dbPTM

FRS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FRS2_HUMAN
UniProt AC	Q8WU20
Protein Name	Fibroblast growth factor receptor substrate 2
Gene Name	FRS2
Organism	Homo sapiens (Human).
Sequence Length	508
Subcellular Localization	Endomembrane system. Cytoplasmic, membrane-bound.
Protein Description	Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1..
Protein Sequence	MGSCCSCPDKDTVPDNHRNKFKVINVDDDGNELGSGIMELTDTELILYTRKRDSVKWHYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCARAEELFNMLQEIMQNNSINVVEEPVVERNNHQTELEVPRTPRTPTTPGFAAQNLPNGYPRYPSFGDASSHPSSRHPSVGSARLPSVGEESTHPLLVAEEQVHTYVNTTGVQEERKNRTSVHVPLEARVSNAESSTPKEEPSSIEDRDPQILLEPEGVKFVLGPTPVQKQLMEKEKLEQLGRDQVSGSGANNTEWDTGYDSDERRDAPSVNKLVYENINGLSIPSASGVRRGRLTSTSTSDTQNINNSAQRRTALLNYENLPSLPPVWEARKLSRDEDDNLGPKTPSLNGYHNNLDPMHNYVNTENVTVPASAHKIEYSRRRDCTPTVFNFDIRRPSLEHRQLNYIQVDLEGGSDSDNPQTPKTPTTPLPQTPTRRTELYAVIDIERTAAMSNLQKALPRDDGTSRKTRHNSTDLPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGSCCSCPD ------CCCCCCCCC	29.41	-
2	Myristoylation	------MGSCCSCPD ------CCCCCCCCC	29.41	10092678
4	S-palmitoylation	----MGSCCSCPDKD ----CCCCCCCCCCC	1.31	31184863
5	S-palmitoylation	---MGSCCSCPDKDT ---CCCCCCCCCCCC	5.13	31184863
35	Phosphorylation	DDGNELGSGIMELTD CCCCEECCCEEEECC	37.46	28102081
41	Phosphorylation	GSGIMELTDTELILY CCCEEEECCCEEEEE	27.80	28102081
43	Phosphorylation	GIMELTDTELILYTR CEEEECCCEEEEEEC	27.70	28102081
48	Phosphorylation	TDTELILYTRKRDSV CCCEEEEEECCCCCC	9.48	28102081
49	Phosphorylation	DTELILYTRKRDSVK CCEEEEEECCCCCCC	26.69	22210691
54	Phosphorylation	LYTRKRDSVKWHYLC EEECCCCCCCEEEEE	29.63	22210691
59	Phosphorylation	RDSVKWHYLCLRRYG CCCCCEEEEEHHHHC	9.67	-
73	Phosphorylation	GYDSNLFSFESGRRC CCCCCCEEECCCCCC	31.13	-
76	Phosphorylation	SNLFSFESGRRCQTG CCCEEECCCCCCCCC	35.27	-
109	Phosphorylation	QEIMQNNSINVVEEP HHHHHCCCCCEEECC	24.08	27251275
125	Phosphorylation	VERNNHQTELEVPRT EECCCCCCEEECCCC	34.68	27273156
132	Phosphorylation	TELEVPRTPRTPTTP CEEECCCCCCCCCCC	15.85	29255136
135	Phosphorylation	EVPRTPRTPTTPGFA ECCCCCCCCCCCCCH	26.62	27273156
137	Phosphorylation	PRTPRTPTTPGFAAQ CCCCCCCCCCCCHHH	45.04	28152594
138	Phosphorylation	RTPRTPTTPGFAAQN CCCCCCCCCCCHHHC	23.71	27273156
150	Phosphorylation	AQNLPNGYPRYPSFG HHCCCCCCCCCCCCC	7.38	-
153	Phosphorylation	LPNGYPRYPSFGDAS CCCCCCCCCCCCCCC	9.95	23312004
155	Phosphorylation	NGYPRYPSFGDASSH CCCCCCCCCCCCCCC	32.69	20363803
160	Phosphorylation	YPSFGDASSHPSSRH CCCCCCCCCCCCCCC	33.64	20363803
161	Phosphorylation	PSFGDASSHPSSRHP CCCCCCCCCCCCCCC	40.93	23312004
164	Phosphorylation	GDASSHPSSRHPSVG CCCCCCCCCCCCCCC	34.28	28857561
165	Phosphorylation	DASSHPSSRHPSVGS CCCCCCCCCCCCCCC	38.77	23312004
169	Phosphorylation	HPSSRHPSVGSARLP CCCCCCCCCCCCCCC	32.74	26670566
172	Phosphorylation	SRHPSVGSARLPSVG CCCCCCCCCCCCCCC	14.20	27794612
177	Phosphorylation	VGSARLPSVGEESTH CCCCCCCCCCCCCCC	47.55	30266825
182	Phosphorylation	LPSVGEESTHPLLVA CCCCCCCCCCCEEEE	27.93	30266825
183	Phosphorylation	PSVGEESTHPLLVAE CCCCCCCCCCEEEEE	30.69	30266825
195	Phosphorylation	VAEEQVHTYVNTTGV EEEEEEHHHCCCCCC	30.24	28348404
196	Phosphorylation	AEEQVHTYVNTTGVQ EEEEEHHHCCCCCCC	4.10	25884760
200	Phosphorylation	VHTYVNTTGVQEERK EHHHCCCCCCCHHHC	30.10	-
210	Phosphorylation	QEERKNRTSVHVPLE CHHHCCCCEEECCCE	44.48	30266825
211	Phosphorylation	EERKNRTSVHVPLEA HHHCCCCEEECCCEE	13.64	30266825
221	Phosphorylation	VPLEARVSNAESSTP CCCEEECCCCCCCCC	25.43	30278072
225	Phosphorylation	ARVSNAESSTPKEEP EECCCCCCCCCCCCC	36.78	29255136
226	Phosphorylation	RVSNAESSTPKEEPS ECCCCCCCCCCCCCC	39.99	29255136
227	Phosphorylation	VSNAESSTPKEEPSS CCCCCCCCCCCCCCC	47.89	29255136
233	Phosphorylation	STPKEEPSSIEDRDP CCCCCCCCCCCCCCC	47.42	28857561
234	Phosphorylation	TPKEEPSSIEDRDPQ CCCCCCCCCCCCCCC	40.49	25849741
256	Phosphorylation	VKFVLGPTPVQKQLM CEEEECCCHHHHHHH	34.00	28674419
267	Ubiquitination	KQLMEKEKLEQLGRD HHHHHHHHHHHHCCC	69.28	-
277	Phosphorylation	QLGRDQVSGSGANNT HHCCCCCCCCCCCCC	22.93	29978859
279	Phosphorylation	GRDQVSGSGANNTEW CCCCCCCCCCCCCCC	27.50	29978859
284	Phosphorylation	SGSGANNTEWDTGYD CCCCCCCCCCCCCCC	37.96	23663014
288	Phosphorylation	ANNTEWDTGYDSDER CCCCCCCCCCCCHHC	38.42	23663014
290	Phosphorylation	NTEWDTGYDSDERRD CCCCCCCCCCHHCCC	17.86	23663014
292	Phosphorylation	EWDTGYDSDERRDAP CCCCCCCCHHCCCCC	32.65	30266825
300	Phosphorylation	DERRDAPSVNKLVYE HHCCCCCCHHHHHHH	39.79	27259358
306	Phosphorylation	PSVNKLVYENINGLS CCHHHHHHHCCCCCC	17.44	21945579
313	Phosphorylation	YENINGLSIPSASGV HHCCCCCCCCCCCCC	33.57	21945579
316	Phosphorylation	INGLSIPSASGVRRG CCCCCCCCCCCCCCC	33.14	21945579
318	Phosphorylation	GLSIPSASGVRRGRL CCCCCCCCCCCCCCC	42.00	21945579
326	Phosphorylation	GVRRGRLTSTSTSDT CCCCCCCCCCCCCCC	28.70	30576142
327	Phosphorylation	VRRGRLTSTSTSDTQ CCCCCCCCCCCCCCC	25.59	27273156
328	Phosphorylation	RRGRLTSTSTSDTQN CCCCCCCCCCCCCCC	30.68	21955146
329	O-linked_Glycosylation	RGRLTSTSTSDTQNI CCCCCCCCCCCCCCC	26.19	31492838
329	Phosphorylation	RGRLTSTSTSDTQNI CCCCCCCCCCCCCCC	26.19	25884760
330	Phosphorylation	GRLTSTSTSDTQNIN CCCCCCCCCCCCCCC	30.61	28985074
331	Phosphorylation	RLTSTSTSDTQNINN CCCCCCCCCCCCCCC	38.13	30576142
333	Phosphorylation	TSTSTSDTQNINNSA CCCCCCCCCCCCCHH	24.23	22210691
339	Phosphorylation	DTQNINNSAQRRTAL CCCCCCCHHHHHHHH	22.69	30177828
344	Phosphorylation	NNSAQRRTALLNYEN CCHHHHHHHHHCCCC	24.68	28796482
349	Phosphorylation	RRTALLNYENLPSLP HHHHHHCCCCCCCCC	13.23	20007894
354	Phosphorylation	LNYENLPSLPPVWEA HCCCCCCCCCCHHHH	57.59	26356563
365	Phosphorylation	VWEARKLSRDEDDNL HHHHHHCCCCCCCCC	40.49	28355574
378	Phosphorylation	NLGPKTPSLNGYHNN CCCCCCCCCCCCCCC	39.43	26356563
392	Phosphorylation	NLDPMHNYVNTENVT CCCCCCCCCCCCCCE	4.76	25884760
395	Phosphorylation	PMHNYVNTENVTVPA CCCCCCCCCCCEEEC	20.92	-
403	Phosphorylation	ENVTVPASAHKIEYS CCCEEECCCCCCEEE	25.49	25884760
428	Phosphorylation	NFDIRRPSLEHRQLN EEECCCCCCCCCCCC	44.57	30266825
436	Phosphorylation	LEHRQLNYIQVDLEG CCCCCCCEEEEECCC	11.00	9632781
436	Dephosphorylation	LEHRQLNYIQVDLEG CCCCCCCEEEEECCC	11.00	9632781
445	Phosphorylation	QVDLEGGSDSDNPQT EEECCCCCCCCCCCC	44.81	28348404
447	Phosphorylation	DLEGGSDSDNPQTPK ECCCCCCCCCCCCCC	40.77	30278072
455	Phosphorylation	DNPQTPKTPTTPLPQ CCCCCCCCCCCCCCC	27.37	27732954
457	Phosphorylation	PQTPKTPTTPLPQTP CCCCCCCCCCCCCCC	46.40	25159151
458	Phosphorylation	QTPKTPTTPLPQTPT CCCCCCCCCCCCCCC	24.83	25159151
463	Phosphorylation	PTTPLPQTPTRRTEL CCCCCCCCCCCCCEE	25.37	25159151
465	Phosphorylation	TPLPQTPTRRTELYA CCCCCCCCCCCEEEE	35.85	27732954
468	Phosphorylation	PQTPTRRTELYAVID CCCCCCCCEEEEEEE	27.35	20068231
471	Phosphorylation	PTRRTELYAVIDIER CCCCCEEEEEEEHHH	7.81	25884760
479	Phosphorylation	AVIDIERTAAMSNLQ EEEEHHHHHHHHHHH	13.13	20068231
483	Phosphorylation	IERTAAMSNLQKALP HHHHHHHHHHHHHCC	29.66	20068231
495	Phosphorylation	ALPRDDGTSRKTRHN HCCCCCCCCCCCCCC	32.14	24702127
496	Phosphorylation	LPRDDGTSRKTRHNS CCCCCCCCCCCCCCC	36.99	24702127
499	Phosphorylation	DDGTSRKTRHNSTDL CCCCCCCCCCCCCCC	35.73	29514088
503	Phosphorylation	SRKTRHNSTDLPM-- CCCCCCCCCCCCC--	19.71	22617229
504	Phosphorylation	RKTRHNSTDLPM--- CCCCCCCCCCCC---	47.04	28985074

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
196	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
306	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
349	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
392	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
436	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
471	Y	Phosphorylation	Kinase	FGFR1	P11362	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:11997436

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FRS2_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 FRS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN11_HUMAN	PTPN11	physical	10650943
GRB2_HUMAN	GRB2	physical	8780727
GRB2_HUMAN	GRB2	physical	11997436
SOS1_HUMAN	SOS1	physical	11997436
CBL_HUMAN	CBL	physical	11997436
NTRK1_HUMAN	NTRK1	physical	10092678
NTRK2_HUMAN	NTRK2	physical	10092678
NTRK3_HUMAN	NTRK3	physical	10092678
RET_HUMAN	RET	physical	11360177
PTN11_HUMAN	PTPN11	physical	11360177
PTN11_HUMAN	PTPN11	physical	9632781
CBL_HUMAN	CBL	physical	17944804
FLOT1_HUMAN	FLOT1	physical	22235335
SRBS1_HUMAN	SORBS1	physical	22235335
SPY2_HUMAN	SPRY2	physical	15004239
GRB2_HUMAN	GRB2	physical	15004239
GRB2_HUMAN	GRB2	physical	22974441
PTN11_HUMAN	PTPN11	physical	22974441
GRB2_HUMAN	GRB2	physical	16893902
SOS1_HUMAN	SOS1	physical	16893902
BECN1_HUMAN	BECN1	physical	25814554
RS6_HUMAN	RPS6	physical	25814554
GRB2_HUMAN	GRB2	physical	25159185
PTN11_HUMAN	PTPN11	physical	25159185
PTN11_MOUSE	Ptpn11	physical	25159185
GRB2_MOUSE	Grb2	physical	25159185
GAB1_MOUSE	Gab1	physical	25159185
FGFR2_HUMAN	FGFR2	physical	15629145
EPHA4_HUMAN	EPHA4	physical	16365308

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 FRS2_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"The signaling adapter FRS-2 competes with Shc for binding to thenerve growth factor receptor TrkA. A model for discriminatingproliferation and differentiation."; Meakin S.O., MacDonald J.I.S., Gryz E.A., Kubu C.J., Verdi J.M.; J. Biol. Chem. 274:9861-9870(1999). Cited for: INTERACTION WITH CKS2; GRB2; PTPN11; SRC; NTRK1; NTRK2 AND NTRK3,MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYROSINE RESIDUES, ANDTISSUE SPECIFICITY.	10092678 [Abstract]
"Novel recognition motif on fibroblast growth factor receptor mediatesdirect association and activation of SNT adapter proteins."; Xu H., Lee K.W., Goldfarb M.P.; J. Biol. Chem. 273:17987-17990(1998). Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR1, MYRISTOYLATION ATGLY-2, AND PHOSPHORYLATION AT TYROSINE RESIDUES.	9660748 [Abstract]