UniProt Accession

 ING5_HUMAN; Q8WYH8; A8K1P3; Q53NU6; Q57Z54; Q9BS30 

Genbank Protein ID

 AF189286; AK074422; AK289958; AC114730; AC133528; BC005370; BC071899 

Genbank Nucleotide ID

 AAL68979.1; BAB85078.1; BAF82647.1; AAX82019.1; AAY14921.1; AAH05370.1; AAH71899.1 

Protein Name

 Inhibitor of growth protein 5 

Protein Synonyms/Alias

 p28ING5 

Gene Name

 ING5 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
67	QRVERLQKIQNAYSK	ubiquitination	[1, 2]
114	FEADLKDKMEGSDFE	acetylation	[3]
154	TSEEDTPKKKKHKGG	acetylation	[4]
226	LTTKPKGKWFCPRCV	acetylation	[3, 4, 5]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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]
 [3] 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]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 

Functional 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. 

Sequence Annotation

 ZN_FING 186 235 PHD-type.
 BINDING 188 188 Histone H3K4me3.
 BINDING 199 199 Histone H3K4me3.
 BINDING 203 203 Histone H3K4me3.
 BINDING 211 211 Histone H3K4me3.
 MOD_RES 114 114 N6-acetyllysine.
 MOD_RES 118 118 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Alternative splicing; Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 240 AA 

Protein Sequence

Gene Ontology

 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 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