ING2_HUMAN - dbPTM
ING2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationGQQQQQLYSSAALLT
HHHHHHHHHHHHHHH
9.0221945579
11PhosphorylationQQQQQLYSSAALLTG
HHHHHHHHHHHHHHC
23.3021945579
12PhosphorylationQQQQLYSSAALLTGE
HHHHHHHHHHHHHCC
12.1921945579
17PhosphorylationYSSAALLTGERSRLL
HHHHHHHHCCHHHHH
37.5424719451
56PhosphorylationLRELDNKYQETLKEI
HHHHHHHHHHHHHHH
20.1720068231
59PhosphorylationLDNKYQETLKEIDDV
HHHHHHHHHHHHHHH
27.8320068231
61UbiquitinationNKYQETLKEIDDVYE
HHHHHHHHHHHHHHH
61.10-
69UbiquitinationEIDDVYEKYKKEDDL
HHHHHHHHHHCCCCC
44.69-
70PhosphorylationIDDVYEKYKKEDDLN
HHHHHHHHHCCCCCH
18.49-
93PhosphorylationLQRALINSQELGDEK
HHHHHHCCHHHCHHH
20.3126330541
143PhosphorylationDKAKMDSSQPERSSR
HHHCCCCCCCHHHCC
45.5523836654
157PhosphorylationRRPRRQRTSESRDLC
CCCCHHCHHHHHHHH
28.6228450419
158PhosphorylationRPRRQRTSESRDLCH
CCCHHCHHHHHHHHH
35.4524719451
160PhosphorylationRRQRTSESRDLCHMA
CHHCHHHHHHHHHHH
30.7528450419
195SumoylationKKKRSKAKQEREASP
HHHHHHHHHHHHCCC
57.3320676127
217UbiquitinationNEPTYCLCNQVSYGE
CCCCEEEECCEEHHH
2.74-
257UbiquitinationKGKWYCPKCRGDNEK
CCCEECCCCCCCCCC
32.76-
264AcetylationKCRGDNEKTMDKSTE
CCCCCCCCCCCHHHH
56.2424849013
265PhosphorylationCRGDNEKTMDKSTEK
CCCCCCCCCCHHHHH
25.1528258704
275AcetylationKSTEKTKKDRRSR--
HHHHHHHHHHHCC--
62.7924849023

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20621832

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ING2_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 ING2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
16387653
HDAC1_HUMANHDAC1physical
16387653
HDAC2_HUMANHDAC2physical
16387653
SDS3_HUMANSUDS3physical
16387653
RBBP7_HUMANRBBP7physical
16387653
RBBP4_HUMANRBBP4physical
16387653
ARI4A_HUMANARID4Aphysical
16387653
ARI4B_HUMANARID4Bphysical
16387653
SP130_HUMANSAP130physical
16387653
BRM1L_HUMANBRMS1Lphysical
16387653
SAP30_HUMANSAP30physical
16387653
SMRC2_HUMANSMARCC2physical
16387653
SMRC1_HUMANSMARCC1physical
16387653
ACL6A_HUMANACTL6Aphysical
16387653
SNF5_HUMANSMARCB1physical
16387653
H3_YEASTHHT1physical
16728974
SAP30_YEASTSAP30physical
16728974
HDAC1_HUMANHDAC1physical
16728974
SIN3A_HUMANSIN3Aphysical
16728974
SKIL_HUMANSKILphysical
18334480
SMAD2_HUMANSMAD2physical
18334480
CSN2_HUMANCOPS2physical
17929852
SMUF1_HUMANSMURF1physical
20621832
A4_HUMANAPPphysical
21832049
SIN3B_HUMANSIN3Bphysical
28514442
ARI4B_HUMANARID4Bphysical
28514442
SP130_HUMANSAP130physical
28514442
HDAC1_HUMANHDAC1physical
28514442
RBBP7_HUMANRBBP7physical
28514442
CENPH_HUMANCENPHphysical
28514442
BRM1L_HUMANBRMS1Lphysical
28514442
SDS3_HUMANSUDS3physical
28514442
ARI4A_HUMANARID4Aphysical
28514442
SP30L_HUMANSAP30Lphysical
28514442
SIN3A_HUMANSIN3Aphysical
28514442
SYTC2_HUMANTARSL2physical
28514442
BRMS1_HUMANBRMS1physical
28514442
SAP30_HUMANSAP30physical
28514442
BAHC1_HUMANBAHCC1physical
28514442
PCM1_HUMANPCM1physical
28514442
AHNK_HUMANAHNAKphysical
28514442
HDAC2_HUMANHDAC2physical
28514442

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 ING2_HUMAN

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Related Literatures of Post-Translational Modification

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