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 20-JUN-2018, entry version 182. 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 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., RA Oda T., 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., 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 [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 RT through 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., 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 [30] 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 [31] 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 RT Cullin-RING ligase complexes."; RL EMBO J. 32:2848-2860(2013). 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 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 RT localization through Nedd8 modification."; RL PLoS ONE 8:E65285-E65285(2013). RN [34] RP FUNCTION IN UBIQUITINATION OF BCL2, AND IDENTIFICATION IN THE RP SCF(FBXO10) 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 RT and human lymphoma."; RL Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013). RN [35] 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., RA Buss E., Shaha M., Rechler W., Ramanathan S.Y., Singh B.; RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity RT of SCCRO (DCUN1D1)."; RL J. Biol. Chem. 289:34728-34742(2014). RN [36] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [37] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY RP MASS 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., RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., RA Vemulapalli V., 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 [38] 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 [39] 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., RA Florens L., Washburn M.P., Pagano M.; RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from RT the PCM to allow centriole separation, disengagement and licensing."; RL Nat. Cell Biol. 17:31-43(2015). RN [40] 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., RA Paulo J.A., de Jong A., Ovaa H., Alpi A.F., Harper J.W., RA 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 [41] 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., RA Inuzuka H.; RT "NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to RT promote osteoporosis."; RL Mol. Cell 68:645-658(2017). RN [42] 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 RT production and canonical NFkappaBeta signaling by stabilizing RT IkappaBalpha."; RL PLoS Pathog. 13:E1006187-E1006187(2017). RN [43] 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 [44] 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 [45] 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). RN [46] {ECO:0000244|PDB:5V89} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 702-776 IN COMPLEX WITH RP DCUN1D4. RX PubMed=28581483; DOI=10.1038/nchembio.2386; RA Scott D.C., Hammill J.T., Min J., Rhee D.Y., Connelly M., RA Sviderskiy V.O., Bhasin D., Chen Y., Ong S.S., Chai S.C., Goktug A.N., RA Huang G., Monda J.K., Low J., Kim H.S., Paulo J.A., Cannon J.R., RA Shelat A.A., Chen T., Kelsall I.R., Alpi A.F., Pagala V., Wang X., RA Peng J., Singh B., Harper J.W., Schulman B.A., Guy R.K.; RT "Blocking an N-terminal acetylation-dependent protein interaction RT inhibits an E3 ligase."; RL Nat. Chem. Biol. 13:850-857(2017). 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. SCF complexes CC and ARIH1 collaborate in tandem to mediate ubiquitination of CC target proteins (PubMed:27565346). In the SCF complex, serves as a CC rigid scaffold that organizes the SKP1-F-box protein and RBX1 CC subunits. May contribute to catalysis through positioning of the CC substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin- CC 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. CC SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. CC SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, CC SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(BTRC) and/or CC SCF(FBXW11) direct ubiquitination of CEP68 (PubMed:25704143, CC PubMed:25503564). SCF(SKP2) directs ubiquitination of CC phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S CC transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, CC ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) CC directs ubiquitination of cyclin E, NOTCH1 released notch CC intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) CC directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination CC of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. CC SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs CC ubiquitination of BCL6 and DTL but does not seem to direct CC ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of CC NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the CC associated NFKB1-RELA dimer to translocate into the nucleus and to CC activate transcription. SCF(CCNF) directs ubiquitination of CC CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 CC and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. CC 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:23263282, CC ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:25503564, CC ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:27565346, CC ECO:0000269|PubMed:9663463}. 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(FBXO10) complex containing CC FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. CC Component of the SCF(FBXO25) complex containing FBXO25. Component CC of the SCF(FBXO33) complex containing FBXO33. Component of the CC probable SCF(FBXO4) complex containing FBXO4. Component of the CC SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component CC of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This CC complex binds phosphorylated NFKBIA. Part of a SCF complex CC 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 DCUN1D3. Interacts with CEP68 as part of the SCF(FBXW11) complex; CC the interaction is probably mediated by FBXW11 and the complex CC also contains CDK5RAP2 and PCNT (PubMed:25503564). Interacts (when CC neddylated) with ARIH1; leading to activate the E3 ligase activity CC of ARIH1 (PubMed:24076655, PubMed:27565346). Interacts with COPS9 CC isoform 2 (PubMed:23776465). Interacts with UBXN1 CC (PubMed:28152074). Interacts with KAT7, probably as part of an SCF CC complex; the interaction mediates KAT7 ubiquitination (By CC similarity). Interacts with NOTCH2 (PubMed:29149593). 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:15537541, CC ECO:0000269|PubMed:15640526, 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:23263282, ECO:0000269|PubMed:23431138, CC ECO:0000269|PubMed:23776465, ECO:0000269|PubMed:24076655, CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:25503564, CC ECO:0000269|PubMed:27565346, ECO:0000269|PubMed:28152074, CC ECO:0000269|PubMed:29149593}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus CC BPLF1. {ECO:0000269|PubMed:20190741}. CC -!- SUBUNIT: (Microbial infection) Interacts with Human adenovirus CC early E1A protein; this interaction inhibits RBX1-CUL1-dependent CC elongation reaction of ubiquitin chains by the SCF(FBXW7) complex. CC {ECO:0000269|PubMed:19679664}. CC -!- INTERACTION: CC Q6TVW2:- (xeno); NbExp=5; IntAct=EBI-359390, EBI-15718527; CC Q9Y4X5:ARIH1; NbExp=6; IntAct=EBI-359390, EBI-2514233; CC Q9Y297:BTRC; NbExp=6; IntAct=EBI-359390, EBI-307461; CC Q86VP6:CAND1; NbExp=21; IntAct=EBI-359390, EBI-456077; CC O60826:CCDC22; NbExp=3; IntAct=EBI-359390, EBI-3943153; CC P41002:CCNF; NbExp=5; IntAct=EBI-359390, EBI-1207574; CC Q8ND76:CCNY; NbExp=3; IntAct=EBI-359390, EBI-1049189; CC P49427:CDC34; NbExp=3; IntAct=EBI-359390, EBI-975634; CC P46527:CDKN1B; NbExp=2; IntAct=EBI-359390, EBI-519280; CC Q8BFZ4:Fbxl21 (xeno); NbExp=3; IntAct=EBI-359390, EBI-6898235; CC Q8C4V4:Fbxl3 (xeno); NbExp=3; IntAct=EBI-359390, EBI-1266589; CC Q9UKT5:FBXO4; NbExp=2; IntAct=EBI-359390, EBI-960409; CC Q9UKB1:FBXW11; NbExp=4; IntAct=EBI-359390, EBI-355189; CC Q83730:m005R (xeno); NbExp=5; IntAct=EBI-359390, EBI-6859930; CC Q00987:MDM2; NbExp=3; IntAct=EBI-359390, EBI-389668; CC O75586:MED6; NbExp=2; IntAct=EBI-359390, EBI-394624; CC Q15843:NEDD8; NbExp=12; IntAct=EBI-359390, EBI-716247; CC P62877:RBX1; NbExp=24; IntAct=EBI-359390, EBI-398523; CC P63208:SKP1; NbExp=10; IntAct=EBI-359390, EBI-307486; CC Q13309:SKP2; NbExp=8; IntAct=EBI-359390, EBI-456291; CC P52491:UBC12 (xeno); NbExp=2; IntAct=EBI-359390, EBI-19772; CC P61081:UBE2M; NbExp=5; IntAct=EBI-359390, EBI-1041660; CC O94888:UBXN7; NbExp=8; IntAct=EBI-359390, EBI-1993627; CC -!- TISSUE SPECIFICITY: Expressed in lung fibroblasts. CC {ECO:0000269|PubMed:9663463}. 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 CC (PubMed:10597293, PubMed:10713156, PubMed:15537541, CC PubMed:18805092). {ECO:0000269|PubMed:10597293, CC ECO:0000269|PubMed:10713156, ECO:0000269|PubMed:15537541, CC ECO:0000269|PubMed:18805092, ECO:0000269|PubMed:20190741, CC ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:27565346}. CC -!- PTM: (Microbial infection) Deneddylated by Epstein-Barr virus CC BPLF1 leading to a S-phase-like environment that is required for CC efficient 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 PDB; 4P5O; X-ray; 3.11 A; A/C=411-776. DR PDB; 5V89; X-ray; 1.55 A; C=702-776. 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 ProteinModelPortal; Q13616; -. DR SMR; Q13616; -. DR BioGrid; 114032; 733. DR CORUM; Q13616; -. DR DIP; DIP-17013N; -. DR IntAct; Q13616; 98. DR MINT; Q13616; -. DR STRING; 9606.ENSP00000326804; -. DR iPTMnet; Q13616; -. DR PhosphoSitePlus; Q13616; -. DR BioMuta; CUL1; -. DR DMDM; 19863257; -. DR EPD; Q13616; -. DR MaxQB; Q13616; -. DR PaxDb; Q13616; -. DR PeptideAtlas; Q13616; -. DR PRIDE; Q13616; -. DR ProteomicsDB; 59604; -. 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.4; human. DR CTD; 8454; -. DR DisGeNET; 8454; -. DR EuPathDB; HostDB:ENSG00000055130.15; -. DR GeneCards; CUL1; -. DR HGNC; HGNC:2551; CUL1. DR HPA; CAB002676; -. DR HPA; HPA064584; -. DR MIM; 603134; gene. DR neXtProt; NX_Q13616; -. DR OpenTargets; ENSG00000055130; -. DR PharmGKB; PA27047; -. DR eggNOG; KOG2166; Eukaryota. DR eggNOG; COG5647; LUCA. DR GeneTree; ENSGT00760000119212; -. DR HOGENOM; HOG000176713; -. DR HOVERGEN; HBG106177; -. DR InParanoid; Q13616; -. DR KO; K03347; -. DR OMA; TTHKHIE; -. DR OrthoDB; EOG091G02WR; -. DR PhylomeDB; Q13616; -. DR TreeFam; TF101151; -. DR BioCyc; MetaCyc:ENSG00000055130-MONOMER; -. 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-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q13616; -. DR SIGNOR; Q13616; -. DR UniPathway; UPA00143; -. DR ChiTaRS; CUL1; human. DR EvolutionaryTrace; Q13616; -. DR GeneWiki; CUL1; -. DR GenomeRNAi; 8454; -. DR PRO; PR:Q13616; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000055130; -. DR CleanEx; HS_CUL1; -. 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:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome. DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl. DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc. DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl. DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc. DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl. DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0010265; P:SCF complex assembly; TAS:Reactome. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome. DR Gene3D; 1.10.10.10; -; 2. 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 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; Complete proteome; Host-virus interaction; KW Isopeptide bond; Methylation; Reference proteome; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1 776 Cullin-1. FT /FTId=PRO_0000119787. FT MOD_RES 63 63 Omega-N-methylarginine. FT {ECO:0000244|PubMed:24129315}. FT CROSSLNK 720 720 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in NEDD8). FT {ECO:0000269|PubMed:10597293, FT ECO:0000269|PubMed:15537541, FT ECO:0000269|PubMed:18805092}. FT CONFLICT 59 82 Missing (in Ref. 1; AAC50544). FT {ECO:0000305}. FT CONFLICT 726 726 K -> R (in Ref. 3; CAD97651). FT {ECO:0000305}. FT HELIX 18 31 {ECO:0000244|PDB:1LDJ}. FT TURN 32 34 {ECO:0000244|PDB:1U6G}. FT HELIX 39 52 {ECO:0000244|PDB:1LDJ}. FT HELIX 87 105 {ECO:0000244|PDB:1LDJ}. FT TURN 106 109 {ECO:0000244|PDB:1U6G}. FT TURN 111 114 {ECO:0000244|PDB:1LDJ}. FT HELIX 115 136 {ECO:0000244|PDB:1LDJ}. FT HELIX 138 143 {ECO:0000244|PDB:1LDJ}. FT STRAND 144 146 {ECO:0000244|PDB:1LDJ}. FT HELIX 159 165 {ECO:0000244|PDB:1LDJ}. FT HELIX 168 171 {ECO:0000244|PDB:1LDJ}. FT TURN 172 177 {ECO:0000244|PDB:1LDJ}. FT HELIX 178 187 {ECO:0000244|PDB:1LDJ}. FT TURN 188 190 {ECO:0000244|PDB:1LDJ}. FT HELIX 199 210 {ECO:0000244|PDB:1LDJ}. FT TURN 211 213 {ECO:0000244|PDB:1LDK}. FT STRAND 215 219 {ECO:0000244|PDB:1LDJ}. FT HELIX 226 231 {ECO:0000244|PDB:1LDJ}. FT HELIX 233 254 {ECO:0000244|PDB:1LDJ}. FT HELIX 261 273 {ECO:0000244|PDB:1LDJ}. FT TURN 274 279 {ECO:0000244|PDB:1LDJ}. FT STRAND 281 284 {ECO:0000244|PDB:1LDJ}. FT HELIX 285 295 {ECO:0000244|PDB:1LDJ}. FT STRAND 296 300 {ECO:0000244|PDB:1LDJ}. FT HELIX 301 312 {ECO:0000244|PDB:1LDJ}. FT HELIX 318 328 {ECO:0000244|PDB:1LDJ}. FT HELIX 333 355 {ECO:0000244|PDB:1LDJ}. FT HELIX 359 361 {ECO:0000244|PDB:1LDJ}. FT HELIX 363 382 {ECO:0000244|PDB:1LDJ}. FT TURN 383 387 {ECO:0000244|PDB:1LDJ}. FT HELIX 389 404 {ECO:0000244|PDB:1LDJ}. FT HELIX 407 412 {ECO:0000244|PDB:1LDJ}. FT HELIX 417 430 {ECO:0000244|PDB:1LDJ}. FT HELIX 439 453 {ECO:0000244|PDB:1LDJ}. FT HELIX 459 475 {ECO:0000244|PDB:1LDJ}. FT HELIX 482 525 {ECO:0000244|PDB:1LDJ}. FT TURN 526 528 {ECO:0000244|PDB:1LDJ}. FT STRAND 532 541 {ECO:0000244|PDB:1LDJ}. FT TURN 542 544 {ECO:0000244|PDB:1LDJ}. FT HELIX 557 559 {ECO:0000244|PDB:1LDJ}. FT HELIX 560 569 {ECO:0000244|PDB:1LDJ}. FT TURN 570 573 {ECO:0000244|PDB:1LDJ}. FT STRAND 579 581 {ECO:0000244|PDB:1LDJ}. FT HELIX 583 585 {ECO:0000244|PDB:1LDJ}. FT STRAND 589 597 {ECO:0000244|PDB:1LDJ}. FT STRAND 600 602 {ECO:0000244|PDB:1LDJ}. FT HELIX 605 612 {ECO:0000244|PDB:1LDJ}. FT HELIX 613 615 {ECO:0000244|PDB:1LDJ}. FT STRAND 616 621 {ECO:0000244|PDB:1LDJ}. FT HELIX 622 628 {ECO:0000244|PDB:1LDJ}. FT HELIX 633 645 {ECO:0000244|PDB:1LDJ}. FT TURN 646 648 {ECO:0000244|PDB:1LDJ}. FT STRAND 652 654 {ECO:0000244|PDB:1LDK}. FT TURN 658 660 {ECO:0000244|PDB:1LDJ}. FT STRAND 668 671 {ECO:0000244|PDB:1LDJ}. FT STRAND 678 682 {ECO:0000244|PDB:1LDJ}. FT HELIX 691 700 {ECO:0000244|PDB:1LDK}. FT HELIX 703 722 {ECO:0000244|PDB:3TDU}. FT STRAND 723 726 {ECO:0000244|PDB:3TDU}. FT HELIX 727 738 {ECO:0000244|PDB:3TDU}. FT TURN 739 741 {ECO:0000244|PDB:3TDU}. FT HELIX 746 758 {ECO:0000244|PDB:3TDU}. FT STRAND 761 765 {ECO:0000244|PDB:3TDU}. FT STRAND 768 774 {ECO:0000244|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 //