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Q06587

- RING1_HUMAN

UniProt

Q06587 - RING1_HUMAN

Protein

E3 ubiquitin-protein ligase RING1

Gene

RING1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      Previous versions | rss
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    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

    1. chromatin binding Source: Ensembl
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: Ensembl
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. camera-type eye morphogenesis Source: Ensembl
    3. histone H2A monoubiquitination Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    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.
    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10018. RING1.

    Subcellular locationi

    Nucleus 1 Publication. Nucleus speckle 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PcG protein complex Source: UniProtKB
    6. PRC1 complex Source: UniProtKB
    7. sex chromatin Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34393.

    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 residuei38 – 381Phosphoserine2 Publications
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei190 – 1901Phosphoserine1 Publication
    Modified residuei220 – 2201Phosphothreonine1 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

    ArrayExpressiQ06587.
    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
    BMI1P3522611EBI-752313,EBI-2341576
    CBX6O955033EBI-752313,EBI-3951758
    CBX7O959313EBI-752313,EBI-3923843
    CBX8Q9HC523EBI-752313,EBI-712912
    PCGF1Q9BSM15EBI-752313,EBI-749901
    PCGF2P352275EBI-752313,EBI-2129767
    PCGF3Q3KNV82EBI-752313,EBI-2339807
    PCGF5Q86SE92EBI-752313,EBI-2827999
    RNF2Q994964EBI-752313,EBI-722416
    RYBPQ8N4882EBI-752313,EBI-752324
    USP11P517844EBI-752313,EBI-306876
    USP7Q930094EBI-752313,EBI-302474

    Protein-protein interaction databases

    BioGridi111947. 58 interactions.
    DIPiDIP-42043N.
    IntActiQ06587. 34 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.
    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. Align

    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

    MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI    50
    CLDMLKNTMT TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD 100
    PNFDALISKI YPSREEYEAH QDRVLIRLSR LHNQQALSSS IEEGLRMQAM 150
    HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE GDGEDVSSDS APDSAPGPAP 200
    KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG GGTLGPPSPP 250
    GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA 300
    LRIALERRQQ QEAGEPGGPG GGASDTGGPD GCGGEGGGAG GGDGPEEPAL 350
    PSLEGVSEKQ YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA 400
    PTKDPK 406
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi90110053.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34424.1. [Q06587-1 ]
    PIRi A47380.
    RefSeqi NP_002922.2. NM_002931.3. [Q06587-1 ]
    UniGenei Hs.631989.

    3D structure databases

    ProteinModelPortali Q06587.
    SMRi Q06587. Positions 12-111, 261-403.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111947. 58 interactions.
    DIPi DIP-42043N.
    IntActi Q06587. 34 interactions.
    MINTi MINT-1327105.
    STRINGi 9606.ENSP00000363787.

    PTM databases

    PhosphoSitei Q06587.

    Polymorphism databases

    DMDMi 90110053.

    Proteomic databases

    MaxQBi Q06587.
    PaxDbi Q06587.
    PeptideAtlasi Q06587.
    PRIDEi Q06587.

    Protocols and materials databases

    DNASUi 6015.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374656 ; 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 ]
    GeneIDi 6015.
    KEGGi hsa:6015.
    UCSCi uc003odk.3. human. [Q06587-1 ]

    Organism-specific databases

    CTDi 6015.
    GeneCardsi GC06P033196.
    GC06Pj33097.
    GC06Pk33154.
    GC06Pl33330.
    GC06Pm33346.
    GC06Pn33105.
    HGNCi HGNC:10018. RING1.
    HPAi HPA008701.
    MIMi 602045. gene.
    neXtProti NX_Q06587.
    PharmGKBi PA34393.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324386.
    HOGENOMi HOG000273917.
    HOVERGENi HBG079942.
    InParanoidi Q06587.
    KOi K10695.
    OMAi QSASKTW.
    OrthoDBi EOG7NGQC3.
    PhylomeDBi Q06587.
    TreeFami TF105501.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    GeneWikii RING1.
    GenomeRNAii 6015.
    NextBioi 23467.
    PROi Q06587.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06587.
    Bgeei Q06587.
    CleanExi HS_RING1.
    Genevestigatori Q06587.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 145 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