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E3 ubiquitin-protein ligase RING1 (EC 2.3.2.27) (Polycomb complex protein RING1) (RING finger protein 1) (RING-type E3 ubiquitin transferase RING1) (Really interesting new gene 1 protein)

 RING1_HUMAN             Reviewed;         406 AA.
Q06587; A8JZZ0; Q5JP96; Q5SQW2; Q86V19;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 2.
28-MAR-2018, entry version 182.
RecName: Full=E3 ubiquitin-protein ligase RING1;
EC=2.3.2.27;
AltName: Full=Polycomb complex protein RING1;
AltName: Full=RING finger protein 1;
AltName: Full=RING-type E3 ubiquitin transferase RING1 {ECO:0000305};
AltName: Full=Really interesting new gene 1 protein;
Name=RING1; Synonyms=RNF1;
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 2).
PubMed=7681583; DOI=10.1073/pnas.90.6.2112;
Lovering R., Hanson I.M., Borden K.L.B., Martin S., O'Reilly N.J.,
Evan G.I., Rahman D., Pappin D.J.C., Trowsdale J., Freemont P.S.;
"Identification and preliminary characterization of a protein motif
related to the zinc finger.";
Proc. Natl. Acad. Sci. U.S.A. 90:2112-2116(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Skin;
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).
[6]
CHARACTERIZATION, AND INTERACTION WITH PHC2.
PubMed=9199346; DOI=10.1128/MCB.17.7.4105;
Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
"RING1 is associated with the polycomb group protein complex and acts
as a transcriptional repressor.";
Mol. Cell. Biol. 17:4105-4113(1997).
[7]
CHARACTERIZATION.
PubMed=9858531; DOI=10.1128/MCB.19.1.57;
Satijn D.P.E., Otte A.P.;
"RING1 interacts with multiple Polycomb-group proteins and displays
tumorigenic activity.";
Mol. Cell. Biol. 19:57-68(1999).
[8]
INTERACTION WITH PCGF6.
PubMed=12167161; DOI=10.1046/j.1365-2443.2002.00565.x;
Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
"MBLR, a new RING finger protein resembling mammalian Polycomb gene
products, is regulated by cell cycle-dependent phosphorylation.";
Genes Cells 7:835-850(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; RNF2; 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 IN A PRC1-LIKE COMPLEX WITH RNF2; BMI1 AND PHC2.
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]
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).
[13]
INTERACTION WITH RYBP; PCGF1; BCOR AND RNF2.
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-187 AND SER-190,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-248 AND
SER-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
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).
[20]
IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-140 AND SER-229,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-38; SER-187;
THR-215; THR-220; SER-229 AND SER-232, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
VARIANT GLN-95.
PubMed=25725044; DOI=10.1136/jmedgenet-2014-102813;
Blanchard M.G., Willemsen M.H., Walker J.B., Dib-Hajj S.D.,
Waxman S.G., Jongmans M.C., Kleefstra T., van de Warrenburg B.P.,
Praamstra P., Nicolai J., Yntema H.G., Bindels R.J., Meisler M.H.,
Kamsteeg E.J.;
"De novo gain-of-function and loss-of-function mutations of SCN8A in
patients with intellectual disabilities and epilepsy.";
J. Med. Genet. 52:330-337(2015).
-!- FUNCTION: Constitutes one of the E3 ubiquitin-protein ligases that
mediate monoubiquitination of 'Lys-119' of histone H2A, thereby
playing a central role in histone code and gene regulation. H2A
'Lys-119' ubiquitination gives a specific tag for epigenetic
transcriptional repression and participates in X chromosome
inactivation of female mammals. Essential component of a Polycomb
group (PcG) multiprotein PRC1-like complex, a complex class
required to maintain the transcriptionally repressive state of
many genes, including Hox genes, throughout development. PcG PRC1
complex acts via chromatin remodeling and modification of
histones, rendering chromatin heritably changed in its
expressibility. Compared to RNF2/RING2, it does not have the main
E3 ubiquitin ligase activity on histone H2A, and it may rather act
as a modulator of RNF2/RING2 activity.
{ECO:0000269|PubMed:16359901}.
-!- 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.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of chromatin-associated Polycomb (PcG)
complexes. Interacts with BMI1 (By similarity). Part of the
E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1,
CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2.
Interacts with CBX2 and PCGF6. Component of a PRC1-like complex.
Component of repressive BCOR complex containing Polycomb group
subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2.
Interacts with PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with
PHC2 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P35226:BMI1; NbExp=16; IntAct=EBI-752313, EBI-2341576;
O95503:CBX6; NbExp=5; IntAct=EBI-752313, EBI-3951758;
O95931:CBX7; NbExp=5; IntAct=EBI-752313, EBI-3923843;
Q9HC52:CBX8; NbExp=13; IntAct=EBI-752313, EBI-712912;
P97447:Fhl1 (xeno); NbExp=2; IntAct=EBI-752313, EBI-643780;
Q9BSM1:PCGF1; NbExp=8; IntAct=EBI-752313, EBI-749901;
P35227:PCGF2; NbExp=11; IntAct=EBI-752313, EBI-2129767;
Q3KNV8:PCGF3; NbExp=4; IntAct=EBI-752313, EBI-2339807;
Q86SE9:PCGF5; NbExp=6; IntAct=EBI-752313, EBI-2827999;
Q9BYE7:PCGF6; NbExp=3; IntAct=EBI-752313, EBI-1048026;
Q99496:RNF2; NbExp=5; IntAct=EBI-752313, EBI-722416;
Q8N488:RYBP; NbExp=16; IntAct=EBI-752313, EBI-752324;
P51668:UBE2D1; NbExp=3; IntAct=EBI-752313, EBI-743540;
Q9Y2X8:UBE2D4; NbExp=3; IntAct=EBI-752313, EBI-745527;
P51784:USP11; NbExp=4; IntAct=EBI-752313, EBI-306876;
Q93009:USP7; NbExp=5; IntAct=EBI-752313, EBI-302474;
Q8IY57:YAF2; NbExp=6; IntAct=EBI-752313, EBI-2842031;
Q8IY57-5:YAF2; NbExp=4; IntAct=EBI-752313, EBI-12111538;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}.
Nucleus speckle {ECO:0000269|PubMed:21282530}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q06587-1; Sequence=Displayed;
Name=2;
IsoId=Q06587-2; Sequence=VSP_017694;
-!- MISCELLANEOUS: The hPRC-H complex purification reported by
PubMed:12167701 probably presents a mixture of different PRC1-like
complexes.
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EMBL; Z14000; CAA78389.1; -; mRNA.
EMBL; BT007352; AAP36016.1; -; mRNA.
EMBL; AK289355; BAF82044.1; -; mRNA.
EMBL; AL031228; CAA20235.1; -; Genomic_DNA.
EMBL; AL031228; CAI95620.1; -; Genomic_DNA.
EMBL; AL713971; CAI17650.1; -; Genomic_DNA.
EMBL; AL645940; CAI18069.1; -; Genomic_DNA.
EMBL; AL844527; CAI41841.1; -; Genomic_DNA.
EMBL; CR759786; CAQ08246.1; -; Genomic_DNA.
EMBL; CR759733; CAQ10303.1; -; Genomic_DNA.
EMBL; CR847841; CAQ10314.1; -; Genomic_DNA.
EMBL; CR547129; CAQ10314.1; JOINED; Genomic_DNA.
EMBL; CR547129; CAQ10355.1; -; Genomic_DNA.
EMBL; CR847841; CAQ10355.1; JOINED; Genomic_DNA.
EMBL; BC002922; AAH02922.2; -; mRNA.
EMBL; BC051866; AAH51866.1; -; mRNA.
CCDS; CCDS34424.1; -. [Q06587-1]
PIR; A47380; A47380.
RefSeq; NP_002922.2; NM_002931.3. [Q06587-1]
UniGene; Hs.631989; -.
ProteinModelPortal; Q06587; -.
SMR; Q06587; -.
BioGrid; 111947; 77.
CORUM; Q06587; -.
DIP; DIP-42043N; -.
IntAct; Q06587; 72.
MINT; Q06587; -.
STRING; 9606.ENSP00000363787; -.
iPTMnet; Q06587; -.
PhosphoSitePlus; Q06587; -.
BioMuta; RING1; -.
DMDM; 90110053; -.
EPD; Q06587; -.
MaxQB; Q06587; -.
PaxDb; Q06587; -.
PeptideAtlas; Q06587; -.
PRIDE; Q06587; -.
TopDownProteomics; Q06587-1; -. [Q06587-1]
TopDownProteomics; Q06587-2; -. [Q06587-2]
DNASU; 6015; -.
Ensembl; ENST00000374656; ENSP00000363787; ENSG00000204227. [Q06587-1]
Ensembl; ENST00000383212; ENSP00000372699; ENSG00000206287. [Q06587-1]
Ensembl; ENST00000415941; ENSP00000412190; ENSG00000226788. [Q06587-1]
Ensembl; ENST00000427374; ENSP00000400572; ENSG00000231115. [Q06587-1]
Ensembl; ENST00000430233; ENSP00000396271; ENSG00000228520. [Q06587-1]
Ensembl; ENST00000436128; ENSP00000396439; ENSG00000235107. [Q06587-1]
GeneID; 6015; -.
KEGG; hsa:6015; -.
UCSC; uc003odk.4; human. [Q06587-1]
CTD; 6015; -.
DisGeNET; 6015; -.
EuPathDB; HostDB:ENSG00000204227.4; -.
GeneCards; RING1; -.
HGNC; HGNC:10018; RING1.
HPA; HPA008701; -.
MIM; 602045; gene.
neXtProt; NX_Q06587; -.
OpenTargets; ENSG00000204227; -.
PharmGKB; PA34393; -.
eggNOG; KOG0311; Eukaryota.
eggNOG; ENOG410XQ5G; LUCA.
GeneTree; ENSGT00390000016977; -.
HOGENOM; HOG000273917; -.
HOVERGEN; HBG079942; -.
InParanoid; Q06587; -.
KO; K10695; -.
OMA; QSASKTW; -.
OrthoDB; EOG091G06VO; -.
PhylomeDB; Q06587; -.
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; Q06587; -.
UniPathway; UPA00143; -.
ChiTaRS; RING1; human.
GeneWiki; RING1; -.
GenomeRNAi; 6015; -.
PRO; PR:Q06587; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204227; -.
CleanEx; HS_RING1; -.
ExpressionAtlas; Q06587; baseline and differential.
Genevisible; Q06587; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:Ensembl.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR032443; RAWUL.
InterPro; IPR038036; RING1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR10825:SF6; PTHR10825:SF6; 1.
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;
Alternative splicing; Chromatin regulator; Complete proteome;
Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 406 E3 ubiquitin-protein ligase RING1.
/FTId=PRO_0000056384.
ZN_FING 48 88 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 30 234 Necessary for transcriptional repression.
{ECO:0000250}.
REGION 230 406 Necessary for interaction with CBX2.
{ECO:0000250}.
MOTIF 201 204 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 205 260 Gly-rich.
COMPBIAS 314 377 Gly-rich.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 215 215 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 29 Missing (in isoform 2).
{ECO:0000303|PubMed:7681583,
ECO:0000303|Ref.2}.
/FTId=VSP_017694.
VARIANT 95 95 R -> Q. {ECO:0000269|PubMed:25725044}.
/FTId=VAR_076618.
SEQUENCE 406 AA; 42429 MW; 6959787479DE9DAB CRC64;
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD PNFDALISKI YPSREEYEAH
QDRVLIRLSR LHNQQALSSS IEEGLRMQAM HRAQRVRRPI PGSDQTTTMS GGEGEPGEGE
GDGEDVSSDS APDSAPGPAP KRPRGGGAGG SSVGTGGGGT GGVGGGAGSE DSGDRGGTLG
GGTLGPPSPP GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
LRIALERRQQ QEAGEPGGPG GGASDTGGPD GCGGEGGGAG GGDGPEEPAL PSLEGVSEKQ
YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA PTKDPK


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