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Cullin-1 (CUL-1)

 CUL1_HUMAN              Reviewed;         776 AA.
Q13616; D3DWG3; O60719; Q08AL6; Q8IYW1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
02-JUN-2021, entry version 206.
RecName: Full=Cullin-1;
Short=CUL-1;
Name=CUL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Cervix 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Endometrium;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
INTERACTION WITH RBX1, AND IDENTIFICATION IN SCF COMPLEX WITH RBX1; SKP1
AND SKP2.
PubMed=10230406; DOI=10.1016/s1097-2765(00)80481-5;
Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.;
"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze
the ubiquitination of I kappa B alpha.";
Mol. Cell 3:527-533(1999).
[8]
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).
[9]
NEDDYLATION AT LYS-720.
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).
[10]
NEDDYLATION.
PubMed=10713156; DOI=10.1128/mcb.20.7.2326-2333.2000;
Read M.A., Brownell J.E., Gladysheva T.B., Hottelet M., Parent L.A.,
Coggins M.B., Pierce J.W., Podust V.N., Luo R.-S., Chau V.,
Palombella V.J.;
"Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent
ubiquitination of IkappaBalpha.";
Mol. Cell. Biol. 20:2326-2333(2000).
[11]
INTERACTION WITH RNF7.
PubMed=10851089; DOI=10.1038/sj.onc.1203635;
Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y.;
"Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth,
but not for germination: chip profiling implicates its role in cell cycle
regulation.";
Oncogene 19:2855-2866(2000).
[12]
INTERACTION WITH COPS2.
PubMed=11337588; DOI=10.1126/science.1059780;
Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
Science 292:1382-1385(2001).
[13]
INTERACTION WITH TIP120A.
PubMed=12504026; DOI=10.1016/s1097-2765(02)00784-0;
Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H.,
Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.;
"CAND1 binds to unneddylated CUL1 and regulates the formation of SCF
ubiquitin E3 ligase complex.";
Mol. Cell 10:1519-1526(2002).
[14]
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).
[15]
IDENTIFICATION IN THE SCF(FBXO7) COMPLEX.
PubMed=15145941; DOI=10.1074/jbc.m404950200;
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated
hepatoma up-regulated protein (HURP) proteolysis by a proline-rich
region.";
J. Biol. Chem. 279:32592-32602(2004).
[16]
RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, AND FUNCTION IN UBIQUITINATION
OF MYOD1.
PubMed=15531760; DOI=10.1074/jbc.m411346200;
Tintignac L.A., Lagirand J., Batonnet S., Sirri V., Leibovitch M.P.,
Leibovitch S.A.;
"Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase.";
J. Biol. Chem. 280:2847-2856(2005).
[17]
INTERACTION WITH GCM1, AND FUNCTION IN UBIQUITINATION OF GCM1.
PubMed=15640526; DOI=10.1074/jbc.m413986200;
Yang C.S., Yu C., Chuang H.C., Chang C.W., Chang G.D., Yao T.P., Chen H.;
"FBW2 targets GCMa to the ubiquitin-proteasome degradation system.";
J. Biol. Chem. 280:10083-10090(2005).
[18]
RECONSTITUTION OF THE SCF(FBXO25) COMPLEX.
PubMed=16714087; DOI=10.1016/j.bbagen.2006.03.020;
Maragno A.L., Baqui M.M., Gomes M.D.;
"FBXO25, an F-box protein homologue of atrogin-1, is not induced in
atrophying muscle.";
Biochim. Biophys. Acta 1760:966-972(2006).
[19]
IDENTIFICATION IN THE SCF(FBXO33) COMPLEX WITH SKP1; RBX1 AND FBXO33.
PubMed=16797541; DOI=10.1016/j.febslet.2006.06.023;
Lutz M., Wempe F., Bahr I., Zopf D., von Melchner H.;
"Proteasomal degradation of the multifunctional regulator YB-1 is mediated
by an F-Box protein induced during programmed cell death.";
FEBS Lett. 580:3921-3930(2006).
[20]
INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, AND INTERACTION WITH TRIM21.
PubMed=16880511; DOI=10.1128/mcb.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING finger
protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[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]
IDENTIFICATION IN THE SCF(FBXO11) COMPLEX WITH SKP1; RBX1 AND FBXO11.
PubMed=17098746; DOI=10.1074/jbc.m609001200;
Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.;
"FBXO11 promotes the neddylation of p53 and inhibits its transcriptional
activity.";
J. Biol. Chem. 282:1797-1804(2007).
[23]
NEDDYLATION AT LYS-720.
PubMed=18805092; DOI=10.1016/j.cell.2008.07.022;
Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.;
"Structural insights into NEDD8 activation of cullin-RING ligases:
conformational control of conjugation.";
Cell 134:995-1006(2008).
[24]
INTERACTION WITH FBXO44; FBXO17 AND FBXO27, AND IDENTIFICATION IN
SCF-COMPLEX.
PubMed=18203720; DOI=10.1074/jbc.m709508200;
Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
"Diversity in tissue expression, substrate binding, and SCF complex
formation for a lectin family of ubiquitin ligases.";
J. Biol. Chem. 283:12717-12729(2008).
[25]
FUNCTION IN CHEK2 UBIQUITINATION, AND INTERACTION WITH CHEK2.
PubMed=18644861; DOI=10.1128/mcb.00821-08;
Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.;
"Regulation of Chk2 ubiquitination and signaling through
autophosphorylation of serine 379.";
Mol. Cell. Biol. 28:5874-5885(2008).
[26]
FUNCTION, AND INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
PubMed=19679664; DOI=10.1074/jbc.m109.006809;
Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T.,
Kitagawa M.;
"Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
J. Biol. Chem. 284:27766-27779(2009).
[27]
INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, AND DENEDDYLATION BY
EPSTEIN-BARR VIRUS BPLF1 (MICROBIAL INFECTION).
PubMed=20190741; DOI=10.1038/ncb2035;
Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M.,
Di Guglielmo C., Masucci M.G.;
"A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication
by regulating the activity of cullin-RING ligases.";
Nat. Cell Biol. 12:351-361(2010).
[28]
IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
PubMed=20596027; DOI=10.1038/nature09140;
D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
Washburn M.P., Dynlacht B., Pagano M.;
"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through
CP110 degradation.";
Nature 466:138-142(2010).
[29]
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).
[30]
IDENTIFICATION IN THE SCF(FBXW7) COMPLEX, FUNCTION, AND PATHWAY.
PubMed=22405651; DOI=10.1016/j.molcel.2012.02.005;
Tron A.E., Arai T., Duda D.M., Kuwabara H., Olszewski J.L., Fujiwara Y.,
Bahamon B.N., Signoretti S., Schulman B.A., DeCaprio J.A.;
"The glomuvenous malformation protein Glomulin binds Rbx1 and regulates
cullin RING ligase-mediated turnover of Fbw7.";
Mol. Cell 46:67-78(2012).
[31]
FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE SCF(FBXO11)
COMPLEX.
PubMed=22113614; DOI=10.1038/nature10688;
Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F.,
Chapuy B., Shipp M., Chiarle R., Pagano M.;
"FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-
cell lymphomas.";
Nature 481:90-93(2012).
[32]
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).
[33]
IDENTIFICATION IN THE SCF(FBXO9) COMPLEX, AND FUNCTION.
PubMed=23263282; DOI=10.1038/ncb2651;
Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C.,
Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M.,
Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.;
"SCF(Fbxo9) and CK2 direct the cellular response to growth factor
withdrawal via Tel2/Tti1 degradation and promote survival in multiple
myeloma.";
Nat. Cell Biol. 15:72-81(2013).
[34]
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).
[35]
FUNCTION IN UBIQUITINATION OF BCL2, AND IDENTIFICATION IN THE SCF(FBXO10)
COMPLEX.
PubMed=23431138; DOI=10.1073/pnas.1217271110;
Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W.,
Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D.,
Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S.,
Staudt L.M.;
"Related F-box proteins control cell death in Caenorhabditis elegans and
human lymphoma.";
Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
[36]
INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
Bennett E.J., Schulman B.A.;
"Structural conservation of distinctive N-terminal acetylation-dependent
interactions across a family of mammalian NEDD8 ligation enzymes.";
Structure 21:42-53(2013).
[37]
INTERACTION WITH DCUN1D5.
PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
"Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
and nuclear localization.";
Clin. Cancer Res. 20:372-381(2014).
[38]
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).
[39]
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).
[40]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[41]
FUNCTION.
PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004;
Man X., Megraw T.L., Lim Y.P.;
"Cep68 can be regulated by Nek2 and SCF complex.";
Eur. J. Cell Biol. 94:162-172(2015).
[42]
FUNCTION, IDENTIFICATION IN SCF(FBXW11) COMPLEX, AND INTERACTION WITH
CEP68.
PubMed=25503564; DOI=10.1038/ncb3076;
Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L.,
Washburn M.P., Pagano M.;
"Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM
to allow centriole separation, disengagement and licensing.";
Nat. Cell Biol. 17:31-43(2015).
[43]
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).
[44]
INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
PubMed=26906416; DOI=10.1242/jcs.181784;
Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
"Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
J. Cell Sci. 129:1441-1454(2016).
[45]
INTERACTION WITH NOTCH2.
PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W., Inuzuka H.;
"NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
promote osteoporosis.";
Mol. Cell 68:645-658(2017).
[46]
INTERACTION WITH UBXN1.
PubMed=28152074; DOI=10.1371/journal.ppat.1006187;
Hu Y., O'Boyle K., Auer J., Raju S., You F., Wang P., Fikrig E.,
Sutton R.E.;
"Multiple UBXN family members inhibit retrovirus and lentivirus production
and canonical NFkappaBeta signaling by stabilizing IkappaBalpha.";
PLoS Pathog. 13:E1006187-E1006187(2017).
[47]
INTERACTION WITH VACCINIA VIRUS PROTEIN C9L (MICROBIAL INFECTION).
PubMed=29444943; DOI=10.1128/jvi.00053-18;
Liu R., Moss B.;
"Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified
Antagonist of the Type I Interferon-Induced Antiviral State.";
J. Virol. 92:0-0(2018).
[48]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108 OF
RBX1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH RBX1;
SKP1 AND SKP2.
PubMed=11961546; DOI=10.1038/416703a;
Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W.,
Harper J.W., Pavletich N.P.;
"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
Nature 416:703-709(2002).
[49]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CAND1 AND ROC1,
NEDDYLATION AT LYS-720, AND SUBUNIT.
PubMed=15537541; DOI=10.1016/j.cell.2004.10.019;
Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y.,
Zheng N.;
"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for
the assembly of the multisubunit cullin-dependent ubiquitin ligases.";
Cell 119:517-528(2004).
[50]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D1
AND UBE2M.
PubMed=21940857; DOI=10.1126/science.1209307;
Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.;
"N-terminal acetylation acts as an avidity enhancer within an
interconnected multiprotein complex.";
Science 334:674-678(2011).
[51] {ECO:0007744|PDB:4F52}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 411-690 IN COMPLEX WITH RBX1 AND
GLMN, AND SUBUNIT.
PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044;
Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J.,
Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.;
"Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase
through masking of its E2-binding surface.";
Mol. Cell 47:371-382(2012).
[52] {ECO:0007744|PDB:5V89}
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D4.
PubMed=28581483; DOI=10.1038/nchembio.2386;
Scott D.C., Hammill J.T., Min J., Rhee D.Y., Connelly M., Sviderskiy V.O.,
Bhasin D., Chen Y., Ong S.S., Chai S.C., Goktug A.N., Huang G., Monda J.K.,
Low J., Kim H.S., Paulo J.A., Cannon J.R., Shelat A.A., Chen T.,
Kelsall I.R., Alpi A.F., Pagala V., Wang X., Peng J., Singh B.,
Harper J.W., Schulman B.A., Guy R.K.;
"Blocking an N-terminal acetylation-dependent protein interaction inhibits
an E3 ligase.";
Nat. Chem. Biol. 13:850-857(2017).
-!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
ubiquitination of proteins involved in cell cycle progression, signal
transduction and transcription. SCF complexes and ARIH1 collaborate in
tandem to mediate ubiquitination of target proteins (PubMed:27565346).
In the SCF complex, serves as a rigid scaffold that organizes the SKP1-
F-box protein and RBX1 subunits. 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 exchange of the substrate
recognition component is mediated by TIP120A/CAND1. The functional
specificity of the SCF complex depends on the F-box protein as
substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct
ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11)
directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs
ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and
probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of
CEP68 (PubMed:25704143, PubMed:25503564). SCF(SKP2) directs
ubiquitination of phosphorylated CDKN1B/p27kip and is involved in
regulation of G1/S transition. SCF(SKP2) directs ubiquitination of
ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and
TAL1. SCF(FBXW7) directs ubiquitination of CCNE1, NOTCH1 released notch
intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs
ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1.
SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33)
directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of
BCL6 and DTL but does not seem to direct ubiquitination of TP53.
SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-
22'; the degradation frees the associated NFKB1-RELA dimer to
translocate into the nucleus and to activate transcription. SCF(CCNF)
directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct
ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of
TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.
{ECO:0000269|PubMed:15531760, ECO:0000269|PubMed:15640526,
ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:19679664,
ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:22405651,
ECO:0000269|PubMed:23263282, ECO:0000269|PubMed:23431138,
ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143,
ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:9663463}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:22405651}.
-!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-
box domain-containing protein as substrate-specific subunit
(PubMed:10230406, PubMed:15145941, PubMed:15531760, PubMed:16714087,
PubMed:16797541, PubMed:17098746, PubMed:18203720, PubMed:20596027,
PubMed:22405651, PubMed:22113614, PubMed:23263282, PubMed:23431138,
PubMed:25503564, PubMed:11961546, PubMed:22748924). Component of the
SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2)
complex containing SKP2, in which it interacts directly with SKP1, SKP2
and RBX1. Component of the SCF(FBXW2) complex containing FBXW2.
Component of the SCF(FBXO32) complex containing FBXO32. Component of
the probable SCF(FBXO7) complex containing FBXO7. Component of the
SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11)
complex containing FBXO11. Component of the SCF(FBXO25) complex
containing FBXO25. Component of the SCF(FBXO33) complex containing
FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4.
Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and
FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and
BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex
consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like
complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the
SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of
the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component
of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF.
Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and
FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1,
RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1,
RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1,
RBX1 and FBXW7 (PubMed:22405651). Interacts with CHEK2; mediates CHEK2
ubiquitination and regulates its function. Part of a complex with
TIP120A/CAND1 and RBX1. The unneddylated form interacts with
TIP120A/CAND1 and the interaction mediates the exchange of the F-box
substrate-specific subunit. Can self-associate. Interacts with FBXW8.
Interacts with RNF7. Interacts with CUL7; the interaction seems to be
mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2.
Interacts with UBE2M (PubMed:21940857). Identified in a complex with
RBX1 and GLMN (PubMed:22405651, PubMed:22748924). Interacts with CEP68
as part of the SCF(FBXW11) complex; the interaction is probably
mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT
(PubMed:25503564). 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 UBXN1 (PubMed:28152074). Interacts with KAT7, probably
as part of an SCF complex; the interaction mediates KAT7 ubiquitination
(By similarity). Interacts with NOTCH2 (PubMed:29149593). Part of a
complex that contains DCUN1D5, CUL1 and RBX1; this complex is bridged
by CUL1 (PubMed:24192928). Interacts (unneddylated form) with DCUN1D1,
DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the
cullin neddylation (PubMed:24192928, PubMed:26906416, PubMed:23201271,
PubMed:21940857, PubMed:25349211, PubMed:28581483).
{ECO:0000250|UniProtKB:Q9WTX6, ECO:0000269|PubMed:10230406,
ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10851089,
ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:11961546,
ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982,
ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:15531760,
ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:15640526,
ECO:0000269|PubMed:16714087, ECO:0000269|PubMed:16797541,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:17098746,
ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:18644861,
ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:20596027,
ECO:0000269|PubMed:21940857, ECO:0000269|PubMed:22113614,
ECO:0000269|PubMed:22405651, ECO:0000269|PubMed:22748924,
ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:23263282,
ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:23776465,
ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:24192928,
ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:25503564,
ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:27565346,
ECO:0000269|PubMed:28152074, ECO:0000269|PubMed:28581483,
ECO:0000269|PubMed:29149593}.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus BPLF1.
{ECO:0000269|PubMed:20190741}.
-!- SUBUNIT: (Microbial infection) Interacts with Human adenovirus early
E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation
reaction of ubiquitin chains by the SCF(FBXW7) complex.
{ECO:0000269|PubMed:19679664}.
-!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
C9L. {ECO:0000269|PubMed:29444943}.
-!- INTERACTION:
Q13616; Q9Y4X5: ARIH1; NbExp=8; IntAct=EBI-359390, EBI-2514233;
Q13616; Q9Y297: BTRC; NbExp=11; IntAct=EBI-359390, EBI-307461;
Q13616; Q86VP6: CAND1; NbExp=33; IntAct=EBI-359390, EBI-456077;
Q13616; O60826: CCDC22; NbExp=3; IntAct=EBI-359390, EBI-3943153;
Q13616; P41002: CCNF; NbExp=5; IntAct=EBI-359390, EBI-1207574;
Q13616; Q8ND76: CCNY; NbExp=3; IntAct=EBI-359390, EBI-1049189;
Q13616; P49427: CDC34; NbExp=3; IntAct=EBI-359390, EBI-975634;
Q13616; P46527: CDKN1B; NbExp=2; IntAct=EBI-359390, EBI-519280;
Q13616; Q96EF6: FBXO17; NbExp=8; IntAct=EBI-359390, EBI-2510157;
Q13616; Q8NEZ5: FBXO22; NbExp=4; IntAct=EBI-359390, EBI-2510137;
Q13616; Q9UK99: FBXO3; NbExp=7; IntAct=EBI-359390, EBI-2509901;
Q13616; Q7Z6M2: FBXO33; NbExp=2; IntAct=EBI-359390, EBI-8555452;
Q13616; Q9UKT5: FBXO4; NbExp=3; IntAct=EBI-359390, EBI-960409;
Q13616; Q9NRD1: FBXO6; NbExp=3; IntAct=EBI-359390, EBI-3938499;
Q13616; Q9UKB1: FBXW11; NbExp=11; IntAct=EBI-359390, EBI-355189;
Q13616; Q9UKT8: FBXW2; NbExp=5; IntAct=EBI-359390, EBI-914727;
Q13616; Q969H0: FBXW7; NbExp=5; IntAct=EBI-359390, EBI-359574;
Q13616; P08238: HSP90AB1; NbExp=2; IntAct=EBI-359390, EBI-352572;
Q13616; Q00987: MDM2; NbExp=3; IntAct=EBI-359390, EBI-389668;
Q13616; O75586: MED6; NbExp=2; IntAct=EBI-359390, EBI-394624;
Q13616; Q15843: NEDD8; NbExp=23; IntAct=EBI-359390, EBI-716247;
Q13616; P62877: RBX1; NbExp=28; IntAct=EBI-359390, EBI-398523;
Q13616; P63208: SKP1; NbExp=17; IntAct=EBI-359390, EBI-307486;
Q13616; Q13309: SKP2; NbExp=15; IntAct=EBI-359390, EBI-456291;
Q13616; P61081: UBE2M; NbExp=5; IntAct=EBI-359390, EBI-1041660;
Q13616; O94888: UBXN7; NbExp=8; IntAct=EBI-359390, EBI-1993627;
Q13616; P67809: YBX1; NbExp=2; IntAct=EBI-359390, EBI-354065;
Q13616; Q8BFZ4: Fbxl21; Xeno; NbExp=3; IntAct=EBI-359390, EBI-6898235;
Q13616; Q8C4V4: Fbxl3; Xeno; NbExp=3; IntAct=EBI-359390, EBI-1266589;
Q13616; Q83730: m005R; Xeno; NbExp=5; IntAct=EBI-359390, EBI-6859930;
Q13616; P52491: UBC12; Xeno; NbExp=2; IntAct=EBI-359390, EBI-19772;
Q13616; Q6TVW2; Xeno; NbExp=5; IntAct=EBI-359390, EBI-15718527;
-!- TISSUE SPECIFICITY: Expressed in lung fibroblasts.
{ECO:0000269|PubMed:9663463}.
-!- PTM: Neddylated; which enhances the ubiquitination activity of SCF and
prevents binding of the inhibitor CAND1. Deneddylated via its
interaction with the COP9 signalosome (CSN) complex (PubMed:10597293,
PubMed:10713156, PubMed:15537541, PubMed:18805092).
{ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:10713156,
ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:18805092,
ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:24076655,
ECO:0000269|PubMed:27565346}.
-!- PTM: (Microbial infection) Deneddylated by Epstein-Barr virus BPLF1
leading to a S-phase-like environment that is required for efficient
replication of the viral genome (PubMed:20190741).
{ECO:0000269|PubMed:20190741}.
-!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
ProRule:PRU00330}.
---------------------------------------------------------------------------
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EMBL; U58087; AAC50544.1; -; mRNA.
EMBL; AF062536; AAC36681.1; -; mRNA.
EMBL; BX537409; CAD97651.1; -; mRNA.
EMBL; AC005229; AAM49153.1; -; Genomic_DNA.
EMBL; CH471146; EAW80074.1; -; Genomic_DNA.
EMBL; BC125119; AAI25120.1; -; mRNA.
EMBL; BC125120; AAI25121.1; -; mRNA.
CCDS; CCDS34772.1; -.
RefSeq; NP_003583.2; NM_003592.2.
RefSeq; XP_005250117.1; XM_005250060.4.
RefSeq; XP_011514931.1; XM_011516629.2.
RefSeq; XP_011514932.1; XM_011516630.2.
RefSeq; XP_011514933.1; XM_011516631.2.
RefSeq; XP_011514934.1; XM_011516632.2.
PDB; 1LDJ; X-ray; 3.00 A; A=17-776.
PDB; 1LDK; X-ray; 3.10 A; A=15-410, B=411-776.
PDB; 1U6G; X-ray; 3.10 A; A=1-776.
PDB; 3RTR; X-ray; 3.21 A; A/C/E/G=411-776.
PDB; 3TDU; X-ray; 1.50 A; C/D=702-776.
PDB; 3TDZ; X-ray; 2.00 A; C/D=702-776.
PDB; 4F52; X-ray; 3.00 A; A/C=411-690.
PDB; 4P5O; X-ray; 3.11 A; A/C=411-776.
PDB; 5V89; X-ray; 1.55 A; C=702-776.
PDB; 6TTU; EM; 3.70 A; C=1-776.
PDB; 6WCQ; EM; 8.50 A; D=1-434.
PDB; 7B5L; EM; 3.80 A; C=1-776.
PDB; 7B5M; EM; 3.91 A; C=1-776.
PDB; 7B5N; EM; 3.60 A; C=1-776.
PDB; 7B5R; EM; 3.80 A; C=1-776.
PDB; 7B5S; EM; 3.60 A; C=1-776.
PDBsum; 1LDJ; -.
PDBsum; 1LDK; -.
PDBsum; 1U6G; -.
PDBsum; 3RTR; -.
PDBsum; 3TDU; -.
PDBsum; 3TDZ; -.
PDBsum; 4F52; -.
PDBsum; 4P5O; -.
PDBsum; 5V89; -.
PDBsum; 6TTU; -.
PDBsum; 6WCQ; -.
PDBsum; 7B5L; -.
PDBsum; 7B5M; -.
PDBsum; 7B5N; -.
PDBsum; 7B5R; -.
PDBsum; 7B5S; -.
SMR; Q13616; -.
BioGRID; 114032; 801.
CORUM; Q13616; -.
DIP; DIP-17013N; -.
IntAct; Q13616; 566.
MINT; Q13616; -.
STRING; 9606.ENSP00000326804; -.
ChEMBL; CHEMBL3758068; -.
iPTMnet; Q13616; -.
MetOSite; Q13616; -.
PhosphoSitePlus; Q13616; -.
BioMuta; CUL1; -.
DMDM; 19863257; -.
EPD; Q13616; -.
jPOST; Q13616; -.
MassIVE; Q13616; -.
MaxQB; Q13616; -.
PaxDb; Q13616; -.
PeptideAtlas; Q13616; -.
PRIDE; Q13616; -.
ProteomicsDB; 59604; -.
Antibodypedia; 3630; 535 antibodies.
DNASU; 8454; -.
Ensembl; ENST00000325222; ENSP00000326804; ENSG00000055130.
Ensembl; ENST00000409469; ENSP00000387160; ENSG00000055130.
Ensembl; ENST00000602748; ENSP00000473318; ENSG00000055130.
Ensembl; ENST00000662716; ENSP00000499277; ENSG00000055130.
Ensembl; ENST00000663044; ENSP00000499398; ENSG00000055130.
Ensembl; ENST00000665936; ENSP00000499255; ENSG00000055130.
GeneID; 8454; -.
KEGG; hsa:8454; -.
UCSC; uc003wey.4; human.
CTD; 8454; -.
DisGeNET; 8454; -.
GeneCards; CUL1; -.
HGNC; HGNC:2551; CUL1.
HPA; ENSG00000055130; Low tissue specificity.
MIM; 603134; gene.
neXtProt; NX_Q13616; -.
OpenTargets; ENSG00000055130; -.
PharmGKB; PA27047; -.
VEuPathDB; HostDB:ENSG00000055130.15; -.
eggNOG; KOG2166; Eukaryota.
GeneTree; ENSGT00940000154774; -.
InParanoid; Q13616; -.
OMA; WLWHLCK; -.
OrthoDB; 1040292at2759; -.
PhylomeDB; Q13616; -.
TreeFam; TF101151; -.
BioCyc; MetaCyc:ENSG00000055130-MONOMER; -.
PathwayCommons; Q13616; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-917937; Iron uptake and transport.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q13616; -.
SIGNOR; Q13616; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 8454; 480 hits in 1006 CRISPR screens.
ChiTaRS; CUL1; human.
EvolutionaryTrace; Q13616; -.
GeneWiki; CUL1; -.
GenomeRNAi; 8454; -.
Pharos; Q13616; Tbio.
PRO; PR:Q13616; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q13616; protein.
Bgee; ENSG00000055130; Expressed in testis and 233 other tissues.
ExpressionAtlas; Q13616; baseline and differential.
Genevisible; Q13616; HS.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; IPI:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0010265; P:SCF complex assembly; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
Gene3D; 1.10.10.10; -; 2.
IDEAL; IID00133; -.
InterPro; IPR016157; Cullin_CS.
InterPro; IPR016158; Cullin_homology.
InterPro; IPR036317; Cullin_homology_sf.
InterPro; IPR001373; Cullin_N.
InterPro; IPR019559; Cullin_neddylation_domain.
InterPro; IPR016159; Cullin_repeat-like_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
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; Host-virus interaction; Isopeptide bond; Methylation;
Reference proteome; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1..776
/note="Cullin-1"
/id="PRO_0000119787"
MOD_RES 63
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
CROSSLNK 720
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in NEDD8)"
/evidence="ECO:0000269|PubMed:10597293,
ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:18805092"
CONFLICT 59..82
/note="Missing (in Ref. 1; AAC50544)"
/evidence="ECO:0000305"
CONFLICT 726
/note="K -> R (in Ref. 3; CAD97651)"
/evidence="ECO:0000305"
HELIX 18..31
/evidence="ECO:0007829|PDB:1LDJ"
TURN 32..34
/evidence="ECO:0007829|PDB:1U6G"
HELIX 39..52
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 87..105
/evidence="ECO:0007829|PDB:1LDJ"
TURN 106..109
/evidence="ECO:0007829|PDB:1U6G"
TURN 111..114
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 115..136
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 138..143
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 144..146
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 159..165
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 168..171
/evidence="ECO:0007829|PDB:1LDJ"
TURN 172..177
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 178..187
/evidence="ECO:0007829|PDB:1LDJ"
TURN 188..190
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 199..210
/evidence="ECO:0007829|PDB:1LDJ"
TURN 211..213
/evidence="ECO:0007829|PDB:1LDK"
STRAND 215..219
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 226..231
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 233..254
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 261..273
/evidence="ECO:0007829|PDB:1LDJ"
TURN 274..279
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 281..284
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 285..295
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 296..300
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 301..312
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 318..328
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 333..355
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 359..361
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 363..382
/evidence="ECO:0007829|PDB:1LDJ"
TURN 383..387
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 389..404
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 407..412
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 417..430
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 439..453
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 459..475
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 482..525
/evidence="ECO:0007829|PDB:1LDJ"
TURN 526..528
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 532..541
/evidence="ECO:0007829|PDB:1LDJ"
TURN 542..544
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 557..559
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 560..569
/evidence="ECO:0007829|PDB:1LDJ"
TURN 570..573
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 579..581
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 583..585
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 589..597
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 600..602
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 605..612
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 613..615
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 616..621
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 622..628
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 633..645
/evidence="ECO:0007829|PDB:1LDJ"
TURN 646..648
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 652..654
/evidence="ECO:0007829|PDB:1LDK"
TURN 658..660
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 668..671
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 678..682
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 691..700
/evidence="ECO:0007829|PDB:1LDK"
HELIX 703..722
/evidence="ECO:0007829|PDB:3TDU"
STRAND 723..726
/evidence="ECO:0007829|PDB:3TDU"
HELIX 727..738
/evidence="ECO:0007829|PDB:3TDU"
TURN 739..741
/evidence="ECO:0007829|PDB:3TDU"
HELIX 746..758
/evidence="ECO:0007829|PDB:3TDU"
STRAND 761..765
/evidence="ECO:0007829|PDB:3TDU"
STRAND 768..774
/evidence="ECO:0007829|PDB:3TDU"
SEQUENCE 776 AA; 89679 MW; 6625A1FFA7799BBA CRC64;
MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA


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Related Genes :
[CUL5 VACM1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[Cul5 Vacm1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[CUL1] Cullin-1 (CUL-1)
[cul-1 lin-19 D2045.6] Cullin-1 (CUL-1) (Abnormal cell lineage protein 19)
[Cul1] Cullin-1 (CUL-1)
[RTT101 CUL8 YJL047C J1166] Cullin-8 (Cullin-C) (Regulator of Ty1 transposition protein 101)
[CUL1 At4g02570 T10P11.26] Cullin-1
[CUL3A CUL3 At1g26830 T2P11.2] Cullin-3A (AtCUL3a)
[CUL3 KIAA0617] Cullin-3 (CUL-3)
[Cul3] Cullin-3 (CUL-3)
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[CUL4A] Cullin-4A (CUL-4A)
[CUL4B KIAA0695] Cullin-4B (CUL-4B)
[CUL7 KIAA0076] Cullin-7 (CUL-7)
[Cul4a] Cullin-4A (CUL-4A)
[Cul7] Cullin-7 (CUL-7)
[Cul4b mKIAA0695] Cullin-4B (CUL-4B)
[CUL2] Cullin-2 (CUL-2)
[Cul3] Cullin-3
[DCUN1D1 DCN1 DCUN1L1 RP42 SCCRO] DCN1-like protein 1 (DCNL1) (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Squamous cell carcinoma-related oncogene)
[DCUN1D2 C13orf17 DCUN1L2] DCN1-like protein 2 (DCNL2) (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2)
[DCUN1D5 SCCRO5] DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)
[DCUN1D3 SCCRO3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) (Squamous cell carcinoma-related oncogene 3)
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Bibliography :
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