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Protein Page:
RNF2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RNF2 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. Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2, MBLR, L3MBTL2 and YAF2. Component of a PRC1-like complex. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with RYBP, HIP2 and TFCP2. Association to the chromosomal DNA is cell-cycle dependent. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RING1. Interacts with Interacts with PCGF2, CBX4, CBX6, CBX7 and CBX8. Interacts with CBX2, BMI and PHC2. Interacts with RYBP, HIP2 and TFCP2. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.19; Ubiquitin conjugating system; EC 6.3.2.-; Ligase; Ubiquitin ligase
Chromosomal Location of Human Ortholog: 1q25.3
Cellular Component: nucleoplasm; nuclear body; sex chromatin; nucleolus; PcG protein complex; nucleus; ubiquitin ligase complex
Molecular Function: protein binding; zinc ion binding; ubiquitin-protein ligase activity; chromatin binding; ligase activity
Biological Process: transcription, DNA-dependent; negative regulation of transcription from RNA polymerase II promoter; gastrulation with mouth forming second; mitotic cell cycle; anterior/posterior axis specification
Reference #:  Q99496 (UniProtKB)
Alt. Names/Synonyms: BAP-1; BAP1; DING; E3 ubiquitin-protein ligase RING2; HIP2-interacting protein 3; HIPI3; Huntingtin-interacting protein 2-interacting protein 3; Protein DinG; RING finger protein 1B; RING finger protein 2; RING finger protein BAP-1; RING1B; RING2; RNF2
Gene Symbols: RNF2
Molecular weight: 37,655 Da
Basal Isoelectric point: 6.38  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RNF2

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S41‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S2-p ______MsQAVQTNG
0 8 S41-p DGLEIVVsPRSLHSE
0 1 S99-p KKLVSKRsLRPDPNF
0 1 S116-p LISKIYPsRDEyEAH
0 7 Y120-p IYPsRDEyEAHQERV
0 7 S143-p NQQALSHsIEEGLkI
0 1 K149-ub HsIEEGLkIQAMNRL
0 2 S168-p KQQIENGsGAEDNGD
0 1 S200-p SNKRTKTsDDSGLEL
0 1 Y247-p DDSAQTRyIkTSGNA
0 1 K249-ac SAQTRyIkTSGNATV
0 1 K249-ub SAQTRyIkTSGNATV
0 1 S260-p NATVDHLskyLAVRL
0 1 K261-ub ATVDHLskyLAVRLA
0 1 Y262-p TVDHLskyLAVRLAL
0 1 K323-ub EKYWKVNkPMELYYA
  mouse

 
S2 ______MSQAVQTNG
S41-p DGLEIVVsPRSLHSE
S99 KKLVSKRSLRPDPNF
S116 LISKIYPSRDEYEAH
Y120 IYPSRDEYEAHQERV
S143-p NQQALSHsIEEGLKI
K149 HsIEEGLKIQAMNRL
S168 KQQIENGSGAEDNGD
S200 SNKRTKTSDDSGLEL
Y247 DDSAQTRYIKTSGNA
K249 SAQTRYIKTSGNATV
K249 SAQTRYIKTSGNATV
S260 NATVDHLSKYLAVRL
K261 ATVDHLSKYLAVRLA
Y262 TVDHLSKYLAVRLAL
K323 EKYWKVNKPMELYYA
  rat

 
S2 ______MSQAVQTNG
S41-p DGLEIVVsPRSLHSE
S99 KKLVSKRSLRPDPNF
S116 LISKIYPSRDEYEAH
Y120 IYPSRDEYEAHQERV
S143 NQQALSHSIEEGLKI
K149 HSIEEGLKIQAMNRL
S168 KQQIENGSGAEDNGD
S200 SNKRTKTSDDSGLEL
Y247 DDSAQTRYIKTSGNA
K249 SAQTRYIKTSGNATV
K249 SAQTRYIKTSGNATV
S260 NATVDHLSKYLAVRL
K261 ATVDHLSKYLAVRLA
Y262 TVDHLSKYLAVRLAL
- gap
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