UniProt ID | ING2_HUMAN | |
---|---|---|
UniProt AC | Q9H160 | |
Protein Name | Inhibitor of growth protein 2 | |
Gene Name | ING2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 280 | |
Subcellular Localization | Nucleus . Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm. | |
Protein Description | Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs).. | |
Protein Sequence | MLGQQQQQLYSSAALLTGERSRLLTCYVQDYLECVESLPHDMQRNVSVLRELDNKYQETLKEIDDVYEKYKKEDDLNQKKRLQQLLQRALINSQELGDEKIQIVTQMLELVENRARQMELHSQCFQDPAESERASDKAKMDSSQPERSSRRPRRQRTSESRDLCHMANGIEDCDDQPPKEKKSKSAKKKKRSKAKQEREASPVEFAIDPNEPTYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPKGKWYCPKCRGDNEKTMDKSTEKTKKDRRSR | |
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 |
---|---|---|---|---|---|
10 | Phosphorylation | GQQQQQLYSSAALLT HHHHHHHHHHHHHHH | 9.02 | 21945579 | |
11 | Phosphorylation | QQQQQLYSSAALLTG HHHHHHHHHHHHHHC | 23.30 | 21945579 | |
12 | Phosphorylation | QQQQLYSSAALLTGE HHHHHHHHHHHHHCC | 12.19 | 21945579 | |
17 | Phosphorylation | YSSAALLTGERSRLL HHHHHHHHCCHHHHH | 37.54 | 24719451 | |
56 | Phosphorylation | LRELDNKYQETLKEI HHHHHHHHHHHHHHH | 20.17 | 20068231 | |
59 | Phosphorylation | LDNKYQETLKEIDDV HHHHHHHHHHHHHHH | 27.83 | 20068231 | |
61 | Ubiquitination | NKYQETLKEIDDVYE HHHHHHHHHHHHHHH | 61.10 | - | |
69 | Ubiquitination | EIDDVYEKYKKEDDL HHHHHHHHHHCCCCC | 44.69 | - | |
70 | Phosphorylation | IDDVYEKYKKEDDLN HHHHHHHHHCCCCCH | 18.49 | - | |
93 | Phosphorylation | LQRALINSQELGDEK HHHHHHCCHHHCHHH | 20.31 | 26330541 | |
143 | Phosphorylation | DKAKMDSSQPERSSR HHHCCCCCCCHHHCC | 45.55 | 23836654 | |
157 | Phosphorylation | RRPRRQRTSESRDLC CCCCHHCHHHHHHHH | 28.62 | 28450419 | |
158 | Phosphorylation | RPRRQRTSESRDLCH CCCHHCHHHHHHHHH | 35.45 | 24719451 | |
160 | Phosphorylation | RRQRTSESRDLCHMA CHHCHHHHHHHHHHH | 30.75 | 28450419 | |
195 | Sumoylation | KKKRSKAKQEREASP HHHHHHHHHHHHCCC | 57.33 | 20676127 | |
217 | Ubiquitination | NEPTYCLCNQVSYGE CCCCEEEECCEEHHH | 2.74 | - | |
257 | Ubiquitination | KGKWYCPKCRGDNEK CCCEECCCCCCCCCC | 32.76 | - | |
264 | Acetylation | KCRGDNEKTMDKSTE CCCCCCCCCCCHHHH | 56.24 | 24849013 | |
265 | Phosphorylation | CRGDNEKTMDKSTEK CCCCCCCCCCHHHHH | 25.15 | 28258704 | |
275 | Acetylation | KSTEKTKKDRRSR-- HHHHHHHHHHHCC-- | 62.79 | 24849023 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ING2_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 ING2_HUMAN !! |
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. |
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