Full text data of CUL1
CUL1
[Confidence: high (present in two of the MS resources)]
Cullin-1; CUL-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cullin-1; CUL-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00014310
IPI00014310 Splice Isoform 1 Of Cullin homolog 1 Ubiquitin conjugation; third step, Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination of proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic GIYEIYSLALVTWR found at its expected molecular weight found at molecular weight
IPI00014310 Splice Isoform 1 Of Cullin homolog 1 Ubiquitin conjugation; third step, Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination of proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic GIYEIYSLALVTWR found at its expected molecular weight found at molecular weight
UniProt
Q13616
ID CUL1_HUMAN Reviewed; 776 AA.
AC Q13616; D3DWG3; O60719; Q08AL6; Q8IYW1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
GN Name=CUL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT novel 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
RT interacts 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RP SKP1 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
RT catalyze 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
RT an 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
RT by 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.,
RA Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell
RT growth, but not for germination: chip profiling implicates its role in
RT cell cycle 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
RT 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-
RT phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a
RT proline-rich region.";
RL J. Biol. Chem. 279:32592-32602(2004).
RN [16]
RP RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, AND FUNCTION IN
RP UBIQUITINATION 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.,
RA 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
RT mediated 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
RP 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
RT finger 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
RT mammalian 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
RT transcriptional activity.";
RL J. Biol. Chem. 282:1797-1804(2007).
RN [23]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [24]
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 [25]
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 [26]
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 [27]
RP FUNCTION, AND INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
RX PubMed=19679664; DOI=10.1074/jbc.M109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I.,
RA Oda T., Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [28]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, AND DENEDDYLATION BY
RP EPSTEIN-BARR VIRUS BPLF1.
RX PubMed=20190741; DOI=10.1038/ncb2035;
RA Gastaldello S., Hildebrand S., Faridani O., Callegari S.,
RA Palmkvist M., Di Guglielmo C., Masucci M.G.;
RT "A deneddylase encoded by Epstein-Barr virus promotes viral DNA
RT replication by regulating the activity of cullin-RING ligases.";
RL Nat. Cell Biol. 12:351-361(2010).
RN [29]
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
RT through CP110 degradation.";
RL Nature 466:138-142(2010).
RN [30]
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.,
RA Buerckstuemmer T., 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 [31]
RP FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE
RP SCF(FBXO11) COMPLEX.
RX PubMed=22113614; DOI=10.1038/nature10688;
RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C.,
RA di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.;
RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse
RT large B-cell lymphomas.";
RL Nature 481:90-93(2012).
RN [32]
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.,
RA Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B.,
RA 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 [33]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108
RP OF RBX1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH
RP RBX1; 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.,
RA Conaway J.W., Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase
RT complex.";
RL Nature 416:703-709(2002).
RN [34]
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.,
RA Xiong Y., Zheng N.;
RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
RT mechanisms for the assembly of the multisubunit cullin-dependent
RT ubiquitin ligases.";
RL Cell 119:517-528(2004).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH
RP DCUN1D1 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).
CC -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-
CC CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which
CC mediate the ubiquitination of proteins involved in cell cycle
CC progression, signal transduction and transcription. In the SCF
CC complex, serves as a rigid scaffold that organizes the SKP1-F-box
CC protein and RBX1 subunits. May contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme.
CC The E3 ubiquitin-protein ligase activity of the complex is
CC dependent on the neddylation of the cullin subunit and exchange of
CC the substrate recognition component is mediated by TIP120A/CAND1.
CC The functional specificity of the SCF complex depends on the F-box
CC protein as substrate recognition component. SCF(BTRC) and
CC SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt
CC signaling. SCF(FBXW11) directs ubiquitination of phosphorylated
CC NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4,
CC SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. 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 cyclin E, NOTCH1
CC released notch intracellular domain (NICD), and probably PSEN1.
CC SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
CC ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of
CC BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1.
CC SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not
CC seem to direct ubiquitination of TP53. SCF(BTRC) mediates the
CC ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation
CC frees the associated NFKB1-RELA dimer to translocate into the
CC nucleus and to activate transcription. SCF(CCNF) directs
CC ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct
CC ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination
CC of TTI1 and TELO2.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable
CC F-box domain-containing protein as substrate-specific subunit.
CC Component of the SCF(FBXW11) complex containing FBXW11. Component
CC of the SCF(SKP2) complex containing SKP2, in which it interacts
CC directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2)
CC complex containing FBXw2. Component of the SCF(FBXO32) complex
CC containing FBXO32. Component of the probable SCF(FBXO7) complex
CC containing FBXO7. Component of the SCF(FBXO11) complex containing
CC FBXO11. Component of the SCF(FBXO25) complex containing FBXO25.
CC Component of the SCF(FBXO33) complex containing FBXO33. Component
CC of the probable SCF(FBXO4) complex containing FBXO4. Component of
CC the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44.
CC Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and
CC BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF
CC complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a
CC SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2.
CC Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and
CC FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1,
CC CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of
CC CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex
CC composed of CUL1, SKP1, RBX1 and FBXL3. Component of the
CC SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21.
CC Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and
CC FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1
CC and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and
CC regulates its function. Part of a complex with TIP120A/CAND1 and
CC RBX1. The unneddylated form interacts with TIP120A/CAND1 and the
CC interaction mediates the exchange of the F-box substrate-specific
CC subunit. Can self-associate. Interacts with FBXW8. Interacts with
CC RNF7. Interacts with CUL7; the interaction seems to be mediated by
CC FBXW8. Interacts with TRIM21. Interacts with COPS2. Interacts with
CC Epstein-Barr virus BPLF1. Interacts with human adenovirus early
CC E1A protein; this interaction inhibits RBX1-CUL1-dependent
CC elongation reaction of ubiquitin chains by the SCF(FBXW7) complex.
CC -!- INTERACTION:
CC Q9Y297:BTRC; NbExp=5; IntAct=EBI-359390, EBI-307461;
CC Q86VP6:CAND1; NbExp=19; IntAct=EBI-359390, EBI-456077;
CC P49427:CDC34; NbExp=3; IntAct=EBI-359390, EBI-975634;
CC Q9UKT5:FBXO4; NbExp=2; IntAct=EBI-359390, EBI-960409;
CC Q83730:m005R (xeno); NbExp=5; IntAct=EBI-359390, EBI-6859930;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-359390, EBI-389668;
CC Q15843:NEDD8; NbExp=5; IntAct=EBI-359390, EBI-716247;
CC P62877:RBX1; NbExp=12; IntAct=EBI-359390, EBI-398523;
CC P63208:SKP1; NbExp=9; IntAct=EBI-359390, EBI-307486;
CC Q13309:SKP2; NbExp=9; IntAct=EBI-359390, EBI-456291;
CC P61081:UBE2M; NbExp=2; IntAct=EBI-359390, EBI-1041660;
CC -!- TISSUE SPECIFICITY: Expressed in lung fibroblasts.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF
CC and prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN) complex. Deneddylated
CC by Epstein-Barr virus BPLF1 leading to a S-phase-like environment
CC that is required for efficient replication of the viral genome.
CC -!- SIMILARITY: Belongs to the cullin family.
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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 RefSeq; NP_003583.2; NM_003592.2.
DR RefSeq; XP_005250117.1; XM_005250060.1.
DR RefSeq; XP_005250118.1; XM_005250061.1.
DR UniGene; Hs.146806; -.
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 PDBsum; 1LDJ; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1U6G; -.
DR PDBsum; 3RTR; -.
DR PDBsum; 3TDU; -.
DR PDBsum; 3TDZ; -.
DR PDBsum; 4F52; -.
DR ProteinModelPortal; Q13616; -.
DR SMR; Q13616; 17-776.
DR DIP; DIP-17013N; -.
DR IntAct; Q13616; 59.
DR MINT; MINT-120495; -.
DR STRING; 9606.ENSP00000326804; -.
DR PhosphoSite; Q13616; -.
DR DMDM; 19863257; -.
DR PaxDb; Q13616; -.
DR PeptideAtlas; Q13616; -.
DR PRIDE; Q13616; -.
DR DNASU; 8454; -.
DR Ensembl; ENST00000325222; ENSP00000326804; ENSG00000055130.
DR Ensembl; ENST00000409469; ENSP00000387160; ENSG00000055130.
DR Ensembl; ENST00000602748; ENSP00000473318; ENSG00000055130.
DR GeneID; 8454; -.
DR KEGG; hsa:8454; -.
DR UCSC; uc003wey.3; human.
DR CTD; 8454; -.
DR GeneCards; GC07P148395; -.
DR HGNC; HGNC:2551; CUL1.
DR HPA; CAB002676; -.
DR MIM; 603134; gene.
DR neXtProt; NX_Q13616; -.
DR PharmGKB; PA27047; -.
DR eggNOG; COG5647; -.
DR HOGENOM; HOG000176713; -.
DR HOVERGEN; HBG106177; -.
DR InParanoid; Q13616; -.
DR KO; K03347; -.
DR OMA; YEIYQLA; -.
DR OrthoDB; EOG7X3QQG; -.
DR PhylomeDB; Q13616; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13616; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; CUL1; human.
DR EvolutionaryTrace; Q13616; -.
DR GeneWiki; CUL1; -.
DR GenomeRNAi; 8454; -.
DR NextBio; 31638; -.
DR PRO; PR:Q13616; -.
DR ArrayExpress; Q13616; -.
DR Bgee; Q13616; -.
DR CleanEx; HS_CUL1; -.
DR Genevestigator; Q13616; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; IEA:Ensembl.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
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 InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 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; Complete proteome; Host-virus interaction;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 776 Cullin-1.
FT /FTId=PRO_0000119787.
FT CROSSLNK 708 708 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 720 720 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in NEDD8).
FT CONFLICT 59 82 Missing (in Ref. 1; AAC50544).
FT CONFLICT 726 726 K -> R (in Ref. 3; CAD97651).
FT HELIX 18 31
FT TURN 32 34
FT HELIX 39 52
FT HELIX 87 105
FT TURN 106 109
FT TURN 111 114
FT HELIX 115 136
FT HELIX 138 143
FT STRAND 144 146
FT HELIX 159 165
FT HELIX 168 171
FT TURN 172 177
FT HELIX 178 187
FT TURN 188 190
FT HELIX 199 210
FT TURN 211 213
FT STRAND 215 219
FT HELIX 226 231
FT HELIX 233 254
FT HELIX 261 273
FT TURN 274 279
FT STRAND 281 284
FT HELIX 285 295
FT STRAND 296 300
FT HELIX 301 312
FT HELIX 318 328
FT HELIX 333 355
FT HELIX 359 361
FT HELIX 363 382
FT TURN 383 387
FT HELIX 389 404
FT HELIX 407 412
FT HELIX 417 430
FT HELIX 439 453
FT HELIX 459 475
FT HELIX 482 525
FT TURN 526 528
FT STRAND 532 541
FT TURN 542 544
FT HELIX 557 559
FT HELIX 560 569
FT TURN 570 573
FT STRAND 579 581
FT HELIX 583 585
FT STRAND 589 597
FT STRAND 600 602
FT HELIX 605 612
FT HELIX 613 615
FT STRAND 616 621
FT HELIX 622 628
FT HELIX 633 645
FT TURN 646 648
FT STRAND 652 654
FT TURN 658 660
FT STRAND 668 671
FT STRAND 678 682
FT HELIX 691 700
FT HELIX 703 722
FT STRAND 723 726
FT HELIX 727 738
FT TURN 739 741
FT HELIX 746 758
FT STRAND 761 765
FT STRAND 768 774
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
//
ID CUL1_HUMAN Reviewed; 776 AA.
AC Q13616; D3DWG3; O60719; Q08AL6; Q8IYW1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Cullin-1;
DE Short=CUL-1;
GN Name=CUL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT novel 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
RT interacts 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
RP SKP1 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
RT catalyze 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
RT an 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
RT by 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.,
RA Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell
RT growth, but not for germination: chip profiling implicates its role in
RT cell cycle 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
RT 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-
RT phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a
RT proline-rich region.";
RL J. Biol. Chem. 279:32592-32602(2004).
RN [16]
RP RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, AND FUNCTION IN
RP UBIQUITINATION 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.,
RA 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
RT mediated 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
RP 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
RT finger 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
RT mammalian 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
RT transcriptional activity.";
RL J. Biol. Chem. 282:1797-1804(2007).
RN [23]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [24]
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 [25]
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 [26]
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 [27]
RP FUNCTION, AND INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
RX PubMed=19679664; DOI=10.1074/jbc.M109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I.,
RA Oda T., Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [28]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, AND DENEDDYLATION BY
RP EPSTEIN-BARR VIRUS BPLF1.
RX PubMed=20190741; DOI=10.1038/ncb2035;
RA Gastaldello S., Hildebrand S., Faridani O., Callegari S.,
RA Palmkvist M., Di Guglielmo C., Masucci M.G.;
RT "A deneddylase encoded by Epstein-Barr virus promotes viral DNA
RT replication by regulating the activity of cullin-RING ligases.";
RL Nat. Cell Biol. 12:351-361(2010).
RN [29]
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
RT through CP110 degradation.";
RL Nature 466:138-142(2010).
RN [30]
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.,
RA Buerckstuemmer T., 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 [31]
RP FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE
RP SCF(FBXO11) COMPLEX.
RX PubMed=22113614; DOI=10.1038/nature10688;
RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C.,
RA di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.;
RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse
RT large B-cell lymphomas.";
RL Nature 481:90-93(2012).
RN [32]
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.,
RA Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B.,
RA 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 [33]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108
RP OF RBX1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH
RP RBX1; 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.,
RA Conaway J.W., Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase
RT complex.";
RL Nature 416:703-709(2002).
RN [34]
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.,
RA Xiong Y., Zheng N.;
RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
RT mechanisms for the assembly of the multisubunit cullin-dependent
RT ubiquitin ligases.";
RL Cell 119:517-528(2004).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH
RP DCUN1D1 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).
CC -!- FUNCTION: Core component of multiple cullin-RING-based SCF (SKP1-
CC CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which
CC mediate the ubiquitination of proteins involved in cell cycle
CC progression, signal transduction and transcription. In the SCF
CC complex, serves as a rigid scaffold that organizes the SKP1-F-box
CC protein and RBX1 subunits. May contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme.
CC The E3 ubiquitin-protein ligase activity of the complex is
CC dependent on the neddylation of the cullin subunit and exchange of
CC the substrate recognition component is mediated by TIP120A/CAND1.
CC The functional specificity of the SCF complex depends on the F-box
CC protein as substrate recognition component. SCF(BTRC) and
CC SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt
CC signaling. SCF(FBXW11) directs ubiquitination of phosphorylated
CC NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4,
CC SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. 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 cyclin E, NOTCH1
CC released notch intracellular domain (NICD), and probably PSEN1.
CC SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
CC ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of
CC BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1.
CC SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not
CC seem to direct ubiquitination of TP53. SCF(BTRC) mediates the
CC ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation
CC frees the associated NFKB1-RELA dimer to translocate into the
CC nucleus and to activate transcription. SCF(CCNF) directs
CC ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct
CC ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination
CC of TTI1 and TELO2.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable
CC F-box domain-containing protein as substrate-specific subunit.
CC Component of the SCF(FBXW11) complex containing FBXW11. Component
CC of the SCF(SKP2) complex containing SKP2, in which it interacts
CC directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2)
CC complex containing FBXw2. Component of the SCF(FBXO32) complex
CC containing FBXO32. Component of the probable SCF(FBXO7) complex
CC containing FBXO7. Component of the SCF(FBXO11) complex containing
CC FBXO11. Component of the SCF(FBXO25) complex containing FBXO25.
CC Component of the SCF(FBXO33) complex containing FBXO33. Component
CC of the probable SCF(FBXO4) complex containing FBXO4. Component of
CC the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44.
CC Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and
CC BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF
CC complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a
CC SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2.
CC Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and
CC FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1,
CC CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of
CC CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex
CC composed of CUL1, SKP1, RBX1 and FBXL3. Component of the
CC SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21.
CC Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and
CC FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1
CC and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and
CC regulates its function. Part of a complex with TIP120A/CAND1 and
CC RBX1. The unneddylated form interacts with TIP120A/CAND1 and the
CC interaction mediates the exchange of the F-box substrate-specific
CC subunit. Can self-associate. Interacts with FBXW8. Interacts with
CC RNF7. Interacts with CUL7; the interaction seems to be mediated by
CC FBXW8. Interacts with TRIM21. Interacts with COPS2. Interacts with
CC Epstein-Barr virus BPLF1. Interacts with human adenovirus early
CC E1A protein; this interaction inhibits RBX1-CUL1-dependent
CC elongation reaction of ubiquitin chains by the SCF(FBXW7) complex.
CC -!- INTERACTION:
CC Q9Y297:BTRC; NbExp=5; IntAct=EBI-359390, EBI-307461;
CC Q86VP6:CAND1; NbExp=19; IntAct=EBI-359390, EBI-456077;
CC P49427:CDC34; NbExp=3; IntAct=EBI-359390, EBI-975634;
CC Q9UKT5:FBXO4; NbExp=2; IntAct=EBI-359390, EBI-960409;
CC Q83730:m005R (xeno); NbExp=5; IntAct=EBI-359390, EBI-6859930;
CC Q00987:MDM2; NbExp=3; IntAct=EBI-359390, EBI-389668;
CC Q15843:NEDD8; NbExp=5; IntAct=EBI-359390, EBI-716247;
CC P62877:RBX1; NbExp=12; IntAct=EBI-359390, EBI-398523;
CC P63208:SKP1; NbExp=9; IntAct=EBI-359390, EBI-307486;
CC Q13309:SKP2; NbExp=9; IntAct=EBI-359390, EBI-456291;
CC P61081:UBE2M; NbExp=2; IntAct=EBI-359390, EBI-1041660;
CC -!- TISSUE SPECIFICITY: Expressed in lung fibroblasts.
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF
CC and prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN) complex. Deneddylated
CC by Epstein-Barr virus BPLF1 leading to a S-phase-like environment
CC that is required for efficient replication of the viral genome.
CC -!- SIMILARITY: Belongs to the cullin family.
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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 RefSeq; NP_003583.2; NM_003592.2.
DR RefSeq; XP_005250117.1; XM_005250060.1.
DR RefSeq; XP_005250118.1; XM_005250061.1.
DR UniGene; Hs.146806; -.
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 PDBsum; 1LDJ; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1U6G; -.
DR PDBsum; 3RTR; -.
DR PDBsum; 3TDU; -.
DR PDBsum; 3TDZ; -.
DR PDBsum; 4F52; -.
DR ProteinModelPortal; Q13616; -.
DR SMR; Q13616; 17-776.
DR DIP; DIP-17013N; -.
DR IntAct; Q13616; 59.
DR MINT; MINT-120495; -.
DR STRING; 9606.ENSP00000326804; -.
DR PhosphoSite; Q13616; -.
DR DMDM; 19863257; -.
DR PaxDb; Q13616; -.
DR PeptideAtlas; Q13616; -.
DR PRIDE; Q13616; -.
DR DNASU; 8454; -.
DR Ensembl; ENST00000325222; ENSP00000326804; ENSG00000055130.
DR Ensembl; ENST00000409469; ENSP00000387160; ENSG00000055130.
DR Ensembl; ENST00000602748; ENSP00000473318; ENSG00000055130.
DR GeneID; 8454; -.
DR KEGG; hsa:8454; -.
DR UCSC; uc003wey.3; human.
DR CTD; 8454; -.
DR GeneCards; GC07P148395; -.
DR HGNC; HGNC:2551; CUL1.
DR HPA; CAB002676; -.
DR MIM; 603134; gene.
DR neXtProt; NX_Q13616; -.
DR PharmGKB; PA27047; -.
DR eggNOG; COG5647; -.
DR HOGENOM; HOG000176713; -.
DR HOVERGEN; HBG106177; -.
DR InParanoid; Q13616; -.
DR KO; K03347; -.
DR OMA; YEIYQLA; -.
DR OrthoDB; EOG7X3QQG; -.
DR PhylomeDB; Q13616; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13616; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; CUL1; human.
DR EvolutionaryTrace; Q13616; -.
DR GeneWiki; CUL1; -.
DR GenomeRNAi; 8454; -.
DR NextBio; 31638; -.
DR PRO; PR:Q13616; -.
DR ArrayExpress; Q13616; -.
DR Bgee; Q13616; -.
DR CleanEx; HS_CUL1; -.
DR Genevestigator; Q13616; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0009887; P:organ morphogenesis; IEA:Ensembl.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
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 InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 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; Complete proteome; Host-virus interaction;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1 776 Cullin-1.
FT /FTId=PRO_0000119787.
FT CROSSLNK 708 708 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 720 720 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in NEDD8).
FT CONFLICT 59 82 Missing (in Ref. 1; AAC50544).
FT CONFLICT 726 726 K -> R (in Ref. 3; CAD97651).
FT HELIX 18 31
FT TURN 32 34
FT HELIX 39 52
FT HELIX 87 105
FT TURN 106 109
FT TURN 111 114
FT HELIX 115 136
FT HELIX 138 143
FT STRAND 144 146
FT HELIX 159 165
FT HELIX 168 171
FT TURN 172 177
FT HELIX 178 187
FT TURN 188 190
FT HELIX 199 210
FT TURN 211 213
FT STRAND 215 219
FT HELIX 226 231
FT HELIX 233 254
FT HELIX 261 273
FT TURN 274 279
FT STRAND 281 284
FT HELIX 285 295
FT STRAND 296 300
FT HELIX 301 312
FT HELIX 318 328
FT HELIX 333 355
FT HELIX 359 361
FT HELIX 363 382
FT TURN 383 387
FT HELIX 389 404
FT HELIX 407 412
FT HELIX 417 430
FT HELIX 439 453
FT HELIX 459 475
FT HELIX 482 525
FT TURN 526 528
FT STRAND 532 541
FT TURN 542 544
FT HELIX 557 559
FT HELIX 560 569
FT TURN 570 573
FT STRAND 579 581
FT HELIX 583 585
FT STRAND 589 597
FT STRAND 600 602
FT HELIX 605 612
FT HELIX 613 615
FT STRAND 616 621
FT HELIX 622 628
FT HELIX 633 645
FT TURN 646 648
FT STRAND 652 654
FT TURN 658 660
FT STRAND 668 671
FT STRAND 678 682
FT HELIX 691 700
FT HELIX 703 722
FT STRAND 723 726
FT HELIX 727 738
FT TURN 739 741
FT HELIX 746 758
FT STRAND 761 765
FT STRAND 768 774
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
//
MIM
603134
*RECORD*
*FIELD* NO
603134
*FIELD* TI
*603134 CULLIN 1; CUL1
*FIELD* TX
CLONING
Kipreos et al. (1996) found that mutations in the cullin-1 (cul1) gene
read moreof C. elegans cause hyperplasia of all tissues. They determined that
cul1 is a negative regulator of the cell cycle; in cul1 mutants, the
G1-to-S-phase progression is accelerated, overriding mechanisms for
mitotic arrest and producing abnormally small cells. Searches of EST
databases revealed that cul1 is a member of a conserved gene family,
with at least 5 members in nematodes, 6 in humans, and 3 in S.
cerevisiae. Human CUL1 is an ortholog of nematode cul1.
GENE FUNCTION
Michel and Xiong (1998) stated that CUL1 has homology to yeast Cdc53,
which is part of a complex known as SCF that mediates the
ubiquitin-dependent degradation of G1 cycles and cyclin-dependent kinase
inhibitors. SCF complexes are composed of SKP1 (601434), Cdc53, and an F
box-containing protein, which may confer substrate specificity. These
authors found that interaction of the predicted 776-amino acid human
CUL1 protein with SKP1 is mediated through the N-terminal domains of
both proteins. Immunoprecipitation studies and Western blot analysis
revealed that the steady-state levels of both CUL1 and SKP1, as well as
their association with one another, remain relatively constant
throughout the cell cycle and in postmitotic cells. However, none of the
other human cullins tested interacted with SKP1. Michel and Xiong (1998)
determined that via SKP1, CUL1 forms a complex with SKP2 (601436), an F
box-containing protein, and cyclin A (123835). The authors concluded
that the SCF proteolytic pathway is evolutionarily conserved and is used
by mammalian CUL1, while the other cullin proteins may use a
SKP1/F-box-independent pathway to mediate protein degradation.
Maniatis (1999) reviewed the work of Winston et al. (1999) and others
concerning the SCF ubiquitin ligase complex. CUL1 acts as a scaffold for
SKP1 and the F-box-containing BTRC protein (603482) in the SCF complex,
which regulates the function of nuclear factor kappa-B (see 164011) and
beta-catenin (see 116806).
Yu et al. (1998) reported studies suggesting that the p19 (SKP1)/p45
(SKP2)/CUL1 complex is likely to function as a conserved ubiquitin E3
enzyme that regulates the mammalian G1/S transition by specifically
targeting mammalian G1 cell cycle regulators, such as p21 and cyclin D
proteins, for ubiquitin-dependent degradation.
The sequential timing of cell cycle transitions is primarily governed by
the availability and activity of key cell cycle proteins. Studies in
yeast identified a class of ubiquitin ligases (E3 enzymes) called SCF
complexes, which regulate the abundance of proteins that promote and
inhibit cell cycle progression at the transition between G1 and S
phases. SCF complexes consist of 3 invariable components, SKP1, CUL1
(CDC53 in yeast), and RBX1 (603814), and a variable F-box protein that
recruits a specific cellular protein to the ubiquitin pathway for
degradation. To study the role of CUL1 in mammalian development and cell
cycle regulation, Dealy et al. (1999) generated mice deficient for Cul1
and analyzed null embryos and heterozygous cell lines. They showed that
Cul1 is required for early mouse development and that Cul1 mutants fail
to regulate the abundance of the G1 cyclin, cyclin E (CCNE1; 123837),
during embryogenesis.
COP9 signalosome cleaves the ubiquitin-like protein NEDD8 (603171) from
the CUL1 subunit of SCF ubiquitin ligases. Cope et al. (2002) found that
the JAB1/MPN domain metalloenzyme (JAMM) motif in the JAB1/COPS5
(604850) subunit underlies the COP9 signalosome's NEDD8 isopeptidase
activity. The JAMM motif consists of a his-X-his-X(10)-asp motif (where
X indicates any residue) accompanied by an upstream glutamate. The JAMM
motif is found in proteins from archaea, bacteria, and eukaryotes,
including the RPN11 subunit of the 26S proteasome. Metal chelators and
point mutations within the JAMM motif abolished COP9
signalosome-dependent cleavage of NEDD8 from CUL1, yet had little effect
on COP9 signalosome complex assembly. Cope et al. (2002) proposed that
JAMM isopeptidases play important roles in a variety of physiologic
pathways.
Zheng et al. (2002) determined that the majority of CUL1 is in a complex
with CAND1 (607727) and ROC1 independent of SKP1 and the F box protein
SKP2. Both in vivo and in vitro, CAND1 prevented binding of SKP1 and
SKP2 to CUL1, while dissociation of CAND1 from CUL1 promoted the reverse
reaction. Neddylation of CUL1 or the presence of SKP1 and ATP caused
CAND1 dissociation. These data suggested that CAND1 regulates the
formation of the SCF complex and that its dissociation from CUL1 is
coupled with the incorporation of F box proteins into the SCF complex,
causing their destabilization.
Liu et al. (2002) showed that CAND1 selectively binds to unneddylated
CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary
complex with CUL1 and ROC1. It dissociated SKP1 from CUL1 and inhibited
SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the
level of the CUL1-SKP1 complex. The authors concluded that, by
restricting SKP1-CUL1 interaction, CAND1 regulates the assembly of
productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be
utilized by a large number of SKP1-F box-substrate subcomplexes.
Staropoli et al. (2003) demonstrated that parkin (602544) associates
with the F-box proteins FBXW7 (606278) and CUL1 in a distinct ubiquitin
ligase complex. FBXW7 serves to target the ligase activity to cyclin E,
a protein previously implicated in the regulation of neuronal apoptosis.
In cells transfected with the parkin T240R mutation (602544.0003),
parkin deficiency potentiated the accumulation of cyclin E in cultured
postmitotic neurons exposed to the glutamatergic excitotoxin kainate and
promoted their apoptosis. Furthermore, parkin overexpression attenuated
cyclin E accumulation in toxin-treated neurons and protected them from
apoptosis.
Scott et al. (2011) found that N-terminal acetylation of the E2 enzyme
UBC12 (603173) dictates distinctive E3-dependent ligation of the
ubiquitin-like protein NEDD8 (603171) to CUL1. Structural, biochemical,
biophysical, and genetic analyses revealed how complete burial of
UBC12's N-acetyl-methionine in a hydrophobic pocket in the E3 DCN1
(DCUN1D1; 605905) promotes cullin neddylation. The results suggested
that the N-terminal acetyl both directs UBC12's interactions with DCN1
and prevents repulsion of a charged N terminus. Scott et al. (2011)
concluded that their data provided a link between acetylation and
ubiquitin-like protein conjugation and defined a mechanism for
N-terminal acetylation-dependent recognition.
BIOCHEMICAL FEATURES
Zheng et al. (2002) reported the crystal structure to 3.2-angstrom
resolution of the quaternary complex containing CUL1, RBX1, SKP1, and
the F box of SKP2, and the 3.0-angstrom structure of the CUL1-RBX1
complex. CUL1 is an elongated protein that consists of a long stalk and
a globular domain. The globular domain binds the RING finger protein
RBX1 through an intermolecular beta-sheet, forming a 2-subunit catalytic
core that recruits the ubiquitin-conjugating enzyme. The long stalk,
which consists of 3 repeats of a novel 5-helix motif, binds the SKP1-F
box(SKP2) protein substrate recognition complex at its tip. CUL1 serves
as a rigid scaffold that organizes the SKP1-F box(SKP2) and RBX1
subunits, holding them over 100 angstroms apart. The structure suggests
that CUL1 may contribute to catalysis through the positioning of the
substrate and the ubiquitin-conjugating enzyme, and that this model is
supported by CUL1 mutations designed to eliminate the rigidity of the
scaffold.
*FIELD* RF
1. Cope, G. A.; Suh, G. S. B.; Aravind, L.; Schwarz, S. E.; Zipursky,
S. L.; Koonin, E. V.; Deshaies, R. J.: Role of predicted metalloprotease
motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298:
608-611, 2002.
2. Dealy, M. J.; Nguyen, K. V. T.; Lo, J.; Gstaiger, M.; Krek, W.;
Elson, D.; Arbeit, J.; Kipreos, E. T.; Johnson, R. S.: Loss of Cul1
results in early embryonic lethality and dysregulation of cyclin E. Nature
Genet. 23: 245-248, 1999.
3. 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.
4. Liu, J.; Furukawa, M.; Matsumoto, T.; Xiong, Y.: NEDD8 modification
of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding
and SCF ligases. Molec. Cell 10: 1511-1518, 2002.
5. Maniatis, T.: A ubiquitin ligase complex essential for the NF-kappa-B,
Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev. 13: 505-510,
1999.
6. 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.
7. 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.
8. Staropoli, J. F.; McDermott, C.; Martinat, C.; Schulman, B.; Demireva,
E.; Abeliovich, A.: Parkin is a component of an SCF-like ubiquitin
ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37:
735-749, 2003.
9. Winston, J. T.; Strack, P.; Beer-Romero, P.; Chu, C. Y.; Elledge,
S. J.; Harper, J. W.: The SCF(beta-TRCP)-ubiquitin ligase complex
associates specifically with phosphorylated destruction motifs in
I-kappa-B-alpha and beta-catenin and stimulates I-kappa-B-alpha ubiquitination
in vitro. Genes Dev. 13: 270-283, 1999. Note: Erratum: Genes Dev.
13: 1050 only, 1999.
10. Yu, Z.-K.; Gervais, J. L. M.; Zhang, H.: Human CUL-1 associates
with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin
D proteins. Proc. Nat. Acad. Sci. 95: 11324-11329, 1998.
11. 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. Molec. Cell 10: 1519-1526, 2002.
12. 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.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Stylianos E. Antonarakis - updated: 4/28/2003
Ada Hamosh - updated: 11/19/2002
Ada Hamosh - updated: 4/30/2002
Paul J. Converse - updated: 9/1/2000
Victor A. McKusick - updated: 9/29/1999
Victor A. McKusick - updated: 12/1/1998
*FIELD* CD
Rebekah S. Rasooly: 10/13/1998
*FIELD* ED
terry: 03/14/2013
alopez: 11/30/2011
terry: 11/29/2011
carol: 7/14/2003
ckniffin: 7/11/2003
mgross: 4/28/2003
alopez: 11/19/2002
terry: 11/18/2002
alopez: 4/30/2002
terry: 4/30/2002
terry: 12/7/2001
mgross: 9/1/2000
alopez: 9/30/1999
terry: 9/29/1999
carol: 12/2/1998
carol: 12/1/1998
alopez: 10/30/1998
dkim: 10/28/1998
alopez: 10/13/1998
*RECORD*
*FIELD* NO
603134
*FIELD* TI
*603134 CULLIN 1; CUL1
*FIELD* TX
CLONING
Kipreos et al. (1996) found that mutations in the cullin-1 (cul1) gene
read moreof C. elegans cause hyperplasia of all tissues. They determined that
cul1 is a negative regulator of the cell cycle; in cul1 mutants, the
G1-to-S-phase progression is accelerated, overriding mechanisms for
mitotic arrest and producing abnormally small cells. Searches of EST
databases revealed that cul1 is a member of a conserved gene family,
with at least 5 members in nematodes, 6 in humans, and 3 in S.
cerevisiae. Human CUL1 is an ortholog of nematode cul1.
GENE FUNCTION
Michel and Xiong (1998) stated that CUL1 has homology to yeast Cdc53,
which is part of a complex known as SCF that mediates the
ubiquitin-dependent degradation of G1 cycles and cyclin-dependent kinase
inhibitors. SCF complexes are composed of SKP1 (601434), Cdc53, and an F
box-containing protein, which may confer substrate specificity. These
authors found that interaction of the predicted 776-amino acid human
CUL1 protein with SKP1 is mediated through the N-terminal domains of
both proteins. Immunoprecipitation studies and Western blot analysis
revealed that the steady-state levels of both CUL1 and SKP1, as well as
their association with one another, remain relatively constant
throughout the cell cycle and in postmitotic cells. However, none of the
other human cullins tested interacted with SKP1. Michel and Xiong (1998)
determined that via SKP1, CUL1 forms a complex with SKP2 (601436), an F
box-containing protein, and cyclin A (123835). The authors concluded
that the SCF proteolytic pathway is evolutionarily conserved and is used
by mammalian CUL1, while the other cullin proteins may use a
SKP1/F-box-independent pathway to mediate protein degradation.
Maniatis (1999) reviewed the work of Winston et al. (1999) and others
concerning the SCF ubiquitin ligase complex. CUL1 acts as a scaffold for
SKP1 and the F-box-containing BTRC protein (603482) in the SCF complex,
which regulates the function of nuclear factor kappa-B (see 164011) and
beta-catenin (see 116806).
Yu et al. (1998) reported studies suggesting that the p19 (SKP1)/p45
(SKP2)/CUL1 complex is likely to function as a conserved ubiquitin E3
enzyme that regulates the mammalian G1/S transition by specifically
targeting mammalian G1 cell cycle regulators, such as p21 and cyclin D
proteins, for ubiquitin-dependent degradation.
The sequential timing of cell cycle transitions is primarily governed by
the availability and activity of key cell cycle proteins. Studies in
yeast identified a class of ubiquitin ligases (E3 enzymes) called SCF
complexes, which regulate the abundance of proteins that promote and
inhibit cell cycle progression at the transition between G1 and S
phases. SCF complexes consist of 3 invariable components, SKP1, CUL1
(CDC53 in yeast), and RBX1 (603814), and a variable F-box protein that
recruits a specific cellular protein to the ubiquitin pathway for
degradation. To study the role of CUL1 in mammalian development and cell
cycle regulation, Dealy et al. (1999) generated mice deficient for Cul1
and analyzed null embryos and heterozygous cell lines. They showed that
Cul1 is required for early mouse development and that Cul1 mutants fail
to regulate the abundance of the G1 cyclin, cyclin E (CCNE1; 123837),
during embryogenesis.
COP9 signalosome cleaves the ubiquitin-like protein NEDD8 (603171) from
the CUL1 subunit of SCF ubiquitin ligases. Cope et al. (2002) found that
the JAB1/MPN domain metalloenzyme (JAMM) motif in the JAB1/COPS5
(604850) subunit underlies the COP9 signalosome's NEDD8 isopeptidase
activity. The JAMM motif consists of a his-X-his-X(10)-asp motif (where
X indicates any residue) accompanied by an upstream glutamate. The JAMM
motif is found in proteins from archaea, bacteria, and eukaryotes,
including the RPN11 subunit of the 26S proteasome. Metal chelators and
point mutations within the JAMM motif abolished COP9
signalosome-dependent cleavage of NEDD8 from CUL1, yet had little effect
on COP9 signalosome complex assembly. Cope et al. (2002) proposed that
JAMM isopeptidases play important roles in a variety of physiologic
pathways.
Zheng et al. (2002) determined that the majority of CUL1 is in a complex
with CAND1 (607727) and ROC1 independent of SKP1 and the F box protein
SKP2. Both in vivo and in vitro, CAND1 prevented binding of SKP1 and
SKP2 to CUL1, while dissociation of CAND1 from CUL1 promoted the reverse
reaction. Neddylation of CUL1 or the presence of SKP1 and ATP caused
CAND1 dissociation. These data suggested that CAND1 regulates the
formation of the SCF complex and that its dissociation from CUL1 is
coupled with the incorporation of F box proteins into the SCF complex,
causing their destabilization.
Liu et al. (2002) showed that CAND1 selectively binds to unneddylated
CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary
complex with CUL1 and ROC1. It dissociated SKP1 from CUL1 and inhibited
SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the
level of the CUL1-SKP1 complex. The authors concluded that, by
restricting SKP1-CUL1 interaction, CAND1 regulates the assembly of
productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be
utilized by a large number of SKP1-F box-substrate subcomplexes.
Staropoli et al. (2003) demonstrated that parkin (602544) associates
with the F-box proteins FBXW7 (606278) and CUL1 in a distinct ubiquitin
ligase complex. FBXW7 serves to target the ligase activity to cyclin E,
a protein previously implicated in the regulation of neuronal apoptosis.
In cells transfected with the parkin T240R mutation (602544.0003),
parkin deficiency potentiated the accumulation of cyclin E in cultured
postmitotic neurons exposed to the glutamatergic excitotoxin kainate and
promoted their apoptosis. Furthermore, parkin overexpression attenuated
cyclin E accumulation in toxin-treated neurons and protected them from
apoptosis.
Scott et al. (2011) found that N-terminal acetylation of the E2 enzyme
UBC12 (603173) dictates distinctive E3-dependent ligation of the
ubiquitin-like protein NEDD8 (603171) to CUL1. Structural, biochemical,
biophysical, and genetic analyses revealed how complete burial of
UBC12's N-acetyl-methionine in a hydrophobic pocket in the E3 DCN1
(DCUN1D1; 605905) promotes cullin neddylation. The results suggested
that the N-terminal acetyl both directs UBC12's interactions with DCN1
and prevents repulsion of a charged N terminus. Scott et al. (2011)
concluded that their data provided a link between acetylation and
ubiquitin-like protein conjugation and defined a mechanism for
N-terminal acetylation-dependent recognition.
BIOCHEMICAL FEATURES
Zheng et al. (2002) reported the crystal structure to 3.2-angstrom
resolution of the quaternary complex containing CUL1, RBX1, SKP1, and
the F box of SKP2, and the 3.0-angstrom structure of the CUL1-RBX1
complex. CUL1 is an elongated protein that consists of a long stalk and
a globular domain. The globular domain binds the RING finger protein
RBX1 through an intermolecular beta-sheet, forming a 2-subunit catalytic
core that recruits the ubiquitin-conjugating enzyme. The long stalk,
which consists of 3 repeats of a novel 5-helix motif, binds the SKP1-F
box(SKP2) protein substrate recognition complex at its tip. CUL1 serves
as a rigid scaffold that organizes the SKP1-F box(SKP2) and RBX1
subunits, holding them over 100 angstroms apart. The structure suggests
that CUL1 may contribute to catalysis through the positioning of the
substrate and the ubiquitin-conjugating enzyme, and that this model is
supported by CUL1 mutations designed to eliminate the rigidity of the
scaffold.
*FIELD* RF
1. Cope, G. A.; Suh, G. S. B.; Aravind, L.; Schwarz, S. E.; Zipursky,
S. L.; Koonin, E. V.; Deshaies, R. J.: Role of predicted metalloprotease
motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298:
608-611, 2002.
2. Dealy, M. J.; Nguyen, K. V. T.; Lo, J.; Gstaiger, M.; Krek, W.;
Elson, D.; Arbeit, J.; Kipreos, E. T.; Johnson, R. S.: Loss of Cul1
results in early embryonic lethality and dysregulation of cyclin E. Nature
Genet. 23: 245-248, 1999.
3. 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.
4. Liu, J.; Furukawa, M.; Matsumoto, T.; Xiong, Y.: NEDD8 modification
of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding
and SCF ligases. Molec. Cell 10: 1511-1518, 2002.
5. Maniatis, T.: A ubiquitin ligase complex essential for the NF-kappa-B,
Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev. 13: 505-510,
1999.
6. 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.
7. 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.
8. Staropoli, J. F.; McDermott, C.; Martinat, C.; Schulman, B.; Demireva,
E.; Abeliovich, A.: Parkin is a component of an SCF-like ubiquitin
ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37:
735-749, 2003.
9. Winston, J. T.; Strack, P.; Beer-Romero, P.; Chu, C. Y.; Elledge,
S. J.; Harper, J. W.: The SCF(beta-TRCP)-ubiquitin ligase complex
associates specifically with phosphorylated destruction motifs in
I-kappa-B-alpha and beta-catenin and stimulates I-kappa-B-alpha ubiquitination
in vitro. Genes Dev. 13: 270-283, 1999. Note: Erratum: Genes Dev.
13: 1050 only, 1999.
10. Yu, Z.-K.; Gervais, J. L. M.; Zhang, H.: Human CUL-1 associates
with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin
D proteins. Proc. Nat. Acad. Sci. 95: 11324-11329, 1998.
11. 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. Molec. Cell 10: 1519-1526, 2002.
12. 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.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Stylianos E. Antonarakis - updated: 4/28/2003
Ada Hamosh - updated: 11/19/2002
Ada Hamosh - updated: 4/30/2002
Paul J. Converse - updated: 9/1/2000
Victor A. McKusick - updated: 9/29/1999
Victor A. McKusick - updated: 12/1/1998
*FIELD* CD
Rebekah S. Rasooly: 10/13/1998
*FIELD* ED
terry: 03/14/2013
alopez: 11/30/2011
terry: 11/29/2011
carol: 7/14/2003
ckniffin: 7/11/2003
mgross: 4/28/2003
alopez: 11/19/2002
terry: 11/18/2002
alopez: 4/30/2002
terry: 4/30/2002
terry: 12/7/2001
mgross: 9/1/2000
alopez: 9/30/1999
terry: 9/29/1999
carol: 12/2/1998
carol: 12/1/1998
alopez: 10/30/1998
dkim: 10/28/1998
alopez: 10/13/1998