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Database: UniProt
Entry: Q99496
LinkDB: Q99496
Original site: Q99496 
ID   RING2_HUMAN             Reviewed;         336 AA.
AC   Q99496; B2RBS7; B3KRH1; Q5TEN1; Q5TEN2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   12-AUG-2020, entry version 198.
DE   RecName: Full=E3 ubiquitin-protein ligase RING2;
DE            EC=2.3.2.27 {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:26151332};
DE   AltName: Full=Huntingtin-interacting protein 2-interacting protein 3;
DE            Short=HIP2-interacting protein 3;
DE   AltName: Full=Protein DinG;
DE   AltName: Full=RING finger protein 1B;
DE            Short=RING1b;
DE   AltName: Full=RING finger protein 2;
DE   AltName: Full=RING finger protein BAP-1;
DE   AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000305};
GN   Name=RNF2; Synonyms=BAP1, DING, HIPI3, RING1B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Dyer M.J.S., Abdul-Rauf M., Heward J.M., Cui X., Cleary M.L., Catovsky D.;
RT   "Interactions of BCL7A with novel ring finger proteins.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Li S.-F.;
RT   "Identification of Bap-1, a protein that binds to integrin and is involved
RT   in integrin-mediated signal transduction.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH HIP2, FUNCTION, AND MUTAGENESIS OF CYS-51; CYS-54 AND
RP   HIS-69.
RX   PubMed=11513855; DOI=10.1016/s0014-5793(01)02689-8;
RA   Lee S.-J., Choi J.-Y., Sung Y.-M., Park H., Rhim H., Kang S.;
RT   "E3 ligase activity of RING finger proteins that interact with Hip-2, a
RT   human ubiquitin-conjugating enzyme.";
RL   FEBS Lett. 503:61-64(2001).
RN   [8]
RP   INTERACTION WITH TFCP2.
RX   PubMed=11865070; DOI=10.1128/mcb.22.6.1936-1946.2002;
RA   Tuckfield A., Clouston D.R., Wilanowski T.M., Zhao L.-L., Cunningham J.M.,
RA   Jane S.M.;
RT   "Binding of the RING polycomb proteins to specific target genes in complex
RT   with the grainyhead-like family of developmental transcription factors.";
RL   Mol. Cell. Biol. 22:1936-1946(2002).
RN   [9]
RP   IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX.
RX   PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA   Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA   Kingston R.E.;
RT   "The core of the polycomb repressive complex is compositionally and
RT   functionally conserved in flies and humans.";
RL   Mol. Cell. Biol. 22:6070-6078(2002).
RN   [10]
RP   IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; BAT8;
RP   CBX3; RNF1; MBLR; L3MBTL2 AND YAF2.
RX   PubMed=12004135; DOI=10.1126/science.1069861;
RA   Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT   "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT   genes in G0 cells.";
RL   Science 296:1132-1136(2002).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE COMPLEX
RP   WITH RING1; PHC2 AND BMI1, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   MUTAGENESIS OF HIS-69 AND ARG-70.
RX   PubMed=15386022; DOI=10.1038/nature02985;
RA   Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA   Zhang Y.;
RT   "Role of histone H2A ubiquitination in Polycomb silencing.";
RL   Nature 431:873-878(2004).
RN   [12]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA   Cao R., Tsukada Y., Zhang Y.;
RT   "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.";
RL   Mol. Cell 20:845-854(2005).
RN   [14]
RP   INTERACTION WITH RYBP; PCGF1; BCOR AND RING1.
RX   PubMed=16943429; DOI=10.1128/mcb.00630-06;
RA   Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
RT   "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex
RT   that is recruited to BCL6 targets.";
RL   Mol. Cell. Biol. 26:6880-6889(2006).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [16]
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH PCGF2.
RX   PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA   Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA   Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT   "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT   tumor suppressor locus.";
RL   PLoS ONE 4:E6380-E6380(2009).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6; CBX7
RP   AND CBX8, AND SUBCELLULAR LOCATION.
RX   PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA   Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT   "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT   Complexes in mammalian cells.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-168, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [20]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH PCGF5;
RP   AUTS2; CSNK2B AND RYBP, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF
RP   SER-41 AND SER-168, AND PHOSPHORYLATION AT SER-41 AND SER-168.
RX   PubMed=25519132; DOI=10.1038/nature13921;
RA   Gao Z., Lee P., Stafford J.M., von Schimmelmann M., Schaefer A.,
RA   Reinberg D.;
RT   "An AUTS2-polycomb complex activates gene expression in the CNS.";
RL   Nature 516:349-354(2014).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1.
RX   PubMed=26687479; DOI=10.1038/srep18388;
RA   Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V.,
RA   Bracken A.P., Cagney G.;
RT   "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a
RT   pluripotency sub-network that includes DPPA4, a regulator of
RT   embryogenesis.";
RL   Sci. Rep. 5:18388-18388(2015).
RN   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249 AND LYS-323, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [23]
RP   INTERACTION WITH NUPR1.
RX   PubMed=28720707; DOI=10.1073/pnas.1619932114;
RA   Santofimia-Castano P., Rizzuti B., Pey A.L., Soubeyran P., Vidal M.,
RA   Urrutia R., Iovanna J.L., Neira J.L.;
RT   "Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal
RT   region of Polycomb RING1B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 15-114 IN COMPLEX WITH BMI1 AND
RP   ZINC IONS, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=16714294; DOI=10.1074/jbc.m602461200;
RA   Li Z., Cao R., Wang M., Myers M.P., Zhang Y., Xu R.M.;
RT   "Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.";
RL   J. Biol. Chem. 281:20643-20649(2006).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 220-330, INTERACTION WITH CBX7,
RP   AND MUTAGENESIS OF TYR-262.
RX   PubMed=19791798; DOI=10.1021/bi901131u;
RA   Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S.,
RA   Arrowsmith C.H.;
RT   "Ring1B contains a ubiquitin-like docking module for interaction with Cbx
RT   proteins.";
RL   Biochemistry 48:10542-10548(2009).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 223-333 IN COMPLEXES WITH CBX7 AND
RP   RYBP, FUNCTION, AND MUTAGENESIS OF TYR-247; HIS-258 AND TYR-262.
RX   PubMed=20696397; DOI=10.1016/j.str.2010.04.013;
RA   Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U.,
RA   Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P.,
RA   McEwen D.G., Kim C.A.;
RT   "Polycomb group targeting through different binding partners of RING1B C-
RT   terminal domain.";
RL   Structure 18:966-975(2010).
RN   [27] {ECO:0000244|PDB:3RPG}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC IONS;
RP   BMI1 AND UB2D3, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF
RP   ASP-56 AND 97-LYS-ARG-98.
RX   PubMed=21772249; DOI=10.1038/emboj.2011.243;
RA   Bentley M.L., Corn J.E., Dong K.C., Phung Q., Cheung T.K., Cochran A.G.;
RT   "Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin
RT   ligase complex.";
RL   EMBO J. 30:3285-3297(2011).
RN   [28] {ECO:0000244|PDB:4R8P}
RP   X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 2-116 IN COMPLEX WITH ZINC IONS;
RP   THE NUCLEOSOME; BMI1 AND UB2D3, FUNCTION, AND MUTAGENESIS OF ARG-81;
RP   LYS-93; LYS-97 AND ARG-98.
RX   PubMed=25355358; DOI=10.1038/nature13890;
RA   McGinty R.K., Henrici R.C., Tan S.;
RT   "Crystal structure of the PRC1 ubiquitylation module bound to the
RT   nucleosome.";
RL   Nature 514:591-596(2014).
RN   [29] {ECO:0000244|PDB:4S3O}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-116 IN COMPLEX WITH ZINC IONS;
RP   UB2D3 AND PCGF5, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=26151332; DOI=10.1038/ncomms8621;
RA   Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT   "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL   Nat. Commun. 6:7621-7621(2015).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC       of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role
CC       in histone code and gene regulation (PubMed:15386022, PubMed:16359901,
CC       PubMed:25519132, PubMed:21772249, PubMed:25355358, PubMed:26151332).
CC       H2AK119Ub gives a specific tag for epigenetic transcriptional
CC       repression and participates in X chromosome inactivation of female
CC       mammals. May be involved in the initiation of both imprinted and random
CC       X inactivation (By similarity). Essential component of a Polycomb group
CC       (PcG) multiprotein PRC1-like complex, a complex class required to
CC       maintain the transcriptionally repressive state of many genes,
CC       including Hox genes, throughout development (PubMed:16359901,
CC       PubMed:26151332). PcG PRC1 complex acts via chromatin remodeling and
CC       modification of histones, rendering chromatin heritably changed in its
CC       expressibility (PubMed:26151332). E3 ubiquitin-protein ligase activity
CC       is enhanced by BMI1/PCGF4 (PubMed:21772249). Acts as the main E3
CC       ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may
CC       rather act as a modulator of RNF2/RING2 activity (Probable).
CC       Association with the chromosomal DNA is cell-cycle dependent. In
CC       resting B- and T-lymphocytes, interaction with AURKB leads to block its
CC       activity, thereby maintaining transcription in resting lymphocytes (By
CC       similarity). {ECO:0000250|UniProtKB:Q9CQJ4,
CC       ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:15386022,
CC       ECO:0000269|PubMed:16359901, ECO:0000269|PubMed:16714294,
CC       ECO:0000269|PubMed:20696397, ECO:0000269|PubMed:21772249,
CC       ECO:0000269|PubMed:25355358, ECO:0000269|PubMed:25519132,
CC       ECO:0000269|PubMed:26151332, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15386022,
CC         ECO:0000269|PubMed:21772249, ECO:0000269|PubMed:26151332};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:21772249,
CC       ECO:0000269|PubMed:26151332}.
CC   -!- SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes.
CC       Component of a number of PRC1-like complexes; these complexes contain
CC       either the polycomb group ring finger protein PCGF1, or PCGF2, or
CC       PCGF3, or PCGF4, or PCGF5, or PCGF6 (PubMed:12167701, PubMed:15386022,
CC       PubMed:19636380, PubMed:21282530, PubMed:26687479, PubMed:26151332).
CC       Part of a complex that contains RNF2, UB2D3 and BMI1; within that
CC       complex RNF2 and BMI1 form a tight heterodimer, where UB2D3 interacts
CC       only with RNF2 (PubMed:21772249, PubMed:25355358). The complex composed
CC       of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with
CC       nucleosomal histone H2A (PubMed:21772249). Part of a complex that
CC       contains PCGF5, RNF2 and UBE2D3 (PubMed:26151332). Part of a complex
CC       that contains AUTS2, PCGF5, RNF2, CSNK2B AND RYBP (PubMed:25519132).
CC       Interacts with RYBP, PCGF2, CBX4, CBX6, CBX7 and CBX8 (PubMed:19636380,
CC       PubMed:21282530, PubMed:19791798, PubMed:20696397). Interacts with
CC       RNF1/RING1, BMI1 and PHC2 (PubMed:15386022, PubMed:16714294).
CC       Interaction with RYBP and CBX7 is mutually exclusive; both compete for
CC       the same binding site on RNF2 (By similarity). Component of repressive
CC       BCOR complex containing a Polycomb group subcomplex at least composed
CC       of RYBP, PCGF1, BCOR and RING1 (PubMed:16943429). Interacts with CBX2
CC       and PHC1. Interacts with CHTOP. Interacts with AURKB (By similarity).
CC       Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX,
CC       TFDP1, CBX3, BAT8, EUHMTASE1, RNF1/RING1, RNF2/RING2, MBLR, L3MBTL2 and
CC       YAF2 (PubMed:12004135). Component of some MLL1/MLL complex, at least
CC       composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and
CC       RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70,
CC       INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
CC       RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
CC       and TEX10 (PubMed:15960975). Interacts with RYBP, HIP2 and TFCP2
CC       (PubMed:11513855, PubMed:11865070, PubMed:20696397). Interacts with
CC       NUPR1 (PubMed:28720707). {ECO:0000250|UniProtKB:Q9CQJ4,
CC       ECO:0000269|PubMed:11513855, ECO:0000269|PubMed:11865070,
CC       ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:12167701,
CC       ECO:0000269|PubMed:15386022, ECO:0000269|PubMed:15960975,
CC       ECO:0000269|PubMed:16714294, ECO:0000269|PubMed:16943429,
CC       ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:19791798,
CC       ECO:0000269|PubMed:21282530, ECO:0000269|PubMed:21772249,
CC       ECO:0000269|PubMed:25355358, ECO:0000269|PubMed:25519132,
CC       ECO:0000269|PubMed:26151332, ECO:0000269|PubMed:26687479,
CC       ECO:0000269|PubMed:28720707}.
CC   -!- INTERACTION:
CC       Q99496; P08183: ABCB1; NbExp=2; IntAct=EBI-722416, EBI-1057359;
CC       Q99496; P35226: BMI1; NbExp=18; IntAct=EBI-722416, EBI-2341576;
CC       Q99496; O00257: CBX4; NbExp=5; IntAct=EBI-722416, EBI-722425;
CC       Q99496; O00257-3: CBX4; NbExp=2; IntAct=EBI-722416, EBI-4392727;
CC       Q99496; O95503: CBX6; NbExp=6; IntAct=EBI-722416, EBI-3951758;
CC       Q99496; O95931: CBX7; NbExp=14; IntAct=EBI-722416, EBI-3923843;
CC       Q99496; Q9HC52: CBX8; NbExp=10; IntAct=EBI-722416, EBI-712912;
CC       Q99496; P68400: CSNK2A1; NbExp=3; IntAct=EBI-722416, EBI-347804;
CC       Q99496; P67870: CSNK2B; NbExp=2; IntAct=EBI-722416, EBI-348169;
CC       Q99496; P0C0S8: H2AC17; NbExp=5; IntAct=EBI-722416, EBI-1390628;
CC       Q99496; Q9H7Z6: KAT8; NbExp=2; IntAct=EBI-722416, EBI-896414;
CC       Q99496; Q9BSM1: PCGF1; NbExp=14; IntAct=EBI-722416, EBI-749901;
CC       Q99496; P35227: PCGF2; NbExp=15; IntAct=EBI-722416, EBI-2129767;
CC       Q99496; Q3KNV8: PCGF3; NbExp=4; IntAct=EBI-722416, EBI-2339807;
CC       Q99496; Q3KNV8-2: PCGF3; NbExp=3; IntAct=EBI-722416, EBI-12818023;
CC       Q99496; Q86SE9: PCGF5; NbExp=8; IntAct=EBI-722416, EBI-2827999;
CC       Q99496; Q9BYE7: PCGF6; NbExp=5; IntAct=EBI-722416, EBI-1048026;
CC       Q99496; Q06587: RING1; NbExp=5; IntAct=EBI-722416, EBI-752313;
CC       Q99496; Q8N488: RYBP; NbExp=17; IntAct=EBI-722416, EBI-752324;
CC       Q99496; P51668: UBE2D1; NbExp=4; IntAct=EBI-722416, EBI-743540;
CC       Q99496; P62837: UBE2D2; NbExp=4; IntAct=EBI-722416, EBI-347677;
CC       Q99496; P61077: UBE2D3; NbExp=6; IntAct=EBI-722416, EBI-348268;
CC       Q99496; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-722416, EBI-745527;
CC       Q99496; Q96LR5: UBE2E2; NbExp=6; IntAct=EBI-722416, EBI-2129763;
CC       Q99496; Q969T4: UBE2E3; NbExp=6; IntAct=EBI-722416, EBI-348496;
CC       Q99496; P51784: USP11; NbExp=4; IntAct=EBI-722416, EBI-306876;
CC       Q99496; Q93009: USP7; NbExp=5; IntAct=EBI-722416, EBI-302474;
CC       Q99496; Q8IY57-5: YAF2; NbExp=5; IntAct=EBI-722416, EBI-12111538;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. Chromosome
CC       {ECO:0000250|UniProtKB:Q9CQJ4}. Note=Enriched on inactive X chromosome
CC       (Xi) in female trophoblast stem (TS) cells as well as differentiating
CC       embryonic stem (ES) cells. The enrichment on Xi is transient during TS
CC       and ES cell differentiation. The association with Xi is mitotically
CC       stable in non-differentiated TS cells. {ECO:0000250|UniProtKB:Q9CQJ4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99496-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99496-2; Sequence=VSP_055439;
CC   -!- PTM: Polyubiquitinated in the presence of UBE2D3 (in vitro).
CC       {ECO:0000269|PubMed:26151332}.
CC   -!- PTM: Monoubiquitinated, by auto-ubiquitination. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The hPRC-H complex purification reported by
CC       PubMed:12167701 probably presents a mixture of different PRC1-like
CC       complexes.
DR   EMBL; Y10571; CAA71596.1; -; mRNA.
DR   EMBL; AF141327; AAD29717.1; -; mRNA.
DR   EMBL; AK091574; BAG52383.1; -; mRNA.
DR   EMBL; AK314793; BAG37324.1; -; mRNA.
DR   EMBL; AL109865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91187.1; -; Genomic_DNA.
DR   EMBL; CH471067; EAW91188.1; -; Genomic_DNA.
DR   EMBL; BC012583; AAH12583.1; -; mRNA.
DR   CCDS; CCDS1365.1; -. [Q99496-1]
DR   RefSeq; NP_009143.1; NM_007212.3. [Q99496-1]
DR   RefSeq; XP_011508153.1; XM_011509851.2. [Q99496-1]
DR   RefSeq; XP_011508154.1; XM_011509852.2. [Q99496-1]
DR   PDB; 2H0D; X-ray; 2.50 A; B=15-114.
DR   PDB; 3GS2; X-ray; 1.70 A; A/C=223-333.
DR   PDB; 3H8H; X-ray; 2.00 A; A=220-330.
DR   PDB; 3IXS; X-ray; 1.70 A; A/C/E/G/I/K=223-333.
DR   PDB; 3RPG; X-ray; 2.65 A; C=1-116.
DR   PDB; 4R8P; X-ray; 3.28 A; L/N=2-116.
DR   PDB; 4S3O; X-ray; 2.00 A; B/E=1-116.
DR   PDBsum; 2H0D; -.
DR   PDBsum; 3GS2; -.
DR   PDBsum; 3H8H; -.
DR   PDBsum; 3IXS; -.
DR   PDBsum; 3RPG; -.
DR   PDBsum; 4R8P; -.
DR   PDBsum; 4S3O; -.
DR   SMR; Q99496; -.
DR   BioGRID; 111972; 753.
DR   CORUM; Q99496; -.
DR   DIP; DIP-40034N; -.
DR   IntAct; Q99496; 105.
DR   MINT; Q99496; -.
DR   STRING; 9606.ENSP00000356480; -.
DR   iPTMnet; Q99496; -.
DR   PhosphoSitePlus; Q99496; -.
DR   BioMuta; RNF2; -.
DR   DMDM; 62901044; -.
DR   EPD; Q99496; -.
DR   jPOST; Q99496; -.
DR   MassIVE; Q99496; -.
DR   MaxQB; Q99496; -.
DR   PaxDb; Q99496; -.
DR   PeptideAtlas; Q99496; -.
DR   PRIDE; Q99496; -.
DR   ProteomicsDB; 3602; -.
DR   ProteomicsDB; 78297; -. [Q99496-1]
DR   Antibodypedia; 20609; 422 antibodies.
DR   DNASU; 6045; -.
DR   Ensembl; ENST00000367509; ENSP00000356479; ENSG00000121481. [Q99496-2]
DR   Ensembl; ENST00000367510; ENSP00000356480; ENSG00000121481. [Q99496-1]
DR   GeneID; 6045; -.
DR   KEGG; hsa:6045; -.
DR   UCSC; uc001grc.2; human. [Q99496-1]
DR   CTD; 6045; -.
DR   DisGeNET; 6045; -.
DR   EuPathDB; HostDB:ENSG00000121481.10; -.
DR   GeneCards; RNF2; -.
DR   HGNC; HGNC:10061; RNF2.
DR   HPA; ENSG00000121481; Low tissue specificity.
DR   MIM; 608985; gene.
DR   neXtProt; NX_Q99496; -.
DR   OpenTargets; ENSG00000121481; -.
DR   PharmGKB; PA34426; -.
DR   eggNOG; KOG0311; Eukaryota.
DR   GeneTree; ENSGT00940000154499; -.
DR   InParanoid; Q99496; -.
DR   KO; K10695; -.
DR   OMA; NCVRYIK; -.
DR   OrthoDB; 1319463at2759; -.
DR   PhylomeDB; Q99496; -.
DR   TreeFam; TF105501; -.
DR   PathwayCommons; Q99496; -.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR   Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR   SIGNOR; Q99496; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 6045; 6 hits in 874 CRISPR screens.
DR   ChiTaRS; RNF2; human.
DR   EvolutionaryTrace; Q99496; -.
DR   GeneWiki; RNF2; -.
DR   GenomeRNAi; 6045; -.
DR   Pharos; Q99496; Tbio.
DR   PRO; PR:Q99496; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q99496; protein.
DR   Bgee; ENSG00000121481; Expressed in cortical plate and 165 other tissues.
DR   ExpressionAtlas; Q99496; baseline and differential.
DR   Genevisible; Q99496; HS.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR   GO; GO:0001739; C:sex chromatin; IEA:Ensembl.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0071535; F:RING-like zinc finger domain binding; IPI:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR   GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR   GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR037937; RING2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076; PTHR46076; 1.
DR   PANTHER; PTHR46076:SF4; PTHR46076:SF4; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromosome;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330"
FT   CHAIN           2..336
FT                   /note="E3 ubiquitin-protein ligase RING2"
FT                   /id="PRO_0000056038"
FT   ZN_FING         51..91
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          2..179
FT                   /note="Interaction with HIP2"
FT                   /evidence="ECO:0000269|PubMed:11513855"
FT   REGION          93..98
FT                   /note="Interaction with nucleosomes via an acidic patch on
FT                   histone H2A and histone H2B"
FT                   /evidence="ECO:0000269|PubMed:25355358"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:19413330"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:25519132"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:25519132"
FT   CROSSLNK        112
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQJ4"
FT   CROSSLNK        249
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        323
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         84..155
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055439"
FT   MUTAGEN         41
FT                   /note="S->A,D: No effect on ubiquitin ligase activity on
FT                   histone H2A."
FT                   /evidence="ECO:0000269|PubMed:25519132"
FT   MUTAGEN         51
FT                   /note="C->W: Strong decrease in HIP2-binding; when
FT                   associated with S-54."
FT                   /evidence="ECO:0000269|PubMed:11513855"
FT   MUTAGEN         54
FT                   /note="C->S: Strong decrease in HIP2-binding; when
FT                   associated with W-51."
FT                   /evidence="ECO:0000269|PubMed:11513855"
FT   MUTAGEN         56
FT                   /note="D->K: Loss of ubiquitin ligase activity on histone
FT                   H2A."
FT                   /evidence="ECO:0000269|PubMed:21772249"
FT   MUTAGEN         69
FT                   /note="H->Y: Loss of HIP2-binding and loss of ubiquitin
FT                   ligase activity on histone H2A."
FT                   /evidence="ECO:0000269|PubMed:11513855,
FT                   ECO:0000269|PubMed:15386022"
FT   MUTAGEN         70
FT                   /note="R->C: Loss of ubiquitin ligase activity on histone
FT                   H2A."
FT                   /evidence="ECO:0000269|PubMed:15386022"
FT   MUTAGEN         81
FT                   /note="R->A: Decreases ubiquitin ligase activity on histone
FT                   H2A."
FT                   /evidence="ECO:0000269|PubMed:25355358"
FT   MUTAGEN         93
FT                   /note="K->A: Mildly decreases ubiquitin ligase activity on
FT                   histone H2A."
FT                   /evidence="ECO:0000269|PubMed:25355358"
FT   MUTAGEN         97..98
FT                   /note="KR->AA: Loss of ubiquitin ligase activity on histone
FT                   H2A."
FT                   /evidence="ECO:0000269|PubMed:21772249"
FT   MUTAGEN         97
FT                   /note="K->A: Strongly decreases ubiquitin ligase activity
FT                   on histone H2A."
FT                   /evidence="ECO:0000269|PubMed:25355358"
FT   MUTAGEN         98
FT                   /note="R->A: Nearly abolishes ubiquitin ligase activity on
FT                   histone H2A."
FT                   /evidence="ECO:0000269|PubMed:25355358"
FT   MUTAGEN         168
FT                   /note="S->E: Decreases ubiquitin ligase activity on histone
FT                   H2A."
FT                   /evidence="ECO:0000269|PubMed:25519132"
FT   MUTAGEN         247
FT                   /note="Y->A: Reduced interaction with CBX7."
FT                   /evidence="ECO:0000269|PubMed:20696397"
FT   MUTAGEN         258
FT                   /note="H->A: Reduced interaction with CBX7."
FT                   /evidence="ECO:0000269|PubMed:20696397"
FT   MUTAGEN         262
FT                   /note="Y->A: Reduced interaction with CBX7."
FT                   /evidence="ECO:0000269|PubMed:19791798,
FT                   ECO:0000269|PubMed:20696397"
FT   HELIX           13..16
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           21..24
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          37..39
FT                   /evidence="ECO:0000244|PDB:2H0D"
FT   HELIX           42..45
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           46..49
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            52..54
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          55..57
FT                   /evidence="ECO:0000244|PDB:4R8P"
FT   STRAND          59..64
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            65..67
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          70..72
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           73..80
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            88..90
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           97..99
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          100..102
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           104..113
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          225..232
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   TURN            234..236
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   STRAND          246..251
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   HELIX           256..277
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   HELIX           283..285
FT                   /evidence="ECO:0000244|PDB:3IXS"
FT   HELIX           288..290
FT                   /evidence="ECO:0000244|PDB:3IXS"
FT   STRAND          291..296
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   STRAND          302..304
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   HELIX           311..318
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   STRAND          321..323
FT                   /evidence="ECO:0000244|PDB:3GS2"
FT   STRAND          325..331
FT                   /evidence="ECO:0000244|PDB:3GS2"
SQ   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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