UniProt Accession

 ING3_HUMAN; Q9NXR8; A8K790; O60394; Q567P3; Q6GMT3; Q7Z762; Q969G0; Q96DT4; Q9HC99; Q9P081 

Genbank Protein ID

 AF074968; AY007790; AK000096; AK291905; AF161419; AL603623; AC004537; BC009777; BC009777; BC010851; BC062634; BC062634; BC073865; BC093091; BC093689; BC101609 

Genbank Nucleotide ID

 AAG12172.1; AAG23285.1; BAA90942.1; BAF84594.1; AAF28979.1; CAC48260.2; AAQ93373.1; AAH09777.1; AAQ93374.1; AAH10851.1; AAH09776.1; AAH62634.1; AAH73865.1; AAH93091.1; AAH93689.1; AAI01610.1 

Protein Name

 Inhibitor of growth protein 3 

Protein Synonyms/Alias

 p47ING3 

Gene Name

 ING3 

Gene Synonyms/Alias

 HSPC301 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
52	EFFMNAKKNKPEWRE	ubiquitination	[1]
66	EEQMASIKKDYYKAL	ubiquitination	[1]
79	ALEDADEKVQLANQI	ubiquitination	[1]
164	TTDHIPEKKFKSEAL	acetylation	[2]
264	NNDFQLGKEFSMARE	acetylation	[2]
264	NNDFQLGKEFSMARE	ubiquitination	[1]
400	LTEAPKGKWYCPQCT	ubiquitination	[1]
411	PQCTAAMKRRGSRHK	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional 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. 

Sequence Annotation

 ZN_FING 360 409 PHD-type.
 BINDING 362 362 Histone H3K4me3 (By similarity).
 BINDING 373 373 Histone H3K4me3 (By similarity).
 BINDING 377 377 Histone H3K4me3 (By similarity).
 BINDING 385 385 Histone H3K4me3 (By similarity).
 MOD_RES 264 264 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Direct protein sequencing; Disease mutation; Growth regulation; Metal-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 418 AA 

Protein Sequence

Gene Ontology

 GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR024610; ING_N.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 

Pfam

 PF12998; ING
 PF00628; PHD 

SMART

 SM00249; PHD 

PROSITE

 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 

PRINTS