Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99496

- RING2_HUMAN

UniProt

Q99496 - RING2_HUMAN

Protein

E3 ubiquitin-protein ligase RING2

Gene

RNF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub 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. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes.5 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. RING-like zinc finger domain binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: Ensembl
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior axis specification Source: Ensembl
    2. gastrulation with mouth forming second Source: Ensembl
    3. histone H2A-K119 monoubiquitination Source: UniProtKB
    4. histone H2A monoubiquitination Source: UniProtKB
    5. mitotic cell cycle Source: Ensembl
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    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 RING2 (EC:6.3.2.-)
    Alternative name(s):
    Huntingtin-interacting protein 2-interacting protein 3
    Short name:
    HIP2-interacting protein 3
    Protein DinG
    RING finger protein 1B
    Short name:
    RING1b
    RING finger protein 2
    RING finger protein BAP-1
    Gene namesi
    Name:RNF2
    Synonyms:BAP1, DING, HIPI3, RING1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10061. RNF2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome By similarity
    Note: Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells By similarity.By similarity

    GO - Cellular componenti

    1. MLL1 complex Source: UniProtKB
    2. nuclear body Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PcG protein complex Source: UniProtKB
    6. PRC1 complex Source: UniProtKB
    7. sex chromatin Source: Ensembl
    8. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511C → W: Strong decrease in HIP2-binding; when associated with S-54. 1 Publication
    Mutagenesisi54 – 541C → S: Strong decrease in HIP2-binding; when associated with W-51. 1 Publication
    Mutagenesisi69 – 691H → Y: Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A. 2 Publications
    Mutagenesisi70 – 701R → C: Loss of ubiquitin ligase activity on histone H2A. 1 Publication
    Mutagenesisi247 – 2471Y → A: Reduced interaction with CBX7. 1 Publication
    Mutagenesisi258 – 2581H → A: Reduced interaction with CBX7. 1 Publication
    Mutagenesisi262 – 2621Y → A: Reduced interaction with CBX7. 2 Publications

    Organism-specific databases

    PharmGKBiPA34426.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 336335E3 ubiquitin-protein ligase RING2PRO_0000056038Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Polyubiquitinated in the presence of UBE2D3 (in vitro).By similarity
    Monoubiquitinated, by auto-ubiquitination.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ99496.
    PaxDbiQ99496.
    PRIDEiQ99496.

    PTM databases

    PhosphoSiteiQ99496.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99496.
    BgeeiQ99496.
    CleanExiHS_BAP1.
    HS_RNF2.
    GenevestigatoriQ99496.

    Organism-specific databases

    HPAiHPA026803.

    Interactioni

    Subunit structurei

    Interacts with CBX2 and PHC1. Interacts with CHTOP. Interacts with AURKB By similarity. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/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 KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, 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. Component of chromatin-associated Polycomb (PcG) complexes. Interacts with RYBP, PCGF2, CBX4, CBX6, CBX7 and CBX8. Interacts with RNF1/RING1, BMI1 and PHC2.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCB1P081832EBI-722416,EBI-1057359
    BMI1P352269EBI-722416,EBI-2341576
    CBX4O00257-32EBI-722416,EBI-4392727
    CBX6O955033EBI-722416,EBI-3951758
    CBX7O959313EBI-722416,EBI-3923843
    CBX8Q9HC525EBI-722416,EBI-712912
    KAT8Q9H7Z62EBI-722416,EBI-896414
    PCGF1Q9BSM14EBI-722416,EBI-749901
    PCGF2P352277EBI-722416,EBI-2129767
    PCGF3Q3KNV82EBI-722416,EBI-2339807
    PCGF5Q86SE92EBI-722416,EBI-2827999
    RING1Q065874EBI-722416,EBI-752313
    USP11P517844EBI-722416,EBI-306876
    USP7Q930094EBI-722416,EBI-302474

    Protein-protein interaction databases

    BioGridi111972. 696 interactions.
    DIPiDIP-40034N.
    IntActiQ99496. 49 interactions.
    MINTiMINT-1420125.
    STRINGi9606.ENSP00000356480.

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 255
    Beta strandi37 – 393
    Beta strandi43 – 453
    Helixi47 – 493
    Turni52 – 543
    Beta strandi60 – 645
    Turni65 – 673
    Beta strandi70 – 723
    Helixi73 – 819
    Turni88 – 903
    Helixi97 – 993
    Beta strandi100 – 1023
    Helixi104 – 11310
    Beta strandi225 – 2328
    Turni234 – 2363
    Beta strandi246 – 2516
    Helixi256 – 27722
    Helixi283 – 2853
    Helixi288 – 2903
    Beta strandi291 – 2966
    Beta strandi302 – 3043
    Helixi311 – 3188
    Beta strandi321 – 3233
    Beta strandi325 – 3317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H0DX-ray2.50B15-114[»]
    3GS2X-ray1.70A/C223-333[»]
    3H8HX-ray2.00A220-330[»]
    3IXSX-ray1.70A/C/E/G/I/K223-333[»]
    3RPGX-ray2.65C1-116[»]
    ProteinModelPortaliQ99496.
    SMRiQ99496. Positions 15-114, 223-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99496.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 179178Interaction with HIP2Add
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 9141RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG324386.
    HOGENOMiHOG000273917.
    HOVERGENiHBG079942.
    InParanoidiQ99496.
    KOiK10695.
    OMAiSDCIITA.
    OrthoDBiEOG7NGQC3.
    PhylomeDBiQ99496.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99496-1) [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

    MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM    50
    CPICLDMLKN TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL 100
    RPDPNFDALI SKIYPSRDEY EAHQERVLAR INKHNNQQAL SHSIEEGLKI 150
    QAMNRLQRGK KQQIENGSGA EDNGDSSHCS NASTHSNQEA GPSNKRTKTS 200
    DDSGLELDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD DSAQTRYIKT 250
    SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG 300
    QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK 336
    Length:336
    Mass (Da):37,655
    Last modified:May 1, 1997 - v1
    Checksum:i90EA546E1F4DB7EC
    GO
    Isoform 2 (identifier: Q99496-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-155: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:264
    Mass (Da):29,258
    Checksum:i332219DF283B16C8
    GO

    Sequence cautioni

    The sequence CAI17849.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI17850.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei84 – 15572Missing in isoform 2. 1 PublicationVSP_055439Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10571 mRNA. Translation: CAA71596.1.
    AF141327 mRNA. Translation: AAD29717.1.
    AK091574 mRNA. Translation: BAG52383.1.
    AK314793 mRNA. Translation: BAG37324.1.
    AL109865 Genomic DNA. Translation: CAC00611.1.
    AL109865 Genomic DNA. Translation: CAI17849.1. Sequence problems.
    AL109865 Genomic DNA. Translation: CAI17850.1. Sequence problems.
    CH471067 Genomic DNA. Translation: EAW91187.1.
    CH471067 Genomic DNA. Translation: EAW91188.1.
    BC012583 mRNA. Translation: AAH12583.1.
    CCDSiCCDS1365.1.
    RefSeqiNP_009143.1. NM_007212.3.
    UniGeneiHs.591490.

    Genome annotation databases

    EnsembliENST00000367509; ENSP00000356479; ENSG00000121481. [Q99496-2]
    ENST00000367510; ENSP00000356480; ENSG00000121481. [Q99496-1]
    GeneIDi6045.
    KEGGihsa:6045.
    UCSCiuc001grc.1. human.

    Polymorphism databases

    DMDMi62901044.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10571 mRNA. Translation: CAA71596.1 .
    AF141327 mRNA. Translation: AAD29717.1 .
    AK091574 mRNA. Translation: BAG52383.1 .
    AK314793 mRNA. Translation: BAG37324.1 .
    AL109865 Genomic DNA. Translation: CAC00611.1 .
    AL109865 Genomic DNA. Translation: CAI17849.1 . Sequence problems.
    AL109865 Genomic DNA. Translation: CAI17850.1 . Sequence problems.
    CH471067 Genomic DNA. Translation: EAW91187.1 .
    CH471067 Genomic DNA. Translation: EAW91188.1 .
    BC012583 mRNA. Translation: AAH12583.1 .
    CCDSi CCDS1365.1.
    RefSeqi NP_009143.1. NM_007212.3.
    UniGenei Hs.591490.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H0D X-ray 2.50 B 15-114 [» ]
    3GS2 X-ray 1.70 A/C 223-333 [» ]
    3H8H X-ray 2.00 A 220-330 [» ]
    3IXS X-ray 1.70 A/C/E/G/I/K 223-333 [» ]
    3RPG X-ray 2.65 C 1-116 [» ]
    ProteinModelPortali Q99496.
    SMRi Q99496. Positions 15-114, 223-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111972. 696 interactions.
    DIPi DIP-40034N.
    IntActi Q99496. 49 interactions.
    MINTi MINT-1420125.
    STRINGi 9606.ENSP00000356480.

    PTM databases

    PhosphoSitei Q99496.

    Polymorphism databases

    DMDMi 62901044.

    Proteomic databases

    MaxQBi Q99496.
    PaxDbi Q99496.
    PRIDEi Q99496.

    Protocols and materials databases

    DNASUi 6045.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367509 ; ENSP00000356479 ; ENSG00000121481 . [Q99496-2 ]
    ENST00000367510 ; ENSP00000356480 ; ENSG00000121481 . [Q99496-1 ]
    GeneIDi 6045.
    KEGGi hsa:6045.
    UCSCi uc001grc.1. human.

    Organism-specific databases

    CTDi 6045.
    GeneCardsi GC01P185014.
    HGNCi HGNC:10061. RNF2.
    HPAi HPA026803.
    MIMi 608985. gene.
    neXtProti NX_Q99496.
    PharmGKBi PA34426.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324386.
    HOGENOMi HOG000273917.
    HOVERGENi HBG079942.
    InParanoidi Q99496.
    KOi K10695.
    OMAi SDCIITA.
    OrthoDBi EOG7NGQC3.
    PhylomeDBi Q99496.
    TreeFami TF105501.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_169436. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    EvolutionaryTracei Q99496.
    GeneWikii RNF2.
    GenomeRNAii 6045.
    NextBioi 23553.
    PROi Q99496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99496.
    Bgeei Q99496.
    CleanExi HS_BAP1.
    HS_RNF2.
    Genevestigatori Q99496.

    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. "Interactions of BCL7A with novel ring finger proteins."
      Dyer M.J.S., Abdul-Rauf M., Heward J.M., Cui X., Cleary M.L., Catovsky D.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Identification of Bap-1, a protein that binds to integrin and is involved in integrin-mediated signal transduction."
      Li S.-F.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    7. "E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme."
      Lee S.-J., Choi J.-Y., Sung Y.-M., Park H., Rhim H., Kang S.
      FEBS Lett. 503:61-64(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIP2, FUNCTION, MUTAGENESIS OF CYS-51; CYS-54 AND HIS-69.
    8. "Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors."
      Tuckfield A., Clouston D.R., Wilanowski T.M., Zhao L.-L., Cunningham J.M., Jane S.M.
      Mol. Cell. Biol. 22:1936-1946(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TFCP2.
    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; RNF1; 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 BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE COMPLEX WITH RING1; PHC2 AND BMI1, FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF HIS-69 AND ARG-70.
    12. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    13. "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.
    14. "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 RING1.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 CBX4; CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
    19. "Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex."
      Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.
      J. Biol. Chem. 281:20643-20649(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-114 IN COMPLEX WITH BMI1 AND ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
    20. "Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins."
      Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S., Arrowsmith C.H.
      Biochemistry 48:10542-10548(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 220-330, INTERACTION WITH CBX7, MUTAGENESIS OF TYR-262.
    21. "Polycomb group targeting through different binding partners of RING1B C-terminal domain."
      Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U., Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P., McEwen D.G., Kim C.A.
      Structure 18:966-975(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 223-333 IN COMPLEXES WITH CBX7 AND RYBP, FUNCTION, MUTAGENESIS OF TYR-247; HIS-258 AND TYR-262.

    Entry informationi

    Entry nameiRING2_HUMAN
    AccessioniPrimary (citable) accession number: Q99496
    Secondary accession number(s): B2RBS7
    , B3KRH1, Q5TEN1, Q5TEN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3