GRB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRB2_MOUSE
• UniProt AC: Q60631
• Protein Name: Growth factor receptor-bound protein 2
• Gene Name: Grb2
• Organism: Mus musculus (Mouse).
• Sequence Length: 217
• Subcellular Localization: Nucleus. Cytoplasm. Endosome. Golgi apparatus .
• Protein Description: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.; Isoform 2 does not bind to phosphorylated epidermal growth factor receptor (EGFR) but inhibits EGF-induced. transactivation of a RAS-responsive element. Isoform 2 acts as a dominant negative protein over GRB2 and by suppressing proliferative signals, may trigger active programmed cell death (By similarity)..
• Protein Sequence: MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQMPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV

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
1	Acetylation	-------MEAIAKYD -------CCCCCCCC	7.67	-
6	Acetylation	--MEAIAKYDFKATA --CCCCCCCCCCCCC	38.96	-
10	Ubiquitination	AIAKYDFKATADDEL CCCCCCCCCCCCCCC	41.76	-
18	Phosphorylation	ATADDELSFKRGDIL CCCCCCCCCCCCCHH	27.03	18779572
38	Ubiquitination	ECDQNWYKAELNGKD HHCCCEEEHHHCCCC	27.31	-
44	Ubiquitination	YKAELNGKDGFIPKN EEHHHCCCCCCCCHH	54.31	-
50	Acetylation	GKDGFIPKNYIEMKP CCCCCCCHHHEECCC	58.53	23806337
52	Phosphorylation	DGFIPKNYIEMKPHP CCCCCHHHEECCCCC	12.37	29514104
88	Phosphorylation	GAFLIRESESAPGDF CEEEEEECCCCCCCE	27.31	27180971
90	Phosphorylation	FLIRESESAPGDFSL EEEEECCCCCCCEEE	49.39	28833060
96	Phosphorylation	ESAPGDFSLSVKFGN CCCCCCEEEEEEECC	25.19	28833060
98	Phosphorylation	APGDFSLSVKFGNDV CCCCEEEEEEECCCC	23.28	28833060
109	Ubiquitination	GNDVQHFKVLRDGAG CCCCEEEEEEECCCC	37.93	-
109	Acetylation	GNDVQHFKVLRDGAG CCCCEEEEEEECCCC	37.93	-
159	Phosphorylation	EQMPQQPTYVQALFD HHCCCCCCEEEEEEC	31.80	23649490
160	Phosphorylation	QMPQQPTYVQALFDF HCCCCCCEEEEEECC	9.39	22817900
198	S-nitrosylation	PNWWKGACHGQTGMF CCCCCCCCCCCCCCC	5.16	21278135
198	Glutathionylation	PNWWKGACHGQTGMF CCCCCCCCCCCCCCC	5.16	24333276
198	S-nitrosocysteine	PNWWKGACHGQTGMF CCCCCCCCCCCCCCC	5.16	-
202	Phosphorylation	KGACHGQTGMFPRNY CCCCCCCCCCCCCHH	34.90	29514104
209	Phosphorylation	TGMFPRNYVTPVNRN CCCCCCHHCCCCCCC	13.64	22817900
211	Phosphorylation	MFPRNYVTPVNRNV- CCCCHHCCCCCCCC-	15.91	-

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
160	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GRB2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GRB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBL_MOUSE	Cbl	physical	9174058
P85A_MOUSE	Pik3r1	physical	9174058
CD28_HUMAN	CD28	physical	9694876
DVL2_MOUSE	Dvl2	physical	19920076
A4_HUMAN	APP	physical	17384289
CBL_MOUSE	Cbl	physical	17372273
EGFR_MOUSE	Egfr	physical	17372273
CBL_MOUSE	Cbl	physical	21703542
CPNE2_MOUSE	Cpne2	physical	20697350
BCR_MOUSE	Bcr	physical	20697350
LRRK1_MOUSE	Lrrk1	physical	20697350
YBOX1_MOUSE	Ybx1	physical	20697350
EGFR_MOUSE	Egfr	physical	9363897
PRIO_MOUSE	Prnp	physical	11571277
MERL_MOUSE	Nf2	physical	16405865
SPY1_MOUSE	Spry1	physical	11585837
SPY2_MOUSE	Spry2	physical	11585837
SPY2_MOUSE	Spry2	physical	16339969
SPY4_MOUSE	Spry4	physical	16339969
SOS1_MOUSE	Sos1	physical	10373493
CD22_MOUSE	Cd22	physical	10373493
SHC1_MOUSE	Shc1	physical	10995764

Drug and Disease Associations

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