RNF12_HUMAN
ID RNF12_HUMAN Reviewed; 624 AA.
AC Q9NVW2; B2RBQ1; D3DTE0; Q96D38; Q9Y598;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=E3 ubiquitin-protein ligase RLIM;
DE EC=2.3.2.27;
DE AltName: Full=LIM domain-interacting RING finger protein;
DE AltName: Full=RING finger LIM domain-binding protein;
DE Short=R-LIM;
DE AltName: Full=RING finger protein 12;
DE AltName: Full=RING-type E3 ubiquitin transferase RLIM {ECO:0000305};
DE AltName: Full=Renal carcinoma antigen NY-REN-43;
GN Name=RLIM; Synonyms=RNF12;
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), AND IDENTIFICATION AS A RENAL
RP CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11013082; DOI=10.1006/geno.2000.6311;
RA Ostendorff H.P., Bossenz M., Mincheva A., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Lichter P., Bach I.;
RT "Functional characterization of the gene encoding RLIM, the corepressor of
RT LIM homeodomain transcription factors.";
RL Genomics 69:120-130(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, and Thymus;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX PubMed=19117995; DOI=10.1158/0008-5472.can-08-1630;
RA Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
RA Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
RA Scheffner M., Pantel K., Gannon F., Bach I.;
RT "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM
RT and RLIM in breast cancer.";
RL Cancer Res. 69:128-136(2009).
RN [9]
RP FUNCTION.
RX PubMed=19945382; DOI=10.1016/j.cell.2009.10.034;
RA Jonkers I., Barakat T.S., Achame E.M., Monkhorst K., Kenter A.,
RA Rentmeester E., Grosveld F., Grootegoed J.A., Gribnau J.;
RT "RNF12 is an X-encoded dose-dependent activator of X chromosome
RT inactivation.";
RL Cell 139:999-1011(2009).
RN [10]
RP FUNCTION, INTERACTION WITH TERF1, AND SUBCELLULAR LOCATION.
RX PubMed=19164295; DOI=10.1074/jbc.m806702200;
RA Her Y.R., Chung I.K.;
RT "Ubiquitin ligase RLIM modulates telomere length homeostasis through a
RT proteolysis of TRF1.";
RL J. Biol. Chem. 284:8557-8566(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195; SER-228; SER-230 AND
RP SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [13]
RP INVOLVEMENT IN TOKAS, AND VARIANT TOKAS CYS-356.
RX PubMed=25735484; DOI=10.1038/ejhg.2015.30;
RA Toenne E., Holdhus R., Stansberg C., Stray-Pedersen A., Petersen K.,
RA Brunner H.G., Gilissen C., Hoischen A., Prescott T., Steen V.M.,
RA Fiskerstrand T.;
RT "Syndromic X-linked intellectual disability segregating with a missense
RT variant in RLIM.";
RL Eur. J. Hum. Genet. 23:1652-1656(2015).
RN [14]
RP VARIANT PRO-590.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
RN [15]
RP VARIANTS TOKAS CYS-387; ARG-587 AND CYS-599.
RX PubMed=25644381; DOI=10.1038/mp.2014.193;
RA Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
RA Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T., Love M.I.,
RA Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M., Fischer U.,
RA Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N., Castelnau L.,
RA Rucci J., Montjean R., Dorseuil O., Billuart P., Stuhlmann T., Shaw M.,
RA Corbett M.A., Gardner A., Willis-Owen S., Tan C., Friend K.L., Belet S.,
RA van Roozendaal K.E., Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R.,
RA O'Keeffe S., Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
RA Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
RA Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
RA Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
RA Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
RA Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
RA Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
RA Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
RA Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
RT "X-exome sequencing of 405 unresolved families identifies seven novel
RT intellectual disability genes.";
RL Mol. Psychiatry 21:133-148(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Acts as a negative coregulator
CC for LIM homeodomain transcription factors by mediating the
CC ubiquitination and subsequent degradation of LIM cofactors LDB1 and
CC LDB2 and by mediating the recruitment the SIN3a/histone deacetylase
CC corepressor complex. Ubiquitination and degradation of LIM cofactors
CC LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to
CC interact with other protein partners such as RLIM. Plays a role in
CC telomere length-mediated growth suppression by mediating the
CC ubiquitination and degradation of TERF1. By targeting ZFP42 for
CC degradation, acts as an activator of random inactivation of X
CC chromosome in the embryo, a stochastic process in which one X
CC chromosome is inactivated to minimize sex-related dosage differences of
CC X-encoded genes in somatic cells of female placental mammals.
CC {ECO:0000269|PubMed:19164295, ECO:0000269|PubMed:19945382}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with LIM/homeobox factors such as LHX3. Interacts
CC with LDB1, LDB2 and SIN3A (By similarity). Interacts with LIMK1 (By
CC similarity). Interacts (via N-terminus) with TERF1. Interacts (via C-
CC terminus) with ESR1. {ECO:0000250, ECO:0000269|PubMed:19117995,
CC ECO:0000269|PubMed:19164295}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19117995,
CC ECO:0000269|PubMed:19164295}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVW2-2; Sequence=VSP_055428, VSP_055429;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC -!- DISEASE: Tonne-Kalscheuer syndrome (TOKAS) [MIM:300978]: An X-linked
CC recessive disorder characterized by global developmental delay apparent
CC from early infancy, impaired intellectual development, speech delay,
CC behavioral abnormalities, abnormal gait, dysmorphic facial features,
CC limb anomalies, and urogenital abnormalities with hypogenitalism. A
CC subset of more severely affected males develop congenital diaphragmatic
CC hernia in utero, which may result in perinatal or premature death.
CC Carrier females may have very mild skeletal or hormonal abnormalities.
CC {ECO:0000269|PubMed:25644381, ECO:0000269|PubMed:25735484}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Acts as a positive coregulator of ESR1-mediated
CC transcription in breast cancer cells.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42875.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF155109; AAD42875.1; ALT_FRAME; mRNA.
DR EMBL; AJ271670; CAC14228.1; -; Genomic_DNA.
DR EMBL; AK001334; BAA91632.1; -; mRNA.
DR EMBL; AK314760; BAG37298.1; -; mRNA.
DR EMBL; AL513007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98639.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98640.1; -; Genomic_DNA.
DR EMBL; BC013357; AAH13357.1; -; mRNA.
DR CCDS; CCDS14427.1; -. [Q9NVW2-1]
DR RefSeq; NP_057204.2; NM_016120.3. [Q9NVW2-1]
DR RefSeq; NP_899196.1; NM_183353.2. [Q9NVW2-1]
DR PDB; 6W7Z; X-ray; 1.80 A; B=530-624.
DR PDB; 6W9A; X-ray; 2.30 A; B/D=530-623.
DR PDB; 6W9D; X-ray; 3.19 A; B/E/H=530-623.
DR PDBsum; 6W7Z; -.
DR PDBsum; 6W9A; -.
DR PDBsum; 6W9D; -.
DR AlphaFoldDB; Q9NVW2; -.
DR SMR; Q9NVW2; -.
DR BioGRID; 119319; 124.
DR IntAct; Q9NVW2; 23.
DR MINT; Q9NVW2; -.
DR STRING; 9606.ENSP00000328059; -.
DR iPTMnet; Q9NVW2; -.
DR MetOSite; Q9NVW2; -.
DR PhosphoSitePlus; Q9NVW2; -.
DR BioMuta; RLIM; -.
DR DMDM; 143811451; -.
DR EPD; Q9NVW2; -.
DR jPOST; Q9NVW2; -.
DR MassIVE; Q9NVW2; -.
DR MaxQB; Q9NVW2; -.
DR PaxDb; Q9NVW2; -.
DR PeptideAtlas; Q9NVW2; -.
DR PRIDE; Q9NVW2; -.
DR ProteomicsDB; 82872; -. [Q9NVW2-1]
DR Antibodypedia; 13786; 194 antibodies from 24 providers.
DR DNASU; 51132; -.
DR Ensembl; ENST00000332687.11; ENSP00000328059.6; ENSG00000131263.13. [Q9NVW2-1]
DR Ensembl; ENST00000349225.2; ENSP00000253571.3; ENSG00000131263.13. [Q9NVW2-1]
DR GeneID; 51132; -.
DR KEGG; hsa:51132; -.
DR MANE-Select; ENST00000332687.11; ENSP00000328059.6; NM_016120.4; NP_057204.2.
DR UCSC; uc004ebu.4; human. [Q9NVW2-1]
DR CTD; 51132; -.
DR DisGeNET; 51132; -.
DR GeneCards; RLIM; -.
DR HGNC; HGNC:13429; RLIM.
DR HPA; ENSG00000131263; Tissue enhanced (bone).
DR MalaCards; RLIM; -.
DR MIM; 300379; gene.
DR MIM; 300978; phenotype.
DR neXtProt; NX_Q9NVW2; -.
DR OpenTargets; ENSG00000131263; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA164725373; -.
DR VEuPathDB; HostDB:ENSG00000131263; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000155753; -.
DR HOGENOM; CLU_025933_1_0_1; -.
DR InParanoid; Q9NVW2; -.
DR OMA; HHNISSQ; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9NVW2; -.
DR TreeFam; TF325756; -.
DR PathwayCommons; Q9NVW2; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NVW2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51132; 59 hits in 745 CRISPR screens.
DR ChiTaRS; RLIM; human.
DR GeneWiki; RNF12; -.
DR GenomeRNAi; 51132; -.
DR Pharos; Q9NVW2; Tbio.
DR PRO; PR:Q9NVW2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NVW2; protein.
DR Bgee; ENSG00000131263; Expressed in middle temporal gyrus and 191 other tissues.
DR Genevisible; Q9NVW2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; NAS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0060816; P:random inactivation of X chromosome; IDA:UniProtKB.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Intellectual disability; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..624
FT /note="E3 ubiquitin-protein ligase RLIM"
FT /id="PRO_0000056052"
FT ZN_FING 570..611
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 621..624
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 90..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTV7"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..3
FT /note="MEN -> MLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055428"
FT VAR_SEQ 4..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055429"
FT VARIANT 356
FT /note="Y -> C (in TOKAS; dbSNP:rs786205133)"
FT /evidence="ECO:0000269|PubMed:25735484"
FT /id="VAR_077826"
FT VARIANT 387
FT /note="R -> C (in TOKAS)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077827"
FT VARIANT 587
FT /note="P -> R (in TOKAS)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077828"
FT VARIANT 590
FT /note="H -> P"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074175"
FT VARIANT 599
FT /note="R -> C (in TOKAS)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077829"
FT CONFLICT 126
FT /note="S -> C (in Ref. 2; CAC14228)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="D -> N (in Ref. 2; CAC14228)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="NR -> YS (in Ref. 2; CAC14228)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="Y -> H (in Ref. 3; BAA91632)"
FT /evidence="ECO:0000305"
FT HELIX 550..554
FT /evidence="ECO:0007829|PDB:6W7Z"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6W7Z"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:6W9A"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:6W7Z"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:6W7Z"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:6W7Z"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:6W7Z"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:6W7Z"
SQ 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
