dbPTM

GRB7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRB7_HUMAN
UniProt AC	Q14451
Protein Name	Growth factor receptor-bound protein 7
Gene Name	GRB7
Organism	Homo sapiens (Human).
Sequence Length	532
Subcellular Localization	Cytoplasm . Cell junction, focal adhesion . Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasmic granule . Cell projection . Predominantly cytoplasmic. Detected in stress granules, where mRNA is stored under stress conditions.
Protein Description	Adapter protein that interacts with the cytoplasmic domain of numerous receptor kinases and modulates down-stream signaling. Promotes activation of down-stream protein kinases, including STAT3, AKT1, MAPK1 and/or MAPK3. Promotes activation of HRAS. Plays a role in signal transduction in response to EGF. Plays a role in the regulation of cell proliferation and cell migration. Plays a role in the assembly and stability of RNA stress granules. Binds to the 5'UTR of target mRNA molecules and represses translation of target mRNA species, when not phosphorylated. Phosphorylation impairs RNA binding and promotes stress granule disassembly during recovery after cellular stress (By similarity)..
Protein Sequence	MELDLSPPHLSSSPEDLCPAPGTPPGTPRPPDTPLPEEVKRSQPLLIPTTGRKLREEERRATSLPSIPNPFPELCSPPSQSPILGGPSSARGLLPRDASRPHVVKVYSEDGACRSVEVAAGATARHVCEMLVQRAHALSDETWGLVECHPHLALERGLEDHESVVEVQAAWPVGGDSRFVFRKNFAKYELFKSSPHSLFPEKMVSSCLDAHTGISHEDLIQNFLNAGSFPEIQGFLQLRGSGRKLWKRFFCFLRRSGLYYSTKGTSKDPRHLQYVADVNESNVYVVTQGRKLYGMPTDFGFCVKPNKLRNGHKGLRIFCSEDEQSRTCWLAAFRLFKYGVQLYKNYQQAQSRHLHPSCLGSPPLRSASDNTLVAMDFSGHAGRVIENPREALSVALEEAQAWRKKTNHRLSLPMPASGTSLSAAIHRTQLWFHGRISREESQRLIGQQGLVDGLFLVRESQRNPQGFVLSLCHLQKVKHYLILPSEEEGRLYFSMDDGQTRFTDLLQLVEFHQLNRGILPCLLRHCCTRVAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MELDLSPPHLSSS --CCCCCCCCCCCCC	35.73	23090842
11	Phosphorylation	DLSPPHLSSSPEDLC CCCCCCCCCCHHHHC	26.24	23090842
12	Phosphorylation	LSPPHLSSSPEDLCP CCCCCCCCCHHHHCC	57.16	23090842
13	Phosphorylation	SPPHLSSSPEDLCPA CCCCCCCCHHHHCCC	29.00	23090842
23	Phosphorylation	DLCPAPGTPPGTPRP HHCCCCCCCCCCCCC	25.83	25849741
27	Phosphorylation	APGTPPGTPRPPDTP CCCCCCCCCCCCCCC	23.15	25106551
33	Phosphorylation	GTPRPPDTPLPEEVK CCCCCCCCCCCHHHH	32.28	23090842
42	Phosphorylation	LPEEVKRSQPLLIPT CCHHHHHCCCEEECC	30.36	24505115
49	Phosphorylation	SQPLLIPTTGRKLRE CCCEEECCCCCCHHH	34.58	23911959
50	Phosphorylation	QPLLIPTTGRKLREE CCEEECCCCCCHHHH	29.63	23911959
62	Phosphorylation	REEERRATSLPSIPN HHHHHHHCCCCCCCC	29.05	27966365
63	Phosphorylation	EEERRATSLPSIPNP HHHHHHCCCCCCCCC	36.98	27422710
65	Phosphorylation	ERRATSLPSIPNPFP HHHHCCCCCCCCCCH	29.94	24719451
66	Phosphorylation	RRATSLPSIPNPFPE HHHCCCCCCCCCCHH	56.84	26657352
76	Phosphorylation	NPFPELCSPPSQSPI CCCHHHCCCCCCCCC	53.09	25106551
79	Phosphorylation	PELCSPPSQSPILGG HHHCCCCCCCCCCCC	46.83	26657352
81	Phosphorylation	LCSPPSQSPILGGPS HCCCCCCCCCCCCCC	20.46	27050516
85	Phosphorylation	PSQSPILGGPSSARG CCCCCCCCCCCCCCC	46.84	24719451
86	Phosphorylation	SQSPILGGPSSARGL CCCCCCCCCCCCCCC	18.57	24719451
88	Phosphorylation	SPILGGPSSARGLLP CCCCCCCCCCCCCCC	39.65	23090842
89	Phosphorylation	PILGGPSSARGLLPR CCCCCCCCCCCCCCC	25.72	23090842
99	Phosphorylation	GLLPRDASRPHVVKV CCCCCCCCCCEEEEE	51.11	24719451
104	Phosphorylation	DASRPHVVKVYSEDG CCCCCEEEEEECCCC	2.93	24719451
106	Phosphorylation	SRPHVVKVYSEDGAC CCCEEEEEECCCCCC	4.26	17016520
107	Phosphorylation	RPHVVKVYSEDGACR CCEEEEEECCCCCCC	10.71	27273156
108	Phosphorylation	PHVVKVYSEDGACRS CEEEEEECCCCCCCE	32.00	28152594
130	Phosphorylation	TARHVCEMLVQRAHA CHHHHHHHHHHHHHH	3.62	27251275
139	Phosphorylation	VQRAHALSDETWGLV HHHHHHCCCCCCCCC	33.90	27251275
142	Phosphorylation	AHALSDETWGLVECH HHHCCCCCCCCCCCC	29.80	27251275
162	Phosphorylation	ERGLEDHESVVEVQA HHCCCCCCCEEEEEE	58.51	27251275
188	Phosphorylation	FRKNFAKYELFKSSP EECCCHHHHHHHCCC	17.90	19473962
193	Phosphorylation	AKYELFKSSPHSLFP HHHHHHHCCCHHHCC	41.59	25159151
194	Phosphorylation	KYELFKSSPHSLFPE HHHHHHCCCHHHCCH	27.50	28985074
197	Phosphorylation	LFKSSPHSLFPEKMV HHHCCCHHHCCHHHH	34.78	27251275
216	Phosphorylation	DAHTGISHEDLIQNF HCCCCCCHHHHHHHH	30.57	27251275
259	Phosphorylation	FLRRSGLYYSTKGTS HHHHCCCEEECCCCC	10.01	26356563
262	Phosphorylation	RSGLYYSTKGTSKDP HCCCEEECCCCCCCC	19.85	26356563
274	Phosphorylation	KDPRHLQYVADVNES CCCCCEEEEEECCCC	12.17	28102081
281	Phosphorylation	YVADVNESNVYVVTQ EEEECCCCCEEEEEC	26.79	28102081
284	Phosphorylation	DVNESNVYVVTQGRK ECCCCCEEEEECCCE	8.08	28152594
287	Phosphorylation	ESNVYVVTQGRKLYG CCCEEEEECCCEEEC	18.43	28152594
291	Acetylation	YVVTQGRKLYGMPTD EEEECCCEEECCCCC	53.54	19807371
307	Acetylation	GFCVKPNKLRNGHKG CEEECCCCCCCCCCC	58.30	19807379
307	Phosphorylation	GFCVKPNKLRNGHKG CEEECCCCCCCCCCC	58.30	27251275
338	Phosphorylation	AAFRLFKYGVQLYKN HHHHHHHHHHHHHHH	18.39	19473962
343	Phosphorylation	FKYGVQLYKNYQQAQ HHHHHHHHHHHHHHH	4.70	-
357	Phosphorylation	QSRHLHPSCLGSPPL HHCCCCHHHHCCCCC	15.95	30108239
361	Phosphorylation	LHPSCLGSPPLRSAS CCHHHHCCCCCCCCC	15.47	9710451
366	Phosphorylation	LGSPPLRSASDNTLV HCCCCCCCCCCCCEE	39.55	27050516
368	Phosphorylation	SPPLRSASDNTLVAM CCCCCCCCCCCEEEE	32.41	28176443
371	Phosphorylation	LRSASDNTLVAMDFS CCCCCCCCEEEEECC	27.83	25106551
378	Phosphorylation	TLVAMDFSGHAGRVI CEEEEECCCCCCCEE	25.96	28176443
384	Phosphorylation	FSGHAGRVIENPREA CCCCCCCEECCHHHH	6.69	24719451
389	Phosphorylation	GRVIENPREALSVAL CCEECCHHHHHHHHH	54.09	24719451
393	Phosphorylation	ENPREALSVALEEAQ CCHHHHHHHHHHHHH	16.64	27251275
401	Phosphorylation	VALEEAQAWRKKTNH HHHHHHHHHHHHCCC	18.32	27251275
406	Phosphorylation	AQAWRKKTNHRLSLP HHHHHHHCCCCCCCC	39.01	28857561
411	Phosphorylation	KKTNHRLSLPMPASG HHCCCCCCCCCCCCC	30.31	28985074
416	Phosphorylation	RLSLPMPASGTSLSA CCCCCCCCCCCCHHH	17.84	27251275
417	Phosphorylation	LSLPMPASGTSLSAA CCCCCCCCCCCHHHH	36.41	27794612
419	Phosphorylation	LPMPASGTSLSAAIH CCCCCCCCCHHHHHH	24.81	27794612
420	Phosphorylation	PMPASGTSLSAAIHR CCCCCCCCHHHHHHH	24.69	28102081
434	Phosphorylation	RTQLWFHGRISREES HHHHHHCCCCCHHHH	21.10	24719451
440	Phosphorylation	HGRISREESQRLIGQ CCCCCHHHHHHHHCC	51.57	27251275
442	Phosphorylation	RISREESQRLIGQQG CCCHHHHHHHHCCCC	47.69	27251275

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
188	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
194	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
338	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRB7_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 GRB7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LY66F_HUMAN	LY6G6F	physical	12852788
ERBB3_HUMAN	ERBB3	physical	9516479
KIT_HUMAN	KIT	physical	10377264
RND1_HUMAN	RND1	physical	10664463
RET_HUMAN	RET	physical	8631863
ERBB2_HUMAN	ERBB2	physical	9079677
FAK1_HUMAN	PTK2	physical	10446223
EPHB1_HUMAN	EPHB1	physical	12223469
INSR_HUMAN	INSR	physical	10803466
RS2_HUMAN	RPS2	physical	21900206
ZBT16_HUMAN	ZBTB16	physical	21900206
A1BG_HUMAN	A1BG	physical	21900206
ATPB_HUMAN	ATP5B	physical	21900206
CPNE6_HUMAN	CPNE6	physical	21900206
KPYM_HUMAN	PKM	physical	21900206
DC1I1_HUMAN	DYNC1I1	physical	21900206
AGAP1_HUMAN	AGAP1	physical	21900206
GBB2_HUMAN	GNB2	physical	21900206
TYB4_HUMAN	TMSB4X	physical	21900206
ODPB_HUMAN	PDHB	physical	21900206
FAD1_HUMAN	FLAD1	physical	21900206
DOCK7_HUMAN	DOCK7	physical	21900206
MSH2_HUMAN	MSH2	physical	21900206
ECHB_HUMAN	HADHB	physical	21900206
TLE1_HUMAN	TLE1	physical	21900206
KMT2B_HUMAN	KMT2B	physical	21900206
FIBB_HUMAN	FGB	physical	21900206
PHAX_HUMAN	PHAX	physical	21900206
SETB1_HUMAN	SETDB1	physical	21900206
ERBB2_HUMAN	ERBB2	physical	17875712
KIT_HUMAN	KIT	physical	12444928
LAX1_HUMAN	LAX1	physical	25416956
TRI36_HUMAN	TRIM36	physical	25416956
KCTD6_HUMAN	KCTD6	physical	25416956
OLIG1_HUMAN	OLIG1	physical	25814554
FAK1_HUMAN	PTK2	physical	25814554
ZNHI1_HUMAN	ZNHIT1	physical	25814554
FAK1_HUMAN	PTK2	physical	11119718

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 GRB7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-361, AND MASSSPECTROMETRY.	18669648 [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-107, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Tyrosine phosphorylation of growth factor receptor-bound protein-7 byfocal adhesion kinase in the regulation of cell migration,proliferation, and tumorigenesis."; Chu P.Y., Huang L.Y., Hsu C.H., Liang C.C., Guan J.L., Hung T.H.,Shen T.L.; J. Biol. Chem. 284:20215-20226(2009). Cited for: PHOSPHORYLATION AT TYR-188 AND TYR-338, AND INTERACTION WITHPTK2/FAK1.	19473962 [Abstract]