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E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) (Renal carcinoma antigen NY-REN-43)

 RNF12_HUMAN             Reviewed;         624 AA.
Q9NVW2; B2RBQ1; D3DTE0; Q96D38; Q9Y598;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 3.
18-JUL-2018, entry version 163.
RecName: Full=E3 ubiquitin-protein ligase RLIM;
EC=2.3.2.27;
AltName: Full=LIM domain-interacting RING finger protein;
AltName: Full=RING finger LIM domain-binding protein;
Short=R-LIM;
AltName: Full=RING finger protein 12;
AltName: Full=RING-type E3 ubiquitin transferase RLIM {ECO:0000305};
AltName: Full=Renal carcinoma antigen NY-REN-43;
Name=RLIM; Synonyms=RNF12;
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), AND IDENTIFICATION AS A RENAL
CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11013082; DOI=10.1006/geno.2000.6311;
Ostendorff H.P., Bossenz M., Mincheva A., Copeland N.G., Gilbert D.J.,
Jenkins N.A., Lichter P., Bach I.;
"Functional characterization of the gene encoding RLIM, the
corepressor of LIM homeodomain transcription factors.";
Genomics 69:120-130(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma, and Thymus;
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=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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).
[8]
INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND MISCELLANEOUS.
PubMed=19117995; DOI=10.1158/0008-5472.CAN-08-1630;
Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
Scheffner M., Pantel K., Gannon F., Bach I.;
"Regulation of estrogen-dependent transcription by the LIM cofactors
CLIM and RLIM in breast cancer.";
Cancer Res. 69:128-136(2009).
[9]
FUNCTION.
PubMed=19945382; DOI=10.1016/j.cell.2009.10.034;
Jonkers I., Barakat T.S., Achame E.M., Monkhorst K., Kenter A.,
Rentmeester E., Grosveld F., Grootegoed J.A., Gribnau J.;
"RNF12 is an X-encoded dose-dependent activator of X chromosome
inactivation.";
Cell 139:999-1011(2009).
[10]
FUNCTION, INTERACTION WITH TERF1, AND SUBCELLULAR LOCATION.
PubMed=19164295; DOI=10.1074/jbc.M806702200;
Her Y.R., Chung I.K.;
"Ubiquitin ligase RLIM modulates telomere length homeostasis through a
proteolysis of TRF1.";
J. Biol. Chem. 284:8557-8566(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-228; SER-230
AND SER-276, 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).
[13]
INVOLVEMENT IN MRX61, AND VARIANT MRX61 CYS-356.
PubMed=25735484; DOI=10.1038/ejhg.2015.30;
Toenne E., Holdhus R., Stansberg C., Stray-Pedersen A., Petersen K.,
Brunner H.G., Gilissen C., Hoischen A., Prescott T., Steen V.M.,
Fiskerstrand T.;
"Syndromic X-linked intellectual disability segregating with a
missense variant in RLIM.";
Eur. J. Hum. Genet. 23:1652-1656(2015).
[14]
VARIANT PRO-590.
PubMed=25787250; DOI=10.1073/pnas.1503696112;
Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D.,
Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T.,
Bjoerklund P., Lifton R.P.;
"Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
insulin-producing adenomas.";
Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
[15]
VARIANTS MRX61 CYS-387; ARG-587 AND CYS-599.
PubMed=25644381; DOI=10.1038/mp.2014.193;
Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T.,
Love M.I., Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M.,
Fischer U., Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N.,
Castelnau L., Rucci J., Montjean R., Dorseuil O., Billuart P.,
Stuhlmann T., Shaw M., Corbett M.A., Gardner A., Willis-Owen S.,
Tan C., Friend K.L., Belet S., van Roozendaal K.E.,
Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R., O'Keeffe S.,
Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
"X-exome sequencing of 405 unresolved families identifies seven novel
intellectual disability genes.";
Mol. Psychiatry 21:133-148(2016).
-!- FUNCTION: E3 ubiquitin-protein ligase. Acts as a negative
coregulator for LIM homeodomain transcription factors by mediating
the ubiquitination and subsequent degradation of LIM cofactors
LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone
deacetylase corepressor complex. Ubiquitination and degradation of
LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain
transcription factors to interact with other protein partners such
as RLIM. Plays a role in telomere length-mediated growth
suppression by mediating the ubiquitination and degradation of
TERF1. By targeting ZFP42 for degradation, acts as an activator of
random inactivation of X chromosome in the embryo, a stochastic
process in which one X chromosome is inactivated to minimize sex-
related dosage differences of X-encoded genes in somatic cells of
female placental mammals. {ECO:0000269|PubMed:19164295,
ECO:0000269|PubMed:19945382}.
-!- 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: Interacts with LIM/homeobox factors such as LHX3.
Interacts with LDB1, LDB2 and SIN3A (By similarity). Interacts
with LIMK1 (By similarity). Interacts (via N-terminus) with TERF1.
Interacts (via C-terminus) with ESR1. {ECO:0000250,
ECO:0000269|PubMed:19117995, ECO:0000269|PubMed:19164295}.
-!- INTERACTION:
O43679:LDB2; NbExp=2; IntAct=EBI-1996544, EBI-2865580;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19117995,
ECO:0000269|PubMed:19164295}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NVW2-1; Sequence=Displayed;
Name=2;
IsoId=Q9NVW2-2; Sequence=VSP_055428, VSP_055429;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in many tissues.
-!- DISEASE: Mental retardation, X-linked 61 (MRX61) [MIM:300978]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:25644381,
ECO:0000269|PubMed:25735484}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Acts as a positive coregulator of ESR1-mediated
transcription in breast cancer cells.
-!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD42875.1; Type=Frameshift; Positions=134, 142; Evidence={ECO:0000305};
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EMBL; AF155109; AAD42875.1; ALT_FRAME; mRNA.
EMBL; AJ271670; CAC14228.1; -; Genomic_DNA.
EMBL; AK001334; BAA91632.1; -; mRNA.
EMBL; AK314760; BAG37298.1; -; mRNA.
EMBL; AL513007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471104; EAW98639.1; -; Genomic_DNA.
EMBL; CH471104; EAW98640.1; -; Genomic_DNA.
EMBL; BC013357; AAH13357.1; -; mRNA.
CCDS; CCDS14427.1; -. [Q9NVW2-1]
RefSeq; NP_057204.2; NM_016120.3. [Q9NVW2-1]
RefSeq; NP_899196.1; NM_183353.2. [Q9NVW2-1]
UniGene; Hs.653288; -.
ProteinModelPortal; Q9NVW2; -.
SMR; Q9NVW2; -.
BioGrid; 119319; 37.
IntAct; Q9NVW2; 17.
MINT; Q9NVW2; -.
STRING; 9606.ENSP00000253571; -.
iPTMnet; Q9NVW2; -.
PhosphoSitePlus; Q9NVW2; -.
BioMuta; RLIM; -.
DMDM; 143811451; -.
EPD; Q9NVW2; -.
MaxQB; Q9NVW2; -.
PaxDb; Q9NVW2; -.
PeptideAtlas; Q9NVW2; -.
PRIDE; Q9NVW2; -.
ProteomicsDB; 82872; -.
DNASU; 51132; -.
Ensembl; ENST00000332687; ENSP00000328059; ENSG00000131263. [Q9NVW2-1]
Ensembl; ENST00000349225; ENSP00000253571; ENSG00000131263. [Q9NVW2-1]
GeneID; 51132; -.
KEGG; hsa:51132; -.
UCSC; uc004ebu.4; human. [Q9NVW2-1]
CTD; 51132; -.
DisGeNET; 51132; -.
EuPathDB; HostDB:ENSG00000131263.12; -.
GeneCards; RLIM; -.
HGNC; HGNC:13429; RLIM.
HPA; HPA018895; -.
MalaCards; RLIM; -.
MIM; 300379; gene.
MIM; 300978; phenotype.
neXtProt; NX_Q9NVW2; -.
OpenTargets; ENSG00000131263; -.
PharmGKB; PA164725373; -.
eggNOG; KOG0800; Eukaryota.
eggNOG; ENOG41121N2; LUCA.
GeneTree; ENSGT00730000110459; -.
HOGENOM; HOG000273881; -.
InParanoid; Q9NVW2; -.
KO; K16271; -.
OMA; MRNFGES; -.
OrthoDB; EOG091G0B6K; -.
PhylomeDB; Q9NVW2; -.
TreeFam; TF325756; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; RLIM; human.
GeneWiki; RNF12; -.
GenomeRNAi; 51132; -.
PRO; PR:Q9NVW2; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000131263; -.
CleanEx; HS_RNF12; -.
Genevisible; Q9NVW2; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003714; F:transcription corepressor activity; NAS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0060816; P:random inactivation of X chromosome; IDA:UniProtKB.
GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Mental retardation; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 624 E3 ubiquitin-protein ligase RLIM.
/FTId=PRO_0000056052.
ZN_FING 570 611 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MOTIF 621 624 PDZ-binding. {ECO:0000255}.
COMPBIAS 422 506 Ser-rich.
COMPBIAS 453 481 Poly-Ser.
COMPBIAS 500 506 Poly-Ser.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WTV7}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 3 MEN -> MLT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055428.
VAR_SEQ 4 144 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055429.
VARIANT 356 356 Y -> C (in MRX61; dbSNP:rs786205133).
{ECO:0000269|PubMed:25735484}.
/FTId=VAR_077826.
VARIANT 387 387 R -> C (in MRX61).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077827.
VARIANT 587 587 P -> R (in MRX61).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077828.
VARIANT 590 590 H -> P. {ECO:0000269|PubMed:25787250}.
/FTId=VAR_074175.
VARIANT 599 599 R -> C (in MRX61).
{ECO:0000269|PubMed:25644381}.
/FTId=VAR_077829.
CONFLICT 126 126 S -> C (in Ref. 2; CAC14228).
{ECO:0000305}.
CONFLICT 134 134 D -> N (in Ref. 2; CAC14228).
{ECO:0000305}.
CONFLICT 144 145 NR -> YS (in Ref. 2; CAC14228).
{ECO:0000305}.
CONFLICT 418 418 Y -> H (in Ref. 3; BAA91632).
{ECO:0000305}.
SEQUENCE 624 AA; 68549 MW; 4D583FA6872B51D3 CRC64;
MENSDSNDKG SGDQSAAQRR SQMDRLDREE AFYQFVNNLS EEDYRLMRDN NLLGTPGEST
EEELLRRLQQ IKEGPPPQNS DENRGGDSSD DVSNGDSIID WLNSVRQTGN TTRSGQRGNQ
SWRAVSRTNP NSGDFRFSLE INVNRNNGSQ NSENENEPSA RRSSGENVEN NSQRQVENPR
SESTSARPSR SERNSTEALT EVPPTRGQRR ARSRSPDHRR TRARAERSRS PLHPMSEIPR
RSHHSISSQT FEHPLVNETE GSSRTRHHVT LRQQISGPEL LSRGLFAASG TRNASQGAGS
SDTAASGEST GSGQRPPTIV LDLQVRRVRP GEYRQRDSIA SRTRSRSQTP NNTVTYESER
GGFRRTFSRS ERAGVRTYVS TIRIPIRRIL NTGLSETTSV AIQTMLRQIM TGFGELSYFM
YSDSDSEPTG SVSNRNMERA ESRSGRGGSG GGSSSGSSSS SSSSSSSSSS SSSSSSPSSS
SGGESSETSS DLFEGSNEGS SSSGSSGARR EGRHRAPVTF DESGSLPFLS LAQFFLLNED
DDDQPRGLTK EQIDNLAMRS FGENDALKTC SVCITEYTEG NKLRKLPCSH EYHVHCIDRW
LSENSTCPIC RRAVLASGNR ESVV


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