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Protein

E3 ubiquitin-protein ligase RING1

Gene

RING1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 8841RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_355174. SUMOylation of DNA damage response and repair proteins.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RING1 (EC:6.3.2.-)
Alternative name(s):
Polycomb complex protein RING1
RING finger protein 1
Really interesting new gene 1 protein
Gene namesi
Name:RING1
Synonyms:RNF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:10018. RING1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
  • sex chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34393.

Polymorphism and mutation databases

BioMutaiRING1.
DMDMi90110053.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406E3 ubiquitin-protein ligase RING1PRO_0000056384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphothreonine1 Publication
Modified residuei38 – 381Phosphoserine3 Publications
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei187 – 1871Phosphoserine2 Publications
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei215 – 2151Phosphothreonine1 Publication
Modified residuei220 – 2201Phosphothreonine2 Publications
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei232 – 2321Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei254 – 2541Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06587.
PaxDbiQ06587.
PeptideAtlasiQ06587.
PRIDEiQ06587.

PTM databases

PhosphoSiteiQ06587.

Expressioni

Gene expression databases

BgeeiQ06587.
CleanExiHS_RING1.
GenevestigatoriQ06587.

Organism-specific databases

HPAiHPA008701.

Interactioni

Subunit structurei

Component of chromatin-associated Polycomb (PcG) complexes. Interacts with BMI1 (By similarity). 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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P3522614EBI-752313,EBI-2341576
CBX6O955033EBI-752313,EBI-3951758
CBX7O959313EBI-752313,EBI-3923843
CBX8Q9HC526EBI-752313,EBI-712912
PCGF1Q9BSM15EBI-752313,EBI-749901
PCGF2P352275EBI-752313,EBI-2129767
PCGF3Q3KNV82EBI-752313,EBI-2339807
PCGF5Q86SE92EBI-752313,EBI-2827999
RNF2Q994964EBI-752313,EBI-722416
RYBPQ8N4888EBI-752313,EBI-752324
USP11P517844EBI-752313,EBI-306876
USP7Q930094EBI-752313,EBI-302474
YAF2Q8IY574EBI-752313,EBI-2842031

Protein-protein interaction databases

BioGridi111947. 59 interactions.
DIPiDIP-42043N.
IntActiQ06587. 36 interactions.
MINTiMINT-1327105.
STRINGi9606.ENSP00000363787.

Structurei

3D structure databases

ProteinModelPortaliQ06587.
SMRiQ06587. Positions 12-111, 261-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 234205Necessary for transcriptional repressionBy similarityAdd
BLAST
Regioni230 – 406177Necessary for interaction with CBX2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 2044Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi205 – 26056Gly-richAdd
BLAST
Compositional biasi314 – 37764Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 8841RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG324386.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ06587.
KOiK10695.
OMAiQSASKTW.
OrthoDBiEOG7NGQC3.
PhylomeDBiQ06587.
TreeFamiTF105501.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06587-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI
60 70 80 90 100
CLDMLKNTMT TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD
110 120 130 140 150
PNFDALISKI YPSREEYEAH QDRVLIRLSR LHNQQALSSS IEEGLRMQAM
160 170 180 190 200
HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE GDGEDVSSDS APDSAPGPAP
210 220 230 240 250
KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG GGTLGPPSPP
260 270 280 290 300
GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
310 320 330 340 350
LRIALERRQQ QEAGEPGGPG GGASDTGGPD GCGGEGGGAG GGDGPEEPAL
360 370 380 390 400
PSLEGVSEKQ YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA

PTKDPK
Length:406
Mass (Da):42,429
Last modified:March 21, 2006 - v2
Checksum:i6959787479DE9DAB
GO
Isoform 2 (identifier: Q06587-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:377
Mass (Da):39,146
Checksum:iF406E93593E0CF69
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 2 PublicationsVSP_017694Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14000 mRNA. Translation: CAA78389.1.
BT007352 mRNA. Translation: AAP36016.1.
AK289355 mRNA. Translation: BAF82044.1.
AL031228 Genomic DNA. Translation: CAA20235.1.
AL031228 Genomic DNA. Translation: CAI95620.1.
AL713971 Genomic DNA. Translation: CAI17650.1.
AL645940 Genomic DNA. Translation: CAI18069.1.
AL844527 Genomic DNA. Translation: CAI41841.1.
CR759786 Genomic DNA. Translation: CAQ08246.1.
CR759733 Genomic DNA. Translation: CAQ10303.1.
CR847841, CR547129 Genomic DNA. Translation: CAQ10314.1.
CR547129, CR847841 Genomic DNA. Translation: CAQ10355.1.
BC002922 mRNA. Translation: AAH02922.2.
BC051866 mRNA. Translation: AAH51866.1.
CCDSiCCDS34424.1. [Q06587-1]
PIRiA47380.
RefSeqiNP_002922.2. NM_002931.3. [Q06587-1]
UniGeneiHs.631989.

Genome annotation databases

EnsembliENST00000374656; ENSP00000363787; ENSG00000204227. [Q06587-1]
ENST00000383212; ENSP00000372699; ENSG00000206287. [Q06587-1]
ENST00000415941; ENSP00000412190; ENSG00000226788. [Q06587-1]
ENST00000427374; ENSP00000400572; ENSG00000231115. [Q06587-1]
ENST00000430233; ENSP00000396271; ENSG00000228520. [Q06587-1]
ENST00000436128; ENSP00000396439; ENSG00000235107. [Q06587-1]
GeneIDi6015.
KEGGihsa:6015.
UCSCiuc003odk.3. human. [Q06587-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14000 mRNA. Translation: CAA78389.1.
BT007352 mRNA. Translation: AAP36016.1.
AK289355 mRNA. Translation: BAF82044.1.
AL031228 Genomic DNA. Translation: CAA20235.1.
AL031228 Genomic DNA. Translation: CAI95620.1.
AL713971 Genomic DNA. Translation: CAI17650.1.
AL645940 Genomic DNA. Translation: CAI18069.1.
AL844527 Genomic DNA. Translation: CAI41841.1.
CR759786 Genomic DNA. Translation: CAQ08246.1.
CR759733 Genomic DNA. Translation: CAQ10303.1.
CR847841, CR547129 Genomic DNA. Translation: CAQ10314.1.
CR547129, CR847841 Genomic DNA. Translation: CAQ10355.1.
BC002922 mRNA. Translation: AAH02922.2.
BC051866 mRNA. Translation: AAH51866.1.
CCDSiCCDS34424.1. [Q06587-1]
PIRiA47380.
RefSeqiNP_002922.2. NM_002931.3. [Q06587-1]
UniGeneiHs.631989.

3D structure databases

ProteinModelPortaliQ06587.
SMRiQ06587. Positions 12-111, 261-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111947. 59 interactions.
DIPiDIP-42043N.
IntActiQ06587. 36 interactions.
MINTiMINT-1327105.
STRINGi9606.ENSP00000363787.

PTM databases

PhosphoSiteiQ06587.

Polymorphism and mutation databases

BioMutaiRING1.
DMDMi90110053.

Proteomic databases

MaxQBiQ06587.
PaxDbiQ06587.
PeptideAtlasiQ06587.
PRIDEiQ06587.

Protocols and materials databases

DNASUi6015.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374656; ENSP00000363787; ENSG00000204227. [Q06587-1]
ENST00000383212; ENSP00000372699; ENSG00000206287. [Q06587-1]
ENST00000415941; ENSP00000412190; ENSG00000226788. [Q06587-1]
ENST00000427374; ENSP00000400572; ENSG00000231115. [Q06587-1]
ENST00000430233; ENSP00000396271; ENSG00000228520. [Q06587-1]
ENST00000436128; ENSP00000396439; ENSG00000235107. [Q06587-1]
GeneIDi6015.
KEGGihsa:6015.
UCSCiuc003odk.3. human. [Q06587-1]

Organism-specific databases

CTDi6015.
GeneCardsiGC06P033202.
GC06Pj33097.
GC06Pk33154.
GC06Pl33330.
GC06Pm33346.
GC06Pn33105.
HGNCiHGNC:10018. RING1.
HPAiHPA008701.
MIMi602045. gene.
neXtProtiNX_Q06587.
PharmGKBiPA34393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG324386.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiQ06587.
KOiK10695.
OMAiQSASKTW.
OrthoDBiEOG7NGQC3.
PhylomeDBiQ06587.
TreeFamiTF105501.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_355174. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiRING1. human.
GeneWikiiRING1.
GenomeRNAii6015.
NextBioi23467.
PROiQ06587.
SOURCEiSearch...

Gene expression databases

BgeeiQ06587.
CleanExiHS_RING1.
GenevestigatoriQ06587.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye and Skin.
  6. "RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor."
    Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W., Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.
    Mol. Cell. Biol. 17:4105-4113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH PHC2.
  7. "RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity."
    Satijn D.P.E., Otte A.P.
    Mol. Cell. Biol. 19:57-68(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation."
    Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.
    Genes Cells 7:835-850(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCGF6.
  9. "The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans."
    Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E.
    Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX.
  10. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
    Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
    Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8; CBX3; RNF2; MBLR; L3MBTL2 AND YAF2.
  11. "Role of histone H2A ubiquitination in Polycomb silencing."
    Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
    Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX WITH RNF2; BMI1 AND PHC2.
  12. "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
    Cao R., Tsukada Y., Zhang Y.
    Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets."
    Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.
    Mol. Cell. Biol. 26:6880-6889(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RYBP; PCGF1; BCOR AND RNF2.
  14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-187 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
    Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
    PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH PCGF2.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-248 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
    Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-38; SER-187; THR-215; THR-220; SER-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRING1_HUMAN
AccessioniPrimary (citable) accession number: Q06587
Secondary accession number(s): A8JZZ0
, Q5JP96, Q5SQW2, Q86V19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 21, 2006
Last modified: May 27, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.