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E3 ubiquitin-protein ligase RNF213 (EC 2.3.2.27) (EC 3.6.4.-) (ALK lymphoma oligomerization partner on chromosome 17) (Mysterin) (RING finger protein 213) (RING-type E3 ubiquitin transferase RNF213)

 RN213_HUMAN             Reviewed;        5207 AA.
Q63HN8; C9JCP4; D6RI12; F8WKS1; Q658P6; Q69YK7; Q6MZR1; Q8IWF4;
Q8IZX1; Q8IZX2; Q8N406; Q8TEU0; Q9H6C9; Q9H6H9; Q9H6P3; Q9H8A9;
Q9HCF4; Q9HCL8;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 3.
22-NOV-2017, entry version 133.
RecName: Full=E3 ubiquitin-protein ligase RNF213 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:21799892};
EC=3.6.4.- {ECO:0000269|PubMed:21799892};
AltName: Full=ALK lymphoma oligomerization partner on chromosome 17 {ECO:0000303|PubMed:12112524};
AltName: Full=Mysterin {ECO:0000303|PubMed:26126547};
AltName: Full=RING finger protein 213 {ECO:0000305};
AltName: Full=RING-type E3 ubiquitin transferase RNF213 {ECO:0000305};
Name=RNF213 {ECO:0000312|HGNC:HGNC:14539};
Synonyms=ALO17 {ECO:0000303|PubMed:12112524},
C17orf27 {ECO:0000312|HGNC:HGNC:14539},
KIAA1554 {ECO:0000303|PubMed:10997877},
KIAA1618 {ECO:0000303|PubMed:10997877},
MYSTR {ECO:0000303|PubMed:26126547};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AUTOUBIQUITINATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS
ASP-3962; GLN-4062; SER-4608; ASN-4863; ASP-4950; VAL-5021; GLU-5160
AND GLY-5176, AND VARIANTS MYMY2 ASN-4013 AND LYS-4810.
PubMed=21799892; DOI=10.1371/journal.pone.0022542;
Liu W., Morito D., Takashima S., Mineharu Y., Kobayashi H., Hitomi T.,
Hashikata H., Matsuura N., Yamazaki S., Toyoda A., Kikuta K.,
Takagi Y., Harada K.H., Fujiyama A., Herzig R., Krischek B., Zou L.,
Kim J.E., Kitakaze M., Miyamoto S., Nagata K., Hashimoto N.,
Koizumi A.;
"Identification of RNF213 as a susceptibility gene for moyamoya
disease and its possible role in vascular development.";
PLoS ONE 6:E22542-E22542(2011).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 3021-5207 (ISOFORMS 1/2).
TISSUE=Endometrium, Lymph node, Melanoma, and Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-163 (ISOFORMS 1 AND 2/3), AND
CHROMOSOMAL TRANSLOCATION WITH ALK.
PubMed=12112524; DOI=10.1002/gcc.10033;
Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B.,
De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.;
"Identification of novel fusion partners of ALK, the anaplastic
lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory
myofibroblastic tumor.";
Genes Chromosomes Cancer 34:354-362(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-1509 AND 3888-5207
(ISOFORMS 1/2).
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3770-5207 (ISOFORMS 1/2).
TISSUE=Spleen, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
INTERACTION WITH M.TUBERCULOSIS RV3655C (MICROBIAL INFECTION), AND
INDUCTION (MICROBIAL INFECTION).
PubMed=20454556; DOI=10.1371/journal.pone.0010474;
Danelishvili L., Yamazaki Y., Selker J., Bermudez L.E.;
"Secreted Mycobacterium tuberculosis Rv3654c and Rv3655c proteins
participate in the suppression of macrophage apoptosis.";
PLoS ONE 5:E10474-E10474(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217 AND SER-1258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-1258 AND
SER-2273, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-217 AND
SER-1258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1151, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[20]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-2426; GLU-2488; LYS-2775 AND
GLU-2845.
PubMed=24658080; DOI=10.1038/srep04442;
Morito D., Nishikawa K., Hoseki J., Kitamura A., Kotani Y., Kiso K.,
Kinjo M., Fujiyoshi Y., Nagata K.;
"Moyamoya disease-associated protein mysterin/RNF213 is a novel AAA+
ATPase, which dynamically changes its oligomeric state.";
Sci. Rep. 4:4442-4442(2014).
[21]
INDUCTION.
PubMed=26070522; DOI=10.1016/j.jstrokecerebrovasdis.2015.01.041;
Zhao S., Gong Z., Zhang J., Xu X., Liu P., Guan W., Jing L., Peng T.,
Teng J., Jia Y.;
"Elevated serum microRNA Let-7c in Moyamoya disease.";
J. Stroke Cerebrovasc. Dis. 24:1709-1714(2015).
[22]
FUNCTION, AND INDUCTION.
PubMed=26278786; DOI=10.1038/srep13191;
Ohkubo K., Sakai Y., Inoue H., Akamine S., Ishizaki Y., Matsushita Y.,
Sanefuji M., Torisu H., Ihara K., Sardiello M., Hara T.;
"Moyamoya disease susceptibility gene RNF213 links inflammatory and
angiogenic signals in endothelial cells.";
Sci. Rep. 5:13191-13191(2015).
[23]
FUNCTION.
PubMed=26766444; DOI=10.1016/j.devcel.2015.12.015;
Scholz B., Korn C., Wojtarowicz J., Mogler C., Augustin I.,
Boutros M., Niehrs C., Augustin H.G.;
"Endothelial RSPO3 controls vascular stability and pruning through
non-canonical WNT/Ca(2+)/NFAT signaling.";
Dev. Cell 36:79-93(2016).
[24]
VARIANTS GLU-2554; VAL-3891; GLY-3915; MET-4567 AND MET-4765, AND
VARIANTS MYMY2 THR-4399 AND LYS-4810.
PubMed=21048783; DOI=10.1038/jhg.2010.132;
Kamada F., Aoki Y., Narisawa A., Abe Y., Komatsuzaki S., Kikuchi A.,
Kanno J., Niihori T., Ono M., Ishii N., Owada Y., Fujimura M.,
Mashimo Y., Suzuki Y., Hata A., Tsuchiya S., Tominaga T.,
Matsubara Y., Kure S.;
"A genome-wide association study identifies RNF213 as the first
Moyamoya disease gene.";
J. Hum. Genet. 56:34-40(2011).
[25]
VARIANTS MYMY2 THR-4399 AND LYS-4810, AND VARIANTS ARG-4007; LEU-4367;
PRO-4586; VAL-4631; ASP-4950; VAL-5021 AND ILE-5136.
PubMed=23110205; DOI=10.1371/journal.pone.0048179;
Wu Z., Jiang H., Zhang L., Xu X., Zhang X., Kang Z., Song D.,
Zhang J., Guan M., Gu Y.;
"Molecular analysis of RNF213 gene for moyamoya disease in the Chinese
Han population.";
PLoS ONE 7:E48179-E48179(2012).
[26]
CHARACTERIZATION OF VARIANT MYMY2 LYS-4810.
PubMed=23994138; DOI=10.1016/j.bbrc.2013.08.067;
Hitomi T., Habu T., Kobayashi H., Okuda H., Harada K.H., Osafune K.,
Taura D., Sone M., Asaka I., Ameku T., Watanabe A., Kasahara T.,
Sudo T., Shiota F., Hashikata H., Takagi Y., Morito D., Miyamoto S.,
Nakao K., Koizumi A.;
"The moyamoya disease susceptibility variant RNF213 R4810K
(rs112735431) induces genomic instability by mitotic abnormality.";
Biochem. Biophys. Res. Commun. 439:419-426(2013).
[27]
VARIANT THR-4185.
PubMed=25043520; DOI=10.1111/ijs.12306;
Smith K.R., Leventer R.J., Mackay M.T., Pope K., Gillies G.,
Delatycki M.B., Amor D.J., Bahlo M., Lockhart P.J.;
"Identification of a novel RNF213 variant in a family with
heterogeneous intracerebral vasculopathy.";
Int. J. Stroke 9:E26-E27(2014).
[28]
VARIANTS MYMY2 ASN-4013 AND LYS-4810, AND VARIANTS ALA-529 DEL;
GLN-3922; TYR-3997; CYS-4019; VAL-4076; LYS-4115 DEL; GLU-4237;
THR-4732 AND ILE-5163.
PubMed=25278557; DOI=10.1161/STROKEAHA.114.006244;
University of Washington Center for Mendelian Genomics;
Cecchi A.C., Guo D., Ren Z., Flynn K., Santos-Cortez R.L., Leal S.M.,
Wang G.T., Regalado E.S., Steinberg G.K., Shendure J., Bamshad M.J.,
Grotta J.C., Nickerson D.A., Pannu H., Milewicz D.M.;
"RNF213 rare variants in an ethnically diverse population with
Moyamoya disease.";
Stroke 45:3200-3207(2014).
[29]
VARIANT PHE-4118, AND INVOLVEMENT IN MYMY2.
PubMed=26198278; DOI=10.1002/ajmg.a.37230;
Harel T., Posey J.E., Graham B.H., Walkiewicz M., Yang Y.,
Lalani S.R., Belmont J.W.;
"Atypical presentation of moyamoya disease in an infant with a de novo
RNF213 variant.";
Am. J. Med. Genet. A 167A:2742-2747(2015).
[30]
CHARACTERIZATION OF VARIANT MYMY2 LYS-4810, FUNCTION, SUBUNIT, AND
MUTAGENESIS OF GLU-2488.
PubMed=26126547; DOI=10.1161/JAHA.115.002146;
Kobayashi H., Matsuda Y., Hitomi T., Okuda H., Shioi H., Matsuda T.,
Imai H., Sone M., Taura D., Harada K.H., Habu T., Takagi Y.,
Miyamoto S., Koizumi A.;
"Biochemical and functional characterization of RNF213 (Mysterin)
R4810K, a susceptibility mutation of Moyamoya disease, in angiogenesis
in vitro and in vivo.";
J. Am. Heart. Assoc. 4:0-0(2015).
[31]
VARIANTS VAL-1622; MET-3933 AND CYS-4131, AND VARIANT MYMY2 LYS-4810.
PubMed=25956231; DOI=10.1016/j.jns.2015.04.019;
Lee M.J., Chen Y.F., Fan P.C., Wang K.C., Wang K., Wang J., Kuo M.F.;
"Mutation genotypes of RNF213 gene from moyamoya patients in Taiwan.";
J. Neurol. Sci. 353:161-165(2015).
[32]
VARIANTS CYS-4019; LYS-4042; ALA-4146 AND LEU-4677, CHARACTERIZATION
OF VARIANT MYMY2 ASN-4013, AND CHARACTERIZATION OF VARIANTS CYS-4019
AND ALA-4146.
PubMed=27736983; DOI=10.1371/journal.pone.0164759;
Kobayashi H., Brozman M., Kyselova K., Viszlayova D., Morimoto T.,
Roubec M., Skoloudik D., Petrovicova A., Juskanic D., Strauss J.,
Halaj M., Kurray P., Hranai M., Harada K.H., Inoue S., Yoshida Y.,
Habu T., Herzig R., Youssefian S., Koizumi A.;
"RNF213 rare variants in Slovakian and Czech moyamoya disease
patients.";
PLoS ONE 11:E0164759-E0164759(2016).
-!- FUNCTION: E3 ubiquitin-protein ligase involved in angiogenesis
(PubMed:21799892, PubMed:26278786, PubMed:26766444,
PubMed:26126547). Involved in the non-canonical Wnt signaling
pathway in vascular development: acts by mediating ubiquitination
and degradation of FLNA and NFATC2 downstream of RSPO3, leading to
inhibit the non-canonical Wnt signaling pathway and promoting
vessel regression (PubMed:26766444). Also has ATPase activity
(PubMed:24658080, PubMed:26126547). {ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:26126547,
ECO:0000269|PubMed:26278786, ECO:0000269|PubMed:26766444}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:21799892}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000305|PubMed:21799892}.
-!- SUBUNIT: Homooligomer; probably forms homohexamers.
{ECO:0000269|PubMed:24658080, ECO:0000269|PubMed:26126547}.
-!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis
protein Rv3655c, which impairs caspase-8 activation and suppresses
macrophage apoptosis by blocking the extrinsic pathway.
{ECO:0000269|PubMed:20454556}.
-!- INTERACTION:
Q08379:GOLGA2; NbExp=3; IntAct=EBI-10248548, EBI-618309;
Q6A162:KRT40; NbExp=3; IntAct=EBI-10248548, EBI-10171697;
Q04864:REL; NbExp=3; IntAct=EBI-10248548, EBI-307352;
P36406:TRIM23; NbExp=3; IntAct=EBI-10248548, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-10248548, EBI-719493;
Q15654:TRIP6; NbExp=3; IntAct=EBI-10248548, EBI-742327;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-10248548, EBI-746004;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:21799892}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q63HN8-3; Sequence=Displayed;
Note=Major isoform detected in all tissues examined.;
Name=2;
IsoId=Q63HN8-4; Sequence=VSP_042417;
Note=Minor isoform with restricted expression. Gene prediction
based on partial EST data.;
Name=3;
IsoId=Q63HN8-5; Sequence=VSP_042418, VSP_042419;
Name=4;
IsoId=Q63HN8-6; Sequence=VSP_042416, VSP_042420;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed (at protein level).
{ECO:0000269|PubMed:21799892}.
-!- INDUCTION: Down-regulated by let-7c miRNA, which binds to the 3'-
UTR transcript of RNF213 (PubMed:26070522). Induced by pro-
inflammatory cytokines (PubMed:26278786).
{ECO:0000269|PubMed:26070522, ECO:0000269|PubMed:26278786}.
-!- INDUCTION: (Microbial infection) Is up-regulated in macrophages
infected by M.tuberculosis. {ECO:0000269|PubMed:20454556}.
-!- DOMAIN: The RING-type zinc finger domain is required for the
ubiquitin-protein ligase activity. {ECO:0000269|PubMed:21799892}.
-!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:21799892}.
-!- DISEASE: Moyamoya disease 2 (MYMY2) [MIM:607151]: A progressive
cerebral angiopathy characterized by bilateral intracranial
carotid artery stenosis and telangiectatic vessels in the region
of the basal ganglia. The abnormal vessels resemble a 'puff of
smoke' (moyamoya) on cerebral angiogram. Affected individuals can
develop transient ischemic attacks and/or cerebral infarction, and
rupture of the collateral vessels can cause intracranial
hemorrhage. Hemiplegia of sudden onset and epileptic seizures
constitute the prevailing presentation in childhood, while
subarachnoid bleeding occurs more frequently in adults.
{ECO:0000269|PubMed:21048783, ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:23110205, ECO:0000269|PubMed:23994138,
ECO:0000269|PubMed:25278557, ECO:0000269|PubMed:25956231,
ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26198278,
ECO:0000269|PubMed:27736983}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=A chromosomal aberration involving RNF213 is
associated with anaplastic large-cell lymphoma (ALCL).
Translocation t(2;17)(p23;q25) with ALK.
{ECO:0000269|PubMed:12112524}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH32220.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB13444.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=BAB14708.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15212.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15280.1; Type=Erroneous termination; Positions=4257; Note=Translated as Gln.; Evidence={ECO:0000305};
Sequence=BAB15330.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH10615.1; Type=Frameshift; Positions=211, 213, 221, 266; Evidence={ECO:0000305};
Sequence=CAH56189.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ALO17ID480.html";
-----------------------------------------------------------------------
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EMBL; AB537889; BAK53191.1; -; mRNA.
EMBL; AL832920; CAH10615.1; ALT_FRAME; mRNA.
EMBL; AL833201; CAH56308.1; -; mRNA.
EMBL; BX640932; CAE45967.1; -; mRNA.
EMBL; BX647946; CAH56189.1; ALT_INIT; mRNA.
EMBL; AC123764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032220; AAH32220.1; ALT_INIT; mRNA.
EMBL; BC036891; AAH36891.1; -; mRNA.
EMBL; BC040341; AAH40341.1; -; mRNA.
EMBL; AF397204; AAN63520.1; -; mRNA.
EMBL; AF397205; AAN63521.1; -; mRNA.
EMBL; AB046774; BAB13380.1; -; mRNA.
EMBL; AB046838; BAB13444.1; ALT_SEQ; mRNA.
EMBL; AK023871; BAB14708.1; ALT_INIT; mRNA.
EMBL; AK025676; BAB15212.1; ALT_INIT; mRNA.
EMBL; AK025914; BAB15280.1; ALT_SEQ; mRNA.
EMBL; AK026038; BAB15330.1; ALT_INIT; mRNA.
EMBL; AK074030; BAB84856.1; -; mRNA.
CCDS; CCDS11772.1; -. [Q63HN8-5]
CCDS; CCDS58606.1; -. [Q63HN8-3]
RefSeq; NP_001243000.2; NM_001256071.2.
RefSeq; NP_066005.2; NM_020954.3. [Q63HN8-5]
UniGene; Hs.195642; -.
UniGene; Hs.740662; -.
UniGene; Hs.745415; -.
ProteinModelPortal; Q63HN8; -.
BioGrid; 121705; 36.
IntAct; Q63HN8; 16.
STRING; 9606.ENSP00000324392; -.
iPTMnet; Q63HN8; -.
PhosphoSitePlus; Q63HN8; -.
BioMuta; RNF213; -.
DMDM; 380865458; -.
EPD; Q63HN8; -.
MaxQB; Q63HN8; -.
PaxDb; Q63HN8; -.
PeptideAtlas; Q63HN8; -.
PRIDE; Q63HN8; -.
DNASU; 57674; -.
Ensembl; ENST00000319921; ENSP00000324392; ENSG00000173821. [Q63HN8-5]
GeneID; 57674; -.
KEGG; hsa:57674; -.
UCSC; uc002jyf.5; human. [Q63HN8-3]
CTD; 57674; -.
DisGeNET; 57674; -.
EuPathDB; HostDB:ENSG00000173821.19; -.
GeneCards; RNF213; -.
H-InvDB; HIX0014240; -.
HGNC; HGNC:14539; RNF213.
HPA; HPA003347; -.
HPA; HPA026790; -.
MalaCards; RNF213; -.
MIM; 607151; phenotype.
MIM; 613768; gene.
neXtProt; NX_Q63HN8; -.
OpenTargets; ENSG00000173821; -.
Orphanet; 2573; Moyamoya disease.
PharmGKB; PA134898812; -.
PharmGKB; PA162401681; -.
eggNOG; ENOG410IE7S; Eukaryota.
eggNOG; ENOG410Z1EV; LUCA.
GeneTree; ENSGT00630000089884; -.
HOGENOM; HOG000185147; -.
HOVERGEN; HBG073493; -.
InParanoid; Q63HN8; -.
TreeFam; TF343131; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; RNF213; human.
GeneWiki; RNF213; -.
GenomeRNAi; 57674; -.
PMAP-CutDB; Q9HCF4; -.
PRO; PR:Q63HN8; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000173821; -.
CleanEx; HS_KIAA1618; -.
ExpressionAtlas; Q63HN8; baseline and differential.
Genevisible; Q63HN8; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR031248; RNF213.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR22605; PTHR22605; 1.
Pfam; PF00097; zf-C3HC4; 1.
SMART; SM00382; AAA; 2.
SMART; SM00184; RING; 1.
SUPFAM; SSF52540; SSF52540; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Chromosomal rearrangement;
Coiled coil; Complete proteome; Cytoplasm; Disease mutation;
Hydrolase; Isopeptide bond; Metal-binding; Phosphoprotein;
Proto-oncogene; Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 5207 E3 ubiquitin-protein ligase RNF213.
/FTId=PRO_0000415917.
ZN_FING 3997 4036 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 343 374 {ECO:0000255}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2273 2273 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 1151 1151 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 1 4650 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042416.
VAR_SEQ 87 87 E -> EGATSEVLVDAAVDLISDEWEAANAIPSKRRKQDAA
PLEAASVPSADCEQ (in isoform 2).
{ECO:0000305}.
/FTId=VSP_042417.
VAR_SEQ 1009 1063 SQTSILQGFSYSDLRKFGIVLSAVITKSWPRTADNFNDILK
HLLTLADVKHVFRL -> VNNLSSWETDSGSQLCSAMTQLR
AMKHPLGLSSSANSEIGKWAPSSLAKGNGAEI (in
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_042418.
VAR_SEQ 1064 5207 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_042419.
VAR_SEQ 4651 4660 QEQHQLSSRR -> MTRKSAPTSG (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042420.
VARIANT 529 529 Missing (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075635.
VARIANT 1622 1622 A -> V (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:25956231}.
/FTId=VAR_075636.
VARIANT 2554 2554 D -> E (in dbSNP:rs138516230).
{ECO:0000269|PubMed:21048783}.
/FTId=VAR_067020.
VARIANT 3891 3891 M -> V (rare variant detected in a
sporadic case of Moyamoya disease).
{ECO:0000269|PubMed:21048783}.
/FTId=VAR_067021.
VARIANT 3915 3915 E -> G (in dbSNP:rs61740658).
{ECO:0000269|PubMed:21048783}.
/FTId=VAR_067022.
VARIANT 3922 3922 R -> Q (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075637.
VARIANT 3933 3933 V -> M (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:25956231}.
/FTId=VAR_075638.
VARIANT 3962 3962 N -> D (variant detected in cases of
Moyamoya disease in Caucasian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067023.
VARIANT 3997 3997 C -> Y (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075639.
VARIANT 4007 4007 P -> R (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:23110205}.
/FTId=VAR_075640.
VARIANT 4013 4013 D -> N (in MYMY2; variant detected in
cases of Moyamoya disease in Caucasian
and Asian populations; inhibitory effect
on angiogenic activity of vascular
endothelial cells).
{ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:25278557,
ECO:0000269|PubMed:27736983}.
/FTId=VAR_067024.
VARIANT 4019 4019 R -> C (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population; associated with K-
4042 in cases of Moyamoya disease in
Slovakian and Czech populations;
inhibitory effect on angiogenic activity
of vascular endothelial cells).
{ECO:0000269|PubMed:25278557,
ECO:0000269|PubMed:27736983}.
/FTId=VAR_075641.
VARIANT 4042 4042 E -> K (rare variant associated with C-
4019 in cases of Moyamoya disease in
Slovakian and Czech populations).
{ECO:0000269|PubMed:27736983}.
/FTId=VAR_079573.
VARIANT 4062 4062 R -> Q (variant detected in cases of
Moyamoya disease in Caucasian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067025.
VARIANT 4076 4076 I -> V (rare variant detected in a
sporadic case of Moyamoya disease in
Asian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075642.
VARIANT 4115 4115 Missing (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075643.
VARIANT 4118 4118 S -> F (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:26198278}.
/FTId=VAR_075644.
VARIANT 4131 4131 R -> C (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:25956231}.
/FTId=VAR_075645.
VARIANT 4146 4146 V -> A (rare variant detected in cases of
Moyamoya disease in Slovakian and Czech
populations; inhibitory effect on
angiogenic activity of vascular
endothelial cells).
{ECO:0000269|PubMed:27736983}.
/FTId=VAR_079574.
VARIANT 4185 4185 K -> T (found in a heterozygous family
with heterogeneous intracerebral
vasculopathy).
{ECO:0000269|PubMed:25043520}.
/FTId=VAR_075646.
VARIANT 4237 4237 D -> E (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075647.
VARIANT 4367 4367 Q -> L (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:23110205}.
/FTId=VAR_075648.
VARIANT 4399 4399 A -> T (in MYMY2; dbSNP:rs148731719).
{ECO:0000269|PubMed:21048783,
ECO:0000269|PubMed:23110205}.
/FTId=VAR_067026.
VARIANT 4567 4567 V -> M (rare variant detected in a
sporadic case of Moyamoya disease;
dbSNP:rs145282452).
{ECO:0000269|PubMed:21048783}.
/FTId=VAR_067027.
VARIANT 4586 4586 T -> P (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:23110205}.
/FTId=VAR_075649.
VARIANT 4608 4608 P -> S (variant detected in cases of
Moyamoya disease in Caucasian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067028.
VARIANT 4631 4631 L -> V (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:23110205}.
/FTId=VAR_075650.
VARIANT 4677 4677 W -> L (rare polymorphism).
{ECO:0000269|PubMed:27736983}.
/FTId=VAR_079575.
VARIANT 4732 4732 K -> T (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075651.
VARIANT 4765 4765 V -> M (rare variant detected in a
sporadic case of Moyamoya disease).
{ECO:0000269|PubMed:21048783}.
/FTId=VAR_067029.
VARIANT 4810 4810 R -> K (in MYMY2; very frequent in
individuals affected by Moyamoya disease;
strongly increases the risk of Moyamoya
disease; induces genomic instability;
shows decreased ATPase activity, possibly
caused by stabilization of the oligomeric
state). {ECO:0000269|PubMed:21048783,
ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:23110205,
ECO:0000269|PubMed:23994138,
ECO:0000269|PubMed:25278557,
ECO:0000269|PubMed:25956231,
ECO:0000269|PubMed:26126547}.
/FTId=VAR_067030.
VARIANT 4863 4863 D -> N (variant detected in cases of
Moyamoya disease in East Asian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067031.
VARIANT 4950 4950 E -> D (variant detected in cases of
Moyamoya disease in East Asian
populations and rare variant detected in
a sporadic case of Moyamoya disease).
{ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:23110205}.
/FTId=VAR_067032.
VARIANT 5021 5021 A -> V (variant detected in cases of
Moyamoya disease in East Asian
populations and rare variant detected in
a sporadic case of Moyamoya disease;
dbSNP:rs138130613).
{ECO:0000269|PubMed:21799892,
ECO:0000269|PubMed:23110205}.
/FTId=VAR_067033.
VARIANT 5136 5136 M -> I (rare variant detected in a
sporadic case of Moyamoya disease in East
Asian population).
{ECO:0000269|PubMed:23110205}.
/FTId=VAR_075652.
VARIANT 5160 5160 D -> E (variant detected in cases of
Moyamoya disease in East Asian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067034.
VARIANT 5163 5163 V -> I (rare variant detected in a
sporadic case of Moyamoya disease in
Caucasian population).
{ECO:0000269|PubMed:25278557}.
/FTId=VAR_075653.
VARIANT 5176 5176 E -> G (variant detected in cases of
Moyamoya disease in East Asian
populations).
{ECO:0000269|PubMed:21799892}.
/FTId=VAR_067035.
MUTAGEN 2426 2426 K->A: Decreased ATPase activity.
{ECO:0000269|PubMed:24658080}.
MUTAGEN 2488 2488 E->A: Decreased ATPase activity.
{ECO:0000269|PubMed:24658080}.
MUTAGEN 2488 2488 E->Q: Loss of ATPase hydrolysis.
Stabilization of the oligomeric state.
Inhibited angiogenesis.
{ECO:0000269|PubMed:26126547}.
MUTAGEN 2775 2775 K->A: Decreased ATPase activity.
{ECO:0000269|PubMed:24658080}.
MUTAGEN 2845 2845 E->A: Decreased ATPase activity.
{ECO:0000269|PubMed:24658080}.
CONFLICT 270 270 M -> T (in Ref. 4; AAH36891/AAH40341).
{ECO:0000305}.
CONFLICT 321 321 M -> T (in Ref. 4; AAH36891/AAH40341).
{ECO:0000305}.
CONFLICT 369 369 K -> N (in Ref. 4; AAH36891).
{ECO:0000305}.
CONFLICT 1045 1045 N -> D (in Ref. 1; BAK53191 and 6;
BAB13444). {ECO:0000305}.
CONFLICT 1133 1133 Q -> K (in Ref. 6; BAB13444).
{ECO:0000305}.
CONFLICT 1195 1195 V -> M (in Ref. 6; BAB13444).
{ECO:0000305}.
CONFLICT 1272 1272 E -> Q (in Ref. 6; BAB13444).
{ECO:0000305}.
CONFLICT 1331 1331 D -> G (in Ref. 6; BAB13444).
{ECO:0000305}.
CONFLICT 3323 3323 R -> G (in Ref. 2; CAH56189).
{ECO:0000305}.
CONFLICT 4220 4220 E -> G (in Ref. 7; BAB15212).
{ECO:0000305}.
CONFLICT 4571 4571 D -> G (in Ref. 7; BAB15280).
{ECO:0000305}.
CONFLICT 4853 4853 K -> R (in Ref. 7; BAB15212).
{ECO:0000305}.
CONFLICT 4892 4892 N -> S (in Ref. 7; BAB15212).
{ECO:0000305}.
CONFLICT 5139 5139 L -> S (in Ref. 7; BAB15280).
{ECO:0000305}.
CONFLICT 5187 5187 L -> P (in Ref. 7; BAB15330).
{ECO:0000305}.
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


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EIAAB07154 Checkpoint with forkhead and RING finger domains protein,CHFR,E3 ubiquitin-protein ligase CHFR,Homo sapiens,Human,RING finger protein 196,RNF196
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