ING3_MOUSE - dbPTM
ING3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ING3_MOUSE
UniProt AC Q8VEK6
Protein Name Inhibitor of growth protein 3
Gene Name Ing3
Organism Mus musculus (Mouse).
Sequence Length 421
Subcellular Localization Nucleus.
Protein Description Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity)..
Protein Sequence MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDAPSQPVNNHHAHSHTPVEKRKYNPTSHHAAADHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASCNNAYNVNSSQPLASYNIGSLSSGAGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSIPRETAGYSSSSALMTTLTQNASSSATDSRSGRKSKNNTKSSSQQSSSSSSSSSSSSLSLCSSSSTVVQEVSQQATVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWFCPQCTAAMKRRGSRHK
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
123PhosphorylationTEILERRSLELDAPS
HHHHHHCCCCCCCCC
32.2025338131
164AcetylationAADHIPEKKFKSEAL
CHHCCCHHHCCHHHH
59.1523806337
167AcetylationHIPEKKFKSEALLST
CCCHHHCCHHHHHHH
57.1523806337
177PhosphorylationALLSTLTSDASKENT
HHHHHHCCCHHHCCC
34.0025521595
180PhosphorylationSTLTSDASKENTLGC
HHHCCCHHHCCCCCC
45.5525521595
181AcetylationTLTSDASKENTLGCR
HHCCCHHHCCCCCCC
57.6223806337
264AcetylationNNDFQLGKEFSIPRE
CCCCCCCCCEECCHH
65.2723806337
267PhosphorylationFQLGKEFSIPRETAG
CCCCCCEECCHHHCC
32.5426525534
272PhosphorylationEFSIPRETAGYSSSS
CEECCHHHCCCCCHH
27.0222871156
275PhosphorylationIPRETAGYSSSSALM
CCHHHCCCCCHHHHH
11.6922871156
276PhosphorylationPRETAGYSSSSALMT
CHHHCCCCCHHHHHH
23.8722871156
403AcetylationLTEAPKGKWFCPQCT
CCCCCCCCCCCHHHH
43.1323806337
410PhosphorylationKWFCPQCTAAMKRRG
CCCCHHHHHHHHHHC
16.53-

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

Oops, there are no upstream regulatory protein records of ING3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ING3_MOUSE !!

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 ING3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ING3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ING3_MOUSE

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Related Literatures of Post-Translational Modification

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