RN213_HUMAN
ID RN213_HUMAN Reviewed; 5207 AA.
AC Q63HN8; C9JCP4; D6RI12; F8WKS1; Q658P6; Q69YK7; Q6MZR1; Q8IWF4; Q8IZX1;
AC Q8IZX2; Q8N406; Q8TEU0; Q9H6C9; Q9H6H9; Q9H6P3; Q9H8A9; Q9HCF4; Q9HCL8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=E3 ubiquitin-protein ligase RNF213 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849};
DE EC=3.6.4.- {ECO:0000269|PubMed:21799892, ECO:0000305|PubMed:24658080, ECO:0000305|PubMed:26126547};
DE AltName: Full=ALK lymphoma oligomerization partner on chromosome 17 {ECO:0000303|PubMed:12112524};
DE AltName: Full=E3 ubiquitin-lipopolysaccharide ligase RNF213 {ECO:0000305};
DE EC=2.3.2.- {ECO:0000269|PubMed:34012115};
DE AltName: Full=Mysterin {ECO:0000303|PubMed:26126547};
DE AltName: Full=RING finger protein 213 {ECO:0000305};
GN Name=RNF213 {ECO:0000312|HGNC:HGNC:14539};
GN Synonyms=ALO17 {ECO:0000303|PubMed:12112524},
GN C17orf27 {ECO:0000312|HGNC:HGNC:14539},
GN KIAA1554 {ECO:0000303|PubMed:10997877},
GN KIAA1618 {ECO:0000303|PubMed:10997877},
GN MYSTR {ECO:0000303|PubMed:26126547};
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), FUNCTION, CATALYTIC ACTIVITY,
RP AUTOUBIQUITINATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS
RP ASP-3962; GLN-4062; SER-4608; ASN-4863; ASP-4950; VAL-5021; GLU-5160 AND
RP GLY-5176, AND VARIANTS MYMY2 ASN-4013 AND LYS-4810.
RX PubMed=21799892; DOI=10.1371/journal.pone.0022542;
RA Liu W., Morito D., Takashima S., Mineharu Y., Kobayashi H., Hitomi T.,
RA Hashikata H., Matsuura N., Yamazaki S., Toyoda A., Kikuta K., Takagi Y.,
RA Harada K.H., Fujiyama A., Herzig R., Krischek B., Zou L., Kim J.E.,
RA Kitakaze M., Miyamoto S., Nagata K., Hashimoto N., Koizumi A.;
RT "Identification of RNF213 as a susceptibility gene for moyamoya disease and
RT its possible role in vascular development.";
RL PLoS ONE 6:E22542-E22542(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3021-5207 (ISOFORMS 1/2).
RC TISSUE=Endometrium, Lymph node, Melanoma, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Eye, and Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-163 (ISOFORMS 1 AND 2/3), AND CHROMOSOMAL
RP TRANSLOCATION WITH ALK.
RX PubMed=12112524; DOI=10.1002/gcc.10033;
RA Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B.,
RA De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.;
RT "Identification of novel fusion partners of ALK, the anaplastic lymphoma
RT kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic
RT tumor.";
RL Genes Chromosomes Cancer 34:354-362(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-1509 AND 3888-5207 (ISOFORMS
RP 1/2).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3770-5207 (ISOFORMS 1/2).
RC TISSUE=Spleen, and Thyroid;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, 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 [13]
RP INTERACTION WITH M.TUBERCULOSIS RV3655C (MICROBIAL INFECTION), AND
RP INDUCTION (MICROBIAL INFECTION).
RX PubMed=20454556; DOI=10.1371/journal.pone.0010474;
RA Danelishvili L., Yamazaki Y., Selker J., Bermudez L.E.;
RT "Secreted Mycobacterium tuberculosis Rv3654c and Rv3655c proteins
RT participate in the suppression of macrophage apoptosis.";
RL PLoS ONE 5:E10474-E10474(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217 AND SER-1258, AND
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-1258 AND SER-2273,
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-217 AND SER-1258,
RP AND IDENTIFICATION BY 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1151, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-2426; GLU-2488;
RP LYS-2775 AND GLU-2845.
RX PubMed=24658080; DOI=10.1038/srep04442;
RA Morito D., Nishikawa K., Hoseki J., Kitamura A., Kotani Y., Kiso K.,
RA Kinjo M., Fujiyoshi Y., Nagata K.;
RT "Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+
RT ATPase, which dynamically changes its oligomeric state.";
RL Sci. Rep. 4:4442-4442(2014).
RN [21]
RP INDUCTION.
RX PubMed=26070522; DOI=10.1016/j.jstrokecerebrovasdis.2015.01.041;
RA Zhao S., Gong Z., Zhang J., Xu X., Liu P., Guan W., Jing L., Peng T.,
RA Teng J., Jia Y.;
RT "Elevated serum microRNA Let-7c in Moyamoya disease.";
RL J. Stroke Cerebrovasc. Dis. 24:1709-1714(2015).
RN [22]
RP FUNCTION, AND INDUCTION.
RX PubMed=26278786; DOI=10.1038/srep13191;
RA Ohkubo K., Sakai Y., Inoue H., Akamine S., Ishizaki Y., Matsushita Y.,
RA Sanefuji M., Torisu H., Ihara K., Sardiello M., Hara T.;
RT "Moyamoya disease susceptibility gene RNF213 links inflammatory and
RT angiogenic signals in endothelial cells.";
RL Sci. Rep. 5:13191-13191(2015).
RN [23]
RP FUNCTION.
RX PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
RA Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I., Boutros M.,
RA Niehrs C., Augustin H.G.;
RT "Endothelial RSPO3 controls vascular stability and pruning through non-
RT canonical WNT/Ca(2+)/NFAT signaling.";
RL Dev. Cell 36:79-93(2016).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-2426; GLU-2488;
RP LYS-2775 AND GLU-2845.
RX PubMed=30705059; DOI=10.1083/jcb.201712120;
RA Sugihara M., Morito D., Ainuki S., Hirano Y., Ogino K., Kitamura A.,
RA Hirata H., Nagata K.;
RT "The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid
RT droplets.";
RL J. Cell Biol. 218:949-960(2019).
RN [25]
RP FUNCTION.
RX PubMed=30846318; DOI=10.1016/j.molcel.2019.01.036;
RA Piccolis M., Bond L.M., Kampmann M., Pulimeno P., Chitraju C.,
RA Jayson C.B.K., Vaites L.P., Boland S., Lai Z.W., Gabriel K.R.,
RA Elliott S.D., Paulo J.A., Harper J.W., Weissman J.S., Walther T.C.,
RA Farese R.V. Jr.;
RT "Probing the global cellular responses to lipotoxicity caused by saturated
RT fatty acids.";
RL Mol. Cell 74:32-44(2019).
RN [26]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2N,
RP CHARACTERIZATION OF VARIANTS TYR-3997; ARG-4007; ASN-4014; SER-4017;
RP CYS-4019; ARG-4024; ARG-4032 AND LEU-4033, AND VARIANT MYMY2 ASN-4013.
RX PubMed=32139119; DOI=10.1016/j.bbrc.2020.02.024;
RA Takeda M., Tezuka T., Kim M., Choi J., Oichi Y., Kobayashi H., Harada K.H.,
RA Mizushima T., Taketani S., Koizumi A., Youssefian S.;
RT "Moyamoya disease patient mutations in the RING domain of RNF213 reduce its
RT ubiquitin ligase activity and enhance NFkappaB activation and apoptosis in
RT an AAA+ domain-dependent manner.";
RL Biochem. Biophys. Res. Commun. 525:668-674(2020).
RN [27]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH UBE2N.
RX PubMed=33842849; DOI=10.1096/fba.2019-00092;
RA Habu T., Harada K.H.;
RT "UBC13 is an RNF213-associated E2 ubiquitin-conjugating enzyme, and Lysine
RT 63-linked ubiquitination by the RNF213-UBC13 axis is responsible for
RT angiogenic activity.";
RL FASEB Bioadv. 3:243-258(2021).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, CHARACTERIZATION OF VARIANTS
RP ILE-4638; ASP-4950 AND VAL-5021, CHARACTERIZATION OF VARIANT MYMY2
RP LYS-4810, AND MUTAGENESIS OF LYS-2426; GLU-2488; LYS-2775; GLU-2845;
RP HIS-4014; TRP-4024 AND HIS-4509.
RX PubMed=34012115; DOI=10.1038/s41586-021-03566-4;
RA Otten E.G., Werner E., Crespillo-Casado A., Boyle K.B., Dharamdasani V.,
RA Pathe C., Santhanam B., Randow F.;
RT "Ubiquitylation of lipopolysaccharide by RNF213 during bacterial
RT infection.";
RL Nature 594:111-116(2021).
RN [29]
RP VARIANTS GLU-2554; VAL-3891; GLY-3915; MET-4567 AND MET-4765, AND VARIANTS
RP MYMY2 THR-4399 AND LYS-4810.
RX PubMed=21048783; DOI=10.1038/jhg.2010.132;
RA Kamada F., Aoki Y., Narisawa A., Abe Y., Komatsuzaki S., Kikuchi A.,
RA Kanno J., Niihori T., Ono M., Ishii N., Owada Y., Fujimura M., Mashimo Y.,
RA Suzuki Y., Hata A., Tsuchiya S., Tominaga T., Matsubara Y., Kure S.;
RT "A genome-wide association study identifies RNF213 as the first Moyamoya
RT disease gene.";
RL J. Hum. Genet. 56:34-40(2011).
RN [30]
RP VARIANT MYMY2 LYS-4810.
RX PubMed=22931863; DOI=10.1038/jhg.2012.105;
RA Miyatake S., Touho H., Miyake N., Ohba C., Doi H., Saitsu H., Taguri M.,
RA Morita S., Matsumoto N.;
RT "Sibling cases of moyamoya disease having homozygous and heterozygous
RT c.14576G>A variant in RNF213 showed varying clinical course and severity.";
RL J. Hum. Genet. 57:804-806(2012).
RN [31]
RP VARIANT MYMY2 LYS-4810.
RX PubMed=22688072; DOI=10.2176/nmc.52.339;
RA Shimoda Y., Fujimura M., Inoue T., Shimizu H., Tominaga T.;
RT "Temporal profile of de novo development of moyamoya vasculopathy in an
RT adult: case report.";
RL Neurol. Med. Chir. 52:339-342(2012).
RN [32]
RP VARIANT MYMY2 LYS-4810.
RX PubMed=22377813; DOI=10.1212/wnl.0b013e318249f71f;
RA Miyatake S., Miyake N., Touho H., Nishimura-Tadaki A., Kondo Y., Okada I.,
RA Tsurusaki Y., Doi H., Sakai H., Saitsu H., Shimojima K., Yamamoto T.,
RA Higurashi M., Kawahara N., Kawauchi H., Nagasaka K., Okamoto N., Mori T.,
RA Koyano S., Kuroiwa Y., Taguri M., Morita S., Matsubara Y., Kure S.,
RA Matsumoto N.;
RT "Homozygous c.14576G>A variant of RNF213 predicts early-onset and severe
RT form of moyamoya disease.";
RL Neurology 78:803-810(2012).
RN [33]
RP VARIANTS MYMY2 THR-4399 AND LYS-4810, AND VARIANTS ARG-4007; LEU-4367;
RP PRO-4586; VAL-4631; ASP-4950; VAL-5021 AND ILE-5136.
RX PubMed=23110205; DOI=10.1371/journal.pone.0048179;
RA Wu Z., Jiang H., Zhang L., Xu X., Zhang X., Kang Z., Song D., Zhang J.,
RA Guan M., Gu Y.;
RT "Molecular analysis of RNF213 gene for moyamoya disease in the Chinese Han
RT population.";
RL PLoS ONE 7:E48179-E48179(2012).
RN [34]
RP CHARACTERIZATION OF VARIANT MYMY2 LYS-4810.
RX PubMed=23994138; DOI=10.1016/j.bbrc.2013.08.067;
RA Hitomi T., Habu T., Kobayashi H., Okuda H., Harada K.H., Osafune K.,
RA Taura D., Sone M., Asaka I., Ameku T., Watanabe A., Kasahara T., Sudo T.,
RA Shiota F., Hashikata H., Takagi Y., Morito D., Miyamoto S., Nakao K.,
RA Koizumi A.;
RT "The moyamoya disease susceptibility variant RNF213 R4810K (rs112735431)
RT induces genomic instability by mitotic abnormality.";
RL Biochem. Biophys. Res. Commun. 439:419-426(2013).
RN [35]
RP VARIANT THR-4185.
RX PubMed=25043520; DOI=10.1111/ijs.12306;
RA Smith K.R., Leventer R.J., Mackay M.T., Pope K., Gillies G.,
RA Delatycki M.B., Amor D.J., Bahlo M., Lockhart P.J.;
RT "Identification of a novel RNF213 variant in a family with heterogeneous
RT intracerebral vasculopathy.";
RL Int. J. Stroke 9:E26-E27(2014).
RN [36]
RP VARIANTS MYMY2 ASN-4013 AND LYS-4810, AND VARIANTS ALA-529 DEL; GLN-3922;
RP TYR-3997; CYS-4019; VAL-4076; LYS-4115 DEL; GLU-4237; THR-4732 AND
RP ILE-5163.
RX PubMed=25278557; DOI=10.1161/strokeaha.114.006244;
RG University of Washington Center for Mendelian Genomics;
RA Cecchi A.C., Guo D., Ren Z., Flynn K., Santos-Cortez R.L., Leal S.M.,
RA Wang G.T., Regalado E.S., Steinberg G.K., Shendure J., Bamshad M.J.,
RA Grotta J.C., Nickerson D.A., Pannu H., Milewicz D.M.;
RT "RNF213 rare variants in an ethnically diverse population with Moyamoya
RT disease.";
RL Stroke 45:3200-3207(2014).
RN [37]
RP VARIANT PHE-4118, AND INVOLVEMENT IN MYMY2.
RX PubMed=26198278; DOI=10.1002/ajmg.a.37230;
RA Harel T., Posey J.E., Graham B.H., Walkiewicz M., Yang Y., Lalani S.R.,
RA Belmont J.W.;
RT "Atypical presentation of moyamoya disease in an infant with a de novo
RT RNF213 variant.";
RL Am. J. Med. Genet. A 167A:2742-2747(2015).
RN [38]
RP CHARACTERIZATION OF VARIANT MYMY2 LYS-4810, FUNCTION, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF GLU-2488.
RX PubMed=26126547; DOI=10.1161/jaha.115.002146;
RA Kobayashi H., Matsuda Y., Hitomi T., Okuda H., Shioi H., Matsuda T.,
RA Imai H., Sone M., Taura D., Harada K.H., Habu T., Takagi Y., Miyamoto S.,
RA Koizumi A.;
RT "Biochemical and functional characterization of RNF213 (Mysterin) R4810K, a
RT susceptibility mutation of Moyamoya disease, in angiogenesis in vitro and
RT in vivo.";
RL J. Am. Heart Assoc. 4:0-0(2015).
RN [39]
RP VARIANTS VAL-1622; MET-3933 AND CYS-4131, AND VARIANT MYMY2 LYS-4810.
RX PubMed=25956231; DOI=10.1016/j.jns.2015.04.019;
RA Lee M.J., Chen Y.F., Fan P.C., Wang K.C., Wang K., Wang J., Kuo M.F.;
RT "Mutation genotypes of RNF213 gene from moyamoya patients in Taiwan.";
RL J. Neurol. Sci. 353:161-165(2015).
RN [40]
RP VARIANTS CYS-4019; LYS-4042; ALA-4146 AND LEU-4677, CHARACTERIZATION OF
RP VARIANT MYMY2 ASN-4013, AND CHARACTERIZATION OF VARIANTS CYS-4019 AND
RP ALA-4146.
RX PubMed=27736983; DOI=10.1371/journal.pone.0164759;
RA Kobayashi H., Brozman M., Kyselova K., Viszlayova D., Morimoto T.,
RA Roubec M., Skoloudik D., Petrovicova A., Juskanic D., Strauss J., Halaj M.,
RA Kurray P., Hranai M., Harada K.H., Inoue S., Yoshida Y., Habu T.,
RA Herzig R., Youssefian S., Koizumi A.;
RT "RNF213 rare variants in Slovakian and Czech moyamoya disease patients.";
RL PLoS ONE 11:E0164759-E0164759(2016).
RN [41]
RP VARIANTS ARG-118; MET-133; ASN-209; LEU-395; VAL-1135; LYS-1705; LEU-1721;
RP THR-1844; HIS-3846; THR-3927; MET-3933; ASN-4014; CYS-4019; ARG-4032;
RP LEU-4033; LYS-4042; PRO-4051; GLN-4062; VAL-4122; SER-4608 AND SER-4640,
RP AND VARIANTS MYMY2 ASN-4013 AND THR-4399.
RX PubMed=28635953; DOI=10.1038/ejhg.2017.92;
RG FREX consortium;
RA Guey S., Kraemer M., Herve D., Ludwig T., Kossorotoff M., Bergametti F.,
RA Schwitalla J.C., Choi S., Broseus L., Callebaut I., Genin E.,
RA Tournier-Lasserve E.;
RT "Rare RNF213 variants in the C-terminal region encompassing the RING-finger
RT domain are associated with moyamoya angiopathy in Caucasians.";
RL Eur. J. Hum. Genet. 25:995-1003(2017).
RN [42]
RP VARIANTS LYS-996; PRO-4058 AND GLN-4062, AND INVOLVEMENT IN MYMY2.
RX PubMed=29387438; DOI=10.1038/hgv.2017.60;
RA Akagawa H., Mukawa M., Nariai T., Nomura S., Aihara Y., Onda H.,
RA Yoneyama T., Kudo T., Sumita K., Maehara T., Kawamata T., Kasuya H.;
RT "Novel and recurrent RNF213 variants in Japanese pediatric patients with
RT moyamoya disease.";
RL Hum. Genome Var. 5:17060-17060(2018).
RN [43]
RP VARIANTS GLU-4185 AND THR-4188, AND INVOLVEMENT IN MYMY2.
RX PubMed=31645973; DOI=10.1038/s41439-019-0066-6;
RA Gagunashvili A.N., Ocaka L., Kelberman D., Munot P., Bacchelli C.,
RA Beales P.L., Ganesan V.;
RT "Novel missense variants in the RNF213 gene from a European family with
RT Moyamoya disease.";
RL Hum. Genome Var. 6:35-35(2019).
RN [44]
RP VARIANTS SER-4017 AND LEU-4677, AND INVOLVEMENT IN MYMY2.
RX PubMed=27787485; DOI=10.23736/s0390-5616.16.03900-x;
RA Raso A., Biassoni R., Mascelli S., Nozza P., Ugolotti E., Di Marco E.,
RA De Marco P., Merello E., Cama A., Pavanello M., Capra V.;
RT "Moyamoya vasculopathy shows a genetic mutational gradient decreasing from
RT East to West.";
RL J. Neurosurg. Sci. 64:165-172(2020).
RN [45]
RP VARIANTS 3996-PRO-CYS-3997 DELINS GLY-LEU-GLY; ARG-4114 AND LEU-4120, AND
RP INVOLVEMENT IN MYMY2.
RX PubMed=33568546; DOI=10.1212/wnl.0000000000011653;
RA Pinard A., Fiander M.D.J., Cecchi A.C., Rideout A.L., Azouz M.,
RA Fraser S.M., McNeely P.D., Walling S., Novara S.C., Hurst A.C.E., Guo D.,
RA Parkash S., Bamshad M.J., Nickerson D.A., Vandersteen A.M., Milewicz D.M.;
RT "Association of de novo RNF213 variants with childhood onset Moyamoya
RT disease and diffuse occlusive vasculopathy.";
RL Neurology 96:e1783-e1791(2021).
CC -!- FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination
CC of both proteins and lipids, and which is involved in various
CC processes, such as lipid metabolism, angiogenesis and cell-autonomous
CC immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786,
CC PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115).
CC Acts as a key immune sensor by catalyzing ubiquitination of the lipid A
CC moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-
CC finger: restricts the proliferation of cytosolic bacteria, such as
CC Salmonella, by generating the bacterial ubiquitin coat through the
CC ubiquitination of LPS (PubMed:34012115). Also acts indirectly by
CC mediating the recruitment of the LUBAC complex, which conjugates linear
CC polyubiquitin chains (PubMed:34012115). Ubiquitination of LPS triggers
CC cell-autonomous immunity, such as antibacterial autophagy, leading to
CC degradation of the microbial invader (PubMed:34012115). Involved in
CC lipid metabolism by regulating fat storage and lipid droplet formation;
CC act by inhibiting the lipolytic process (PubMed:30705059). Also
CC regulates lipotoxicity by inhibiting desaturation of fatty acids
CC (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its
CC RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of
CC target proteins (PubMed:32139119, PubMed:33842849). Involved in the
CC non-canonical Wnt signaling pathway in vascular development: acts by
CC mediating ubiquitination and degradation of FLNA and NFATC2 downstream
CC of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway
CC and promoting vessel regression (PubMed:26766444). Also has ATPase
CC activity; ATPase activity is required for ubiquitination of LPS
CC (PubMed:34012115). {ECO:0000269|PubMed:21799892,
CC ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26278786,
CC ECO:0000269|PubMed:26766444, ECO:0000269|PubMed:30705059,
CC ECO:0000269|PubMed:30846318, ECO:0000269|PubMed:32139119,
CC ECO:0000269|PubMed:33842849, ECO:0000269|PubMed:34012115}.
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:21799892,
CC ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:21799892, ECO:0000305|PubMed:24658080,
CC ECO:0000305|PubMed:26126547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:21799892, ECO:0000305|PubMed:24658080,
CC ECO:0000305|PubMed:26126547};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33842849,
CC ECO:0000305|PubMed:21799892}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with UBE2L3/UBCH7;
CC UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for
CC the ubiquitin ligase activity (By similarity). Interacts with
CC UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target
CC proteins (PubMed:32139119, PubMed:33842849).
CC {ECO:0000250|UniProtKB:E9Q555, ECO:0000269|PubMed:32139119,
CC ECO:0000269|PubMed:33842849}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis protein
CC Rv3655c, which impairs caspase-8 activation and suppresses macrophage
CC apoptosis by blocking the extrinsic pathway.
CC {ECO:0000269|PubMed:20454556}.
CC -!- INTERACTION:
CC Q63HN8-6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10248548, EBI-618309;
CC Q63HN8-6; Q6A162: KRT40; NbExp=3; IntAct=EBI-10248548, EBI-10171697;
CC Q63HN8-6; Q04864: REL; NbExp=3; IntAct=EBI-10248548, EBI-307352;
CC Q63HN8-6; P36406: TRIM23; NbExp=3; IntAct=EBI-10248548, EBI-740098;
CC Q63HN8-6; P14373: TRIM27; NbExp=3; IntAct=EBI-10248548, EBI-719493;
CC Q63HN8-6; Q15654: TRIP6; NbExp=3; IntAct=EBI-10248548, EBI-742327;
CC Q63HN8-6; Q5T124: UBXN11; NbExp=3; IntAct=EBI-10248548, EBI-746004;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21799892,
CC ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115}. Lipid
CC droplet {ECO:0000269|PubMed:30705059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q63HN8-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63HN8-4; Sequence=VSP_042417;
CC Name=3;
CC IsoId=Q63HN8-5; Sequence=VSP_042418, VSP_042419;
CC Name=4;
CC IsoId=Q63HN8-6; Sequence=VSP_042416, VSP_042420;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:21799892}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Major isoform detected in all tissues
CC examined. {ECO:0000269|PubMed:21799892}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Minor isoform with restricted
CC expression. {ECO:0000269|PubMed:21799892}.
CC -!- INDUCTION: Down-regulated by let-7c miRNA, which binds to the 3'-UTR
CC transcript of RNF213 (PubMed:26070522). Induced by pro-inflammatory
CC cytokines (PubMed:26278786). {ECO:0000269|PubMed:26070522,
CC ECO:0000269|PubMed:26278786}.
CC -!- INDUCTION: (Microbial infection) Up-regulated in macrophages infected
CC by M.tuberculosis. {ECO:0000269|PubMed:20454556}.
CC -!- DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised
CC of two catalytically active and four inactive ATPase domains, and a C-
CC terminal E3 module. The ATPase regions do not generate movement but
CC rather act like an intricate molecular 'switch'.
CC {ECO:0000250|UniProtKB:E9Q555}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for the ubiquitin-
CC protein ligase activity. {ECO:0000269|PubMed:21799892}.
CC -!- DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the
CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide
CC (LPS). {ECO:0000269|PubMed:34012115}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:21799892}.
CC -!- DISEASE: Moyamoya disease 2 (MYMY2) [MIM:607151]: A progressive
CC cerebral angiopathy characterized by bilateral intracranial carotid
CC artery stenosis and telangiectatic vessels in the region of the basal
CC ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on
CC cerebral angiogram. Affected individuals can develop transient ischemic
CC attacks and/or cerebral infarction, and rupture of the collateral
CC vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset
CC and epileptic seizures constitute the prevailing presentation in
CC childhood, while subarachnoid bleeding occurs more frequently in
CC adults. {ECO:0000269|PubMed:21048783, ECO:0000269|PubMed:21799892,
CC ECO:0000269|PubMed:22377813, ECO:0000269|PubMed:22688072,
CC ECO:0000269|PubMed:22931863, ECO:0000269|PubMed:23110205,
CC ECO:0000269|PubMed:23994138, ECO:0000269|PubMed:25278557,
CC ECO:0000269|PubMed:25956231, ECO:0000269|PubMed:26126547,
CC ECO:0000269|PubMed:26198278, ECO:0000269|PubMed:27736983,
CC ECO:0000269|PubMed:27787485, ECO:0000269|PubMed:28635953,
CC ECO:0000269|PubMed:29387438, ECO:0000269|PubMed:31645973,
CC ECO:0000269|PubMed:32139119, ECO:0000269|PubMed:33568546,
CC ECO:0000269|PubMed:34012115}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving RNF213 is associated
CC with anaplastic large-cell lymphoma (ALCL). Translocation
CC t(2;17)(p23;q25) with ALK. {ECO:0000269|PubMed:12112524}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: The stoichiometry is unclear: was initially thought to form
CC homohexamers (PubMed:24658080, PubMed:26126547). However, the electron
CC microscopy structure showed that it is monomeric and is composed of six
CC ATPase modules within a single polypeptide chain (By similarity).
CC {ECO:0000250|UniProtKB:E9Q555, ECO:0000269|PubMed:24658080,
CC ECO:0000269|PubMed:26126547}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32220.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13444.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB14708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15212.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15280.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15330.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10615.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH56189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ALO17ID480.html";
CC ---------------------------------------------------------------------------
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DR EMBL; AB537889; BAK53191.1; -; mRNA.
DR EMBL; AL832920; CAH10615.1; ALT_FRAME; mRNA.
DR EMBL; AL833201; CAH56308.1; -; mRNA.
DR EMBL; BX640932; CAE45967.1; -; mRNA.
DR EMBL; BX647946; CAH56189.1; ALT_INIT; mRNA.
DR EMBL; AC123764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032220; AAH32220.1; ALT_INIT; mRNA.
DR EMBL; BC036891; AAH36891.1; -; mRNA.
DR EMBL; BC040341; AAH40341.1; -; mRNA.
DR EMBL; AF397204; AAN63520.1; -; mRNA.
DR EMBL; AF397205; AAN63521.1; -; mRNA.
DR EMBL; AB046774; BAB13380.1; -; mRNA.
DR EMBL; AB046838; BAB13444.1; ALT_SEQ; mRNA.
DR EMBL; AK023871; BAB14708.1; ALT_INIT; mRNA.
DR EMBL; AK025676; BAB15212.1; ALT_INIT; mRNA.
DR EMBL; AK025914; BAB15280.1; ALT_SEQ; mRNA.
DR EMBL; AK026038; BAB15330.1; ALT_INIT; mRNA.
DR EMBL; AK074030; BAB84856.1; -; mRNA.
DR CCDS; CCDS11772.1; -. [Q63HN8-5]
DR CCDS; CCDS58606.1; -. [Q63HN8-3]
DR RefSeq; NP_001243000.2; NM_001256071.2.
DR RefSeq; NP_066005.2; NM_020954.3. [Q63HN8-5]
DR SMR; Q63HN8; -.
DR BioGRID; 121705; 151.
DR IntAct; Q63HN8; 46.
DR MINT; Q63HN8; -.
DR STRING; 9606.ENSP00000464087; -.
DR GlyGen; Q63HN8; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; Q63HN8; -.
DR MetOSite; Q63HN8; -.
DR PhosphoSitePlus; Q63HN8; -.
DR SwissPalm; Q63HN8; -.
DR BioMuta; RNF213; -.
DR DMDM; 380865458; -.
DR EPD; Q63HN8; -.
DR jPOST; Q63HN8; -.
DR MassIVE; Q63HN8; -.
DR MaxQB; Q63HN8; -.
DR PaxDb; Q63HN8; -.
DR PeptideAtlas; Q63HN8; -.
DR PRIDE; Q63HN8; -.
DR ProteomicsDB; 65884; -. [Q63HN8-3]
DR ProteomicsDB; 65885; -. [Q63HN8-4]
DR ProteomicsDB; 65886; -. [Q63HN8-5]
DR ProteomicsDB; 65887; -. [Q63HN8-6]
DR Antibodypedia; 46314; 195 antibodies from 27 providers.
DR DNASU; 57674; -.
DR Ensembl; ENST00000319921.4; ENSP00000324392.4; ENSG00000173821.20. [Q63HN8-5]
DR GeneID; 57674; -.
DR KEGG; hsa:57674; -.
DR UCSC; uc002jyf.5; human. [Q63HN8-3]
DR CTD; 57674; -.
DR DisGeNET; 57674; -.
DR GeneCards; RNF213; -.
DR HGNC; HGNC:14539; RNF213.
DR HPA; ENSG00000173821; Low tissue specificity.
DR MalaCards; RNF213; -.
DR MIM; 607151; phenotype.
DR MIM; 613768; gene.
DR neXtProt; NX_Q63HN8; -.
DR OpenTargets; ENSG00000173821; -.
DR Orphanet; 2573; Moyamoya disease.
DR PharmGKB; PA162401681; -.
DR VEuPathDB; HostDB:ENSG00000173821; -.
DR eggNOG; ENOG502QQ65; Eukaryota.
DR GeneTree; ENSGT00630000089884; -.
DR HOGENOM; CLU_011233_0_0_1; -.
DR InParanoid; Q63HN8; -.
DR TreeFam; TF343131; -.
DR PathwayCommons; Q63HN8; -.
DR Reactome; R-HSA-9635465; Suppression of apoptosis.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q63HN8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57674; 15 hits in 1117 CRISPR screens.
DR ChiTaRS; RNF213; human.
DR GeneWiki; RNF213; -.
DR GenomeRNAi; 57674; -.
DR Pharos; Q63HN8; Tbio.
DR PRO; PR:Q63HN8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q63HN8; protein.
DR Bgee; ENSG00000173821; Expressed in granulocyte and 174 other tissues.
DR ExpressionAtlas; Q63HN8; baseline and differential.
DR Genevisible; Q63HN8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; IDA:UniProtKB.
DR GO; GO:0120323; P:lipid ubiquitination; IDA:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0098792; P:xenophagy; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031248; RNF213.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22605; PTHR22605; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; ATP-binding; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; Disease variant; Hydrolase; Immunity;
KW Isopeptide bond; Lipid droplet; Lipid metabolism; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..5207
FT /note="E3 ubiquitin-protein ligase RNF213"
FT /id="PRO_0000415917"
FT ZN_FING 3997..4036
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 4483..4555
FT /note="RZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325,
FT ECO:0000269|PubMed:34012115"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 343..374
FT /evidence="ECO:0000255"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4516
FT /note="Nucleophile; for E3 ubiquitin-lipopolysaccharide
FT ligase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1995..2000
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2098
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3997
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4000
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4014
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4035
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 1151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..4650
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042416"
FT VAR_SEQ 87
FT /note="E -> EGATSEVLVDAAVDLISDEWEAANAIPSKRRKQDAAPLEAASVPSAD
FT CEQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042417"
FT VAR_SEQ 1009..1063
FT /note="SQTSILQGFSYSDLRKFGIVLSAVITKSWPRTADNFNDILKHLLTLADVKHV
FT FRL -> VNNLSSWETDSGSQLCSAMTQLRAMKHPLGLSSSANSEIGKWAPSSLAKGNG
FT AEI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_042418"
FT VAR_SEQ 1064..5207
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_042419"
FT VAR_SEQ 4651..4660
FT /note="QEQHQLSSRR -> MTRKSAPTSG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042420"
FT VARIANT 118
FT /note="C -> R (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085287"
FT VARIANT 133
FT /note="L -> M (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085288"
FT VARIANT 209
FT /note="I -> N (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085289"
FT VARIANT 395
FT /note="P -> L (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085290"
FT VARIANT 529
FT /note="Missing (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075635"
FT VARIANT 996
FT /note="E -> K (rare variant detected in cases of Moyamoya
FT disease in East Asian populations)"
FT /evidence="ECO:0000269|PubMed:29387438"
FT /id="VAR_085291"
FT VARIANT 1135
FT /note="A -> V (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085292"
FT VARIANT 1622
FT /note="A -> V (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:25956231"
FT /id="VAR_075636"
FT VARIANT 1705
FT /note="T -> K (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085293"
FT VARIANT 1721
FT /note="P -> L (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085294"
FT VARIANT 1844
FT /note="A -> T (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085295"
FT VARIANT 2554
FT /note="D -> E (in dbSNP:rs138516230)"
FT /evidence="ECO:0000269|PubMed:21048783"
FT /id="VAR_067020"
FT VARIANT 3846
FT /note="R -> H (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085296"
FT VARIANT 3891
FT /note="M -> V (rare variant detected in a sporadic case of
FT Moyamoya disease)"
FT /evidence="ECO:0000269|PubMed:21048783"
FT /id="VAR_067021"
FT VARIANT 3915
FT /note="E -> G (in dbSNP:rs61740658)"
FT /evidence="ECO:0000269|PubMed:21048783"
FT /id="VAR_067022"
FT VARIANT 3922
FT /note="R -> Q (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075637"
FT VARIANT 3927
FT /note="A -> T (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085297"
FT VARIANT 3933
FT /note="V -> M (rare variant detected in patients with
FT Moyamoya disease in East Asian and Caucasian populations)"
FT /evidence="ECO:0000269|PubMed:25956231,
FT ECO:0000269|PubMed:28635953"
FT /id="VAR_075638"
FT VARIANT 3962
FT /note="N -> D (variant detected in cases of Moyamoya
FT disease in Caucasian populations)"
FT /evidence="ECO:0000269|PubMed:21799892"
FT /id="VAR_067023"
FT VARIANT 3996..3997
FT /note="PC -> GLG (rare variant detected in cases of
FT Moyamoya disease)"
FT /evidence="ECO:0000269|PubMed:33568546"
FT /id="VAR_085298"
FT VARIANT 3997
FT /note="C -> Y (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population; abolished E3
FT ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:25278557,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_075639"
FT VARIANT 4007
FT /note="P -> R (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population; abolished E3
FT ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:23110205,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_075640"
FT VARIANT 4013
FT /note="D -> N (in MYMY2; variant detected in cases of
FT Moyamoya disease in Caucasian and Asian populations;
FT inhibitory effect on angiogenic activity of vascular
FT endothelial cells; does not affect E3 ubiquitin-protein
FT ligase activity)"
FT /evidence="ECO:0000269|PubMed:21799892,
FT ECO:0000269|PubMed:25278557, ECO:0000269|PubMed:27736983,
FT ECO:0000269|PubMed:28635953, ECO:0000269|PubMed:32139119"
FT /id="VAR_067024"
FT VARIANT 4014
FT /note="H -> N (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population; abolished E3
FT ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:28635953,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_085299"
FT VARIANT 4017
FT /note="C -> S (rare variant detected in patients with
FT Moyamoya disease; abolished E3 ubiquitin-protein ligase
FT activity)"
FT /evidence="ECO:0000269|PubMed:27787485,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_085300"
FT VARIANT 4019
FT /note="R -> C (rare variant detected in patients with
FT Moyamoya disease in Caucasian population; strongly
FT decreased E3 ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:25278557,
FT ECO:0000269|PubMed:27736983, ECO:0000269|PubMed:28635953,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_075641"
FT VARIANT 4024
FT /note="W -> R (variant detected in patients with Moyamoya
FT disease; strongly decreased E3 ubiquitin-protein ligase
FT activity)"
FT /evidence="ECO:0000269|PubMed:32139119"
FT /id="VAR_085301"
FT VARIANT 4032
FT /note="C -> R (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population; abolished E3
FT ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:28635953,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_085302"
FT VARIANT 4033
FT /note="P -> L (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population; abolished E3
FT ubiquitin-protein ligase activity)"
FT /evidence="ECO:0000269|PubMed:28635953,
FT ECO:0000269|PubMed:32139119"
FT /id="VAR_085303"
FT VARIANT 4042
FT /note="E -> K (rare variant detected in patients with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:27736983,
FT ECO:0000269|PubMed:28635953"
FT /id="VAR_079573"
FT VARIANT 4051
FT /note="H -> P (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085304"
FT VARIANT 4058
FT /note="H -> P (rare variant detected in cases of Moyamoya
FT disease in East Asian populations)"
FT /evidence="ECO:0000269|PubMed:29387438"
FT /id="VAR_085305"
FT VARIANT 4062
FT /note="R -> Q (variant detected in cases of Moyamoya
FT disease in Caucasian and East Asian populations)"
FT /evidence="ECO:0000269|PubMed:21799892,
FT ECO:0000269|PubMed:28635953, ECO:0000269|PubMed:29387438"
FT /id="VAR_067025"
FT VARIANT 4076
FT /note="I -> V (rare variant detected in a sporadic case of
FT Moyamoya disease in Asian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075642"
FT VARIANT 4114
FT /note="T -> R (rare variant detected in cases of Moyamoya
FT disease)"
FT /evidence="ECO:0000269|PubMed:33568546"
FT /id="VAR_085306"
FT VARIANT 4115
FT /note="Missing (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075643"
FT VARIANT 4118
FT /note="S -> F (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:26198278"
FT /id="VAR_075644"
FT VARIANT 4120
FT /note="F -> L (rare variant detected in cases of Moyamoya
FT disease)"
FT /evidence="ECO:0000269|PubMed:33568546"
FT /id="VAR_085307"
FT VARIANT 4122
FT /note="D -> V (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085308"
FT VARIANT 4131
FT /note="R -> C (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:25956231"
FT /id="VAR_075645"
FT VARIANT 4146
FT /note="V -> A (rare variant detected in cases of Moyamoya
FT disease in Slovakian and Czech populations; inhibitory
FT effect on angiogenic activity of vascular endothelial
FT cells)"
FT /evidence="ECO:0000269|PubMed:27736983"
FT /id="VAR_079574"
FT VARIANT 4185
FT /note="K -> E (variant detected in cases of Moyamoya
FT disease in a Caucasian family)"
FT /evidence="ECO:0000269|PubMed:31645973"
FT /id="VAR_085309"
FT VARIANT 4185
FT /note="K -> T (found in a heterozygous family with
FT heterogeneous intracerebral vasculopathy)"
FT /evidence="ECO:0000269|PubMed:25043520"
FT /id="VAR_075646"
FT VARIANT 4188
FT /note="A -> T (variant detected in cases of Moyamoya
FT disease in a Caucasian family)"
FT /evidence="ECO:0000269|PubMed:31645973"
FT /id="VAR_085310"
FT VARIANT 4237
FT /note="D -> E (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075647"
FT VARIANT 4367
FT /note="Q -> L (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:23110205"
FT /id="VAR_075648"
FT VARIANT 4399
FT /note="A -> T (in MYMY2; dbSNP:rs148731719)"
FT /evidence="ECO:0000269|PubMed:21048783,
FT ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:28635953"
FT /id="VAR_067026"
FT VARIANT 4567
FT /note="V -> M (rare variant detected in a sporadic case of
FT Moyamoya disease; dbSNP:rs145282452)"
FT /evidence="ECO:0000269|PubMed:21048783"
FT /id="VAR_067027"
FT VARIANT 4586
FT /note="T -> P (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:23110205"
FT /id="VAR_075649"
FT VARIANT 4608
FT /note="P -> S (variant detected in cases of Moyamoya
FT disease in Caucasian populations)"
FT /evidence="ECO:0000269|PubMed:21799892,
FT ECO:0000269|PubMed:28635953"
FT /id="VAR_067028"
FT VARIANT 4631
FT /note="L -> V (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:23110205"
FT /id="VAR_075650"
FT VARIANT 4638
FT /note="T -> I (rare variant detected in a case of Moyamoya
FT disease; does not affect ubiquitination of
FT lipopolysaccharide)"
FT /evidence="ECO:0000269|PubMed:34012115"
FT /id="VAR_085311"
FT VARIANT 4640
FT /note="G -> S (rare variant detected in a patient with
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:28635953"
FT /id="VAR_085312"
FT VARIANT 4677
FT /note="W -> L (rare variant detected in patients with
FT Moyamoya disease)"
FT /evidence="ECO:0000269|PubMed:27736983,
FT ECO:0000269|PubMed:27787485"
FT /id="VAR_079575"
FT VARIANT 4732
FT /note="K -> T (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075651"
FT VARIANT 4765
FT /note="V -> M (rare variant detected in a sporadic case of
FT Moyamoya disease)"
FT /evidence="ECO:0000269|PubMed:21048783"
FT /id="VAR_067029"
FT VARIANT 4810
FT /note="R -> K (in MYMY2; very frequent in individuals
FT affected by Moyamoya disease; strongly increases the risk
FT of Moyamoya disease; induces genomic instability; shows
FT decreased ATPase activity; does not affect ubiquitination
FT of lipopolysaccharide)"
FT /evidence="ECO:0000269|PubMed:21048783,
FT ECO:0000269|PubMed:21799892, ECO:0000269|PubMed:22377813,
FT ECO:0000269|PubMed:22688072, ECO:0000269|PubMed:22931863,
FT ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:23994138,
FT ECO:0000269|PubMed:25278557, ECO:0000269|PubMed:25956231,
FT ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:34012115"
FT /id="VAR_067030"
FT VARIANT 4863
FT /note="D -> N (variant detected in cases of Moyamoya
FT disease in East Asian populations)"
FT /evidence="ECO:0000269|PubMed:21799892"
FT /id="VAR_067031"
FT VARIANT 4950
FT /note="E -> D (variant detected in cases of Moyamoya
FT disease in East Asian populations and rare variant detected
FT in a sporadic case of Moyamoya disease; does not affect
FT ubiquitination of lipopolysaccharide)"
FT /evidence="ECO:0000269|PubMed:21799892,
FT ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:34012115"
FT /id="VAR_067032"
FT VARIANT 5021
FT /note="A -> V (variant detected in cases of Moyamoya
FT disease in East Asian populations and rare variant detected
FT in a sporadic case of Moyamoya disease; does not affect
FT ubiquitination of lipopolysaccharide; dbSNP:rs138130613)"
FT /evidence="ECO:0000269|PubMed:21799892,
FT ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:34012115"
FT /id="VAR_067033"
FT VARIANT 5136
FT /note="M -> I (rare variant detected in a sporadic case of
FT Moyamoya disease in East Asian population)"
FT /evidence="ECO:0000269|PubMed:23110205"
FT /id="VAR_075652"
FT VARIANT 5160
FT /note="D -> E (variant detected in cases of Moyamoya
FT disease in East Asian populations)"
FT /evidence="ECO:0000269|PubMed:21799892"
FT /id="VAR_067034"
FT VARIANT 5163
FT /note="V -> I (rare variant detected in a sporadic case of
FT Moyamoya disease in Caucasian population)"
FT /evidence="ECO:0000269|PubMed:25278557"
FT /id="VAR_075653"
FT VARIANT 5176
FT /note="E -> G (variant detected in cases of Moyamoya
FT disease in East Asian populations)"
FT /evidence="ECO:0000269|PubMed:21799892"
FT /id="VAR_067035"
FT MUTAGEN 2426
FT /note="K->A: Impaired ATP-binding leading to decreased
FT ATPase activity; abolished ubiquitination of
FT lipopolysaccharide. In mutant A1A2; abolished ATP-binding
FT and localization to lipid droplets; when associated with A-
FT 2775."
FT /evidence="ECO:0000269|PubMed:24658080,
FT ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115"
FT MUTAGEN 2488
FT /note="E->A: Decreased ATPase activity; abolished
FT ubiquitination of lipopolysaccharide. In mutant B1B2;
FT abolished ATPase activity and localization to lipid
FT droplets; when associated with A-2845."
FT /evidence="ECO:0000269|PubMed:24658080,
FT ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115"
FT MUTAGEN 2488
FT /note="E->Q: Loss of ATPase hydrolysis."
FT /evidence="ECO:0000269|PubMed:26126547"
FT MUTAGEN 2775
FT /note="K->A: Impaired ATP-binding leading to decreased
FT ATPase activity; abolished ubiquitination of
FT lipopolysaccharide. In mutant A1A2; abolished ATP-binding
FT and localization to lipid droplets; when associated with A-
FT 2426."
FT /evidence="ECO:0000269|PubMed:24658080,
FT ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115"
FT MUTAGEN 2845
FT /note="E->A: Decreased ATPase activity; abolished
FT ubiquitination of lipopolysaccharide. In mutant B1B2;
FT abolished ATPase activity and localization to lipid
FT droplets; when associated with A-2488."
FT /evidence="ECO:0000269|PubMed:24658080,
FT ECO:0000269|PubMed:30705059, ECO:0000269|PubMed:34012115"
FT MUTAGEN 4014
FT /note="H->N: Abolished E3 ubiquitin-protein ligase
FT activity; does not affect ubiquitination of
FT lipopolysaccharide."
FT /evidence="ECO:0000269|PubMed:34012115"
FT MUTAGEN 4024
FT /note="W->R: Abolished E3 ubiquitin-protein ligase
FT activity; does not affect ubiquitination of
FT lipopolysaccharide."
FT /evidence="ECO:0000269|PubMed:34012115"
FT MUTAGEN 4509
FT /note="H->A: Abolished ability to ubiquitinate
FT lipopolysaccharide."
FT /evidence="ECO:0000269|PubMed:34012115"
FT CONFLICT 270
FT /note="M -> T (in Ref. 4; AAH36891/AAH40341)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="M -> T (in Ref. 4; AAH36891/AAH40341)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> N (in Ref. 4; AAH36891)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="N -> D (in Ref. 1; BAK53191 and 6; BAB13444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="Q -> K (in Ref. 6; BAB13444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1195
FT /note="V -> M (in Ref. 6; BAB13444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="E -> Q (in Ref. 6; BAB13444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="D -> G (in Ref. 6; BAB13444)"
FT /evidence="ECO:0000305"
FT CONFLICT 3323
FT /note="R -> G (in Ref. 2; CAH56189)"
FT /evidence="ECO:0000305"
FT CONFLICT 4220
FT /note="E -> G (in Ref. 7; BAB15212)"
FT /evidence="ECO:0000305"
FT CONFLICT 4571
FT /note="D -> G (in Ref. 7; BAB15280)"
FT /evidence="ECO:0000305"
FT CONFLICT 4853
FT /note="K -> R (in Ref. 7; BAB15212)"
FT /evidence="ECO:0000305"
FT CONFLICT 4892
FT /note="N -> S (in Ref. 7; BAB15212)"
FT /evidence="ECO:0000305"
FT CONFLICT 5139
FT /note="L -> S (in Ref. 7; BAB15280)"
FT /evidence="ECO:0000305"
FT CONFLICT 5187
FT /note="L -> P (in Ref. 7; BAB15330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5207 AA; 591407 MW; 9BA6847099EE6E08 CRC64;
MECPSCQHVS KEETPKFCSQ CGERLPPAAP IADSENNNST MASASEGEME CGQELKEEGG
PCLFPGSDSW QENPEEPCSK ASWTVQESKK KKRKKKKKGN KSASSELASL PLSPASPCHL
TLLSNPWPQD TALPHSQAQQ SGPTGQPSQP PGTATTPLEG DGLSAPTEVG DSPLQAQALG
EAGVATGSEA QSSPQFQDHT EGEDQDASIP SGGRGLSQEG TGPPTSAGEG HSRTEDAAQE
LLLPESKGGS SEPGTELQTT EQQAGASASM AVDAVAEPAN AVKGAGKEMK EKTQRMKQPP
ATTPPFKTHC QEAETKTKDE MAAAEEKVGK NEQGEPEDLK KPEGKNRSAA AVKNEKEQKN
QEADVQEVKA STLSPGGGVT VFFHAIISLH FPFNPDLHKV FIRGGEEFGE SKWDSNICEL
HYTRDLGHDR VLVEGIVCIS KKHLDKYIPY KYVIYNGESF EYEFIYKHQQ KKGEYVNRCL
FIKSSLLGSG DWHQYYDIVY MKPHGRLQKV MNHITDGPRK DLVKGKQIAA ALMLDSTFSI
LQTWDTINLN SFFTQFEQFC FVLQQPMIYE GQAQLWTDLQ YREKEVKRYL WQHLKKHVVP
LPDGKSTDFL PVDCPVRSKL KTGLIVLFVV EKIELLLEGS LDWLCHLLTS DASSPDEFHR
DLSHILGIPQ SWRLYLVNLC QRCMDTRTYT WLGALPVLHC CMELAPRHKD AWRQPEDTWA
ALEGLSFSPF REQMLDTSSL LQFMREKQHL LSIDEPLFRS WFSLLPLSHL VMYMENFIEH
LGRFPAHILD CLSGIYYRLP GLEQVLNTQD VQDVQNVQNI LEMLLRLLDT YRDKIPEEAL
SPSYLTVCLK LHEAICSSTK LLKFYELPAL SAEIVCRMIR LLSLVDSAGQ RDETGNNSVQ
TVFQGTLAAT KRWLREVFTK NMLTSSGASF TYVKEIEVWR RLVEIQFPAE HGWKESLLGD
MEWRLTKEEP LSQITAYCNS CWDTKGLEDS VAKTFEKCII EAVSSACQSQ TSILQGFSYS
DLRKFGIVLS AVITKSWPRT ADNFNDILKH LLTLADVKHV FRLCGTDEKI LANVTEDAKR
LIAVADSVLT KVVGDLLSGT ILVGQLELII KHKNQFLDIW QLREKSLSPQ DEQCAVEEAL
DWRREELLLL KKEKRCVDSL LKMCGNVKHL IQVDFGVLAV RHSQDLSSKR LNDTVTVRLS
TSSNSQRATH YHLSSQVQEM AGKIDLLRDS HIFQLFWREA AEPLSEPKED QEAAELLSEP
EEESERHILE LEEVYDYLYQ PSYRKFIKLH QDLKSGEVTL AEIDVIFKDF VNKYTDLDSE
LKIMCTVDHQ DQRDWIKDRV EQIKEYHHLH QAVHAAKVIL QVKESLGLNG DFSVLNTLLN
FTDNFDDFRR ETLDQINQEL IQAKKLLQDI SEARCKGLQA LSLRKEFICW VREALGGINE
LKVFVDLASI SAGENDIDVD RVACFHDAVQ GYASLLFKLD PSVDFSAFMK HLKKLWKALD
KDQYLPRKLC DSARNLEWLK TVNESHGSVE RSSLTLATAI NQRGIYVIQA PKGGQKISPD
TVLHLILPES PGSHEESREY SLEEVKELLN KLMLMSGKKD RNNTEVERFS EVFCSVQRLS
QAFIDLHSAG NMLFRTWIAM AYCSPKQGVS LQMDFGLDLV TELKEGGDVT ELLAALCRQM
EHFLDSWKRF VTQKRMEHFY LNFYTAEQLV YLSTELRKQP PSDAALTMLS FIKSNCTLRD
VLRASVGCGS EAARYRMRRV MEELPLMLLS EFSLVDKLRI IMEQSMRCLP AFLPDCLDLE
TLGHCLAHLA GMGGSPVERC LPRGLQVGQP NLVVCGHSEV LPAALAVYMQ TPSQPLPTYD
EVLLCTPATT FEEVALLLRR CLTLGSLGHK VYSLLFADQL SYEVARQAEE LFHNLCTQQH
REDYQLVMVC DGDWEHCYLP SAFSQHKVFV TPQAPLEAIQ AYLAGHYRVP KQTLSAAAVF
NDRLCVGIVA SERAGVGKSL YVKRLHDKMK MQLNVKNVPL KTIRLIDPQV DESRVLGALL
PFLDAQYQKV PVLFHLDVTS SVQTGIWVFL FKLLILQYLM DINGKMWLRN PCHLYIVEIL
ERRTSVPSRS SSALRTRVPQ FSFLDIFPKV TCRPPKEVID MELSALRSDT EPGMDLWEFC
SETFQRPYQY LRRFNQNQDL DTFQYQEGSV EGTPEECLQH FLFHCGVINP SWSELRNFAR
FLNYQLRDCE ASLFCNPSFI GDTLRGFKKF VVTFMIFMAR DFATPSLHTS DQSPGKHMVT
MDGVREEDLA PFSLRKRWES EPHPYVFFND DHTTMTFIGF HLQPNINGSV DAISHLTGKV
IKRDVMTRDL YQGLLLQRVP FNVDFDKLPR HKKLERLCLT LGIPQATDPD KTYELTTDNM
LKILAIEMRF RCGIPVIIMG ETGCGKTRLI KFLSDLRRGG TNADTIKLVK VHGGTTADMI
YSRVREAENV AFANKDQHQL DTILFFDEAN TTEAISCIKE VLCDHMVDGQ PLAEDSGLHI
IAACNPYRKH SEEMICRLES AGLGYRVSME ETADRLGSIP LRQLVYRVHA LPPSLIPLVW
DFGQLSDVAE KLYIQQIVQR LVESISLDEN GTRVITEVLC ASQGFMRKTE DECSFVSLRD
VERCVKVFRW FHEHSAMLLA QLNAFLSKSS VSKNHTERDP VLWSLMLAIG VCYHASLEKK
DSYRKAIARF FPKPYDDSRL LLDEITRAQD LFLDGVPLRK TIAKNLALKE NVFMMVVCIE
LKIPLFLVGK PGSSKSLAKT IVADAMQGPA AYSDLFRSLK QVHLVSFQCS PHSTPQGIIS
TFRQCARFQQ GKDLQQYVSV VVLDEVGLAE DSPKMPLKTL HPLLEDGCIE DDPAPHKKVG
FVGISNWALD PAKMNRGIFV SRGSPNETEL IESAKGICSS DILVQDRVQG YFASFAKAYE
TVCKRQDKEF FGLRDYYSLI KMVFAAAKAS NRKPSPQDIA QAVLRNFSGK DDIQALDIFL
ANLPEAKCSE EVSPMQLIKQ NIFGPSQKVP GGEQEDAESR YLLVLTKNYV ALQILQQTFF
EGDQQPEIIF GSGFPKDQEY TQLCRNINRV KICMETGKMV LLLNLQNLYE SLYDALNQYY
VHLGGQKYVD LGLGTHRVKC RVHPNFRLIV IEEKDVVYKH FPIPLINRLE KHYLDINTVL
EKWQKSIVEE LCAWVEKFIN VKAHHFQKRH KYSPSDVFIG YHSDACASVV LQVIERQGPR
ALTEELHQKV SEEAKSILLN CATPDAVVRL SAYSLGGFAA EWLSQEYFHR QRHNSFADFL
QAHLHTADLE RHAIFTEITT FSRLLTSHDC EILESEVTGR APKPTLLWLQ QFDTEYSFLK
EVRNCLTNTA KCKILIFQTD FEDGIRSAQL IASAKYSVIN EINKIRENED RIFVYFITKL
SRVGRGTAYV GFHGGLWQSV HIDDLRRSTL MVSDVTRLQH VTISQLFAPG DLPELGLEHR
AEDGHEEAME TEASTSGEVA EVAEEAMETE SSEKVGKETS ELGGSDVSIL DTTRLLRSCV
QSAVGMLRDQ NESCTRNMRR VVLLLGLLNE DDACHASFLR VSKMRLSVFL KKQEESQFHP
LEWLAREACN QDALQEAGTF RHTLWKRVQG AVTPLLASMI SFIDRDGNLE LLTRPDTPPW
ARDLWMFIFS DTMLLNIPLV MNNERHKGEM AYIVVQNHMN LSENASNNVP FSWKIKDYLE
ELWVQAQYIT DAEGLPKKFV DIFQQTPLGR FLAQLHGEPQ QELLQCYLKD FILLTMRVST
EEELKFLQMA LWSCTRKLKA ASEAPEEEVS LPWVHLAYQR FRSRLQNFSR ILTIYPQVLH
SLMEARWNHE LAGCEMTLDA FAAMACTEML TRNTLKPSPQ AWLQLVKNLS MPLELICSDE
HMQGSGSLAQ AVIREVRAQW SRIFSTALFV EHVLLGTESR VPELQGLVTE HVFLLDKCLR
ENSDVKTHGP FEAVMRTLCE CKETASKTLS RFGIQPCSIC LGDAKDPVCL PCDHVHCLRC
LRAWFASEQM ICPYCLTALP DEFSPAVSQA HREAIEKHAR FRQMCNSFFV DLVSTICFKD
NAPPEKEVIE SLLSLLFVQK GRLRDAAQRH CEHTKSLSPF NDVVDKTPVI RSVILKLLLK
YSFHDVKDYI QEYLTLLKKK AFITEDKTEL YMLFINCLED SILEKTSAYS RNDELNHLEE
EGRFLKAYSP ASRGREPANE ASVEYLQEVA RIRLCLDRAA DFLSEPEGGP EMAKEKQCYL
QQVKQFCIRV ENDWHRVYLV RKLSSQRGME FVQGLSKPGR PHQWVFPKDV VKQQGLRQDH
PGQMDRYLVY GDEYKALRDA VAKAVLECKP LGIKTALKAC KTPQSQQSAY FLLTLFREVA
ILYRSHNASL HPTPEQCEAV SKFIGECKIL SPPDISRFAT SLVDNSVPLL RAGPSDSNLD
GTVTEMAIHA AAVLLCGQNE LLEPLKNLAF SPATMAHAFL PTMPEDLLAQ ARRWKGLERV
HWYTCPNGHP CSVGECGRPM EQSICIDCHA PIGGIDHKPR DGFHLVKDKA DRTQTGHVLG
NPQRRDVVTC DRGLPPVVFL LIRLLTHLAL LLGASQSSQA LINIIKPPVR DPKGFLQQHI
LKDLEQLAKM LGHSADETIG VVHLVLRRLL QEQHQLSSRR LLNFDTELST KEMRNNWEKE
IAAVISPELE HLDKTLPTMN NLISQDKRIS SNPVAKIIYG DPVTFLPHLP RKSVVHCSKI
WSCRKRITVE YLQHIVEQKN GKERVPILWH FLQKEAELRL VKFLPEILAL QRDLVKQFQN
VQQVEYSSIR GFLSKHSSDG LRQLLHNRIT VFLSTWNKLR RSLETNGEIN LPKDYCSTDL
DLDTEFEILL PRRRGLGLCA TALVSYLIRL HNEIVYAVEK LSKENNSYSV DAAEVTELHV
ISYEVERDLT PLILSNCQYQ VEEGRETVQE FDLEKIQRQI VSRFLQGKPR LSLKGIPTLV
YRHDWNYEHL FMDIKNKMAQ DSLPSSVISA ISGQLQSYSD ACEVLSVVEV TLGFLSTAGG
DPNMQLNVYT QDILQMGDQT IHVLKALNRC QLKHTIALWQ FLSAHKSEQL LRLHKEPFGE
ISSRYKADLS PENAKLLSTF LNQTGLDAFL LELHEMIILK LKNPQTQTEE RFRPQWSLRD
TLVSYMQTKE SEILPEMASQ FPEEILLASC VSVWKTAAVL KWNREMR
