405	GPS
349	Y	Phosphorylation	Kinase	SRC	P12931	PSP
349	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
349	Y	Phosphorylation	Kinase	FLT4	P35916	GPS
350	Y	Phosphorylation	Kinase	ZAP70	P43403	PhosphoELM
350	Y	Phosphorylation	Kinase	SYK	P43405	GPS
350	Y	Phosphorylation	Kinase	SRC	P12931	PSP
350	Y	Phosphorylation	Kinase	FLT4	P35916	GPS
350	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
386	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
410	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
427	Y	Phosphorylation	Kinase	ZAP70	P43403	PhosphoELM
427	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
427	Y	Phosphorylation	Kinase	FLT4	P35916	GPS
427	Y	Phosphorylation	Kinase	SRC	P12931	PSP
427	Y	Phosphorylation	Kinase	SYK	P43405	GPS
427	Y	Phosphorylation	Kinase	MET	P08581	PSP
448	Y	Phosphorylation	Kinase	JAK3	P52333	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
36	S	Phosphorylation		15837797
Isoform p66Shc is phosphorylated on Ser-36 by PRKCB upon treatment with insulin, hydrogen peroxide or irradiation with ultraviolet light (By similarity).

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 SHC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CACO2_HUMAN	CALCOCO2	physical	16189514
P85A_HUMAN	PIK3R1	physical	7537361
DOK1_HUMAN	DOK1	physical	10822173
DOK2_HUMAN	DOK2	physical	10822173
SHIP1_HUMAN	INPP5D	physical	10822173
MAPK2_HUMAN	MAPKAPK2	physical	15094067
PLS1_HUMAN	PLSCR1	physical	12871937
LRP1_HUMAN	LRP1	physical	12789267
CADH5_HUMAN	CDH5	physical	11950700
VGFR2_HUMAN	KDR	physical	11950700
GRAP2_MOUSE	Grap2	physical	9872323
ABL1_HUMAN	ABL1	physical	10194451
SHIP1_HUMAN	INPP5D	physical	10194451
SHIP2_HUMAN	INPPL1	physical	10194451
CD22_HUMAN	CD22	physical	10748054
ITB4_HUMAN	ITGB4	physical	11044453
SHIP2_HUMAN	INPPL1	physical	11349134
GRB2_HUMAN	GRB2	physical	8491186
ERBB2_HUMAN	ERBB2	physical	10085134
GRB2_HUMAN	GRB2	physical	8647288
FAK1_HUMAN	PTK2	physical	11980671
EPHA2_HUMAN	EPHA2	physical	12400011
GRB2_HUMAN	GRB2	physical	8662733
PLCG1_HUMAN	PLCG1	physical	8662733
CEAM1_HUMAN	CEACAM1	physical	11694516
CSF3R_HUMAN	CSF3R	physical	9824671
SHIP1_HUMAN	INPP5D	physical	12024011
KPCD_HUMAN	PRKCD	physical	12024011
RET_HUMAN	RET	physical	9047384
IL2RG_HUMAN	IL2RG	physical	8643566
PLCG2_HUMAN	PLCG2	physical	12135708
GAB2_HUMAN	GAB2	physical	12135708
PTN12_HUMAN	PTPN12	physical	8626541
PTN12_MOUSE	Ptpn12	physical	8626541
SHCBP_HUMAN	SHCBP1	physical	10086341
RET_HUMAN	RET	physical	8183561
NTRK1_HUMAN	NTRK1	physical	8183561
PHAG1_HUMAN	PAG1	physical	10790433
GRB2_HUMAN	GRB2	physical	9083103
GRB2_HUMAN	GRB2	physical	9927207
VGFR3_HUMAN	FLT4	physical	9927207
EPOR_HUMAN	EPOR	physical	8400282
VAV3_HUMAN	VAV3	physical	11094073
PLS1_HUMAN	PLSCR1	physical	12009895
AP2A2_HUMAN	AP2A2	physical	8617812
GRB2_HUMAN	GRB2	physical	8294403
IL2RB_HUMAN	IL2RB	physical	8294403
NTRK1_HUMAN	NTRK1	physical	10092678
NTRK2_HUMAN	NTRK2	physical	10092678
NTRK3_HUMAN	NTRK3	physical	10092678
ESR1_HUMAN	ESR1	physical	11773443
A4_HUMAN	APP	physical	11877420
GRB2_HUMAN	GRB2	physical	11302736
TNR16_HUMAN	NGFR	physical	7541035
GRB2_HUMAN	GRB2	physical	10570290
SHIP1_HUMAN	INPP5D	physical	8643691
GRB2_HUMAN	GRB2	physical	11505033
GRB2_HUMAN	GRB2	physical	8195171
PGFRB_HUMAN	PDGFRB	physical	8195171
SOS1_HUMAN	SOS1	physical	9344843
RPGF1_HUMAN	RAPGEF1	physical	9344843
STA5A_HUMAN	STAT5A	physical	10996427
STA5B_HUMAN	STAT5B	physical	10996427
JAK2_HUMAN	JAK2	physical	7535773
GHR_HUMAN	GHR	physical	7535773
GRB2_HUMAN	GRB2	physical	7535773
CALD1_HUMAN	CALD1	physical	10559276
SHIP1_HUMAN	INPP5D	physical	10900203
GRB2_HUMAN	GRB2	physical	9045692
DDR1_HUMAN	DDR1	physical	9659899
IL6RB_HUMAN	IL6ST	physical	9126968
JAK2_HUMAN	JAK2	physical	9126968
HIF1A_HUMAN	HIF1A	physical	12114320
SHIP1_HUMAN	INPP5D	physical	15470047
GRB2_HUMAN	GRB2	physical	8621719
SPTB2_HUMAN	SPTBN1	physical	19380743
SPTN1_HUMAN	SPTAN1	physical	19380743
USP9X_HUMAN	USP9X	physical	19380743
AP2A1_HUMAN	AP2A1	physical	19380743
PTN12_HUMAN	PTPN12	physical	19380743
SHIP2_HUMAN	INPPL1	physical	19380743
K2C1_HUMAN	KRT1	physical	19380743
HSP7C_HUMAN	HSPA8	physical	19380743
MYH10_HUMAN	MYH10	physical	19380743
K1C10_HUMAN	KRT10	physical	19380743
K1C9_HUMAN	KRT9	physical	19380743
K22E_HUMAN	KRT2	physical	19380743
TBB5_HUMAN	TUBB	physical	19380743
TBB4B_HUMAN	TUBB4B	physical	19380743
TBA1B_HUMAN	TUBA1B	physical	19380743
TBA1C_HUMAN	TUBA1C	physical	19380743
TBA1A_HUMAN	TUBA1A	physical	19380743
AP2B1_HUMAN	AP2B1	physical	19380743
USP9Y_HUMAN	USP9Y	physical	19380743
GRB2_HUMAN	GRB2	physical	19380743
KPCD_HUMAN	PRKCD	physical	19380743
TBB2B_HUMAN	TUBB2B	physical	19380743
ACACA_HUMAN	ACACA	physical	19380743
K2C5_HUMAN	KRT5	physical	19380743
ACTN4_HUMAN	ACTN4	physical	19380743
SPTA1_HUMAN	SPTA1	physical	19380743
TBB3_HUMAN	TUBB3	physical	19380743
K2C6A_HUMAN	KRT6A	physical	19380743
FAS_HUMAN	FASN	physical	19380743
GRP78_HUMAN	HSPA5	physical	19380743
MYH9_HUMAN	MYH9	physical	19380743
ACTB_HUMAN	ACTB	physical	19380743
PYR1_HUMAN	CAD	physical	19380743
IQGA1_HUMAN	IQGAP1	physical	19380743
PPIP2_HUMAN	PSTPIP2	physical	19380743
K1C14_HUMAN	KRT14	physical	19380743
SOS1_HUMAN	SOS1	physical	19380743
MYO1D_HUMAN	MYO1D	physical	19380743
GRP75_HUMAN	HSPA9	physical	19380743
HS71L_HUMAN	HSPA1L	physical	19380743
K1C16_HUMAN	KRT16	physical	19380743
ACTS_HUMAN	ACTA1	physical	19380743
TBB6_HUMAN	TUBB6	physical	19380743
HS90B_HUMAN	HSP90AB1	physical	19380743
CSK_HUMAN	CSK	physical	19380743
HSP76_HUMAN	HSPA6	physical	19380743
MYH11_HUMAN	MYH11	physical	19380743
ACLY_HUMAN	ACLY	physical	19380743
AP2A2_HUMAN	AP2A2	physical	19380743
RUVB2_HUMAN	RUVBL2	physical	19380743
ABL1_HUMAN	ABL1	physical	19380743
K2C3_HUMAN	KRT3	physical	19380743
UBS3B_HUMAN	UBASH3B	physical	19380743
DYN2_HUMAN	DNM2	physical	19380743
HS90A_HUMAN	HSP90AA1	physical	19380743
CRK_HUMAN	CRK	physical	19380743
RBGPR_HUMAN	RAB3GAP2	physical	19380743
MYH14_HUMAN	MYH14	physical	19380743
P85B_HUMAN	PIK3R2	physical	19380743
PRKDC_HUMAN	PRKDC	physical	19380743
K1C17_HUMAN	KRT17	physical	19380743
AP2M1_HUMAN	AP2M1	physical	19380743
ELP1_HUMAN	IKBKAP	physical	19380743
TBAL3_HUMAN	TUBAL3	physical	19380743
RUVB1_HUMAN	RUVBL1	physical	19380743
BCR_HUMAN	BCR	physical	19380743
COR1C_HUMAN	CORO1C	physical	19380743
TIM50_HUMAN	TIMM50	physical	19380743
ANM5_HUMAN	PRMT5	physical	19380743
SC16A_HUMAN	SEC16A	physical	19380743
K2C1B_HUMAN	KRT77	physical	19380743
DNJA2_HUMAN	DNAJA2	physical	19380743
NEB2_HUMAN	PPP1R9B	physical	19380743
SOS2_HUMAN	SOS2	physical	19380743
MYO1C_HUMAN	MYO1C	physical	19380743
K1C13_HUMAN	KRT13	physical	19380743
DNJA1_HUMAN	DNAJA1	physical	19380743
P85A_HUMAN	PIK3R1	physical	19380743
SYIC_HUMAN	IARS	physical	19380743
S10A8_HUMAN	S100A8	physical	19380743
RS19_HUMAN	RPS19	physical	19380743
ATD3B_HUMAN	ATAD3B	physical	19380743
TCPB_HUMAN	CCT2	physical	19380743
AIFM1_HUMAN	AIFM1	physical	19380743
SYVC_HUMAN	VARS	physical	19380743
S10A9_HUMAN	S100A9	physical	19380743
HNRH1_HUMAN	HNRNPH1	physical	19380743
ARAP1_HUMAN	ARAP1	physical	19380743
CLH1_HUMAN	CLTC	physical	19380743
UBP15_HUMAN	USP15	physical	19380743
PRDX1_HUMAN	PRDX1	physical	19380743
TEC_HUMAN	TEC	physical	19380743
DDX5_HUMAN	DDX5	physical	19380743
HAX1_HUMAN	HAX1	physical	19380743
TCPZ_HUMAN	CCT6A	physical	19380743
CBL_HUMAN	CBL	physical	19380743
DDB1_HUMAN	DDB1	physical	19380743
S10A7_HUMAN	S100A7	physical	19380743
ANXA2_HUMAN	ANXA2	physical	19380743
CRK_HUMAN	CRK	physical	9617486
CBL_HUMAN	CBL	physical	9541596
GRB2_HUMAN	GRB2	physical	9541596
P85A_HUMAN	PIK3R1	physical	9541596
GRB2_HUMAN	GRB2	physical	10049786
GRB2_HUMAN	GRB2	physical	22974441
ERBB4_HUMAN	ERBB4	physical	16273093
EGFR_HUMAN	EGFR	physical	23799367
HGF_RAT	Hgf	physical	7953556
GRB2_RAT	Grb2	physical	7953556
EGFR_HUMAN	EGFR	physical	7506413
SOCS5_MOUSE	Socs5	physical	23990909
GRB2_HUMAN	GRB2	physical	11370743
CLIC4_HUMAN	CLIC4	physical	26344197
METK1_HUMAN	MAT1A	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
SERB_HUMAN	PSPH	physical	26344197
INSR_HUMAN	INSR	physical	7499194
ACTB_HUMAN	ACTB	physical	24189400
ACTG_HUMAN	ACTG1	physical	24189400
AP2A1_HUMAN	AP2A1	physical	24189400
AP2A2_HUMAN	AP2A2	physical	24189400
ARHG5_HUMAN	ARHGEF5	physical	24189400
EGFR_HUMAN	EGFR	physical	24189400
ERRFI_HUMAN	ERRFI1	physical	24189400
GFAP_HUMAN	GFAP	physical	24189400
GRB2_HUMAN	GRB2	physical	24189400
HNRPU_HUMAN	HNRNPU	physical	24189400
HSP7C_HUMAN	HSPA8	physical	24189400
LG3BP_HUMAN	LGALS3BP	physical	24189400
MYH9_HUMAN	MYH9	physical	24189400
PTN12_HUMAN	PTPN12	physical	24189400
SHC1_HUMAN	SHC1	physical	24189400
TRY3_HUMAN	PRSS3	physical	24189400
AP2M1_HUMAN	AP2M1	physical	24189400
ROA2_HUMAN	HNRNPA2B1	physical	24189400
S10A8_HUMAN	S100A8	physical	24189400
S10A9_HUMAN	S100A9	physical	24189400
UBS3B_HUMAN	UBASH3B	physical	24189400
CSF3R_HUMAN	CSF3R	physical	14557262
LTK_HUMAN	LTK	physical	7650032
GRB2_HUMAN	GRB2	physical	8810340
EGFR_HUMAN	EGFR	physical	8810340
EGFR_HUMAN	EGFR	physical	10766863
GRB2_HUMAN	GRB2	physical	24430869
EGFR_HUMAN	EGFR	physical	24430869
SHC2_HUMAN	SHC2	physical	28514442
NGAP_HUMAN	RASAL2	physical	28514442
PEAK1_HUMAN	PEAK1	physical	28514442
GARE1_HUMAN	GAREM	physical	28514442
AP2A1_HUMAN	AP2A1	physical	28514442
DCAM_HUMAN	AMD1	physical	28514442
AP1B1_HUMAN	AP1B1	physical	28514442
GRB2_HUMAN	GRB2	physical	9032244
SHIP1_HUMAN	INPP5D	physical	12149229
GRB2_HUMAN	GRB2	physical	12149229
GRB2_HUMAN	GRB2	physical	16371368
SOS1_HUMAN	SOS1	physical	16371368

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
There are no disease associations of PTM sites.

Regulatory Network of SHC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-426 AND TYR-427, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"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-139 AND TYR-427, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-139, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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-139 AND TYR-427, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"The Shc adaptor protein is highly phosphorylated at conserved, twintyrosine residues (Y239/240) that mediate protein-proteininteractions."; van der Geer P., Wiley S., Gish G.D., Pawson T.; Curr. Biol. 6:1435-1444(1996). Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES.	8939605 [Abstract]
"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 TYR-427, AND MASSSPECTROMETRY.	19690332 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349 AND TYR-427, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349; TYR-350 ANDTYR-427, AND MASS SPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349; TYR-350 ANDTYR-427, AND MASS SPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349; TYR-350 ANDTYR-427, AND MASS SPECTROMETRY.	15951569 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-427, AND MASSSPECTROMETRY.	12522270 [Abstract]

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