dbPTM

PTN11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN11_HUMAN
UniProt AC	Q06124
Protein Name	Tyrosine-protein phosphatase non-receptor type 11
Gene Name	PTPN11
Organism	Homo sapiens (Human).
Sequence Length	597
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. [PubMed: 28074573 Dephosphorylates GAB1, ARHGAP35 and EGFR]
Protein Sequence	MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQALLQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTSRRWFHP ------CCCCCCCCC	30.82	19413330
28	Phosphorylation	LTRGVDGSFLARPSK EECCCCCCEECCCCC	16.78	17855441
34	Phosphorylation	GSFLARPSKSNPGDF CCEECCCCCCCCCCC	43.07	23312004
35	Ubiquitination	SFLARPSKSNPGDFT CEECCCCCCCCCCCE	57.86	33845483
35	Malonylation	SFLARPSKSNPGDFT CEECCCCCCCCCCCE	57.86	26320211
36	Phosphorylation	FLARPSKSNPGDFTL EECCCCCCCCCCCEE	53.23	20873877
42	Phosphorylation	KSNPGDFTLSVRRNG CCCCCCCEEEEEECC	23.90	28270605
52	Phosphorylation	VRRNGAVTHIKIQNT EEECCEEEEEEEEEC	19.83	30576142
55	Acetylation	NGAVTHIKIQNTGDY CCEEEEEEEEECCCE	30.54	25953088
59	Phosphorylation	THIKIQNTGDYYDLY EEEEEEECCCEECCC	18.30	23927012
62	Phosphorylation	KIQNTGDYYDLYGGE EEEECCCEECCCCCC	10.54	25159151
63	Phosphorylation	IQNTGDYYDLYGGEK EEECCCEECCCCCCH	12.29	27273156
66	Phosphorylation	TGDYYDLYGGEKFAT CCCEECCCCCCHHHH	21.86	23927012
73	Phosphorylation	YGGEKFATLAELVQY CCCCHHHHHHHHHHH	29.63	-
80	Phosphorylation	TLAELVQYYMEHHGQ HHHHHHHHHHHHCCC	9.41	-
82	Sulfoxidation	AELVQYYMEHHGQLK HHHHHHHHHHCCCCC	3.17	30846556
91	Malonylation	HHGQLKEKNGDVIEL HCCCCCHHCCCEEEE	65.72	26320211
91	Acetylation	HHGQLKEKNGDVIEL HCCCCCHHCCCEEEE	65.72	25953088
99	Acetylation	NGDVIELKYPLNCAD CCCEEEEEEECCCCC	31.84	26051181
119	Ubiquitination	WFHGHLSGKEAEKLL CCCCCCCHHHHHHHH	37.88	32015554
120	Ubiquitination	FHGHLSGKEAEKLLT CCCCCCHHHHHHHHH	50.83	32015554
123	Ubiquitination	HLSGKEAEKLLTEKG CCCHHHHHHHHHHCC	45.38	33845483
124	Ubiquitination	LSGKEAEKLLTEKGK CCHHHHHHHHHHCCC	56.71	33845483
131	Ubiquitination	KLLTEKGKHGSFLVR HHHHHCCCCCCEEEE	56.72	29967540
131	Malonylation	KLLTEKGKHGSFLVR HHHHHCCCCCCEEEE	56.72	26320211
131	Acetylation	KLLTEKGKHGSFLVR HHHHHCCCCCCEEEE	56.72	25953088
140	Phosphorylation	GSFLVRESQSHPGDF CCEEEEECCCCCCCE	26.81	25159151
142	Phosphorylation	FLVRESQSHPGDFVL EEEEECCCCCCCEEE	40.71	25159151
153	Phosphorylation	DFVLSVRTGDDKGES CEEEEEEECCCCCCC	42.69	-
156	Ubiquitination	LSVRTGDDKGESNDG EEEEECCCCCCCCCC	63.30	24816145
157	Ubiquitination	SVRTGDDKGESNDGK EEEECCCCCCCCCCC	70.13	24816145
160	Phosphorylation	TGDDKGESNDGKSKV ECCCCCCCCCCCCCE	49.22	26552605
165	Phosphorylation	GESNDGKSKVTHVMI CCCCCCCCCEEEEEE	37.58	26552605
178	Acetylation	MIRCQELKYDVGGGE EEEEEEEEEECCCCC	38.36	26051181
179	Phosphorylation	IRCQELKYDVGGGER EEEEEEEEECCCCCC	28.61	-
189	Phosphorylation	GGGERFDSLTDLVEH CCCCCCCCHHHHHHH	30.38	23312004
191	Phosphorylation	GERFDSLTDLVEHYK CCCCCCHHHHHHHHH	31.10	23312004
197	Ubiquitination	LTDLVEHYKKNPMVE HHHHHHHHHHCCHHH	15.34	21890473
197	Phosphorylation	LTDLVEHYKKNPMVE HHHHHHHHHHCCHHH	15.34	23312004
198	Acetylation	TDLVEHYKKNPMVET HHHHHHHHHCCHHHH	48.24	23954790
198	Ubiquitination	TDLVEHYKKNPMVET HHHHHHHHHCCHHHH	48.24	21890473
198 (in isoform 1)	Ubiquitination	-	48.24	21890473
198 (in isoform 2)	Ubiquitination	-	48.24	21890473
198 (in isoform 3)	Ubiquitination	-	48.24	21890473
213	Acetylation	LGTVLQLKQPLNTTR HHHHHHHCCCCCCCC	36.59	25953088
228	Phosphorylation	INAAEIESRVRELSK CCHHHHHHHHHHHHH	41.56	21130716
234	Phosphorylation	ESRVRELSKLAETTD HHHHHHHHHHHHHCH	22.37	29449344
235	Ubiquitination	SRVRELSKLAETTDK HHHHHHHHHHHHCHH	65.43	29967540
242	Ubiquitination	KLAETTDKVKQGFWE HHHHHCHHHHHHHHH	49.60	29967540
242	Acetylation	KLAETTDKVKQGFWE HHHHHCHHHHHHHHH	49.60	25953088
244	Ubiquitination	AETTDKVKQGFWEEF HHHCHHHHHHHHHHH	50.90	29967540
244	2-Hydroxyisobutyrylation	AETTDKVKQGFWEEF HHHCHHHHHHHHHHH	50.90	-
260	Ubiquitination	TLQQQECKLLYSRKE HHHHHHHHHHHHCHH	40.55	29967540
263	Phosphorylation	QQECKLLYSRKEGQR HHHHHHHHHCHHHHC	19.50	20736484
264	Phosphorylation	QECKLLYSRKEGQRQ HHHHHHHHCHHHHCH	36.52	24719451
274	Acetylation	EGQRQENKNKNRYKN HHHCHHCCCCCCCCC	69.42	18526083
276	Acetylation	QRQENKNKNRYKNIL HCHHCCCCCCCCCCC	44.40	18526093
279	Phosphorylation	ENKNKNRYKNILPFD HCCCCCCCCCCCCCC	20.13	18707149
280	Acetylation	NKNKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	19608861
280	Ubiquitination	NKNKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	29967540
280	Malonylation	NKNKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	26320211
302	Phosphorylation	GDPNEPVSDYINANI CCCCCCHHHHCCCEE	35.10	29978859
304	Phosphorylation	PNEPVSDYINANIIM CCCCHHHHCCCEEEC	6.64	25884760
316	Phosphorylation	IIMPEFETKCNNSKP EECCCCCCCCCCCCC	46.33	26552605
317	Ubiquitination	IMPEFETKCNNSKPK ECCCCCCCCCCCCCC	27.97	29967540
355	Sulfoxidation	ENSRVIVMTTKEVER CCCEEEEEECCCHHC	2.43	30846556
357	Ubiquitination	SRVIVMTTKEVERGK CEEEEEECCCHHCCC	13.70	24816145
358	Ubiquitination	RVIVMTTKEVERGKS EEEEEECCCHHCCCC	51.07	24816145
358	Acetylation	RVIVMTTKEVERGKS EEEEEECCCHHCCCC	51.07	26051181
370	Phosphorylation	GKSKCVKYWPDEYAL CCCCCCCCCCCHHHH	11.19	28270605
375	Phosphorylation	VKYWPDEYALKEYGV CCCCCCHHHHHHHCC	25.31	28270605
389	Ubiquitination	VMRVRNVKESAAHDY CEEEECCCHHHHCCC	49.88	29967540
389	2-Hydroxyisobutyrylation	VMRVRNVKESAAHDY CEEEECCCHHHHCCC	49.88	-
397	Phosphorylation	ESAAHDYTLRELKLS HHHHCCCCHHHHCHH	25.95	24719451
401	Ubiquitination	HDYTLRELKLSKVGQ CCCCHHHHCHHHHHH	5.67	27667366
402	Ubiquitination	DYTLRELKLSKVGQA CCCHHHHCHHHHHHH	46.06	27667366
415	Phosphorylation	QALLQGNTERTVWQY HHHHCCCCCCEEEEE	33.40	17855441
486	Acetylation	LIDIIREKGVDCDID HHHHHHHHCCCCCCC	55.15	23954790
486	Malonylation	LIDIIREKGVDCDID HHHHHHHHCCCCCCC	55.15	26320211
496	Acetylation	DCDIDVPKTIQMVRS CCCCCCCHHHHHHHH	59.10	26051181
496	Malonylation	DCDIDVPKTIQMVRS CCCCCCCHHHHHHHH	59.10	26320211
503	Phosphorylation	KTIQMVRSQRSGMVQ HHHHHHHHCCCCCCC	20.66	29438985
511	Phosphorylation	QRSGMVQTEAQYRFI CCCCCCCCHHHHHHH	23.13	29438985
515	Phosphorylation	MVQTEAQYRFIYMAV CCCCHHHHHHHHHHH	17.97	20090780
519	Phosphorylation	EAQYRFIYMAVQHYI HHHHHHHHHHHHHHH	4.02	23898821
535	Phosphorylation	TLQRRIEEEQKSKRK HHHHHHHHHHHHHHC	64.45	24719451
535	Ubiquitination	TLQRRIEEEQKSKRK HHHHHHHHHHHHHHC	64.45	24816145
536	Ubiquitination	LQRRIEEEQKSKRKG HHHHHHHHHHHHHCC	50.98	24816145
538	Ubiquitination	RRIEEEQKSKRKGHE HHHHHHHHHHHCCCC	62.31	29967540
539	Ubiquitination	RIEEEQKSKRKGHEY HHHHHHHHHHCCCCC	37.07	24816145
539	Phosphorylation	RIEEEQKSKRKGHEY HHHHHHHHHHCCCCC	37.07	24719451
540	Ubiquitination	IEEEQKSKRKGHEYT HHHHHHHHHCCCCCC	66.23	24816145
542	Phosphorylation	EEQKSKRKGHEYTNI HHHHHHHCCCCCCCC	69.25	8041791
542	Ubiquitination	EEQKSKRKGHEYTNI HHHHHHHCCCCCCCC	69.25	29967540
546	Phosphorylation	SKRKGHEYTNIKYSL HHHCCCCCCCCCEEE	10.22	27273156
547	Phosphorylation	KRKGHEYTNIKYSLA HHCCCCCCCCCEEEC	27.73	27273156
551	Phosphorylation	HEYTNIKYSLADQTS CCCCCCCEEECCCCC	12.72	28122231
552	Phosphorylation	EYTNIKYSLADQTSG CCCCCCEEECCCCCC	16.45	25159151
557	Phosphorylation	KYSLADQTSGDQSPL CEEECCCCCCCCCCC	34.91	23401153
558	Phosphorylation	YSLADQTSGDQSPLP EEECCCCCCCCCCCC	34.44	30278072
561	Phosphorylation	ADQTSGDQSPLPPCT CCCCCCCCCCCCCCC	50.93	32142685
562	Phosphorylation	DQTSGDQSPLPPCTP CCCCCCCCCCCCCCC	32.89	30278072
564	Phosphorylation	TSGDQSPLPPCTPTP CCCCCCCCCCCCCCC	10.02	24719451
566	Phosphorylation	GDQSPLPPCTPTPPC CCCCCCCCCCCCCCC	42.15	32142685
568	Phosphorylation	QSPLPPCTPTPPCAE CCCCCCCCCCCCCHH	35.65	25159151
568	O-linked_Glycosylation	QSPLPPCTPTPPCAE CCCCCCCCCCCCCHH	35.65	OGP
570	Phosphorylation	PLPPCTPTPPCAEMR CCCCCCCCCCCHHHC	23.01	25159151
570	O-linked_Glycosylation	PLPPCTPTPPCAEMR CCCCCCCCCCCHHHC	23.01	OGP
576	Phosphorylation	PTPPCAEMREDSARV CCCCCHHHCCCHHHH	2.79	11781100
580	Phosphorylation	CAEMREDSARVYENV CHHHCCCHHHHHHHH	17.14	21945579
584	Phosphorylation	REDSARVYENVGLMQ CCCHHHHHHHHHHHH	9.02	12634870
589	Ubiquitination	RVYENVGLMQQQKSF HHHHHHHHHHHHHHC	2.14	23000965
590	Sumoylation	VYENVGLMQQQKSFR HHHHHHHHHHHHHCC	2.51	-
590	Sulfoxidation	VYENVGLMQQQKSFR HHHHHHHHHHHHHCC	2.51	30846556
590	Ubiquitination	VYENVGLMQQQKSFR HHHHHHHHHHHHHCC	2.51	23000965
591	Phosphorylation	YENVGLMQQQKSFR- HHHHHHHHHHHHCC-	47.82	24719451
593	Ubiquitination	NVGLMQQQKSFR--- HHHHHHHHHHCC---	26.86	23000965
594	Ubiquitination	VGLMQQQKSFR---- HHHHHHHHHCC----	47.42	23000965
594	Acetylation	VGLMQQQKSFR---- HHHHHHHHHCC----	47.42	25953088
595	Phosphorylation	GLMQQQKSFR----- HHHHHHHHCC-----	23.16	23401153

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
73	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
73	T	Phosphorylation	Kinase	PKACA	P17612	PSP
189	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
189	S	Phosphorylation	Kinase	PKACA	P17612	PSP
542	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP
542	Y	Phosphorylation	Kinase	PDGFRB	P09619	GPS
542	Y	Phosphorylation	Kinase	PDGFRB	P05622	PSP
542	Y	Phosphorylation	Kinase	PDGFR	-	Uniprot
542	Y	Phosphorylation	Kinase	FYN	P06241	PSP
546	Y	Phosphorylation	Kinase	FYN	P06241	GPS
546	Y	Phosphorylation	Kinase	ALK	Q9UM73	GPS
546	Y	Phosphorylation	Kinase	PDGFR-FAMILY	-	GPS
546	Y	Phosphorylation	Kinase	PDGFRB	P05622	GPS
546	Y	Phosphorylation	Kinase	PGFRB	P09619	PhosphoELM
576	S	Phosphorylation	Kinase	PKCA	P17252	PSP
576	S	Phosphorylation	Kinase	PKCB	P05771	PSP
576	S	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
576	S	Phosphorylation	Kinase	PKCH	P24723	PSP
580	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP
580	Y	Phosphorylation	Kinase	PDGFR	-	Uniprot
580	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
580	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
580	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
584	Y	Phosphorylation	Kinase	PDGFR-FAMILY	-	GPS
584	Y	Phosphorylation	Kinase	ALK	Q9UM73	GPS
591	S	Phosphorylation	Kinase	PKCH	P24723	PSP
591	S	Phosphorylation	Kinase	PKCB ISO2	P05771-2	PSP
591	S	Phosphorylation	Kinase	PKCB	P05771	PSP
591	S	Phosphorylation	Kinase	PKCA	P17252	PSP
595	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
595	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
595	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTN11_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PTN11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STA5A_HUMAN	STAT5A	physical	10617656
STA5B_HUMAN	STAT5B	physical	10617656
CSF3R_HUMAN	CSF3R	physical	9824671
JAK1_HUMAN	JAK1	physical	8995399
JAK2_HUMAN	JAK2	physical	8995399
SOCS3_HUMAN	SOCS3	physical	12403768
JAK1_HUMAN	JAK1	physical	12403768
PLCG2_HUMAN	PLCG2	physical	12135708
GAB2_HUMAN	GAB2	physical	12135708
IRS1_HUMAN	IRS1	physical	8505282
GAB3_HUMAN	GAB3	physical	11739737
IRS1_HUMAN	IRS1	physical	9756938
KIT_HUMAN	KIT	physical	7523381
LYAM2_HUMAN	SELE	physical	11602579
CAV1_HUMAN	CAV1	physical	12176037
CADH5_HUMAN	CDH5	physical	10681592
CTNB1_HUMAN	CTNNB1	physical	10681592
GRB2_HUMAN	GRB2	physical	10212213
PGFRB_HUMAN	PDGFRB	physical	7691811
FAK2_HUMAN	PTK2B	physical	10880513
GHR_HUMAN	GHR	physical	10976913
SOS1_HUMAN	SOS1	physical	9344843
GHR_HUMAN	GHR	physical	9632636
GRB2_HUMAN	GRB2	physical	8702859
CEAM1_HUMAN	CEACAM1	physical	9867848
INSR_HUMAN	INSR	physical	7493946
PTN11_HUMAN	PTPN11	physical	9847309
CBL_HUMAN	CBL	physical	18519587
P85A_HUMAN	PIK3R1	physical	9886492
FAK1_HUMAN	PTK2	physical	21726809
PAF1_HUMAN	PAF1	physical	21726809
CDC73_HUMAN	CDC73	physical	21726809
LEO1_HUMAN	LEO1	physical	21726809
CTR9_HUMAN	CTR9	physical	21726809
RTF1_HUMAN	RTF1	physical	21726809
WDR61_HUMAN	WDR61	physical	21726809
KIT_HUMAN	KIT	physical	12444928
SOCS3_HUMAN	SOCS3	physical	10777583
SHIP1_HUMAN	INPP5D	physical	11157475
CBL_HUMAN	CBL	physical	11157475
M3K5_HUMAN	MAP3K5	physical	19287004
FAS_HUMAN	FASN	physical	23269672
RFWD2_HUMAN	RFWD2	physical	23269672
IRS1_HUMAN	IRS1	physical	11781100
SIG12_MOUSE	Siglece	physical	11171044
GAB2_HUMAN	GAB2	physical	15356145
MTPN_HUMAN	MTPN	physical	22863883
RPIA_HUMAN	RPIA	physical	25416956
TRI32_HUMAN	TRIM32	physical	25416956
GRB2_HUMAN	GRB2	physical	7534299
LNX1_HUMAN	LNX1	physical	25814554
TXNIP_HUMAN	TXNIP	physical	26527736
TXNIP_HUMAN	TXNIP	physical	26919541
GAB1_HUMAN	GAB1	physical	14701753
DYN2_HUMAN	DNM2	physical	21996738
PGFRA_HUMAN	PDGFRA	physical	21996738
PRP19_HUMAN	PRPF19	physical	27213290
SHPS1_HUMAN	SIRPA	physical	10962556
P85A_HUMAN	PIK3R1	physical	10962556
P85A_HUMAN	PIK3R1	physical	11593409
ERBB4_HUMAN	ERBB4	physical	28065597
CTR9_HUMAN	CTR9	physical	27880917
PAF1_HUMAN	PAF1	physical	27880917
PTN11_HUMAN	PTPN11	physical	27432908
PTN6_HUMAN	PTPN6	physical	27432908
GAB1_HUMAN	GAB1	physical	20473329
GRB2_HUMAN	GRB2	physical	20473329
SHPS1_HUMAN	SIRPA	physical	20473329
ERBB2_HUMAN	ERBB2	physical	8959326
GRB2_HUMAN	GRB2	physical	8959326
BEX1_HUMAN	BEX1	physical	27229929
BEX2_HUMAN	BEX2	physical	27229929
GO45_HUMAN	BLZF1	physical	27229929
CI062_HUMAN	C9orf62	physical	27229929
CTDS1_HUMAN	CTDSP1	physical	27229929
DMRTC_HUMAN	DMRTC1	physical	27229929
F71E1_HUMAN	FAM71E1	physical	27229929
GOGA2_HUMAN	GOLGA2	physical	27229929
T2AG_HUMAN	GTF2A2	physical	27229929
NSUN5_HUMAN	NSUN5	physical	27229929
ORML3_HUMAN	ORMDL3	physical	27229929
PKHA4_HUMAN	PLEKHA4	physical	27229929
KCC1B_HUMAN	PNCK	physical	27229929
OBF1_HUMAN	POU2AF1	physical	27229929
MOG1_HUMAN	RANGRF	physical	27229929
SERF2_HUMAN	SERF2	physical	27229929
PEDF_HUMAN	SERPINF1	physical	27229929
SRS10_HUMAN	SRSF10	physical	27229929
S38A1_HUMAN	SLC38A1	physical	27229929
SARCO_HUMAN	SLN	physical	27229929
STAT1_HUMAN	STAT1	physical	27229929
TLK1_HUMAN	TLK1	physical	27229929
TRI32_HUMAN	TRIM32	physical	27229929
TRM2_HUMAN	TRMT2B	physical	27229929
GAB2_HUMAN	GAB2	physical	16371368
P85A_HUMAN	PIK3R1	physical	16371368
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
151100	LEOPARD syndrome 1 (LPRD1)
163950	Noonan syndrome 1 (NS1)
607785	Leukemia, juvenile myelomonocytic (JMML)
156250	Metachondromatosis (MC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PTN11_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-280, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-562, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584 AND SER-595, ANDMASS SPECTROMETRY.	17287340 [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-62 AND TYR-584, 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-62; TYR-63 AND TYR-584,AND MASS 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-62, AND MASSSPECTROMETRY.	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-62; TYR-63 AND TYR-584,AND MASS SPECTROMETRY.	18083107 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, AND MASSSPECTROMETRY.	16094384 [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-62, AND MASSSPECTROMETRY.	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-62, AND MASSSPECTROMETRY.	15951569 [Abstract]