CPLM-019717

Genbank Nucleotide ID

E3 ubiquitin-protein ligase RING2

Protein Synonyms/Alias

Huntingtin-interacting protein 2-interacting protein 3; HIP2-interacting protein 3; Protein DinG; RING finger protein 1B; RING1b; RING finger protein 2; RING finger protein BAP-1

BAP1; DING; HIPI3; RING1B

Homo sapiens (Human)

Position	Peptide	Type	References
149	HSIEEGLKIQAMNRL	ubiquitination	[1, 2]
249	SAQTRYIKTSGNATV	acetylation	[3]
249	SAQTRYIKTSGNATV	ubiquitination	[1, 2]
261	ATVDHLSKYLAVRLA	ubiquitination	[1, 2, 4]
320	LVSEKYWKVNKPMEL	ubiquitination	[1, 2]
323	EKYWKVNKPMELYYA	ubiquitination	[1, 2]

[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] 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]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[4] 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]

Functional Description

E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin- protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity.

ZN_FING 51 91 RING-type.
REGION 2 179 Interaction with HIP2.
MOD_RES 2 2 N-acetylserine.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Chromosome; Complete proteome; Isopeptide bond; Ligase; Metal-binding; Nucleus; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO:0016604; C:nuclear body; IEA:Compara.
GO:0035102; C:PRC1 complex; IDA:UniProtKB.
GO:0001739; C:sex chromatin; IEA:Compara.
GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO:0003682; F:chromatin binding; IEA:Compara.
GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO:0009948; P:anterior/posterior axis specification; IEA:Compara.
GO:0001702; P:gastrulation with mouth forming second; IEA:Compara.
GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
GO:0000278; P:mitotic cell cycle; IEA:Compara.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR017907; Znf_RING_CS.

PS00518; ZF_RING_1
PS50089; ZF_RING_2