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Protein Page:
RING1 (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
RING1 Constitutes one of the E3 ubiquitin-protein ligases that mediate 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. 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. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity. Component of chromatin-associated Polycomb (PcG) complexes. Interacts with BMI1. 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. Interacts with CBX2 and PCGF6. Component of a PRC1-like complex. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2. Interacts with PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with PHC2. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ligase; Ubiquitin conjugating system; Ubiquitin ligase; Transcription factor; EC 6.3.2.19; EC 6.3.2.-
Chromosomal Location of Human Ortholog: 6p21.3
Cellular Component: nucleoplasm; sex chromatin; cytoplasm; nucleolus; nuclear speck; PcG protein complex; nucleus
Molecular Function: protein binding; zinc ion binding; ubiquitin-protein ligase activity; chromatin binding; ligase activity
Biological Process: anterior/posterior pattern formation; camera-type eye morphogenesis; transcription, DNA-dependent; negative regulation of transcription, DNA-dependent
Reference #:  Q06587 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase RING1; Polycomb complex protein RING1; Really interesting new gene 1 protein; RING finger protein 1; RING1; RING1A; RNF1
Gene Symbols: RING1
Molecular weight: 42,429 Da
Basal Isoelectric point: 5.44  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RING1

Protein Structure Not Found.


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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 1 K12-ub ANAQNASkTWELSLy
0 10 Y19-p kTWELSLyELHRtPQ
0 1 T24-p SLyELHRtPQEAIMD
0 14 S38-p DGTEIAVsPRSLHSE
0 1 S96-p KKLVSKRsLRPDPNF
0 1 Y117-p IYPSREEyEAHQDRV
0 1 S139-p HNQQALSssIEEGLR
0 3 S140-p NQQALSssIEEGLRM
0 3 S187-p EGDGEDVssDsAPDS
0 3 S188-p GDGEDVssDsAPDSA
0 2 S190-p GEDVssDsAPDSAPG
0 1 R202-m1 APGPAPKrPRGGGAG
0 6 S211-p RGGGAGGsSVGtGGG
0 2 T215-p AGGsSVGtGGGGtGG
0 2 T220-p VGtGGGGtGGVGGGA
0 3 S229-p GVGGGAGsEDsGDRG
0 1 S232-p GGAGsEDsGDRGGtL
0 1 T238-p DsGDRGGtLGGGTLG
0 3 S248-p GGTLGPPsPPGAPsP
0 3 S254-p PsPPGAPsPPEPGGE
0 1 K275-ub PHPLLVEkGEYCQTR
0 1 K285 YCQTRYVKTTGNATV
0 1 K297-ub ATVDHLSkYLALRIA
0 1 K403-ub ELCYAPTkDPK____
  mouse

 
K12 ANAQNASKTWELSLY
Y19 KTWELSLYELHRTPQ
T24 SLYELHRTPQEAIMD
S38-p DGTEIAVsPRSLHSE
S96 KKLVSKRSLRPDPNF
Y117 IYPSREEYEAHQDRV
S139 HNQQALSSSIEEGLR
S140 NQQALSSSIEEGLRM
S187 EGDGEDVSSDSAPDS
S188 GDGEDVSSDSAPDSA
S190 GEDVSSDSAPDSAPG
R202 APGPAPKRPRGAGAG
S211 RGAGAGASSVGTGGG
T215 AGASSVGTGGGAAGG
A220 VGTGGGAAGGACGGA
S229 GACGGAGSEDSGDRG
S232 GGAGSEDSGDRGGTL
T238 DSGDRGGTLGGGTLG
S248 GGTLGPPSPPGAPSP
S254 PSPPGAPSPPEPGGE
K275 PHPLLVEKGEYCQTR
K285-ub YCQTRYVkTTGNATV
K297 ATVDHLSKYLALRIA
K403 ELCYAPTKDPK____
  rat

 
K12 ANAQNASKTWELSLY
Y19 KTWELSLYELHRTPQ
T24 SLYELHRTPQEAIMD
S38 DGTEIAVSPRSLHSE
S96 KKLVSKRSLRPDPNF
Y117 IYPSREEYEAHQDRV
S139 HNQQALSSSIEEGLR
S140 NQQALSSSIEEGLRM
S187 EGDGEDISSDSAPDS
S188 GDGEDISSDSAPDSA
S190 GEDISSDSAPDSAPG
R202 APGPAPKRPRGGGAG
S211 RGGGAGGSSVGTGGG
T215 AGGSSVGTGGGAAGG
A220 VGTGGGAAGGACGGA
S229 GACGGAGSEDSGDRG
S232 GGAGSEDSGDRGGTL
T238 DSGDRGGTLGGGTLG
S248 GGTLGPPSPPGAPSP
S254 PSPPGAPSPPEPGGE
K275 PHPLLVEKGEYCQTR
K285 YCQTRYVKTTGNATV
K297 ATVDHLSKYLALRIA
K403 ELCYAPTKDPK____
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