CUL1_HUMAN
ID CUL1_HUMAN Reviewed; 776 AA.
AC Q13616; D3DWG3; O60719; Q08AL6; Q8IYW1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
GN Name=CUL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8681378; DOI=10.1016/s0092-8674(00)81267-2;
RA Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.;
RT "cul-1 is required for cell cycle exit in C. elegans and identifies a novel
RT gene family.";
RL Cell 85:829-839(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9663463;
RA Michel J.J., Xiong Y.;
RT "Human CUL-1, but not other cullin family members, selectively interacts
RT with SKP1 to form a complex with SKP2 and cyclin A.";
RL Cell Growth Differ. 9:435-449(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RBX1, AND IDENTIFICATION IN SCF COMPLEX WITH RBX1; SKP1
RP AND SKP2.
RX PubMed=10230406; DOI=10.1016/s1097-2765(00)80481-5;
RA Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.;
RT "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze
RT the ubiquitination of I kappa B alpha.";
RL Mol. Cell 3:527-533(1999).
RN [8]
RP INTERACTION WITH RBX1 AND RNF7.
RX PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with an
RT associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [9]
RP NEDDYLATION AT LYS-720.
RX PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA Kato S., Tanaka K.;
RT "Covalent modification of all members of human cullin family proteins by
RT NEDD8.";
RL Oncogene 18:6829-6834(1999).
RN [10]
RP NEDDYLATION.
RX PubMed=10713156; DOI=10.1128/mcb.20.7.2326-2333.2000;
RA Read M.A., Brownell J.E., Gladysheva T.B., Hottelet M., Parent L.A.,
RA Coggins M.B., Pierce J.W., Podust V.N., Luo R.-S., Chau V.,
RA Palombella V.J.;
RT "Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent
RT ubiquitination of IkappaBalpha.";
RL Mol. Cell. Biol. 20:2326-2333(2000).
RN [11]
RP INTERACTION WITH RNF7.
RX PubMed=10851089; DOI=10.1038/sj.onc.1203635;
RA Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth,
RT but not for germination: chip profiling implicates its role in cell cycle
RT regulation.";
RL Oncogene 19:2855-2866(2000).
RN [12]
RP INTERACTION WITH COPS2.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [13]
RP INTERACTION WITH TIP120A.
RX PubMed=12504026; DOI=10.1016/s1097-2765(02)00784-0;
RA Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H.,
RA Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.;
RT "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF
RT ubiquitin E3 ligase complex.";
RL Mol. Cell 10:1519-1526(2002).
RN [14]
RP INTERACTION WITH TIP120A.
RX PubMed=12609982; DOI=10.1074/jbc.m213070200;
RA Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
RT "TIP120A associates with cullins and modulates ubiquitin ligase activity.";
RL J. Biol. Chem. 278:15905-15910(2003).
RN [15]
RP IDENTIFICATION IN THE SCF(FBXO7) COMPLEX.
RX PubMed=15145941; DOI=10.1074/jbc.m404950200;
RA Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
RT "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated
RT hepatoma up-regulated protein (HURP) proteolysis by a proline-rich
RT region.";
RL J. Biol. Chem. 279:32592-32602(2004).
RN [16]
RP RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, AND FUNCTION IN UBIQUITINATION
RP OF MYOD1.
RX PubMed=15531760; DOI=10.1074/jbc.m411346200;
RA Tintignac L.A., Lagirand J., Batonnet S., Sirri V., Leibovitch M.P.,
RA Leibovitch S.A.;
RT "Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase.";
RL J. Biol. Chem. 280:2847-2856(2005).
RN [17]
RP INTERACTION WITH GCM1, AND FUNCTION IN UBIQUITINATION OF GCM1.
RX PubMed=15640526; DOI=10.1074/jbc.m413986200;
RA Yang C.S., Yu C., Chuang H.C., Chang C.W., Chang G.D., Yao T.P., Chen H.;
RT "FBW2 targets GCMa to the ubiquitin-proteasome degradation system.";
RL J. Biol. Chem. 280:10083-10090(2005).
RN [18]
RP RECONSTITUTION OF THE SCF(FBXO25) COMPLEX.
RX PubMed=16714087; DOI=10.1016/j.bbagen.2006.03.020;
RA Maragno A.L., Baqui M.M., Gomes M.D.;
RT "FBXO25, an F-box protein homologue of atrogin-1, is not induced in
RT atrophying muscle.";
RL Biochim. Biophys. Acta 1760:966-972(2006).
RN [19]
RP IDENTIFICATION IN THE SCF(FBXO33) COMPLEX WITH SKP1; RBX1 AND FBXO33.
RX PubMed=16797541; DOI=10.1016/j.febslet.2006.06.023;
RA Lutz M., Wempe F., Bahr I., Zopf D., von Melchner H.;
RT "Proteasomal degradation of the multifunctional regulator YB-1 is mediated
RT by an F-Box protein induced during programmed cell death.";
RL FEBS Lett. 580:3921-3930(2006).
RN [20]
RP INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, AND INTERACTION WITH TRIM21.
RX PubMed=16880511; DOI=10.1128/mcb.01630-05;
RA Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
RA Krek W.;
RT "Regulation of p27 degradation and S-phase progression by Ro52 RING finger
RT protein.";
RL Mol. Cell. Biol. 26:5994-6004(2006).
RN [21]
RP SELF-ASSOCIATION.
RX PubMed=17254749; DOI=10.1016/j.cellsig.2006.12.002;
RA Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.;
RT "Characterization of cullin-based E3 ubiquitin ligases in intact mammalian
RT cells -- evidence for cullin dimerization.";
RL Cell. Signal. 19:1071-1080(2007).
RN [22]
RP IDENTIFICATION IN THE SCF(FBXO11) COMPLEX WITH SKP1; RBX1 AND FBXO11.
RX PubMed=17098746; DOI=10.1074/jbc.m609001200;
RA Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.;
RT "FBXO11 promotes the neddylation of p53 and inhibits its transcriptional
RT activity.";
RL J. Biol. Chem. 282:1797-1804(2007).
RN [23]
RP NEDDYLATION AT LYS-720.
RX PubMed=18805092; DOI=10.1016/j.cell.2008.07.022;
RA Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.;
RT "Structural insights into NEDD8 activation of cullin-RING ligases:
RT conformational control of conjugation.";
RL Cell 134:995-1006(2008).
RN [24]
RP INTERACTION WITH FBXO44; FBXO17 AND FBXO27, AND IDENTIFICATION IN
RP SCF-COMPLEX.
RX PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT "Diversity in tissue expression, substrate binding, and SCF complex
RT formation for a lectin family of ubiquitin ligases.";
RL J. Biol. Chem. 283:12717-12729(2008).
RN [25]
RP FUNCTION IN CHEK2 UBIQUITINATION, AND INTERACTION WITH CHEK2.
RX PubMed=18644861; DOI=10.1128/mcb.00821-08;
RA Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.;
RT "Regulation of Chk2 ubiquitination and signaling through
RT autophosphorylation of serine 379.";
RL Mol. Cell. Biol. 28:5874-5885(2008).
RN [26]
RP FUNCTION, AND INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=19679664; DOI=10.1074/jbc.m109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T.,
RA Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [27]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, AND DENEDDYLATION BY
RP EPSTEIN-BARR VIRUS BPLF1 (MICROBIAL INFECTION).
RX PubMed=20190741; DOI=10.1038/ncb2035;
RA Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M.,
RA Di Guglielmo C., Masucci M.G.;
RT "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication
RT by regulating the activity of cullin-RING ligases.";
RL Nat. Cell Biol. 12:351-361(2010).
RN [28]
RP IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
RX PubMed=20596027; DOI=10.1038/nature09140;
RA D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
RA Washburn M.P., Dynlacht B., Pagano M.;
RT "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through
RT CP110 degradation.";
RL Nature 466:138-142(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP IDENTIFICATION IN THE SCF(FBXW7) COMPLEX, FUNCTION, AND PATHWAY.
RX PubMed=22405651; DOI=10.1016/j.molcel.2012.02.005;
RA Tron A.E., Arai T., Duda D.M., Kuwabara H., Olszewski J.L., Fujiwara Y.,
RA Bahamon B.N., Signoretti S., Schulman B.A., DeCaprio J.A.;
RT "The glomuvenous malformation protein Glomulin binds Rbx1 and regulates
RT cullin RING ligase-mediated turnover of Fbw7.";
RL Mol. Cell 46:67-78(2012).
RN [31]
RP FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE SCF(FBXO11)
RP COMPLEX.
RX PubMed=22113614; DOI=10.1038/nature10688;
RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F.,
RA Chapuy B., Shipp M., Chiarle R., Pagano M.;
RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-
RT cell lymphomas.";
RL Nature 481:90-93(2012).
RN [32]
RP INTERACTION WITH ARIH1, AND NEDDYLATION.
RX PubMed=24076655; DOI=10.1038/emboj.2013.209;
RA Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A.,
RA Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.;
RT "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-
RT RING ligase complexes.";
RL EMBO J. 32:2848-2860(2013).
RN [33]
RP IDENTIFICATION IN THE SCF(FBXO9) COMPLEX, AND FUNCTION.
RX PubMed=23263282; DOI=10.1038/ncb2651;
RA Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C.,
RA Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M.,
RA Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.;
RT "SCF(Fbxo9) and CK2 direct the cellular response to growth factor
RT withdrawal via Tel2/Tti1 degradation and promote survival in multiple
RT myeloma.";
RL Nat. Cell Biol. 15:72-81(2013).
RN [34]
RP INTERACTION WITH COPS9.
RX PubMed=23776465; DOI=10.1371/journal.pone.0065285;
RA Ebina M., Tsuruta F., Katoh M.C., Kigoshi Y., Someya A., Chiba T.;
RT "Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization
RT through Nedd8 modification.";
RL PLoS ONE 8:E65285-E65285(2013).
RN [35]
RP FUNCTION IN UBIQUITINATION OF BCL2, AND IDENTIFICATION IN THE SCF(FBXO10)
RP COMPLEX.
RX PubMed=23431138; DOI=10.1073/pnas.1217271110;
RA Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W.,
RA Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D.,
RA Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S.,
RA Staudt L.M.;
RT "Related F-box proteins control cell death in Caenorhabditis elegans and
RT human lymphoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
RN [36]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA Bennett E.J., Schulman B.A.;
RT "Structural conservation of distinctive N-terminal acetylation-dependent
RT interactions across a family of mammalian NEDD8 ligation enzymes.";
RL Structure 21:42-53(2013).
RN [37]
RP INTERACTION WITH DCUN1D5.
RX PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
RA Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
RA Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
RT "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
RT and nuclear localization.";
RL Clin. Cancer Res. 20:372-381(2014).
RN [38]
RP INTERACTION WITH DCUN1D3.
RX PubMed=25349211; DOI=10.1074/jbc.m114.585505;
RA Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E.,
RA Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of
RT SCCRO (DCUN1D1).";
RL J. Biol. Chem. 289:34728-34742(2014).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [41]
RP FUNCTION.
RX PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004;
RA Man X., Megraw T.L., Lim Y.P.;
RT "Cep68 can be regulated by Nek2 and SCF complex.";
RL Eur. J. Cell Biol. 94:162-172(2015).
RN [42]
RP FUNCTION, IDENTIFICATION IN SCF(FBXW11) COMPLEX, AND INTERACTION WITH
RP CEP68.
RX PubMed=25503564; DOI=10.1038/ncb3076;
RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L.,
RA Washburn M.P., Pagano M.;
RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM
RT to allow centriole separation, disengagement and licensing.";
RL Nat. Cell Biol. 17:31-43(2015).
RN [43]
RP FUNCTION, INTERACTION WITH ARIH1, AND NEDDYLATION.
RX PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
RA Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L., Paulo J.A.,
RA de Jong A., Ovaa H., Alpi A.F., Harper J.W., Schulman B.A.;
RT "Two distinct types of E3 ligases work in unison to regulate substrate
RT ubiquitylation.";
RL Cell 166:1198-1214(2016).
RN [44]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX PubMed=26906416; DOI=10.1242/jcs.181784;
RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL J. Cell Sci. 129:1441-1454(2016).
RN [45]
RP INTERACTION WITH CCNF.
RX PubMed=26818844; DOI=10.1038/ncomms10530;
RA Walter D., Hoffmann S., Komseli E.S., Rappsilber J., Gorgoulis V.,
RA Soerensen C.S.;
RT "SCF(Cyclin F)-dependent degradation of CDC6 suppresses DNA re-
RT replication.";
RL Nat. Commun. 7:10530-10530(2016).
RN [46]
RP INTERACTION WITH NOTCH2.
RX PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
RA Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
RA Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
RA Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W., Inuzuka H.;
RT "NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
RT promote osteoporosis.";
RL Mol. Cell 68:645-658(2017).
RN [47]
RP INTERACTION WITH UBXN1.
RX PubMed=28152074; DOI=10.1371/journal.ppat.1006187;
RA Hu Y., O'Boyle K., Auer J., Raju S., You F., Wang P., Fikrig E.,
RA Sutton R.E.;
RT "Multiple UBXN family members inhibit retrovirus and lentivirus production
RT and canonical NFkappaBeta signaling by stabilizing IkappaBalpha.";
RL PLoS Pathog. 13:E1006187-E1006187(2017).
RN [48]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN C9L (MICROBIAL INFECTION).
RX PubMed=29444943; DOI=10.1128/jvi.00053-18;
RA Liu R., Moss B.;
RT "Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified
RT Antagonist of the Type I Interferon-Induced Antiviral State.";
RL J. Virol. 92:0-0(2018).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108 OF
RP RBX1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH RBX1;
RP SKP1 AND SKP2.
RX PubMed=11961546; DOI=10.1038/416703a;
RA Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
RA Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W.,
RA Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
RL Nature 416:703-709(2002).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CAND1 AND ROC1,
RP NEDDYLATION AT LYS-720, AND SUBUNIT.
RX PubMed=15537541; DOI=10.1016/j.cell.2004.10.019;
RA Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y.,
RA Zheng N.;
RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for
RT the assembly of the multisubunit cullin-dependent ubiquitin ligases.";
RL Cell 119:517-528(2004).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D1
RP AND UBE2M.
RX PubMed=21940857; DOI=10.1126/science.1209307;
RA Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.;
RT "N-terminal acetylation acts as an avidity enhancer within an
RT interconnected multiprotein complex.";
RL Science 334:674-678(2011).
RN [52] {ECO:0007744|PDB:4F52}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 411-690 IN COMPLEX WITH RBX1 AND
RP GLMN, AND SUBUNIT.
RX PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044;
RA Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J.,
RA Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.;
RT "Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase
RT through masking of its E2-binding surface.";
RL Mol. Cell 47:371-382(2012).
RN [53] {ECO:0007744|PDB:5V89}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D4.
RX PubMed=28581483; DOI=10.1038/nchembio.2386;
RA Scott D.C., Hammill J.T., Min J., Rhee D.Y., Connelly M., Sviderskiy V.O.,
RA Bhasin D., Chen Y., Ong S.S., Chai S.C., Goktug A.N., Huang G., Monda J.K.,
RA Low J., Kim H.S., Paulo J.A., Cannon J.R., Shelat A.A., Chen T.,
RA Kelsall I.R., Alpi A.F., Pagala V., Wang X., Peng J., Singh B.,
RA Harper J.W., Schulman B.A., Guy R.K.;
RT "Blocking an N-terminal acetylation-dependent protein interaction inhibits
RT an E3 ligase.";
RL Nat. Chem. Biol. 13:850-857(2017).
CC -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
CC F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
CC ubiquitination of proteins involved in cell cycle progression, signal
CC transduction and transcription. SCF complexes and ARIH1 collaborate in
CC tandem to mediate ubiquitination of target proteins (PubMed:27565346).
CC In the SCF complex, serves as a rigid scaffold that organizes the SKP1-
CC F-box protein and RBX1 subunits. May contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC E3 ubiquitin-protein ligase activity of the complex is dependent on the
CC neddylation of the cullin subunit and exchange of the substrate
CC recognition component is mediated by TIP120A/CAND1. The functional
CC specificity of the SCF complex depends on the F-box protein as
CC substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct
CC ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11)
CC directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs
CC ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and
CC probably NFKB2. SCF(BTRC) and/or SCF(FBXW11) direct ubiquitination of
CC CEP68 (PubMed:25704143, PubMed:25503564). SCF(SKP2) directs
CC ubiquitination of phosphorylated CDKN1B/p27kip and is involved in
CC regulation of G1/S transition. SCF(SKP2) directs ubiquitination of
CC ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and
CC TAL1. SCF(FBXW7) directs ubiquitination of CCNE1, NOTCH1 released notch
CC intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs
CC ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1.
CC SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33)
CC directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of
CC BCL6 and DTL but does not seem to direct ubiquitination of TP53.
CC SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-
CC 22'; the degradation frees the associated NFKB1-RELA dimer to
CC translocate into the nucleus and to activate transcription. SCF(CCNF)
CC directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct
CC ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of
CC TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.
CC {ECO:0000269|PubMed:15531760, ECO:0000269|PubMed:15640526,
CC ECO:0000269|PubMed:18644861, ECO:0000269|PubMed:19679664,
CC ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:22405651,
CC ECO:0000269|PubMed:23263282, ECO:0000269|PubMed:23431138,
CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25704143,
CC ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:9663463}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:22405651}.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-
CC box domain-containing protein as substrate-specific subunit
CC (PubMed:10230406, PubMed:15145941, PubMed:15531760, PubMed:16714087,
CC PubMed:16797541, PubMed:17098746, PubMed:18203720, PubMed:20596027,
CC PubMed:22405651, PubMed:22113614, PubMed:23263282, PubMed:23431138,
CC PubMed:25503564, PubMed:11961546, PubMed:22748924). Component of the
CC SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2)
CC complex containing SKP2, in which it interacts directly with SKP1, SKP2
CC and RBX1. Component of the SCF(FBXW2) complex containing FBXW2.
CC Component of the SCF(FBXO32) complex containing FBXO32. Component of
CC the probable SCF(FBXO7) complex containing FBXO7. Component of the
CC SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11)
CC complex containing FBXO11. Component of the SCF(FBXO25) complex
CC containing FBXO25. Component of the SCF(FBXO33) complex containing
CC FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4.
CC Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and
CC FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and
CC BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex
CC consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like
CC complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the
CC SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of
CC the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component
CC of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF
CC (PubMed:20596027). Interacts with CCNF (PubMed:26818844). Component of
CC the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3.
CC Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and
CC FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and
CC FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and
CC FBXW7 (PubMed:22405651). Interacts with CHEK2; mediates CHEK2
CC ubiquitination and regulates its function. Part of a complex with
CC TIP120A/CAND1 and RBX1. The unneddylated form interacts with
CC TIP120A/CAND1 and the interaction mediates the exchange of the F-box
CC substrate-specific subunit. Can self-associate. Interacts with FBXW8.
CC Interacts with RNF7. Interacts with CUL7; the interaction seems to be
CC mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2.
CC Interacts with UBE2M (PubMed:21940857). Identified in a complex with
CC RBX1 and GLMN (PubMed:22405651, PubMed:22748924). Interacts with CEP68
CC as part of the SCF(FBXW11) complex; the interaction is probably
CC mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT
CC (PubMed:25503564). Interacts (when neddylated) with ARIH1; leading to
CC activate the E3 ligase activity of ARIH1 (PubMed:24076655,
CC PubMed:27565346). Interacts with COPS9 isoform 2 (PubMed:23776465).
CC Interacts with UBXN1 (PubMed:28152074). Interacts with KAT7, probably
CC as part of an SCF complex; the interaction mediates KAT7 ubiquitination
CC (By similarity). Interacts with NOTCH2 (PubMed:29149593). Part of a
CC complex that contains DCUN1D5, CUL1 and RBX1; this complex is bridged
CC by CUL1 (PubMed:24192928). Interacts (unneddylated form) with DCUN1D1,
CC DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the
CC cullin neddylation (PubMed:24192928, PubMed:26906416, PubMed:23201271,
CC PubMed:21940857, PubMed:25349211, PubMed:28581483).
CC {ECO:0000250|UniProtKB:Q9WTX6, ECO:0000269|PubMed:10230406,
CC ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10851089,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:11961546,
CC ECO:0000269|PubMed:12504026, ECO:0000269|PubMed:12609982,
CC ECO:0000269|PubMed:15145941, ECO:0000269|PubMed:15531760,
CC ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:15640526,
CC ECO:0000269|PubMed:16714087, ECO:0000269|PubMed:16797541,
CC ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:17098746,
CC ECO:0000269|PubMed:18203720, ECO:0000269|PubMed:18644861,
CC ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:20596027,
CC ECO:0000269|PubMed:21940857, ECO:0000269|PubMed:22113614,
CC ECO:0000269|PubMed:22405651, ECO:0000269|PubMed:22748924,
CC ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:23263282,
CC ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:23776465,
CC ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:24192928,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:25503564,
CC ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:26906416,
CC ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:28152074,
CC ECO:0000269|PubMed:28581483, ECO:0000269|PubMed:29149593}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus BPLF1.
CC {ECO:0000269|PubMed:20190741}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Human adenovirus early
CC E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation
CC reaction of ubiquitin chains by the SCF(FBXW7) complex.
CC {ECO:0000269|PubMed:19679664}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC C9L. {ECO:0000269|PubMed:29444943}.
CC -!- INTERACTION:
CC Q13616; Q9Y4X5: ARIH1; NbExp=8; IntAct=EBI-359390, EBI-2514233;
CC Q13616; Q9Y297: BTRC; NbExp=11; IntAct=EBI-359390, EBI-307461;
CC Q13616; Q86VP6: CAND1; NbExp=33; IntAct=EBI-359390, EBI-456077;
CC Q13616; O60826: CCDC22; NbExp=3; IntAct=EBI-359390, EBI-3943153;
CC Q13616; P41002: CCNF; NbExp=5; IntAct=EBI-359390, EBI-1207574;
CC Q13616; Q8ND76: CCNY; NbExp=3; IntAct=EBI-359390, EBI-1049189;
CC Q13616; P49427: CDC34; NbExp=3; IntAct=EBI-359390, EBI-975634;
CC Q13616; P46527: CDKN1B; NbExp=2; IntAct=EBI-359390, EBI-519280;
CC Q13616; Q96EF6: FBXO17; NbExp=8; IntAct=EBI-359390, EBI-2510157;
CC Q13616; Q8NEZ5: FBXO22; NbExp=4; IntAct=EBI-359390, EBI-2510137;
CC Q13616; Q9UK99: FBXO3; NbExp=7; IntAct=EBI-359390, EBI-2509901;
CC Q13616; Q7Z6M2: FBXO33; NbExp=2; IntAct=EBI-359390, EBI-8555452;
CC Q13616; Q9UKT5: FBXO4; NbExp=3; IntAct=EBI-359390, EBI-960409;
CC Q13616; Q9NRD1: FBXO6; NbExp=3; IntAct=EBI-359390, EBI-3938499;
CC Q13616; Q9UKB1: FBXW11; NbExp=11; IntAct=EBI-359390, EBI-355189;
CC Q13616; Q9UKT8: FBXW2; NbExp=5; IntAct=EBI-359390, EBI-914727;
CC Q13616; Q969H0: FBXW7; NbExp=5; IntAct=EBI-359390, EBI-359574;
CC Q13616; P08238: HSP90AB1; NbExp=2; IntAct=EBI-359390, EBI-352572;
CC Q13616; Q00987: MDM2; NbExp=3; IntAct=EBI-359390, EBI-389668;
CC Q13616; O75586: MED6; NbExp=2; IntAct=EBI-359390, EBI-394624;
CC Q13616; Q15843: NEDD8; NbExp=23; IntAct=EBI-359390, EBI-716247;
CC Q13616; P62877: RBX1; NbExp=28; IntAct=EBI-359390, EBI-398523;
CC Q13616; P63208: SKP1; NbExp=17; IntAct=EBI-359390, EBI-307486;
CC Q13616; Q13309: SKP2; NbExp=15; IntAct=EBI-359390, EBI-456291;
CC Q13616; P61081: UBE2M; NbExp=5; IntAct=EBI-359390, EBI-1041660;
CC Q13616; O94888: UBXN7; NbExp=8; IntAct=EBI-359390, EBI-1993627;
CC Q13616; P67809: YBX1; NbExp=2; IntAct=EBI-359390, EBI-354065;
CC Q13616; Q8BFZ4: Fbxl21; Xeno; NbExp=3; IntAct=EBI-359390, EBI-6898235;
CC Q13616; Q8C4V4: Fbxl3; Xeno; NbExp=3; IntAct=EBI-359390, EBI-1266589;
CC Q13616; Q83730: m005R; Xeno; NbExp=5; IntAct=EBI-359390, EBI-6859930;
CC Q13616; P52491: UBC12; Xeno; NbExp=2; IntAct=EBI-359390, EBI-19772;
CC Q13616; Q6TVW2; Xeno; NbExp=5; IntAct=EBI-359390, EBI-15718527;
CC -!- TISSUE SPECIFICITY: Expressed in lung fibroblasts.
CC {ECO:0000269|PubMed:9663463}.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF and
CC prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN) complex (PubMed:10597293,
CC PubMed:10713156, PubMed:15537541, PubMed:18805092).
CC {ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:10713156,
CC ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:18805092,
CC ECO:0000269|PubMed:20190741, ECO:0000269|PubMed:24076655,
CC ECO:0000269|PubMed:27565346}.
CC -!- PTM: (Microbial infection) Deneddylated by Epstein-Barr virus BPLF1
CC leading to a S-phase-like environment that is required for efficient
CC replication of the viral genome (PubMed:20190741).
CC {ECO:0000269|PubMed:20190741}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; U58087; AAC50544.1; -; mRNA.
DR EMBL; AF062536; AAC36681.1; -; mRNA.
DR EMBL; BX537409; CAD97651.1; -; mRNA.
DR EMBL; AC005229; AAM49153.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80074.1; -; Genomic_DNA.
DR EMBL; BC125119; AAI25120.1; -; mRNA.
DR EMBL; BC125120; AAI25121.1; -; mRNA.
DR CCDS; CCDS34772.1; -.
DR RefSeq; NP_003583.2; NM_003592.2.
DR RefSeq; XP_005250117.1; XM_005250060.4.
DR RefSeq; XP_011514931.1; XM_011516629.2.
DR RefSeq; XP_011514932.1; XM_011516630.2.
DR RefSeq; XP_011514933.1; XM_011516631.2.
DR RefSeq; XP_011514934.1; XM_011516632.2.
DR PDB; 1LDJ; X-ray; 3.00 A; A=17-776.
DR PDB; 1LDK; X-ray; 3.10 A; A=15-410, B=411-776.
DR PDB; 1U6G; X-ray; 3.10 A; A=1-776.
DR PDB; 3RTR; X-ray; 3.21 A; A/C/E/G=411-776.
DR PDB; 3TDU; X-ray; 1.50 A; C/D=702-776.
DR PDB; 3TDZ; X-ray; 2.00 A; C/D=702-776.
DR PDB; 4F52; X-ray; 3.00 A; A/C=411-690.
DR PDB; 4P5O; X-ray; 3.11 A; A/C=411-776.
DR PDB; 5V89; X-ray; 1.55 A; C=702-776.
DR PDB; 6TTU; EM; 3.70 A; C=1-776.
DR PDB; 6WCQ; EM; 8.50 A; D=1-434.
DR PDB; 7B5L; EM; 3.80 A; C=1-776.
DR PDB; 7B5M; EM; 3.91 A; C=1-776.
DR PDB; 7B5N; EM; 3.60 A; C=1-776.
DR PDB; 7B5R; EM; 3.80 A; C=1-776.
DR PDB; 7B5S; EM; 3.60 A; C=1-776.
DR PDBsum; 1LDJ; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1U6G; -.
DR PDBsum; 3RTR; -.
DR PDBsum; 3TDU; -.
DR PDBsum; 3TDZ; -.
DR PDBsum; 4F52; -.
DR PDBsum; 4P5O; -.
DR PDBsum; 5V89; -.
DR PDBsum; 6TTU; -.
DR PDBsum; 6WCQ; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5N; -.
DR PDBsum; 7B5R; -.
DR PDBsum; 7B5S; -.
DR AlphaFoldDB; Q13616; -.
DR SMR; Q13616; -.
DR BioGRID; 114032; 850.
DR CORUM; Q13616; -.
DR DIP; DIP-17013N; -.
DR IntAct; Q13616; 569.
DR MINT; Q13616; -.
DR STRING; 9606.ENSP00000326804; -.
DR ChEMBL; CHEMBL3758068; -.
DR iPTMnet; Q13616; -.
DR MetOSite; Q13616; -.
DR PhosphoSitePlus; Q13616; -.
DR BioMuta; CUL1; -.
DR DMDM; 19863257; -.
DR EPD; Q13616; -.
DR jPOST; Q13616; -.
DR MassIVE; Q13616; -.
DR MaxQB; Q13616; -.
DR PaxDb; Q13616; -.
DR PeptideAtlas; Q13616; -.
DR PRIDE; Q13616; -.
DR ProteomicsDB; 59604; -.
DR Antibodypedia; 3630; 550 antibodies from 42 providers.
DR DNASU; 8454; -.
DR Ensembl; ENST00000325222.9; ENSP00000326804.3; ENSG00000055130.18.
DR Ensembl; ENST00000409469.5; ENSP00000387160.1; ENSG00000055130.18.
DR Ensembl; ENST00000602748.5; ENSP00000473318.1; ENSG00000055130.18.
DR Ensembl; ENST00000662716.1; ENSP00000499277.1; ENSG00000055130.18.
DR Ensembl; ENST00000663044.1; ENSP00000499398.1; ENSG00000055130.18.
DR Ensembl; ENST00000665936.1; ENSP00000499255.1; ENSG00000055130.18.
DR GeneID; 8454; -.
DR KEGG; hsa:8454; -.
DR MANE-Select; ENST00000325222.9; ENSP00000326804.3; NM_003592.3; NP_003583.2.
DR UCSC; uc003wey.4; human.
DR CTD; 8454; -.
DR DisGeNET; 8454; -.
DR GeneCards; CUL1; -.
DR HGNC; HGNC:2551; CUL1.
DR HPA; ENSG00000055130; Low tissue specificity.
DR MIM; 603134; gene.
DR neXtProt; NX_Q13616; -.
DR OpenTargets; ENSG00000055130; -.
DR PharmGKB; PA27047; -.
DR VEuPathDB; HostDB:ENSG00000055130; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000154774; -.
DR InParanoid; Q13616; -.
DR OMA; GVYTAVH; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q13616; -.
DR TreeFam; TF101151; -.
DR BioCyc; MetaCyc:ENSG00000055130-MON; -.
DR PathwayCommons; Q13616; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q13616; -.
DR SIGNOR; Q13616; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8454; 495 hits in 1134 CRISPR screens.
DR ChiTaRS; CUL1; human.
DR EvolutionaryTrace; Q13616; -.
DR GeneWiki; CUL1; -.
DR GenomeRNAi; 8454; -.
DR Pharos; Q13616; Tbio.
DR PRO; PR:Q13616; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q13616; protein.
DR Bgee; ENSG00000055130; Expressed in secondary oocyte and 192 other tissues.
DR ExpressionAtlas; Q13616; baseline and differential.
DR Genevisible; Q13616; HS.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR IDEAL; IID00133; -.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction; Isopeptide bond; Methylation;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..776
FT /note="Cullin-1"
FT /id="PRO_0000119787"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 720
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000269|PubMed:10597293,
FT ECO:0000269|PubMed:15537541, ECO:0000269|PubMed:18805092"
FT CONFLICT 59..82
FT /note="Missing (in Ref. 1; AAC50544)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="K -> R (in Ref. 3; CAD97651)"
FT /evidence="ECO:0000305"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1U6G"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 87..105
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1U6G"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 115..136
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1LDK"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 274..279
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 333..355
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 363..382
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 439..453
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 459..475
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 482..525
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 532..541
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 560..569
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 605..612
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 616..621
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 633..645
FT /evidence="ECO:0007829|PDB:1LDJ"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:1LDK"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 668..671
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 691..700
FT /evidence="ECO:0007829|PDB:1LDK"
FT HELIX 703..722
FT /evidence="ECO:0007829|PDB:3TDU"
FT STRAND 723..726
FT /evidence="ECO:0007829|PDB:3TDU"
FT HELIX 727..738
FT /evidence="ECO:0007829|PDB:3TDU"
FT TURN 739..741
FT /evidence="ECO:0007829|PDB:3TDU"
FT HELIX 746..758
FT /evidence="ECO:0007829|PDB:3TDU"
FT STRAND 761..765
FT /evidence="ECO:0007829|PDB:3TDU"
FT STRAND 768..774
FT /evidence="ECO:0007829|PDB:3TDU"
SQ 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
