ID R113A_HUMAN Reviewed; 343 AA.
AC O15541; B2RBR7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=E3 ubiquitin-protein ligase RNF113A;
DE EC=2.3.2.27 {ECO:0000269|PubMed:28978524, ECO:0000269|PubMed:29144457};
DE AltName: Full=Cwc24 homolog {ECO:0000305};
DE AltName: Full=RING finger protein 113A;
DE AltName: Full=Zinc finger protein 183 {ECO:0000303|PubMed:9224902};
GN Name=RNF113A; Synonyms=RNF113, ZNF183 {ECO:0000303|PubMed:9224902};
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], AND TISSUE SPECIFICITY.
RX PubMed=9224902; DOI=10.1016/s0378-1119(97)00108-x;
RA Frattini A., Faranda S., Bagnasco L., Patrosso C., Nulli P., Zucchi I.,
RA Vezzoni P.;
RT "Identification of a new member (ZNF183) of the Ring finger gene family in
RT Xq24-25.";
RL Gene 192:291-298(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 MRNA].
RC TISSUE=Cervix, and Placenta;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85 AND SER-253, AND
RP IDENTIFICATION BY 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-85 AND SER-253, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION IN THE SPLICEOSOME, AND SUBUNIT.
RX PubMed=22365833; DOI=10.1016/j.molcel.2011.12.034;
RA Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S., Weimann M.,
RA Will C.L., Pena V., Luehrmann R., Stelzl U.;
RT "Dynamic protein-protein interaction wiring of the human spliceosome.";
RL Mol. Cell 45:567-580(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-253, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INVOLVEMENT IN TTD5.
RX PubMed=25612912; DOI=10.1136/jmedgenet-2014-102418;
RA Corbett M.A., Dudding-Byth T., Crock P.A., Botta E., Christie L.M.,
RA Nardo T., Caligiuri G., Hobson L., Boyle J., Mansour A., Friend K.L.,
RA Crawford J., Jackson G., Vandeleur L., Hackett A., Tarpey P.,
RA Stratton M.R., Turner G., Gecz J., Field M.;
RT "A novel X-linked trichothiodystrophy associated with a nonsense mutation
RT in RNF113A.";
RL J. Med. Genet. 52:269-274(2015).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CXCR4, AND
RP MUTAGENESIS OF 50-GLY--VAL-61; CYS-262 AND CYS-277.
RX PubMed=28978524; DOI=10.1152/ajpcell.00193.2017;
RA Lear T., Dunn S.R., McKelvey A.C., Mir A., Evankovich J., Chen B.B.,
RA Liu Y.;
RT "RING finger protein 113A regulates C-X-C chemokine receptor type 4
RT stability and signaling.";
RL Am. J. Physiol. 313:C584-C592(2017).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH SNRNP200,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2-ALA--ARG-60; ILE-264 AND
RP 301-GLN--THR-343.
RX PubMed=29144457; DOI=10.1038/nature24484;
RA Brickner J.R., Soll J.M., Lombardi P.M., Vaagboe C.B., Mudge M.C.,
RA Oyeniran C., Rabe R., Jackson J., Sullender M.E., Blazosky E., Byrum A.K.,
RA Zhao Y., Corbett M.A., Gecz J., Field M., Vindigni A., Slupphaug G.,
RA Wolberger C., Mosammaparast N.;
RT "A ubiquitin-dependent signalling axis specific for ALKBH-mediated DNA
RT dealkylation repair.";
RL Nature 551:389-393(2017).
RN [20] {ECO:0007744|PDB:6FF4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010;
RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O.,
RA Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact
RT Complex.";
RL Cell 172:454-464(2018).
RN [21] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z58}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
RN [22] {ECO:0007744|PDB:7DVQ}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=33509932; DOI=10.1126/science.abg0879;
RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.;
RT "Structure of the activated human minor spliceosome.";
RL Science 371:0-0(2021).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:29361316, PubMed:29360106). As a component of the
CC minor spliceosome, involved in the splicing of U12-type introns in pre-
CC mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the
CC transfer of ubiquitin onto target proteins (PubMed:28978524,
CC PubMed:29144457). Catalyzes polyubiquitination of SNRNP200/BRR2 with
CC non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:29144457).
CC Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-
CC linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to
CC sites of DNA damage by alkylating agents (PubMed:29144457).
CC Ubiquitinates CXCR4, leading to its degradation, and thereby
CC contributes to the termination of CXCR4 signaling (PubMed:28978524).
CC {ECO:0000269|PubMed:28978524, ECO:0000269|PubMed:29144457,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000305|PubMed:33509932}.
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:28978524,
CC ECO:0000269|PubMed:29144457};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:28978524, ECO:0000269|PubMed:29144457}.
CC -!- SUBUNIT: Component of pre-catalytic and catalytic spliceosome complexes
CC (PubMed:22365833, PubMed:29361316, PubMed:29360106). Interacts (via N-
CC terminus) with the spliceosome subunit SNRNP200/BRR2 (PubMed:29144457).
CC Component of the minor spliceosome, which splices U12-type introns.
CC Within this complex, interacts with SCNM1 and CRIPT (PubMed:33509932).
CC {ECO:0000269|PubMed:22365833, ECO:0000269|PubMed:29144457,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000269|PubMed:33509932}.
CC -!- INTERACTION:
CC O15541; Q13123: IK; NbExp=2; IntAct=EBI-2130294, EBI-713456;
CC O15541; Q13435: SF3B2; NbExp=2; IntAct=EBI-2130294, EBI-749111;
CC O15541; O75643: SNRNP200; NbExp=2; IntAct=EBI-2130294, EBI-1045395;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29360106,
CC ECO:0000269|PubMed:29361316}. Nucleus speckle
CC {ECO:0000269|PubMed:29144457}. Note=Colocalizes with ASCC2 in nuclear
CC foci after DNA damage by alkylating agents. In the absence of DNA
CC damage, colocalizes with the spliceosome components SNRNP200/BRR2 and
CC PRPF8 in nuclear speckles. {ECO:0000269|PubMed:29144457}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9224902}.
CC -!- DISEASE: Trichothiodystrophy 5, non-photosensitive (TTD5) [MIM:300953]:
CC An X-linked form of trichothiodystrophy, a disease characterized by
CC sulfur-deficient brittle hair and multisystem variable abnormalities.
CC The spectrum of clinical features varies from mild disease with only
CC hair involvement to severe disease with cutaneous, neurologic and
CC profound developmental defects. Ichthyosis, intellectual and
CC developmental disabilities, decreased fertility, abnormal
CC characteristics at birth, ocular abnormalities, short stature, and
CC infections are common manifestations. There are both photosensitive and
CC non-photosensitive forms of the disorder. TTD5 features include
CC microcephaly, profound intellectual disability, sparse brittle hair,
CC aged appearance, short stature, facial dysmorphism, seizures, an
CC immunoglobulin deficiency, multiple endocrine abnormalities, cerebellar
CC hypoplasia and partial absence of the corpus callosum, in the absence
CC of cellular photosensitivity and ichthyosis.
CC {ECO:0000269|PubMed:25612912}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; X98253; CAA66907.1; -; mRNA.
DR EMBL; AK314778; BAG37314.1; -; mRNA.
DR EMBL; BT007175; AAP35839.1; -; mRNA.
DR EMBL; AC002477; AAB67605.1; -; Genomic_DNA.
DR EMBL; BC000832; AAH00832.1; -; mRNA.
DR EMBL; BC020556; AAH20556.1; -; mRNA.
DR CCDS; CCDS14589.1; -.
DR RefSeq; NP_008909.1; NM_006978.2.
DR PDB; 5Z56; EM; 5.10 A; M=1-343.
DR PDB; 5Z58; EM; 4.90 A; M=1-343.
DR PDB; 6FF4; EM; 16.00 A; t=1-343.
DR PDB; 6FF7; EM; 4.50 A; t=1-343.
DR PDB; 7DVQ; EM; 2.89 A; M=1-343.
DR PDB; 7QTT; EM; 3.10 A; Z=1-343.
DR PDB; 8CH6; EM; 5.90 A; Z=1-343.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7QTT; -.
DR PDBsum; 8CH6; -.
DR AlphaFoldDB; O15541; -.
DR EMDB; EMD-14146; -.
DR EMDB; EMD-16658; -.
DR EMDB; EMD-30875; -.
DR EMDB; EMD-4255; -.
DR EMDB; EMD-6889; -.
DR EMDB; EMD-6891; -.
DR SMR; O15541; -.
DR BioGRID; 113523; 693.
DR IntAct; O15541; 20.
DR MINT; O15541; -.
DR STRING; 9606.ENSP00000360497; -.
DR GlyGen; O15541; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15541; -.
DR PhosphoSitePlus; O15541; -.
DR BioMuta; RNF113A; -.
DR EPD; O15541; -.
DR jPOST; O15541; -.
DR MassIVE; O15541; -.
DR MaxQB; O15541; -.
DR PaxDb; 9606-ENSP00000360497; -.
DR PeptideAtlas; O15541; -.
DR ProteomicsDB; 48749; -.
DR Pumba; O15541; -.
DR Antibodypedia; 382; 121 antibodies from 17 providers.
DR DNASU; 7737; -.
DR Ensembl; ENST00000371442.4; ENSP00000360497.2; ENSG00000125352.6.
DR GeneID; 7737; -.
DR KEGG; hsa:7737; -.
DR MANE-Select; ENST00000371442.4; ENSP00000360497.2; NM_006978.3; NP_008909.1.
DR UCSC; uc004esb.4; human.
DR AGR; HGNC:12974; -.
DR CTD; 7737; -.
DR DisGeNET; 7737; -.
DR GeneCards; RNF113A; -.
DR HGNC; HGNC:12974; RNF113A.
DR HPA; ENSG00000125352; Low tissue specificity.
DR MalaCards; RNF113A; -.
DR MIM; 300951; gene.
DR MIM; 300953; phenotype.
DR neXtProt; NX_O15541; -.
DR OpenTargets; ENSG00000125352; -.
DR Orphanet; 33364; Trichothiodystrophy.
DR PharmGKB; PA37556; -.
DR VEuPathDB; HostDB:ENSG00000125352; -.
DR eggNOG; KOG1813; Eukaryota.
DR GeneTree; ENSGT00390000016292; -.
DR HOGENOM; CLU_050460_1_0_1; -.
DR InParanoid; O15541; -.
DR OMA; ICRDSFK; -.
DR OrthoDB; 21858at2759; -.
DR PhylomeDB; O15541; -.
DR TreeFam; TF313469; -.
DR PathwayCommons; O15541; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O15541; -.
DR SIGNOR; O15541; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7737; 412 hits in 823 CRISPR screens.
DR GenomeRNAi; 7737; -.
DR Pharos; O15541; Tbio.
DR PRO; PR:O15541; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15541; Protein.
DR Bgee; ENSG00000125352; Expressed in granulocyte and 158 other cell types or tissues.
DR Genevisible; O15541; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0034247; P:snoRNA splicing; IBA:GO_Central.
DR CDD; cd16539; RING-HC_RNF113A_B; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039971; CWC24-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12930:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF113A; 1.
DR PANTHER; PTHR12930; ZINC FINGER PROTEIN 183; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 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; DNA damage; DNA repair; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..343
FT /note="E3 ubiquitin-protein ligase RNF113A"
FT /id="PRO_0000056087"
FT ZN_FING 196..224
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 262..300
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 2..60
FT /note="Important for interaction with SNRNP200/BRR2"
FT /evidence="ECO:0000269|PubMed:29144457"
FT REGION 22..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..61
FT /note="Important for interaction with CXCR4"
FT /evidence="ECO:0000269|PubMed:28978524"
FT REGION 322..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MUTAGEN 2..60
FT /note="Missing: Strongly decreased interaction with
FT SNRNP200/BRR2."
FT /evidence="ECO:0000269|PubMed:29144457"
FT MUTAGEN 50..61
FT /note="Missing: Strongly decreased interaction with CXCR4.
FT Abolishes the ability to promote CXCR4 degradation."
FT /evidence="ECO:0000269|PubMed:28978524"
FT MUTAGEN 262
FT /note="C->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:28978524"
FT MUTAGEN 264
FT /note="I->A: Strongly reduced E3 ubiquitin ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:29144457"
FT MUTAGEN 277
FT /note="C->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:28978524"
FT MUTAGEN 301..343
FT /note="Missing: Cells are hypersensitive to DNA damage by
FT alkylating agents."
FT /evidence="ECO:0000269|PubMed:29144457"
FT CONFLICT 21
FT /note="K -> R (in Ref. 2; BAG37314)"
FT /evidence="ECO:0000305"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7QTT"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:7QTT"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:7QTT"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7QTT"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 343 AA; 38787 MW; F76E28037A6FF78B CRC64;
MAEQLSPGKA VDQVCTFLFK KPGRKGAAGR RKRPACDPEP GESGSSSDEG CTVVRPEKKR
VTHNPMIQKT RDSGKQKAAY GDLSSEEEEE NEPESLGVVY KSTRSAKPVG PEDMGATAVY
ELDTEKERDA QAIFERSQKI QEELRGKEDD KIYRGINNYQ KYMKPKDTSM GNASSGMVRK
GPIRAPEHLR ATVRWDYQPD ICKDYKETGF CGFGDSCKFL HDRSDYKHGW QIERELDEGR
YGVYEDENYE VGSDDEEIPF KCFICRQSFQ NPVVTKCRHY FCESCALQHF RTTPRCYVCD
QQTNGVFNPA KELIAKLEKH RATGEGGASD LPEDPDEDAI PIT
//
