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Cullin-3 (CUL-3)

 CUL3_HUMAN              Reviewed;         768 AA.
Q13618; A8K536; B8ZZC3; O75415; Q569L3; Q9UBI8; Q9UET7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
27-SEP-2017, entry version 180.
RecName: Full=Cullin-3;
Short=CUL-3;
Name=CUL3; Synonyms=KIAA0617;
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).
PubMed=9733711; DOI=10.1074/jbc.273.38.24289;
Du M., Sansores-Garcia L., Zu Z., Wu K.K.;
"Cloning and expression analysis of a novel salicylate suppressible
gene, Hs-CUL-3, a member of cullin/Cdc53 family.";
J. Biol. Chem. 273:24289-24292(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon carcinoma;
PubMed=9663463;
Michel J.J., Xiong Y.;
"Human CUL-1, but not other cullin family members, selectively
interacts with SKP1 to form a complex with SKP2 and cyclin A.";
Cell Growth Differ. 9:435-449(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
Xu M., Huang X.Y., Yin L.L., Xu Z.Y., Lu L., Zhou Z.M., Sha J.H.;
"Cloning and characterization of a new isoform of CUL3 gene in
testis.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary, Skin, and Uterus;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 192-768.
PubMed=8681378; DOI=10.1016/S0092-8674(00)81267-2;
Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.;
"cul-1 is required for cell cycle exit in C. elegans and identifies a
novel gene family.";
Cell 85:829-839(1996).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 398-768.
TISSUE=Brain;
Yu W., Sarginson J., Gibbs R.A.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[11]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH CYCE, AND NEDDYLATION.
PubMed=10500095; DOI=10.1101/gad.13.18.2375;
Singer J.D., Gurian-West M., Clurman B., Roberts J.M.;
"Cullin-3 targets cyclin E for ubiquitination and controls S phase in
mammalian cells.";
Genes Dev. 13:2375-2387(1999).
[12]
FUNCTION.
PubMed=11311237; DOI=10.1016/S0014-5793(01)02343-2;
Maeda I., Ohta T., Koizumi H., Fukuda M.;
"In vitro ubiquitination of cyclin D1 by ROC1-CUL1 and ROC1-CUL3.";
FEBS Lett. 494:181-185(2001).
[13]
NEDDYLATION.
PubMed=10597293; DOI=10.1038/sj.onc.1203093;
Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
Kato S., Tanaka K.;
"Covalent modification of all members of human cullin family proteins
by NEDD8.";
Oncogene 18:6829-6834(1999).
[14]
INTERACTION WITH RBX1 AND RNF7.
PubMed=10230407; DOI=10.1016/S1097-2765(00)80482-7;
Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
"ROC1, a homolog of APC11, represents a family of cullin partners with
an associated ubiquitin ligase activity.";
Mol. Cell 3:535-541(1999).
[15]
INTERACTION WITH TIP120A.
PubMed=12609982; DOI=10.1074/jbc.M213070200;
Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
"TIP120A associates with cullins and modulates ubiquitin ligase
activity.";
J. Biol. Chem. 278:15905-15910(2003).
[16]
INTERACTION WITH GAN; ZBTB16; KLHL9; KLHL13; KLHL21; KLHL3; KLHL15;
KLHL20; KLHL36; GMCL1P1; BTBD1 AND SPOP.
PubMed=14528312; DOI=10.1038/ncb1056;
Furukawa M., He Y.J., Borchers C., Xiong Y.;
"Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
ligases.";
Nat. Cell Biol. 5:1001-1007(2003).
[17]
FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN
THE BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, AND
IDENTIFICATION IN THE BCR(GAN) COMPLEX.
PubMed=15983046; DOI=10.1074/jbc.M501279200;
Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
Cul3, targets Keap1 for degradation by a proteasome-independent
pathway.";
J. Biol. Chem. 280:30091-30099(2005).
[18]
IDENTIFICATION IN A COMPLEX WITH SPOP AND BMI1, IDENTIFICATION IN A
COMPLEX WITH SPOP AND H2AFY, AND FUNCTION.
PubMed=15897469; DOI=10.1073/pnas.0408918102;
Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E.,
Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y.,
van Lohuizen M.;
"Stable X chromosome inactivation involves the PRC1 Polycomb complex
and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3
ligase.";
Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005).
[19]
IDENTIFICATION IN THE BCR(SPOP) COMPLEX, INTERACTION WITH SPOP, AND
FUNCTION IN UBIQUITINATION OF DAXX.
PubMed=16524876; DOI=10.1074/jbc.M600204200;
Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H.,
Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.;
"BTB domain-containing speckle-type POZ protein (SPOP) serves as an
adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.";
J. Biol. Chem. 281:12664-12672(2006).
[20]
FUNCTION, AND INTERACTION WITH KLHL9 AND KLHL13.
PubMed=17543862; DOI=10.1016/j.devcel.2007.03.019;
Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R.,
Peter M.;
"A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
regulating mitotic progression and completion of cytokinesis in human
cells.";
Dev. Cell 12:887-900(2007).
[21]
SELF-ASSOCIATION.
PubMed=17254749; DOI=10.1016/j.cellsig.2006.12.002;
Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.;
"Characterization of cullin-based E3 ubiquitin ligases in intact
mammalian cells -- evidence for cullin dimerization.";
Cell. Signal. 19:1071-1080(2007).
[22]
BCR COMPLEX HOMODIMERIZATION.
PubMed=17192413; DOI=10.1091/mbc.E06-06-0542;
Wimuttisuk W., Singer J.D.;
"The Cullin3 ubiquitin ligase functions as a Nedd8-bound
heterodimer.";
Mol. Biol. Cell 18:899-909(2007).
[23]
INTERACTION WITH KCTD5.
PubMed=18573101; DOI=10.1111/j.1742-4658.2008.06537.x;
Bayon Y., Trinidad A.G., de la Puerta M.L., Del Carmen Rodriguez M.,
Bogetz J., Rojas A., De Pereda J.M., Rahmouni S., Williams S.,
Matsuzawa S., Reed J.C., Crespo M.S., Mustelin T., Alonso A.;
"KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases.";
FEBS J. 275:3900-3910(2008).
[24]
FUNCTION, AND INTERACTION WITH ATF2 AND KAT5.
PubMed=18397884; DOI=10.1074/jbc.M802030200;
Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
"Regulation of TIP60 by ATF2 modulates ATM activation.";
J. Biol. Chem. 283:17605-17614(2008).
[25]
IDENTIFICATION IN THE BCR(KLHL42) COMPLEX, FUNCTION IN UBIQUITINATION
OF KATNA1, AND INTERACTION WITH KATNA1 AND KLHL42.
PubMed=19261606; DOI=10.1074/jbc.M809374200;
Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.;
"The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for
normal mitosis in mammalian cells.";
J. Biol. Chem. 284:11663-11675(2009).
[26]
IDENTIFICATION IN THE BCR(KLHL21) COMPLEX, AND FUNCTION.
PubMed=19995937; DOI=10.1083/jcb.200906117;
Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W.,
Quadroni M., Sumara I., Peter M.;
"The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
microtubules in anaphase and is required for cytokinesis.";
J. Cell Biol. 187:791-800(2009).
[27]
FUNCTION, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN
LIGASE COMPLEX.
PubMed=20389280; DOI=10.1038/emboj.2010.62;
Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.;
"The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to
control interferon responses.";
EMBO J. 29:1748-1761(2010).
[28]
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).
[29]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH
SPOP AND BRMS1.
PubMed=22085717; DOI=10.1016/j.bbrc.2011.10.154;
Kim B., Nam H.J., Pyo K.E., Jang M.J., Kim I.S., Kim D., Boo K.,
Lee S.H., Yoon J.B., Baek S.H., Kim J.H.;
"Breast cancer metastasis suppressor 1 (BRMS1) is destabilized by the
Cul3-SPOP E3 ubiquitin ligase complex.";
Biochem. Biophys. Res. Commun. 415:720-726(2011).
[30]
FUNCTION, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN
LIGASE COMPLEX.
PubMed=21840486; DOI=10.1016/j.ccr.2011.07.008;
Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C.,
Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H.,
Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.;
"A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to
potentiate HIF-1 signaling and prostate cancer progression.";
Cancer Cell 20:214-228(2011).
[31]
FUNCTION, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN
LIGASE COMPLEX.
PubMed=21670212; DOI=10.1083/jcb.201103015;
Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.;
"PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-
induced neurite outgrowth.";
J. Cell Biol. 193:985-994(2011).
[32]
INTERACTION WITH KCTD7.
PubMed=22748208; DOI=10.1016/j.ajhg.2012.05.023;
Staropoli J.F., Karaa A., Lim E.T., Kirby A., Elbalalesy N.,
Romansky S.G., Leydiker K.B., Coppel S.H., Barone R., Xin W.,
MacDonald M.E., Abdenur J.E., Daly M.J., Sims K.B., Cotman S.L.;
"A homozygous mutation in KCTD7 links neuronal ceroid lipofuscinosis
to the ubiquitin-proteasome system.";
Am. J. Hum. Genet. 91:202-208(2012).
[33]
INTERACTION WITH PPP2R5B.
PubMed=23135275; DOI=10.1074/jbc.M112.420281;
Oberg E.A., Nifoussi S.K., Gingras A.C., Strack S.;
"Selective proteasomal degradation of the B'beta subunit of protein
phosphatase 2A by the E3 ubiquitin ligase adaptor Kelch-like 15.";
J. Biol. Chem. 287:43378-43389(2012).
[34]
IDENTIFICATION IN THE BCR(KLHL25) COMPLEX, AND FUNCTION.
PubMed=22578813; DOI=10.1016/j.molcel.2012.04.004;
Yanagiya A., Suyama E., Adachi H., Svitkin Y.V., Aza-Blanc P.,
Imataka H., Mikami S., Martineau Y., Ronai Z.A., Sonenberg N.;
"Translational homeostasis via the mRNA cap-binding protein, eIF4E.";
Mol. Cell 46:847-858(2012).
[35]
IDENTIFICATION IN THE BCR(KLHL12) COMPLEX, AND FUNCTION.
PubMed=22358839; DOI=10.1038/nature10822;
Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C.,
Schekman R., Rape M.;
"Ubiquitin-dependent regulation of COPII coat size and function.";
Nature 482:495-500(2012).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[37]
FUNCTION, AND INTERACTION WITH KLHL3.
PubMed=23387299; DOI=10.1042/BJ20121903;
Ohta A., Schumacher F.R., Mehellou Y., Johnson C., Knebel A.,
Macartney T.J., Wood N.T., Alessi D.R., Kurz T.;
"The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension
syndrome interacts with and ubiquitylates WNK isoforms: disease-
causing mutations in KLHL3 and WNK4 disrupt interaction.";
Biochem. J. 451:111-122(2013).
[38]
FUNCTION, AND IDENTIFICATION IN THE BCR(KLHL3) COMPLEX.
PubMed=23453970; DOI=10.1016/j.celrep.2013.02.024;
Wakabayashi M., Mori T., Isobe K., Sohara E., Susa K., Araki Y.,
Chiga M., Kikuchi E., Nomura N., Mori Y., Matsuo H., Murata T.,
Nomura S., Asano T., Kawaguchi H., Nonoyama S., Rai T., Sasaki S.,
Uchida S.;
"Impaired KLHL3-mediated ubiquitination of WNK4 causes human
hypertension.";
Cell Rep. 3:858-868(2013).
[39]
INTERACTION WITH ARIH1, AND NEDDYLATION.
PubMed=24076655; DOI=10.1038/emboj.2013.209;
Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A.,
Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.;
"TRIAD1 and HHARI bind to and are activated by distinct neddylated
Cullin-RING ligase complexes.";
EMBO J. 32:2848-2860(2013).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[41]
IDENTIFICATION IN THE BCR(KLHL22) COMPLEX, AND FUNCTION.
PubMed=23455478; DOI=10.1038/ncb2695;
Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H.,
Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.;
"Ubiquitylation-dependent localization of PLK1 in mitosis.";
Nat. Cell Biol. 15:430-439(2013).
[42]
INTERACTION WITH COPS9.
PubMed=23776465; DOI=10.1371/journal.pone.0065285;
Ebina M., Tsuruta F., Katoh M.C., Kigoshi Y., Someya A., Chiba T.;
"Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear
localization through Nedd8 modification.";
PLoS ONE 8:E65285-E65285(2013).
[43]
FUNCTION, AND IDENTIFICATION IN THE BCR(KLHL3) COMPLEX.
PubMed=23576762; DOI=10.1073/pnas.1304592110;
Shibata S., Zhang J., Puthumana J., Stone K.L., Lifton R.P.;
"Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via
ubiquitination and degradation of WNK4.";
Proc. Natl. Acad. Sci. U.S.A. 110:7838-7843(2013).
[44]
INTERACTION WITH DCUN1D3.
PubMed=25349211; DOI=10.1074/jbc.M114.585505;
Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S.,
Buss E., Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
"SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity
of SCCRO (DCUN1D1).";
J. Biol. Chem. 289:34728-34742(2014).
[45]
FUNCTION, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN
LIGASE COMPLEX.
PubMed=24768539; DOI=10.1016/j.molcel.2014.03.035;
Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C.,
Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.;
"K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin
E3 ligase regulates protein trafficking.";
Mol. Cell 54:586-600(2014).
[46]
INTERACTION WITH KCTD17, IDENTIFICATION IN THE BCR(KCTD17) E3
UBIQUITIN LIGASE COMPLEX, AND FUNCTION.
PubMed=25270598; DOI=10.1038/ncomms6081;
Kasahara K., Kawakami Y., Kiyono T., Yonemura S., Kawamura Y., Era S.,
Matsuzaki F., Goshima N., Inagaki M.;
"Ubiquitin-proteasome system controls ciliogenesis at the initial step
of axoneme extension.";
Nat. Commun. 5:5081-5081(2014).
[47]
FUNCTION, AND INTERACTION WITH KBTBD8.
PubMed=26399832; DOI=10.1038/nature14978;
Werner A., Iwasaki S., McGourty C.A., Medina-Ruiz S., Teerikorpi N.,
Fedrigo I., Ingolia N.T., Rape M.;
"Cell-fate determination by ubiquitin-dependent regulation of
translation.";
Nature 525:523-527(2015).
[48]
FUNCTION.
PubMed=27716508; DOI=10.1016/j.cell.2016.09.026;
McGourty C.A., Akopian D., Walsh C., Gorur A., Werner A., Schekman R.,
Bautista D., Rape M.;
"Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-
adaptor.";
Cell 167:525-538(2016).
[49]
FUNCTION, INTERACTION WITH ARIH1, AND NEDDYLATION.
PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L.,
Paulo J.A., de Jong A., Ovaa H., Alpi A.F., Harper J.W.,
Schulman B.A.;
"Two distinct types of E3 ligases work in unison to regulate substrate
ubiquitylation.";
Cell 166:1198-1214(2016).
[50]
INTERACTION WITH KLHL15 AND RBBP8, AND NEDDYLATION.
PubMed=27561354; DOI=10.1038/ncomms12628;
Ferretti L.P., Himmels S.F., Trenner A., Walker C., von Aesch C.,
Eggenschwiler A., Murina O., Enchev R.I., Peter M., Freire R.,
Porro A., Sartori A.A.;
"Cullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to
fine-tune DNA-end resection.";
Nat. Commun. 7:12628-12628(2016).
[51]
FUNCTION, IDENTIFICATION IN THE BCR(KLHL24) COMPLEX, AND INTERACTION
WITH KLHL24.
PubMed=27798626; DOI=10.1038/ng.3701;
Lin Z., Li S., Feng C., Yang S., Wang H., Ma D., Zhang J., Gou M.,
Bu D., Zhang T., Kong X., Wang X., Sarig O., Ren Y., Dai L., Liu H.,
Zhang J., Li F., Hu Y., Padalon-Brauch G., Vodo D., Zhou F., Chen T.,
Deng H., Sprecher E., Yang Y., Tan X.;
"Stabilizing mutations of KLHL24 ubiquitin ligase cause loss of
keratin 14 and human skin fragility.";
Nat. Genet. 48:1508-1516(2016).
[52]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-381 IN COMPLEX WITH SPOP,
FUNCTION, IDENTIFICATION IN UBIQUITIN LIGASE COMPLEXES WITH SPOP AND
SPOPL, AND SUBUNIT.
PubMed=22632832; DOI=10.1016/j.str.2012.04.009;
Errington W.J., Khan M.Q., Bueler S.A., Rubinstein J.L.,
Chakrabartty A., Prive G.G.;
"Adaptor protein self-assembly drives the control of a cullin-RING
ubiquitin ligase.";
Structure 20:1141-1153(2012).
[53]
X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 20-381 IN COMPLEX WITH
KLHL3.
PubMed=23573258; DOI=10.1371/journal.pone.0060445;
Ji A.X., Prive G.G.;
"Crystal structure of KLHL3 in complex with Cullin3.";
PLoS ONE 8:E60445-E60445(2013).
[54]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-388 IN COMPLEX WITH KLHL11,
AND INTERACTION WITH KLHL11.
PubMed=23349464; DOI=10.1074/jbc.M112.437996;
Canning P., Cooper C.D., Krojer T., Murray J.W., Pike A.C.,
Chaikuad A., Keates T., Thangaratnarajah C., Hojzan V., Marsden B.D.,
Gileadi O., Knapp S., von Delft F., Bullock A.N.;
"Structural basis for Cul3 assembly with the BTB-Kelch family of E3
ubiquitin ligases.";
J. Biol. Chem. 288:7803-7814(2013).
[55]
VARIANTS PHA2E GLY-413 AND ARG-459.
PubMed=22266938; DOI=10.1038/nature10814;
Boyden L.M., Choi M., Choate K.A., Nelson-Williams C.J., Farhi A.,
Toka H.R., Tikhonova I.R., Bjornson R., Mane S.M., Colussi G.,
Lebel M., Gordon R.D., Semmekrot B.A., Poujol A., Valimaki M.J.,
De Ferrari M.E., Sanjad S.A., Gutkin M., Karet F.E., Tucci J.R.,
Stockigt J.R., Keppler-Noreuil K.M., Porter C.C., Anand S.K.,
Whiteford M.L., Davis I.D., Dewar S.B., Bettinelli A., Fadrowski J.J.,
Belsha C.W., Hunley T.E., Nelson R.D., Trachtman H., Cole T.R.,
Pinsk M., Bockenhauer D., Shenoy M., Vaidyanathan P., Foreman J.W.,
Rasoulpour M., Thameem F., Al-Shahrouri H.Z., Radhakrishnan J.,
Gharavi A.G., Goilav B., Lifton R.P.;
"Mutations in kelch-like 3 and cullin 3 cause hypertension and
electrolyte abnormalities.";
Nature 482:98-102(2012).
[56]
VARIANT ARG-719.
PubMed=25969726; DOI=10.1186/s13229-015-0017-0;
Codina-Sola M., Rodriguez-Santiago B., Homs A., Santoyo J., Rigau M.,
Aznar-Lain G., Del Campo M., Gener B., Gabau E., Botella M.P.,
Gutierrez-Arumi A., Antinolo G., Perez-Jurado L.A., Cusco I.;
"Integrated analysis of whole-exome sequencing and transcriptome
profiling in males with autism spectrum disorders.";
Mol. Autism 6:21-21(2015).
-!- FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-
CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the
ubiquitination and subsequent proteasomal degradation of target
proteins. BCR complexes and ARIH1 collaborate in tandem to mediate
ubiquitination of target proteins (PubMed:27565346). As a scaffold
protein may contribute to catalysis through positioning of the
substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-
protein ligase activity of the complex is dependent on the
neddylation of the cullin subunit and is inhibited by the
association of the deneddylated cullin subunit with TIP120A/CAND1.
The functional specificity of the BCR complex depends on the BTB
domain-containing protein as the substrate recognition component.
BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is
involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX,
GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-
RBX1) E3 ubiquitin-protein ligase complex containing homodimeric
SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes
have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls
the dynamic behavior of AURKB on mitotic chromosomes and thereby
coordinates faithful mitotic progression and completion of
cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by
regulating the size of COPII coats, thereby playing a key role in
collagen export, which is required for embryonic stem (ES) cells
division: BCR(KLHL12) acts by mediating monoubiquitination of
SEC31 (SEC31A or SEC31B) (PubMed:22358839, PubMed:27716508).
BCR(KLHL3) acts as a regulator of ion transport in the distal
nephron; by mediating ubiquitination of WNK4 (PubMed:23387299,
PubMed:23453970, PubMed:23576762). The BCR(KLHL20) E3 ubiquitin
ligase complex is involved in interferon response and anterograde
Golgi to endosome transport: it mediates both ubiquitination
leading to degradation and 'Lys-33'-linked ubiquitination
(PubMed:20389280, PubMed:21840486, PubMed:21670212,
PubMed:24768539). The BCR(KLHL21) E3 ubiquitin ligase complex
regulates localization of the chromosomal passenger complex (CPC)
from chromosomes to the spindle midzone in anaphase and mediates
the ubiquitination of AURKB (PubMed:19995937). The BCR(KLHL22)
ubiquitin ligase complex mediates monoubiquitination of PLK1,
leading to PLK1 dissociation from phosphoreceptor proteins and
subsequent removal from kinetochores, allowing silencing of the
spindle assembly checkpoint (SAC) and chromosome segregation
(PubMed:23455478). The BCR(KLHL25) ubiquitin ligase complex is
involved in translational homeostasis by mediating ubiquitination
and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1)
(PubMed:22578813). The BCR(KBTBD8) complex acts by mediating
monoubiquitination of NOLC1 and TCOF1, leading to remodel the
translational program of differentiating cells in favor of neural
crest specification (PubMed:26399832). Involved in ubiquitination
of cyclin E and of cyclin D1 (in vitro) thus involved in
regulation of G1/S transition. Involved in the ubiquitination of
KEAP1, ENC1 and KLHL41. In concert with ATF2 and RBX1, promotes
degradation of KAT5 thereby attenuating its ability to acetylate
and activate ATM. The BCR(KCTD17) E3 ubiquitin ligase complex
mediates ubiquitination and degradation of TCHP, a down-regulator
of cilium assembly, thereby inducing ciliogenesis
(PubMed:25270598). The BCR(KLHL24) E3 ubiquitin ligase complex
mediates ubiquitination of KRT14, controls KRT14 levels during
keratinocytes differentiation, and is essential for skin integrity
(PubMed:27798626). {ECO:0000269|PubMed:10500095,
ECO:0000269|PubMed:11311237, ECO:0000269|PubMed:15897469,
ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16524876,
ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:18397884,
ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19995937,
ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212,
ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22085717,
ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:22578813,
ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:23387299,
ECO:0000269|PubMed:23453970, ECO:0000269|PubMed:23455478,
ECO:0000269|PubMed:23576762, ECO:0000269|PubMed:24768539,
ECO:0000269|PubMed:25270598, ECO:0000269|PubMed:26399832,
ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:27716508,
ECO:0000269|PubMed:27798626}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Forms neddylation-dependent homodimers. Component of
multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
formed of CUL3, RBX1 and a variable BTB domain-containing protein
acting as both, adapter to cullin and substrate recognition
subunit. The BCR complex may be active as a heterodimeric complex,
in which NEDD8, covalently attached to one CUL3 molecule, binds to
the C-terminus of a second CUL3 molecule. Interacts with RBX1,
RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing
SPOP, and of BCR containing homodimeric SPOPL or the heterodimer
formed by SPOP and SPOPL. Part of the probable BCR(KLHL9-KLHL13)
complex with BTB domain proteins KLHL9 and KLHL13. Part of the
BCR(KLHL41) complex containing KLHL41. Component of the
BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3
and KLHL12 and RBX1. Component of the BCR(KLHL3) E3 ubiquitin
ligase complex, at least composed of CUL3 and KLHL3 and RBX1
(Probable). Part of the BCR(ENC1) complex containing ENC1. Part of
a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a
complex consisting of BRMS1, CUL3 and SPOP. Component of the
BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of
CUL3, KLHL21 and RBX1. Component of the BCR(KLHL22) E3 ubiquitin
ligase complex, at least composed of CUL3, KLHL22 and RBX1.
Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at least
composed of CUL3, KLHL25 and RBX1. Part of a complex consisting of
H2AFY, CUL3 and SPOP. Component of the BCR(KLHL42) E3 ubiquitin
ligase complex, at least composed of CUL3 and KLHL42. Interacts
with KLHL42 (via the BTB domain). Interacts with KATNA1; the
interaction is enhanced by KLHL42. Component of the BCR(KBTBD8) E3
ubiquitin ligase complex, at least composed of CUL3, KBTBD8 and
RBX1 (PubMed:26399832). Interacts with KCTD5, KLHL9, KLHL11,
KLHL13, GAN, ZBTB16, KLHL3, KLHL15, KLHL20, KLHL36, GMCL1P1,
BTBD1. Part of a complex that contains CUL3, RBX1 and GAN.
Interacts (via BTB domain) with KLHL17; the interaction regulates
surface GRIK2 expression. Interacts with KCTD7. Part of the
BCR(GAN) complex containing GAN. Part of the BCR(KEAP1) complex
containing KEAP1. Interacts with KLHL10 (By similarity). Interacts
with KAT5 and ATF2. Interacts with DCUN1D3. Interacts with KCTD17
in the BCR(KCTD17) E3 ubiquitin ligase complex, at least composed
of CUL3, KCTD17 and RBX1 (PubMed:25270598). Interacts (when
neddylated) with ARIH1; leading to activate the E3 ligase activity
of ARIH1 (PubMed:24076655, PubMed:27565346). Interacts with COPS9
isoform 2 (PubMed:23776465). Interacts with PPP2R5B; this
interaction is indirect and mediated through KLHL15-binding and
leads to PPP2R5B proteasomal degradation (PubMed:23135275).
Interacts with RBBP8/CtIP; this interaction is indirect and
mediated through KLHL15-binding and leads to RBBP8 proteasomal
degradation (PubMed:27561354). Interacts with KLHL24 in the
BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1
and KLHL24 (PubMed:27798626). {ECO:0000250,
ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10500095,
ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:14528312,
ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:15983046,
ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:17543862,
ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:18573101,
ECO:0000269|PubMed:19261606, ECO:0000269|PubMed:19995937,
ECO:0000269|PubMed:20389280, ECO:0000269|PubMed:21670212,
ECO:0000269|PubMed:21840486, ECO:0000269|PubMed:22085717,
ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:22578813,
ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:22748208,
ECO:0000269|PubMed:23135275, ECO:0000269|PubMed:23349464,
ECO:0000269|PubMed:23387299, ECO:0000269|PubMed:23453970,
ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23573258,
ECO:0000269|PubMed:23576762, ECO:0000269|PubMed:23776465,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:24768539,
ECO:0000269|PubMed:25270598, ECO:0000269|PubMed:25349211,
ECO:0000269|PubMed:26399832, ECO:0000269|PubMed:27561354,
ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:27798626,
ECO:0000305}.
-!- INTERACTION:
Q969K4:ABTB1; NbExp=3; IntAct=EBI-456129, EBI-7223971;
Q86VP6:CAND1; NbExp=2; IntAct=EBI-456129, EBI-456077;
Q14790:CASP8; NbExp=6; IntAct=EBI-456129, EBI-78060;
O60826:CCDC22; NbExp=2; IntAct=EBI-456129, EBI-3943153;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-456129, EBI-10172181;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-456129, EBI-352572;
Q8WZ19:KCTD13; NbExp=5; IntAct=EBI-456129, EBI-742916;
Q8NC69:KCTD6; NbExp=6; IntAct=EBI-456129, EBI-2511344;
Q7L273:KCTD9; NbExp=5; IntAct=EBI-456129, EBI-4397613;
Q53G59:KLHL12; NbExp=5; IntAct=EBI-456129, EBI-740929;
O95198:KLHL2; NbExp=3; IntAct=EBI-456129, EBI-746999;
Q9Y2M5:KLHL20; NbExp=2; IntAct=EBI-456129, EBI-714379;
Q8N4I8:KLHL3; NbExp=3; IntAct=EBI-456129, EBI-10230467;
Q9UH77:KLHL3; NbExp=3; IntAct=EBI-456129, EBI-8524663;
Q8IXQ5:KLHL7; NbExp=7; IntAct=EBI-456129, EBI-6153160;
Q8TBC3:SHKBP1; NbExp=5; IntAct=EBI-456129, EBI-724292;
O43791:SPOP; NbExp=2; IntAct=EBI-456129, EBI-743549;
Q13829:TNFAIP1; NbExp=3; IntAct=EBI-456129, EBI-2505861;
P50591:TNFSF10; NbExp=2; IntAct=EBI-456129, EBI-495373;
Q9H898:ZMAT4; NbExp=3; IntAct=EBI-456129, EBI-2548542;
-!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Cul-3 Long;
IsoId=Q13618-1; Sequence=Displayed;
Name=2;
IsoId=Q13618-2; Sequence=VSP_008824;
Name=3; Synonyms=Cul-3 Short;
IsoId=Q13618-3; Sequence=VSP_008825;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- PTM: Neddylated. Attachment of NEDD8 is required for the E3
ubiquitin-protein ligase activity of the BCR complex. Deneddylated
via its interaction with the COP9 signalosome (CSN) complex.
{ECO:0000269|PubMed:10500095, ECO:0000269|PubMed:10597293,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:27565346}.
-!- DISEASE: Pseudohypoaldosteronism 2E (PHA2E) [MIM:614496]: An
autosomal dominant disorder characterized by severe hypertension,
hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis,
and correction of physiologic abnormalities by thiazide diuretics.
{ECO:0000269|PubMed:22266938}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
ProRule:PRU00330}.
-!- SEQUENCE CAUTION:
Sequence=AAC28621.1; Type=Frameshift; Positions=452; Evidence={ECO:0000305};
Sequence=AAC36682.1; Type=Frameshift; Positions=159, 179; Evidence={ECO:0000305};
Sequence=BAA31592.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF064087; AAC36304.1; -; mRNA.
EMBL; AB014517; BAA31592.2; ALT_INIT; mRNA.
EMBL; AF062537; AAC36682.1; ALT_FRAME; mRNA.
EMBL; AY337761; AAQ01660.1; -; mRNA.
EMBL; AK291151; BAF83840.1; -; mRNA.
EMBL; AC073052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW70828.1; -; Genomic_DNA.
EMBL; BC031844; AAH31844.1; -; mRNA.
EMBL; BC039598; AAH39598.1; -; mRNA.
EMBL; BC092409; AAH92409.1; -; mRNA.
EMBL; U58089; AAC50546.1; -; mRNA.
EMBL; AF052147; AAC28621.1; ALT_FRAME; mRNA.
CCDS; CCDS2462.1; -. [Q13618-1]
CCDS; CCDS58751.1; -. [Q13618-3]
RefSeq; NP_001244126.1; NM_001257197.1. [Q13618-3]
RefSeq; NP_001244127.1; NM_001257198.1.
RefSeq; NP_003581.1; NM_003590.4. [Q13618-1]
UniGene; Hs.372286; -.
PDB; 2MYL; NMR; -; A=49-68.
PDB; 2MYM; NMR; -; A=49-68.
PDB; 4AP2; X-ray; 2.80 A; B=1-388.
PDB; 4APF; X-ray; 3.10 A; B=23-388.
PDB; 4EOZ; X-ray; 2.40 A; B/D=20-381.
PDB; 4HXI; X-ray; 3.51 A; B=20-381.
PDB; 5NLB; X-ray; 3.45 A; B=26-381.
PDBsum; 2MYL; -.
PDBsum; 2MYM; -.
PDBsum; 4AP2; -.
PDBsum; 4APF; -.
PDBsum; 4EOZ; -.
PDBsum; 4HXI; -.
PDBsum; 5NLB; -.
ProteinModelPortal; Q13618; -.
SMR; Q13618; -.
BioGrid; 114030; 1211.
CORUM; Q13618; -.
DIP; DIP-31611N; -.
IntAct; Q13618; 65.
MINT; MINT-3028280; -.
STRING; 9606.ENSP00000264414; -.
iPTMnet; Q13618; -.
PhosphoSitePlus; Q13618; -.
BioMuta; CUL3; -.
DMDM; 12643396; -.
EPD; Q13618; -.
MaxQB; Q13618; -.
PaxDb; Q13618; -.
PeptideAtlas; Q13618; -.
PRIDE; Q13618; -.
Ensembl; ENST00000264414; ENSP00000264414; ENSG00000036257. [Q13618-1]
Ensembl; ENST00000344951; ENSP00000343601; ENSG00000036257. [Q13618-3]
Ensembl; ENST00000409096; ENSP00000387200; ENSG00000036257. [Q13618-2]
Ensembl; ENST00000409777; ENSP00000386525; ENSG00000036257. [Q13618-2]
GeneID; 8452; -.
KEGG; hsa:8452; -.
UCSC; uc002vny.4; human. [Q13618-1]
CTD; 8452; -.
DisGeNET; 8452; -.
EuPathDB; HostDB:ENSG00000036257.12; -.
GeneCards; CUL3; -.
HGNC; HGNC:2553; CUL3.
HPA; CAB002678; -.
MalaCards; CUL3; -.
MIM; 603136; gene.
MIM; 614496; phenotype.
neXtProt; NX_Q13618; -.
OpenTargets; ENSG00000036257; -.
Orphanet; 300530; Pseudohypoaldosteronism type 2E.
PharmGKB; PA27049; -.
eggNOG; KOG2167; Eukaryota.
eggNOG; COG5647; LUCA.
GeneTree; ENSGT00760000119212; -.
HOVERGEN; HBG003619; -.
InParanoid; Q13618; -.
KO; K03869; -.
OMA; AAIKWVD; -.
OrthoDB; EOG091G02DP; -.
PhylomeDB; Q13618; -.
TreeFam; TF105858; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q13618; -.
SIGNOR; Q13618; -.
UniPathway; UPA00143; -.
ChiTaRS; CUL3; human.
GeneWiki; CUL3; -.
GenomeRNAi; 8452; -.
PRO; PR:Q13618; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000036257; -.
CleanEx; HS_CUL3; -.
ExpressionAtlas; Q13618; baseline and differential.
Genevisible; Q13618; HS.
GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005827; C:polar microtubule; IDA:UniProtKB.
GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
GO; GO:0005112; F:Notch binding; IPI:MGI.
GO; GO:0031208; F:POZ domain binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0048208; P:COPII vesicle coating; IMP:UniProtKB.
GO; GO:0040016; P:embryonic cleavage; ISS:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IDA:UniProtKB.
GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0072576; P:liver morphogenesis; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0017145; P:stem cell division; ISS:UniProtKB.
GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
GO; GO:0001831; P:trophectodermal cellular morphogenesis; IEA:Ensembl.
GO; GO:0071630; P:ubiquitin-dependent catabolism of misfolded proteins by nucleus-associated proteasome; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
Gene3D; 1.10.10.10; -; 2.
InterPro; IPR016157; Cullin_CS.
InterPro; IPR016158; Cullin_homology.
InterPro; IPR001373; Cullin_N.
InterPro; IPR019559; Cullin_neddylation_domain.
InterPro; IPR016159; Cullin_repeat-like_dom.
InterPro; IPR011991; WHTH_DNA-bd_dom.
Pfam; PF00888; Cullin; 1.
Pfam; PF10557; Cullin_Nedd8; 1.
SMART; SM00182; CULLIN; 1.
SMART; SM00884; Cullin_Nedd8; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF74788; SSF74788; 1.
SUPFAM; SSF75632; SSF75632; 1.
PROSITE; PS01256; CULLIN_1; 1.
PROSITE; PS50069; CULLIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Cilium biogenesis/degradation; Complete proteome; Disease mutation;
ER-Golgi transport; Golgi apparatus; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transport;
Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 768 Cullin-3.
/FTId=PRO_0000119793.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 712 712 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in NEDD8).
{ECO:0000250|UniProtKB:Q13616}.
VAR_SEQ 1 24 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_008824.
VAR_SEQ 23 88 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_008825.
VARIANT 13 13 D -> H (in dbSNP:rs2969802).
/FTId=VAR_017194.
VARIANT 184 184 R -> S (in dbSNP:rs17480168).
/FTId=VAR_048839.
VARIANT 413 413 D -> G (in PHA2E; dbSNP:rs199469656).
{ECO:0000269|PubMed:22266938}.
/FTId=VAR_067532.
VARIANT 459 459 K -> R (in PHA2E; dbSNP:rs199469658).
{ECO:0000269|PubMed:22266938}.
/FTId=VAR_067533.
VARIANT 567 567 V -> I (in dbSNP:rs3738952).
/FTId=VAR_017195.
VARIANT 719 719 H -> R (found in a patient with autism
spectrum disorder; unknown pathological
significance; dbSNP:rs763087632).
{ECO:0000269|PubMed:25969726}.
/FTId=VAR_078688.
CONFLICT 13 13 D -> G (in Ref. 3; AAC36682).
{ECO:0000305}.
CONFLICT 397 397 K -> T (in Ref. 4; AAQ01660).
{ECO:0000305}.
CONFLICT 481 481 N -> T (in Ref. 4; AAQ01660).
{ECO:0000305}.
CONFLICT 609 609 E -> G (in Ref. 8; AAH31844).
{ECO:0000305}.
CONFLICT 666 666 T -> I (in Ref. 4; AAQ01660).
{ECO:0000305}.
HELIX 26 45 {ECO:0000244|PDB:4EOZ}.
HELIX 49 51 {ECO:0000244|PDB:4EOZ}.
HELIX 54 66 {ECO:0000244|PDB:4EOZ}.
HELIX 70 87 {ECO:0000244|PDB:4EOZ}.
HELIX 89 94 {ECO:0000244|PDB:4EOZ}.
TURN 95 98 {ECO:0000244|PDB:4EOZ}.
HELIX 101 122 {ECO:0000244|PDB:4EOZ}.
HELIX 124 129 {ECO:0000244|PDB:4EOZ}.
HELIX 132 134 {ECO:0000244|PDB:4EOZ}.
HELIX 139 150 {ECO:0000244|PDB:4EOZ}.
TURN 151 153 {ECO:0000244|PDB:4EOZ}.
HELIX 155 173 {ECO:0000244|PDB:4EOZ}.
HELIX 180 192 {ECO:0000244|PDB:4EOZ}.
STRAND 195 198 {ECO:0000244|PDB:4EOZ}.
HELIX 199 204 {ECO:0000244|PDB:4EOZ}.
HELIX 206 227 {ECO:0000244|PDB:4EOZ}.
HELIX 230 251 {ECO:0000244|PDB:4EOZ}.
HELIX 254 256 {ECO:0000244|PDB:4EOZ}.
HELIX 257 268 {ECO:0000244|PDB:4EOZ}.
TURN 269 272 {ECO:0000244|PDB:4EOZ}.
HELIX 273 277 {ECO:0000244|PDB:4EOZ}.
TURN 280 282 {ECO:0000244|PDB:4EOZ}.
HELIX 284 287 {ECO:0000244|PDB:4EOZ}.
TURN 288 291 {ECO:0000244|PDB:4EOZ}.
HELIX 293 303 {ECO:0000244|PDB:4EOZ}.
HELIX 309 323 {ECO:0000244|PDB:4EOZ}.
HELIX 339 358 {ECO:0000244|PDB:4AP2}.
HELIX 364 380 {ECO:0000244|PDB:4AP2}.
SEQUENCE 768 AA; 88930 MW; A1A02022480BF099 CRC64;
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLGCMY
KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLLESF
NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIENGHIFT
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA


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