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E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (Huntingtin-interacting protein 2-interacting protein 3) (HIP2-interacting protein 3) (Protein DinG) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING finger protein BAP-1) (RING-type E3 ubiquitin transferase RING2)

 RING2_HUMAN             Reviewed;         336 AA.
Q99496; B2RBS7; B3KRH1; Q5TEN1; Q5TEN2;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
20-DEC-2017, entry version 174.
RecName: Full=E3 ubiquitin-protein ligase RING2;
EC=2.3.2.27 {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:26151332};
AltName: Full=Huntingtin-interacting protein 2-interacting protein 3;
Short=HIP2-interacting protein 3;
AltName: Full=Protein DinG;
AltName: Full=RING finger protein 1B;
Short=RING1b;
AltName: Full=RING finger protein 2;
AltName: Full=RING finger protein BAP-1;
AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000305};
Name=RNF2; Synonyms=BAP1, DING, HIPI3, RING1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Dyer M.J.S., Abdul-Rauf M., Heward J.M., Cui X., Cleary M.L.,
Catovsky D.;
"Interactions of BCL7A with novel ring finger proteins.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Li S.-F.;
"Identification of Bap-1, a protein that binds to integrin and is
involved in integrin-mediated signal transduction.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH HIP2, FUNCTION, AND MUTAGENESIS OF CYS-51; CYS-54 AND
HIS-69.
PubMed=11513855; DOI=10.1016/S0014-5793(01)02689-8;
Lee S.-J., Choi J.-Y., Sung Y.-M., Park H., Rhim H., Kang S.;
"E3 ligase activity of RING finger proteins that interact with Hip-2,
a human ubiquitin-conjugating enzyme.";
FEBS Lett. 503:61-64(2001).
[8]
INTERACTION WITH TFCP2.
PubMed=11865070; DOI=10.1128/MCB.22.6.1936-1946.2002;
Tuckfield A., Clouston D.R., Wilanowski T.M., Zhao L.-L.,
Cunningham J.M., Jane S.M.;
"Binding of the RING polycomb proteins to specific target genes in
complex with the grainyhead-like family of developmental transcription
factors.";
Mol. Cell. Biol. 22:1936-1946(2002).
[9]
IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX.
PubMed=12167701; DOI=10.1128/MCB.22.17.6070-6078.2002;
Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
Kingston R.E.;
"The core of the polycomb repressive complex is compositionally and
functionally conserved in flies and humans.";
Mol. Cell. Biol. 22:6070-6078(2002).
[10]
IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8;
CBX3; RNF1; MBLR; L3MBTL2 AND YAF2.
PubMed=12004135; DOI=10.1126/science.1069861;
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
"A complex with chromatin modifiers that occupies E2F- and Myc-
responsive genes in G0 cells.";
Science 296:1132-1136(2002).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE
COMPLEX WITH RING1; PHC2 AND BMI1, FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, AND MUTAGENESIS OF HIS-69 AND ARG-70.
PubMed=15386022; DOI=10.1038/nature02985;
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H2A ubiquitination in Polycomb silencing.";
Nature 431:873-878(2004).
[12]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
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.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[13]
FUNCTION.
PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
Cao R., Tsukada Y., Zhang Y.;
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene
silencing.";
Mol. Cell 20:845-854(2005).
[14]
INTERACTION WITH RYBP; PCGF1; BCOR AND RING1.
PubMed=16943429; DOI=10.1128/MCB.00630-06;
Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
"Polycomb group and SCF ubiquitin ligases are found in a novel BCOR
complex that is recruited to BCL6 targets.";
Mol. Cell. Biol. 26:6880-6889(2006).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH PCGF2.
PubMed=19636380; DOI=10.1371/journal.pone.0006380;
Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K.,
Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.;
"Several distinct polycomb complexes regulate and co-localize on the
INK4a tumor suppressor locus.";
PLoS ONE 4:E6380-E6380(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6;
CBX7 AND CBX8, AND SUBCELLULAR LOCATION.
PubMed=21282530; DOI=10.1074/mcp.M110.002642;
Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
"Interaction proteomics analysis of polycomb proteins defines distinct
PRC1 Complexes in mammalian cells.";
Mol. Cell. Proteomics 0:0-0(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-168, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH
PCGF5; AUTS2; CSNK2B AND RYBP, IDENTIFICATION BY MASS SPECTROMETRY,
MUTAGENESIS OF SER-41 AND SER-168, AND PHOSPHORYLATION AT SER-41 AND
SER-168.
PubMed=25519132; DOI=10.1038/nature13921;
Gao Z., Lee P., Stafford J.M., von Schimmelmann M., Schaefer A.,
Reinberg D.;
"An AUTS2-polycomb complex activates gene expression in the CNS.";
Nature 516:349-354(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1.
PubMed=26687479; DOI=10.1038/srep18388;
Oliviero G., Munawar N., Watson A., Streubel G., Manning G.,
Bardwell V., Bracken A.P., Cagney G.;
"The variant Polycomb Repressor Complex 1 component PCGF1 interacts
with a pluripotency sub-network that includes DPPA4, a regulator of
embryogenesis.";
Sci. Rep. 5:18388-18388(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249 AND LYS-323, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-114 IN COMPLEX WITH BMI1
AND ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBUNIT.
PubMed=16714294; DOI=10.1074/jbc.M602461200;
Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.;
"Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase
complex.";
J. Biol. Chem. 281:20643-20649(2006).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 220-330, INTERACTION WITH
CBX7, AND MUTAGENESIS OF TYR-262.
PubMed=19791798; DOI=10.1021/bi901131u;
Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S.,
Arrowsmith C.H.;
"Ring1B contains a ubiquitin-like docking module for interaction with
Cbx proteins.";
Biochemistry 48:10542-10548(2009).
[25]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 223-333 IN COMPLEXES WITH
CBX7 AND RYBP, FUNCTION, AND MUTAGENESIS OF TYR-247; HIS-258 AND
TYR-262.
PubMed=20696397; DOI=10.1016/j.str.2010.04.013;
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.;
"Polycomb group targeting through different binding partners of RING1B
C-terminal domain.";
Structure 18:966-975(2010).
[26] {ECO:0000244|PDB:3RPG}
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC
IONS; BMI1 AND UB2D3, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
MUTAGENESIS OF ASP-56 AND 97-LYS-ARG-98.
PubMed=21772249; DOI=10.1038/emboj.2011.243;
Bentley M.L., Corn J.E., Dong K.C., Phung Q., Cheung T.K.,
Cochran A.G.;
"Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin
ligase complex.";
EMBO J. 30:3285-3297(2011).
[27] {ECO:0000244|PDB:4R8P}
X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 2-116 IN COMPLEX WITH ZINC
IONS; THE NUCLEOSOME; BMI1 AND UB2D3, FUNCTION, AND MUTAGENESIS OF
ARG-81; LYS-93; LYS-97 AND ARG-98.
PubMed=25355358; DOI=10.1038/nature13890;
McGinty R.K., Henrici R.C., Tan S.;
"Crystal structure of the PRC1 ubiquitylation module bound to the
nucleosome.";
Nature 514:591-596(2014).
[28] {ECO:0000244|PDB:4S3O}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC
IONS; UB2D3 AND PCGF5, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND
PATHWAY.
PubMed=26151332; DOI=10.1038/ncomms8621;
Taherbhoy A.M., Huang O.W., Cochran A.G.;
"BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
Nat. Commun. 6:7621-7621(2015).
-!- FUNCTION: 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
(PubMed:15386022, PubMed:16359901, PubMed:25519132,
PubMed:21772249, PubMed:25355358, PubMed:26151332). 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 (By similarity). 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
(PubMed:16359901, PubMed:26151332). PcG PRC1 complex acts via
chromatin remodeling and modification of histones, rendering
chromatin heritably changed in its expressibility
(PubMed:26151332). E3 ubiquitin-protein ligase activity is
enhanced by BMI1/PCGF4 (PubMed:21772249). 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 (Probable).
Association with the chromosomal DNA is cell-cycle dependent. In
resting B- and T-lymphocytes, interaction with AURKB leads to
block its activity, thereby maintaining transcription in resting
lymphocytes (By similarity). {ECO:0000250|UniProtKB:Q9CQJ4,
ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294,
ECO:0000269|PubMed:20696397, ECO:0000269|PubMed:21772249,
ECO:0000269|PubMed:25355358, ECO:0000269|PubMed:25519132,
ECO:0000269|PubMed:26151332, ECO:0000305}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:26151332}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:21772249,
ECO:0000269|PubMed:26151332}.
-!- SUBUNIT: Component of chromatin-associated Polycomb (PcG)
complexes. Component of a number of PRC1-like complexes; these
complexes contain either the polycomb group ring finger protein
PCGF1, or PCGF2, or PCGF3, or PCGF4, or PCGF5, or PCGF6
(PubMed:12167701, PubMed:15386022, PubMed:19636380,
PubMed:21282530, PubMed:26687479, PubMed:26151332). Part of a
complex that contains RNF2, UB2D3 and BMI1; within that complex
RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts only
with RNF2 (PubMed:21772249, PubMed:25355358). The complex composed
of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only
with nucleosomal histone H2A (PubMed:21772249). Part of a complex
that contains PCGF5, RNF2 and UBE2D3 (PubMed:26151332). Part of a
complex that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP
(PubMed:25519132). Interacts with RYBP, PCGF2, CBX4, CBX6, CBX7
and CBX8 (PubMed:19636380, PubMed:21282530, PubMed:19791798,
PubMed:20696397). Interacts with RNF1/RING1, BMI1 and PHC2
(PubMed:15386022, PubMed:16714294). Interaction with RYBP and CBX7
is mutually exclusive; both compete for the same binding site on
RNF2 (By similarity). Component of repressive BCOR complex
containing a Polycomb group subcomplex at least composed of RYBP,
PCGF1, BCOR and RING1 (PubMed:16943429). 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 (PubMed:12004135). 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
(PubMed:15960975). Interacts with RYBP, HIP2 and TFCP2
(PubMed:11513855, PubMed:11865070, PubMed:20696397).
{ECO:0000250|UniProtKB:Q9CQJ4, ECO:0000269|PubMed:11513855,
ECO:0000269|PubMed:11865070, ECO:0000269|PubMed:12004135,
ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:15386022,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16714294,
ECO:0000269|PubMed:16943429, ECO:0000269|PubMed:19636380,
ECO:0000269|PubMed:19791798, ECO:0000269|PubMed:21282530,
ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:25355358,
ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:26151332,
ECO:0000269|PubMed:26687479}.
-!- INTERACTION:
P08183:ABCB1; NbExp=2; IntAct=EBI-722416, EBI-1057359;
P35226:BMI1; NbExp=17; IntAct=EBI-722416, EBI-2341576;
O00257:CBX4; NbExp=5; IntAct=EBI-722416, EBI-722425;
O00257-3:CBX4; NbExp=2; IntAct=EBI-722416, EBI-4392727;
O95503:CBX6; NbExp=6; IntAct=EBI-722416, EBI-3951758;
O95931:CBX7; NbExp=13; IntAct=EBI-722416, EBI-3923843;
Q9HC52:CBX8; NbExp=10; IntAct=EBI-722416, EBI-712912;
P68400:CSNK2A1; NbExp=3; IntAct=EBI-722416, EBI-347804;
P67870:CSNK2B; NbExp=2; IntAct=EBI-722416, EBI-348169;
P0C0S8:HIST1H2AM; NbExp=5; IntAct=EBI-722416, EBI-1390628;
Q9H7Z6:KAT8; NbExp=2; IntAct=EBI-722416, EBI-896414;
Q9BSM1:PCGF1; NbExp=15; IntAct=EBI-722416, EBI-749901;
P35227:PCGF2; NbExp=11; IntAct=EBI-722416, EBI-2129767;
Q3KNV8:PCGF3; NbExp=4; IntAct=EBI-722416, EBI-2339807;
Q86SE9:PCGF5; NbExp=7; IntAct=EBI-722416, EBI-2827999;
Q9BYE7:PCGF6; NbExp=4; IntAct=EBI-722416, EBI-1048026;
Q06587:RING1; NbExp=5; IntAct=EBI-722416, EBI-752313;
Q8N488:RYBP; NbExp=13; IntAct=EBI-722416, EBI-752324;
P51668:UBE2D1; NbExp=3; IntAct=EBI-722416, EBI-743540;
P62837:UBE2D2; NbExp=3; IntAct=EBI-722416, EBI-347677;
P61077:UBE2D3; NbExp=3; IntAct=EBI-722416, EBI-348268;
Q9Y2X8:UBE2D4; NbExp=5; IntAct=EBI-722416, EBI-745527;
Q96LR5:UBE2E2; NbExp=3; IntAct=EBI-722416, EBI-2129763;
Q969T4:UBE2E3; NbExp=3; IntAct=EBI-722416, EBI-348496;
P51784:USP11; NbExp=4; IntAct=EBI-722416, EBI-306876;
Q93009:USP7; NbExp=5; IntAct=EBI-722416, EBI-302474;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}.
Chromosome {ECO:0000250|UniProtKB:Q9CQJ4}. 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. {ECO:0000250|UniProtKB:Q9CQJ4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99496-1; Sequence=Displayed;
Name=2;
IsoId=Q99496-2; Sequence=VSP_055439;
Note=No experimental confirmation available.;
-!- PTM: Polyubiquitinated in the presence of UBE2D3 (in vitro).
{ECO:0000269|PubMed:26151332}.
-!- PTM: Monoubiquitinated, by auto-ubiquitination. {ECO:0000250}.
-!- MISCELLANEOUS: The hPRC-H complex purification reported by
PubMed:12167701 probably presents a mixture of different PRC1-like
complexes.
-!- SEQUENCE CAUTION:
Sequence=CAI17849.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI17850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y10571; CAA71596.1; -; mRNA.
EMBL; AF141327; AAD29717.1; -; mRNA.
EMBL; AK091574; BAG52383.1; -; mRNA.
EMBL; AK314793; BAG37324.1; -; mRNA.
EMBL; AL109865; CAC00611.1; -; Genomic_DNA.
EMBL; AL109865; CAI17849.1; ALT_SEQ; Genomic_DNA.
EMBL; AL109865; CAI17850.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471067; EAW91187.1; -; Genomic_DNA.
EMBL; CH471067; EAW91188.1; -; Genomic_DNA.
EMBL; BC012583; AAH12583.1; -; mRNA.
CCDS; CCDS1365.1; -. [Q99496-1]
RefSeq; NP_009143.1; NM_007212.3. [Q99496-1]
RefSeq; XP_011508153.1; XM_011509851.2. [Q99496-1]
RefSeq; XP_011508154.1; XM_011509852.2. [Q99496-1]
UniGene; Hs.591490; -.
PDB; 2H0D; X-ray; 2.50 A; B=15-114.
PDB; 3GS2; X-ray; 1.70 A; A/C=223-333.
PDB; 3H8H; X-ray; 2.00 A; A=220-330.
PDB; 3IXS; X-ray; 1.70 A; A/C/E/G/I/K=223-333.
PDB; 3RPG; X-ray; 2.65 A; C=1-116.
PDB; 4R8P; X-ray; 3.28 A; L/N=2-116.
PDB; 4S3O; X-ray; 2.00 A; B/E=1-116.
PDBsum; 2H0D; -.
PDBsum; 3GS2; -.
PDBsum; 3H8H; -.
PDBsum; 3IXS; -.
PDBsum; 3RPG; -.
PDBsum; 4R8P; -.
PDBsum; 4S3O; -.
ProteinModelPortal; Q99496; -.
SMR; Q99496; -.
BioGrid; 111972; 730.
CORUM; Q99496; -.
DIP; DIP-40034N; -.
IntAct; Q99496; 95.
MINT; MINT-1420125; -.
STRING; 9606.ENSP00000356480; -.
iPTMnet; Q99496; -.
PhosphoSitePlus; Q99496; -.
BioMuta; RNF2; -.
DMDM; 62901044; -.
EPD; Q99496; -.
MaxQB; Q99496; -.
PaxDb; Q99496; -.
PeptideAtlas; Q99496; -.
PRIDE; Q99496; -.
DNASU; 6045; -.
Ensembl; ENST00000367509; ENSP00000356479; ENSG00000121481. [Q99496-2]
Ensembl; ENST00000367510; ENSP00000356480; ENSG00000121481. [Q99496-1]
GeneID; 6045; -.
KEGG; hsa:6045; -.
UCSC; uc001grc.2; human. [Q99496-1]
CTD; 6045; -.
DisGeNET; 6045; -.
EuPathDB; HostDB:ENSG00000121481.10; -.
GeneCards; RNF2; -.
HGNC; HGNC:10061; RNF2.
HPA; HPA026803; -.
MIM; 608985; gene.
neXtProt; NX_Q99496; -.
OpenTargets; ENSG00000121481; -.
PharmGKB; PA34426; -.
eggNOG; KOG0311; Eukaryota.
eggNOG; ENOG410XQ5G; LUCA.
GeneTree; ENSGT00390000016977; -.
HOGENOM; HOG000273917; -.
HOVERGEN; HBG079942; -.
InParanoid; Q99496; -.
KO; K10695; -.
OMA; FNQTQSQ; -.
OrthoDB; EOG091G06VO; -.
PhylomeDB; Q99496; -.
TreeFam; TF105501; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SIGNOR; Q99496; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q99496; -.
GeneWiki; RNF2; -.
GenomeRNAi; 6045; -.
PRO; PR:Q99496; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000121481; -.
CleanEx; HS_BAP1; -.
CleanEx; HS_RNF2; -.
ExpressionAtlas; Q99496; baseline and differential.
Genevisible; Q99496; HS.
GO; GO:0000791; C:euchromatin; IEA:Ensembl.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0071535; F:RING-like zinc finger domain binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR032443; RAWUL.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF16207; RAWUL; 1.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromosome;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 336 E3 ubiquitin-protein ligase RING2.
/FTId=PRO_0000056038.
ZN_FING 51 91 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 2 179 Interaction with HIP2.
{ECO:0000269|PubMed:11513855}.
REGION 93 98 Interaction with nucleosomes via an
acidic patch on histone H2A and histone
H2B. {ECO:0000269|PubMed:25355358}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000269|PubMed:25519132}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25519132}.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9CQJ4}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 323 323 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 84 155 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055439.
MUTAGEN 41 41 S->A,D: No effect on ubiquitin ligase
activity on histone H2A.
{ECO:0000269|PubMed:25519132}.
MUTAGEN 51 51 C->W: Strong decrease in HIP2-binding;
when associated with S-54.
{ECO:0000269|PubMed:11513855}.
MUTAGEN 54 54 C->S: Strong decrease in HIP2-binding;
when associated with W-51.
{ECO:0000269|PubMed:11513855}.
MUTAGEN 56 56 D->K: Loss of ubiquitin ligase activity
on histone H2A.
{ECO:0000269|PubMed:21772249}.
MUTAGEN 69 69 H->Y: Loss of HIP2-binding and loss of
ubiquitin ligase activity on histone H2A.
{ECO:0000269|PubMed:11513855,
ECO:0000269|PubMed:15386022}.
MUTAGEN 70 70 R->C: Loss of ubiquitin ligase activity
on histone H2A.
{ECO:0000269|PubMed:15386022}.
MUTAGEN 81 81 R->A: Decreases ubiquitin ligase activity
on histone H2A.
{ECO:0000269|PubMed:25355358}.
MUTAGEN 93 93 K->A: Mildly decreases ubiquitin ligase
activity on histone H2A.
{ECO:0000269|PubMed:25355358}.
MUTAGEN 97 98 KR->AA: Loss of ubiquitin ligase activity
on histone H2A.
{ECO:0000269|PubMed:21772249}.
MUTAGEN 97 97 K->A: Strongly decreases ubiquitin ligase
activity on histone H2A.
{ECO:0000269|PubMed:25355358}.
MUTAGEN 98 98 R->A: Nearly abolishes ubiquitin ligase
activity on histone H2A.
{ECO:0000269|PubMed:25355358}.
MUTAGEN 168 168 S->E: Decreases ubiquitin ligase activity
on histone H2A.
{ECO:0000269|PubMed:25519132}.
MUTAGEN 247 247 Y->A: Reduced interaction with CBX7.
{ECO:0000269|PubMed:20696397}.
MUTAGEN 258 258 H->A: Reduced interaction with CBX7.
{ECO:0000269|PubMed:20696397}.
MUTAGEN 262 262 Y->A: Reduced interaction with CBX7.
{ECO:0000269|PubMed:19791798,
ECO:0000269|PubMed:20696397}.
HELIX 13 16 {ECO:0000244|PDB:4S3O}.
HELIX 21 24 {ECO:0000244|PDB:4S3O}.
STRAND 37 39 {ECO:0000244|PDB:2H0D}.
HELIX 42 45 {ECO:0000244|PDB:4S3O}.
HELIX 46 49 {ECO:0000244|PDB:4S3O}.
TURN 52 54 {ECO:0000244|PDB:4S3O}.
STRAND 59 64 {ECO:0000244|PDB:4S3O}.
TURN 65 67 {ECO:0000244|PDB:4S3O}.
STRAND 70 72 {ECO:0000244|PDB:4S3O}.
HELIX 73 80 {ECO:0000244|PDB:4S3O}.
TURN 88 90 {ECO:0000244|PDB:4S3O}.
HELIX 97 99 {ECO:0000244|PDB:4S3O}.
STRAND 100 102 {ECO:0000244|PDB:4S3O}.
HELIX 104 113 {ECO:0000244|PDB:4S3O}.
STRAND 225 232 {ECO:0000244|PDB:3GS2}.
TURN 234 236 {ECO:0000244|PDB:3GS2}.
STRAND 246 251 {ECO:0000244|PDB:3GS2}.
HELIX 256 277 {ECO:0000244|PDB:3GS2}.
HELIX 283 285 {ECO:0000244|PDB:3IXS}.
HELIX 288 290 {ECO:0000244|PDB:3IXS}.
STRAND 291 296 {ECO:0000244|PDB:3GS2}.
STRAND 302 304 {ECO:0000244|PDB:3GS2}.
HELIX 311 318 {ECO:0000244|PDB:3GS2}.
STRAND 321 323 {ECO:0000244|PDB:3GS2}.
STRAND 325 331 {ECO:0000244|PDB:3GS2}.
SEQUENCE 336 AA; 37655 MW; 90EA546E1F4DB7EC CRC64;
MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN
TMTTKECLHR FCADCIITAL RSGNKECPTC RKKLVSKRSL RPDPNFDALI SKIYPSRDEY
EAHQERVLAR INKHNNQQAL SHSIEEGLKI QAMNRLQRGK KQQIENGSGA EDNGDSSHCS
NASTHSNQEA GPSNKRTKTS DDSGLELDNN NAAMAIDPVM DGASEIELVF RPHPTLMEKD
DSAQTRYIKT SGNATVDHLS KYLAVRLALE ELRSKGESNQ MNLDTASEKQ YTIYIATASG
QFTVLNGSFS LELVSEKYWK VNKPMELYYA PTKEHK


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