UniProt Accession

 ING4_MOUSE; Q8C0D7; Q8C1S7; Q8K3Q5; Q8K3Q6; Q8K3Q7; Q9D7F9 

Genbank Protein ID

 AY035880; AY035881; AY036107; AK002821; AK009267; AK031633; AK050522; BC009127 

Genbank Nucleotide ID

 AAK63168.1; AAK63169.1; AAK64509.1; BAC25009.1; BAB26183.1; BAC27489.1; BAC34304.1; AAH09127.1 

Protein Name

 Inhibitor of growth protein 4 

Protein Synonyms/Alias

 p29ING4 

Gene Name

 Ing4 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
127	DYDSSSSKGKKKGRT	acetylation	[1, 2, 3, 4, 5, 6, 7]
129	DSSSSKGKKKGRTQK	acetylation	[1, 2, 3, 5, 6, 7]
146	KAARARSKGKNSDEE	acetylation	[1, 2, 7, 8]
148	ARARSKGKNSDEEAP	acetylation	[1, 2, 3, 7, 8]
156	NSDEEAPKAAQKKLK	acetylation	[3, 7]
236	LTTKPRGKWFCPRCS	acetylation	[3]

Reference

 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [7] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [8] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

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. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1) (By similarity). 

Sequence Annotation

 ZN_FING 196 245 PHD-type.
 MOTIF 127 148 Bipartite nuclear localization signal (By
 BINDING 198 198 Histone H3K4me3 (By similarity).
 BINDING 209 209 Histone H3K4me3 (By similarity).
 BINDING 213 213 Histone H3K4me3 (By similarity).
 BINDING 221 221 Histone H3K4me3 (By similarity).
 MOD_RES 112 112 N6-acetyllysine (By similarity).
 MOD_RES 127 127 N6-acetyllysine (By similarity).
 MOD_RES 129 129 N6-acetyllysine (By similarity).
 MOD_RES 133 133 Citrulline.
 MOD_RES 146 146 N6-acetyllysine (By similarity).
 MOD_RES 148 148 N6-acetyllysine (By similarity).
 MOD_RES 150 150 Phosphoserine.
 MOD_RES 156 156 N6-acetyllysine (By similarity).
 MOD_RES 166 166 Citrulline.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Cell cycle; Chromatin regulator; Citrullination; Coiled coil; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 249 AA 

Protein Sequence

Gene Ontology

 GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0007050; P:cell cycle arrest; IEA:Compara.
 GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
 GO:0006260; P:DNA replication; ISS:UniProtKB.
 GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
 GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045926; P:negative regulation of growth; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. 

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