UniProt ID | GRB2_HUMAN | |
---|---|---|
UniProt AC | P62993 | |
Protein Name | Growth factor receptor-bound protein 2 | |
Gene Name | GRB2 | |
Organism | Homo sapiens (Human). | |
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.. | |
Protein Sequence | MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MEAIAKYD -------CCCCCCCC | 7.67 | 22814378 | |
6 | Acetylation | --MEAIAKYDFKATA --CCCCCCCCCCCCC | 38.96 | 19608861 | |
7 | Phosphorylation | -MEAIAKYDFKATAD -CCCCCCCCCCCCCC | 20.00 | 28152594 | |
10 | Ubiquitination | AIAKYDFKATADDEL CCCCCCCCCCCCCCC | 41.76 | - | |
18 | Phosphorylation | ATADDELSFKRGDIL CCCCCCCCCCCCCHH | 27.03 | 25159151 | |
20 | 2-Hydroxyisobutyrylation | ADDELSFKRGDILKV CCCCCCCCCCCHHHH | 52.69 | - | |
20 | Ubiquitination | ADDELSFKRGDILKV CCCCCCCCCCCHHHH | 52.69 | 21890473 | |
20 (in isoform 1) | Ubiquitination | - | 52.69 | 21890473 | |
20 | Acetylation | ADDELSFKRGDILKV CCCCCCCCCCCHHHH | 52.69 | 25953088 | |
20 (in isoform 2) | Ubiquitination | - | 52.69 | 21890473 | |
26 | Ubiquitination | FKRGDILKVLNEECD CCCCCHHHHHCHHHC | 45.04 | - | |
32 | Glutathionylation | LKVLNEECDQNWYKA HHHHCHHHCCCEEEH | 5.49 | 22555962 | |
32 | S-nitrosylation | LKVLNEECDQNWYKA HHHHCHHHCCCEEEH | 5.49 | 19483679 | |
32 | S-nitrosocysteine | LKVLNEECDQNWYKA HHHHCHHHCCCEEEH | 5.49 | - | |
37 | Phosphorylation | EECDQNWYKAELNGK HHHCCCEEEHHHCCC | 14.10 | 22817900 | |
38 | Ubiquitination | ECDQNWYKAELNGKD HHCCCEEEHHHCCCC | 27.31 | 19608861 | |
38 | Acetylation | ECDQNWYKAELNGKD HHCCCEEEHHHCCCC | 27.31 | 23749302 | |
44 (in isoform 1) | Ubiquitination | - | 54.31 | 21890473 | |
44 | Ubiquitination | YKAELNGKDGFIPKN EEHHHCCCCCCCCHH | 54.31 | 21890473 | |
44 (in isoform 2) | Ubiquitination | - | 54.31 | 21890473 | |
50 | Acetylation | GKDGFIPKNYIEMKP CCCCCCCHHHEECCC | 58.53 | 19608861 | |
52 (in isoform 2) | Phosphorylation | - | 12.37 | - | |
52 | Phosphorylation | DGFIPKNYIEMKPHP CCCCCHHHEECCCCC | 12.37 | 22817900 | |
56 | Ubiquitination | PKNYIEMKPHPWFFG CHHHEECCCCCCCCC | 27.64 | 21890473 | |
56 | Acetylation | PKNYIEMKPHPWFFG CHHHEECCCCCCCCC | 27.64 | 25953088 | |
56 (in isoform 1) | Ubiquitination | - | 27.64 | 21890473 | |
64 | Acetylation | PHPWFFGKIPRAKAE CCCCCCCCCCHHHHH | 44.36 | 23749302 | |
68 (in isoform 2) | Ubiquitination | - | 15.28 | 21890473 | |
68 | Acetylation | FFGKIPRAKAEEMLS CCCCCCHHHHHHHHH | 15.28 | 19608861 | |
68 | Ubiquitination | FFGKIPRAKAEEMLS CCCCCCHHHHHHHHH | 15.28 | 19608861 | |
69 (in isoform 1) | Ubiquitination | - | 58.57 | 21890473 | |
69 | Ubiquitination | FGKIPRAKAEEMLSK CCCCCHHHHHHHHHH | 58.57 | 6983 | |
76 (in isoform 1) | Ubiquitination | - | 47.60 | 21890473 | |
76 | 2-Hydroxyisobutyrylation | KAEEMLSKQRHDGAF HHHHHHHHCCCCCEE | 47.60 | - | |
76 | Ubiquitination | KAEEMLSKQRHDGAF HHHHHHHHCCCCCEE | 47.60 | 21906983 | |
78 | Methylation | EEMLSKQRHDGAFLI HHHHHHCCCCCEEEE | 33.33 | - | |
88 | Phosphorylation | GAFLIRESESAPGDF CEEEEEECCCCCCCE | 27.31 | 21815630 | |
90 | Phosphorylation | FLIRESESAPGDFSL EEEEECCCCCCCEEE | 49.39 | 25159151 | |
96 | Phosphorylation | ESAPGDFSLSVKFGN CCCCCCEEEEEEECC | 25.19 | 24719451 | |
109 (in isoform 1) | Ubiquitination | - | 37.93 | 21890473 | |
109 | Acetylation | GNDVQHFKVLRDGAG CCCCEEEEEEECCCC | 37.93 | 19608861 | |
109 | Ubiquitination | GNDVQHFKVLRDGAG CCCCEEEEEEECCCC | 37.93 | 21890473 | |
109 | Malonylation | GNDVQHFKVLRDGAG CCCCEEEEEEECCCC | 37.93 | 26320211 | |
117 | Acetylation | VLRDGAGKYFLWVVK EEECCCCCEEEEEEE | 32.09 | 129889 | |
118 | Phosphorylation | LRDGAGKYFLWVVKF EECCCCCEEEEEEEC | 11.73 | 23882029 | |
127 | Phosphorylation | LWVVKFNSLNELVDY EEEEECCCHHHHHHH | 35.39 | 29449344 | |
134 | Phosphorylation | SLNELVDYHRSTSVS CHHHHHHHHHCCCCC | 7.52 | 28152594 | |
159 | Phosphorylation | EQVPQQPTYVQALFD HHCCCCCCEEEEEEC | 31.80 | 26552605 | |
160 | Phosphorylation | QVPQQPTYVQALFDF HCCCCCCEEEEEECC | 9.39 | 21082442 | |
195 | Ubiquitination | NSDPNWWKGACHGQT CCCCCCCCCCCCCCC | 28.39 | - | |
204 | Sulfoxidation | ACHGQTGMFPRNYVT CCCCCCCCCCCHHCC | 4.79 | 30846556 | |
209 | Nitration | TGMFPRNYVTPVNRN CCCCCCHHCCCCCCC | 13.64 | - | |
209 | Phosphorylation | TGMFPRNYVTPVNRN CCCCCCHHCCCCCCC | 13.64 | 21945579 | |
211 | Phosphorylation | MFPRNYVTPVNRNV- CCCCHHCCCCCCCC- | 15.91 | 21945579 | |
215 | Methylation | NYVTPVNRNV----- HHCCCCCCCC----- | 45.59 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
7 | Y | Phosphorylation | Kinase | JAK2 | O60674 | PSP |
37 | Y | Phosphorylation | Kinase | JAK2 | O60674 | PSP |
52 | Y | Phosphorylation | Kinase | JAK2 | O60674 | PSP |
160 | Y | Phosphorylation | Kinase | ALK | Q9UM73 | PSP |
160 | Y | Phosphorylation | Kinase | FGFR2 | P21802 | PSP |
209 | Y | Phosphorylation | Kinase | BCR-ABL1 | A9UF07 | PSP |
209 | Y | Phosphorylation | Kinase | EGFR | P00533 | PhosphoELM |
209 | Y | Phosphorylation | Kinase | JAK2 | O60674 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GRB2_HUMAN !! |
* 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 GRB2_HUMAN !! |
Kegg Disease | |
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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 | |
DB00061 | Pegademase bovine |
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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-6; LYS-50 AND LYS-109, ANDMASS SPECTROMETRY. | |
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 THR-211, AND MASSSPECTROMETRY. | |
"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 TYR-160 AND TYR-209, ANDMASS SPECTROMETRY. |