CPLM-023245

Genbank Nucleotide ID

Inhibitor of growth protein 4

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
66	EEKLALLKQIQEAYG	ubiquitination	[1, 2, 3]
112	ARFEADLKEKQIESS	acetylation	[4, 5, 6]
112	ARFEADLKEKQIESS	ubiquitination	[2]
114	FEADLKEKQIESSDY	acetylation	[4, 5]
127	DYDSSSSKGKKKGRT	acetylation	[4, 5, 6, 7, 8, 9]
129	DSSSSKGKKKGRTQK	acetylation	[4, 5, 6, 7, 9]
130	SSSSKGKKKGRTQKE	acetylation	[4, 8]
146	KAARARSKGKNSDEE	acetylation	[4, 5, 6, 7, 9]
148	ARARSKGKNSDEEAP	acetylation	[4, 5, 6, 7, 9]
156	NSDEEAPKTAQKKLK	acetylation	[4, 5, 6]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[4] 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]
[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]
[6] 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]
[7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[8] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[9] 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]

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).

ZN_FING 196 245 PHD-type.
MOTIF 127 148 Bipartite nuclear localization signal.
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.
MOD_RES 127 127 N6-acetyllysine.
MOD_RES 129 129 N6-acetyllysine.
MOD_RES 133 133 Citrulline.
MOD_RES 146 146 N6-acetyllysine.
MOD_RES 148 148 N6-acetyllysine.
MOD_RES 150 150 Phosphoserine (By similarity).
MOD_RES 156 156 N6-acetyllysine.
MOD_RES 166 166 Citrulline.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
GO:0006260; P:DNA replication; IDA:UniProtKB.
GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.

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.

PF12998; ING
PF00628; PHD

PS01359; ZF_PHD_1
PS50016; ZF_PHD_2