UniProt Accession

 RING1_HUMAN; Q06587; A8JZZ0; Q5JP96; Q5SQW2; Q86V19 

Genbank Protein ID

 Z14000; BT007352; AK289355; AL031228; AL031228; AL713971; AL645940; AL844527; CR759786; CR759733; CR847841; CR547129; CR547129; CR847841; BC002922; BC051866 

Genbank Nucleotide ID

 CAA78389.1; AAP36016.1; BAF82044.1; CAA20235.1; CAI95620.1; CAI17650.1; CAI18069.1; CAI41841.1; CAQ08246.1; CAQ10303.1; CAQ10314.1; CAQ10314.1; CAQ10355.1; CAQ10355.1; AAH02922.2; AAH51866.1 

Protein Name

 E3 ubiquitin-protein ligase RING1 

Protein Synonyms/Alias

 Polycomb complex protein RING1; RING finger protein 1; Really interesting new gene 1 protein 

Gene Name

 RING1 

Gene Synonyms/Alias

 RNF1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
12	ANAQNASKTWELSLY	ubiquitination	[1, 2]
62	LKNTMTTKECLHRFC	ubiquitination	[3]
275	PHPLLVEKGEYCQTR	ubiquitination	[1, 2]
285	YCQTRYVKTTGNATV	ubiquitination	[3, 4]
297	ATVDHLSKYLALRIA	acetylation	[4, 5]
297	ATVDHLSKYLALRIA	ubiquitination	[1, 2, 3, 6]
403	ELCYAPTKDPK****	ubiquitination	[4]

Reference

 [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] 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]
 [4] 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]
 [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] 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

 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. 

Sequence Annotation

 ZN_FING 48 88 RING-type.
 REGION 30 234 Necessary for transcriptional repression
 REGION 230 406 Necessary for interaction with CBX2 (By
 MOTIF 201 204 Nuclear localization signal (Potential).
 MOD_RES 38 38 Phosphoserine.
 MOD_RES 140 140 Phosphoserine.
 MOD_RES 187 187 Phosphoserine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 220 220 Phosphothreonine.
 MOD_RES 248 248 Phosphoserine.
 MOD_RES 254 254 Phosphoserine.  

Keyword

 Alternative splicing; Chromatin regulator; Complete proteome; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 406 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0035102; C:PRC1 complex; IDA:UniProtKB.
 GO:0001739; C:sex chromatin; IEA:Compara.
 GO:0000151; C:ubiquitin ligase complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0009952; P:anterior/posterior pattern specification; IEA:Compara.
 GO:0048593; P:camera-type eye morphogenesis; IEA:Compara.
 GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 

Pfam

 PF00097; zf-C3HC4 

SMART

 SM00184; RING 

PROSITE

 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 

PRINTS