dbPTM

ING5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ING5_HUMAN
UniProt AC	Q8WYH8
Protein Name	Inhibitor of growth protein 5
Gene Name	ING5
Organism	Homo sapiens (Human).
Sequence Length	240
Subcellular Localization	Nucleus .
Protein Description	Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator..
Protein Sequence	MATAMYLEHYLDSIENLPCELQRNFQLMRELDQRTEDKKAEIDILAAEYISTVKTLSPDQRVERLQKIQNAYSKCKEYSDDKVQLAMQTYEMVDKHIRRLDADLARFEADLKDKMEGSDFESSGGRGLKKGRGQKEKRGSRGRGRRTSEEDTPKKKKHKGGSEFTDTILSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCVQEKRKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Ubiquitination	AEYISTVKTLSPDQR HHHHHHHCCCCHHHH	43.78	-
55	Phosphorylation	EYISTVKTLSPDQRV HHHHHHCCCCHHHHH	28.29	26074081
57	Phosphorylation	ISTVKTLSPDQRVER HHHHCCCCHHHHHHH	31.49	21815630
67	Ubiquitination	QRVERLQKIQNAYSK HHHHHHHHHHHHHHH	51.34	-
67	Acetylation	QRVERLQKIQNAYSK HHHHHHHHHHHHHHH	51.34	25953088
95	Ubiquitination	QTYEMVDKHIRRLDA HHHHHHHHHHHHHHH	29.53	-
106	Methylation	RLDADLARFEADLKD HHHHHHHHHHHHHHH	36.92	115480347
112	Acetylation	ARFEADLKDKMEGSD HHHHHHHHHHHCCCC	56.71	23749302
114	Acetylation	FEADLKDKMEGSDFE HHHHHHHHHCCCCCC	36.95	19608861
118	Phosphorylation	LKDKMEGSDFESSGG HHHHHCCCCCCCCCC	26.31	29255136
122	Phosphorylation	MEGSDFESSGGRGLK HCCCCCCCCCCCCCC	33.99	25159151
123	Phosphorylation	EGSDFESSGGRGLKK CCCCCCCCCCCCCCC	37.76	23927012
126	Methylation	DFESSGGRGLKKGRG CCCCCCCCCCCCCCC	51.28	24129315
129	Acetylation	SSGGRGLKKGRGQKE CCCCCCCCCCCCCCC	56.88	7431111
130	Acetylation	SGGRGLKKGRGQKEK CCCCCCCCCCCCCCC	59.90	7431121
135	Acetylation	LKKGRGQKEKRGSRG CCCCCCCCCCCCCCC	68.94	156159
147	Phosphorylation	SRGRGRRTSEEDTPK CCCCCCCCCCCCCCC	38.85	28176443
148	Phosphorylation	RGRGRRTSEEDTPKK CCCCCCCCCCCCCCC	36.86	27273156
152	Phosphorylation	RRTSEEDTPKKKKHK CCCCCCCCCCCCCCC	40.04	30576142
154	Acetylation	TSEEDTPKKKKHKGG CCCCCCCCCCCCCCC	78.35	23749302
155	Acetylation	SEEDTPKKKKHKGGS CCCCCCCCCCCCCCC	69.15	25953088
222	Acetylation	ACVDLTTKPKGKWFC EEEECCCCCCCCCCC	39.22	3751039
226	Acetylation	LTTKPKGKWFCPRCV CCCCCCCCCCCHHHH	43.13	25825284

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
152	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ING5_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 ING5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAV2_HUMAN	NAV2	physical	16189514
EP300_HUMAN	EP300	physical	12750254
P53_HUMAN	TP53	physical	12750254
KAT6A_HUMAN	KAT6A	physical	16387653
KAT6B_HUMAN	KAT6B	physical	16387653
BRPF3_HUMAN	BRPF3	physical	16387653
BRD1_HUMAN	BRD1	physical	16387653
JADE1_HUMAN	JADE1	physical	16387653
JADE2_HUMAN	JADE2	physical	16387653
JADE3_HUMAN	JADE3	physical	16387653
KAT7_HUMAN	KAT7	physical	16387653
EAF6_HUMAN	MEAF6	physical	16387653
BRPF1_HUMAN	BRPF1	physical	16387653
MCM4_HUMAN	MCM4	physical	16387653
MCM6_HUMAN	MCM6	physical	16387653
MCM2_HUMAN	MCM2	physical	16387653
KAT7_HUMAN	KAT7	physical	17954561
P53_HUMAN	TP53	physical	17954561
BRPF1_HUMAN	BRPF1	physical	18794358
EAF6_HUMAN	MEAF6	physical	18794358
JADE1_HUMAN	JADE1	physical	22144582
ANM5_HUMAN	PRMT5	physical	23455924
NAV2_HUMAN	NAV2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
DEUP1_HUMAN	CCDC67	physical	25416956
CC062_HUMAN	C3orf62	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
P53_HUMAN	TP53	physical	21177815

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 ING5_HUMAN

Related Literatures of Post-Translational Modification

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-114 AND LYS-226, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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 SER-118, AND MASSSPECTROMETRY.	17081983 [Abstract]