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Database: UniProt
Entry: Q13620
LinkDB: Q13620
Original site: Q13620 
ID   CUL4B_HUMAN             Reviewed;         913 AA.
AC   Q13620; B1APK5; B3KVX4; B7Z5K8; Q6PIE4; Q6UP07; Q7Z673; Q9BY37; Q9UEB7;
AC   Q9UED7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   07-APR-2021, entry version 200.
DE   RecName: Full=Cullin-4B;
DE            Short=CUL-4B;
GN   Name=CUL4B; Synonyms=KIAA0695;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP   CDT1.
RX   PubMed=14578910; DOI=10.1038/ncb1061;
RA   Higa L.A., Mihaylov I.S., Banks D.P., Zheng J., Zhang H.;
RT   "Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes
RT   constitutes a new checkpoint.";
RL   Nat. Cell Biol. 5:1008-1015(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Du M., Zu Z., Sansores-Garcia L., Wu K.K.;
RT   "Molecular cloning of a full-length cullin, CUL4B and identification of its
RT   interacting proteins.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Chondrocyte, Teratocarcinoma, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal liver;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-913 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [9]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 626-913.
RX   PubMed=8681378; DOI=10.1016/s0092-8674(00)81267-2;
RA   Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.;
RT   "cul-1 is required for cell cycle exit in C. elegans and identifies a novel
RT   gene family.";
RL   Cell 85:829-839(1996).
RN   [11]
RP   NEDDYLATION.
RX   PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA   Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA   Kato S., Tanaka K.;
RT   "Covalent modification of all members of human cullin family proteins by
RT   NEDD8.";
RL   Oncogene 18:6829-6834(1999).
RN   [12]
RP   INTERACTION WITH RBX1.
RX   PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
RA   Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT   "ROC1, a homolog of APC11, represents a family of cullin partners with an
RT   associated ubiquitin ligase activity.";
RL   Mol. Cell 3:535-541(1999).
RN   [13]
RP   INTERACTION WITH TIP120A, AND IDENTIFICATION IN A COMPLEX WITH RBX1 AND
RP   TIP120A.
RX   PubMed=12609982; DOI=10.1074/jbc.m213070200;
RA   Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
RT   "TIP120A associates with cullins and modulates ubiquitin ligase activity.";
RL   J. Biol. Chem. 278:15905-15910(2003).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH CYCLIN E.
RX   PubMed=16322693; DOI=10.4161/cc.5.1.2266;
RA   Higa L.A., Yang X., Zheng J., Banks D., Wu M., Ghosh P., Sun H., Zhang H.;
RT   "Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors
RT   Dacapo/p27Kip1 and cyclin E degradation.";
RL   Cell Cycle 5:71-77(2006).
RN   [15]
RP   IDENTIFICATION IN COMPLEX WITH DDB1; DDB2 AND RBX1, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND FUNCTION.
RX   PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
RA   Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
RA   Tempst P., Xiong Y., Zhang Y.;
RT   "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase
RT   facilitates cellular response to DNA damage.";
RL   Mol. Cell 22:383-394(2006).
RN   [16]
RP   INTERACTION WITH DCAF1; DDA1; DCAF6; DCAF17; DDB2 AND DCAF8.
RX   PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA   Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT   "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT   required for S phase destruction of the replication factor Cdt1.";
RL   Mol. Cell 23:709-721(2006).
RN   [17]
RP   INTERACTION WITH DTL; DDB2; TMEM113; WDR5B; WDR82; WDR26; GRWD1; WDR51B;
RP   SNRNP40; DCAF8; WDR61; WDR76; WDR5; SMU1; TLE2 AND TLE3.
RX   PubMed=17041588; DOI=10.1038/ncb1490;
RA   Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT   "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
RT   and regulates histone methylation.";
RL   Nat. Cell Biol. 8:1277-1283(2006).
RN   [18]
RP   INVOLVEMENT IN MRXS15.
RX   PubMed=17273978; DOI=10.1086/512489;
RA   Zou Y., Liu Q., Chen B., Zhang X., Guo C., Zhou H., Li J., Gao G., Guo Y.,
RA   Yan C., Wei J., Shao C., Gong Y.;
RT   "Mutation in CUL4B, which encodes a member of cullin-RING ubiquitin ligase
RT   complex, causes X-linked mental retardation.";
RL   Am. J. Hum. Genet. 80:561-566(2007).
RN   [19]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=18593899; DOI=10.1158/0008-5472.can-07-6162;
RA   Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I.,
RA   Levine A.S., Rapic-Otrin V.;
RT   "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-
RT   damaged chromatin and ubiquitinates histone H2A.";
RL   Cancer Res. 68:5014-5022(2008).
RN   [20]
RP   FUNCTION, AND INTERACTION WITH MLST8.
RX   PubMed=18235224; DOI=10.4161/cc.7.3.5267;
RA   Ghosh P., Wu M., Zhang H., Sun H.;
RT   "mTORC1 signaling requires proteasomal function and the involvement of
RT   CUL4-DDB1 ubiquitin E3 ligase.";
RL   Cell Cycle 7:373-381(2008).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-53; SER-146 AND
RP   SER-193, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [23]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KPNA2; KPNA4; KPNA1 AND
RP   KPNB1, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF LYS-55; LYS-56;
RP   ARG-57; LYS-58 AND 55-LYS--LYS-58.
RX   PubMed=19801544; DOI=10.1074/jbc.m109.050427;
RA   Zou Y., Mi J., Cui J., Lu D., Zhang X., Guo C., Gao G., Liu Q., Chen B.,
RA   Shao C., Gong Y.;
RT   "Characterization of nuclear localization signal in the N terminus of CUL4B
RT   and its essential role in cyclin E degradation and cell cycle
RT   progression.";
RL   J. Biol. Chem. 284:33320-33332(2009).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-146, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [25]
RP   DISEASE, AND INVOLVEMENT IN MRXS15.
RX   PubMed=20002452; DOI=10.1111/j.1399-0004.2009.01331.x;
RA   Badura-Stronka M., Jamsheer A., Materna-Kiryluk A., Sowinska A.,
RA   Kiryluk K., Budny B., Latos-Bielenska A.;
RT   "A novel nonsense mutation in CUL4B gene in three brothers with X-linked
RT   mental retardation syndrome.";
RL   Clin. Genet. 77:141-144(2010).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-8 AND SER-10 (ISOFORM 2), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [29]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [30]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-193, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [31]
RP   INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX   PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA   Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA   Bennett E.J., Schulman B.A.;
RT   "Structural conservation of distinctive N-terminal acetylation-dependent
RT   interactions across a family of mammalian NEDD8 ligation enzymes.";
RL   Structure 21:42-53(2013).
RN   [32]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [33]
RP   FUNCTION.
RX   PubMed=26711351; DOI=10.1016/j.celrep.2015.11.061;
RA   Badertscher L., Wild T., Montellese C., Alexander L.T., Bammert L.,
RA   Sarazova M., Stebler M., Csucs G., Mayer T.U., Zamboni N., Zemp I.,
RA   Horvath P., Kutay U.;
RT   "Genome-wide RNAi Screening Identifies Protein Modules Required for 40S
RT   Subunit Synthesis in Human Cells.";
RL   Cell Rep. 13:2879-2891(2015).
RN   [34]
RP   INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3 AND DCUN1D5.
RX   PubMed=26906416; DOI=10.1242/jcs.181784;
RA   Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT   "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL   J. Cell Sci. 129:1441-1454(2016).
RN   [35]
RP   STRUCTURE BY NMR OF 826-913.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the winged helix-turn-helix motif of human cul-4b.";
RL   Submitted (APR-2007) to the PDB data bank.
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 192-913 IN COMPLEXES WITH CAND1;
RP   RBX1 AND DDB1, SUBUNIT, AND FUNCTION.
RX   PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
RA   Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M.,
RA   Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H.,
RA   Sugasawa K., Thoma N.H.;
RT   "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
RT   targeting, and activation.";
RL   Cell 147:1024-1039(2011).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 206-557.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the N-terminal domain of human Cul4B at 2.57 A
RT   resolution.";
RL   Submitted (OCT-2011) to the PDB data bank.
RN   [38]
RP   VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745, AND VARIANT PRO-103.
RX   PubMed=17236139; DOI=10.1086/511134;
RA   Tarpey P.S., Raymond F.L., O'Meara S., Edkins S., Teague J., Butler A.,
RA   Dicks E., Stevens C., Tofts C., Avis T., Barthorpe S., Buck G., Cole J.,
RA   Gray K., Halliday K., Harrison R., Hills K., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Varian J., West S., Widaa S., Mallya U., Moon J., Luo Y.,
RA   Holder S., Smithson S.F., Hurst J.A., Clayton-Smith J., Kerr B., Boyle J.,
RA   Shaw M., Vandeleur L., Rodriguez J., Slaugh R., Easton D.F., Wooster R.,
RA   Bobrow M., Srivastava A.K., Stevenson R.E., Schwartz C.E., Turner G.,
RA   Gecz J., Futreal P.A., Stratton M.R., Partington M.;
RT   "Mutations in CUL4B, which encodes a ubiquitin E3 ligase subunit, cause an
RT   X-linked mental retardation syndrome associated with aggressive outbursts,
RT   seizures, relative macrocephaly, central obesity, hypogonadism, pes cavus,
RT   and tremor.";
RL   Am. J. Hum. Genet. 80:345-352(2007).
RN   [39]
RP   VARIANTS MRXS15 ILE-213; CYS-572 AND ALA-745.
RX   PubMed=19377476; DOI=10.1038/ng.367;
RA   Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C.,
RA   O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M.,
RA   Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.,
RA   Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M.,
RA   Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P.,
RA   Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R.,
RA   Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R.,
RA   de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M.,
RA   Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U.,
RA   Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M.,
RA   Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T.,
RA   Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C.,
RA   Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L.,
RA   Futreal P.A., Stratton M.R.;
RT   "A systematic, large-scale resequencing screen of X-chromosome coding exons
RT   in mental retardation.";
RL   Nat. Genet. 41:535-543(2009).
CC   -!- FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-
CC       protein ligase complexes which mediate the ubiquitination and
CC       subsequent proteasomal degradation of target proteins. The functional
CC       specificity of the E3 ubiquitin-protein ligase complex depends on the
CC       variable substrate recognition subunit. CUL4B may act within the
CC       complex as a scaffold protein, contributing to catalysis through
CC       positioning of the substrate and the ubiquitin-conjugating enzyme.
CC       Plays a role as part of the E3 ubiquitin-protein ligase complex in
CC       polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in
CC       response to radiation-induced DNA damage. Targeted to UV damaged
CC       chromatin by DDB2 and may be important for DNA repair and DNA
CC       replication. Required for ubiquitination of cyclin E, and consequently,
CC       normal G1 cell cycle progression. Regulates the mammalian target-of-
CC       rapamycin (mTOR) pathway involved in control of cell growth, size and
CC       metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is
CC       dependent upon 26S proteasome function and requires interaction between
CC       CUL4B and MLST8. With CUL4A, contributes to ribosome biogenesis
CC       (PubMed:26711351). {ECO:0000269|PubMed:14578910,
CC       ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110,
CC       ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899,
CC       ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460,
CC       ECO:0000269|PubMed:26711351}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complexes that seem to be formed of DDB1, CUL4A or
CC       CUL4B, RBX1 and a variable substrate recognition component which seems
CC       to belong to a protein family described as DCAF (Ddb1- and Cul4-
CC       associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins.
CC       Component of the DCX(DTL) complex with the putative substrate
CC       recognition component DTL. Component of the DCX(DDB2) complex with the
CC       putative substrate recognition component DDB2. Part of a complex with
CC       RBX1 and TIP120A/CAND1. Interacts with RBX1 GRWD1, MLST8, SMU1, TLE2,
CC       TLE3, DCAF1, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and
CC       TMEM113. Interacts with cyclin E and with importins alpha-1 (KPNA2),
CC       alpha-3 (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1). May interact with
CC       WDR26, WDR51B, SNRNP40, WDR61, WDR76 and WDR5. Interacts (unneddylated
CC       form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these
CC       interactions promote the cullin neddylation (PubMed:26906416,
CC       PubMed:23201271). {ECO:0000269|PubMed:10230407,
CC       ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:14578910,
CC       ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110,
CC       ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:17041588,
CC       ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899,
CC       ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460,
CC       ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:26906416}.
CC   -!- INTERACTION:
CC       Q13620; Q86VP6: CAND1; NbExp=13; IntAct=EBI-456067, EBI-456077;
CC       Q13620; Q16543: CDC37; NbExp=2; IntAct=EBI-456067, EBI-295634;
CC       Q13620; Q16531: DDB1; NbExp=21; IntAct=EBI-456067, EBI-350322;
CC       Q13620; P08238: HSP90AB1; NbExp=2; IntAct=EBI-456067, EBI-352572;
CC       Q13620; P62877: RBX1; NbExp=5; IntAct=EBI-456067, EBI-398523;
CC       Q13620; O94888: UBXN7; NbExp=3; IntAct=EBI-456067, EBI-1993627;
CC       Q13620; Q9H898-2: ZMAT4; NbExp=3; IntAct=EBI-456067, EBI-11529334;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18593899,
CC       ECO:0000269|PubMed:19801544}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q13620-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13620-1; Sequence=VSP_039085;
CC       Name=3;
CC         IsoId=Q13620-3; Sequence=VSP_039084, VSP_039086;
CC   -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC       signalosome (CSN) complex. {ECO:0000269|PubMed:10597293}.
CC   -!- DISEASE: Mental retardation, X-linked, syndromic, 15 (MRXS15)
CC       [MIM:300354]: A syndromic form of X-linked mental retardation
CC       characterized by severe intellectual deficit associated with short
CC       stature, craniofacial dysmorphism, small testes, muscle wasting in
CC       lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet,
CC       and abnormalities of the toes. Additional neurologic manifestations
CC       include speech delay and impairment, tremor, seizures, gait ataxia,
CC       hyperactivity and decreased attention span.
CC       {ECO:0000269|PubMed:17236139, ECO:0000269|PubMed:17273978,
CC       ECO:0000269|PubMed:19377476, ECO:0000269|PubMed:20002452}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB67315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAK16812.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY365125; AAR13073.1; -; mRNA.
DR   EMBL; AF212995; AAK16812.1; ALT_FRAME; mRNA.
DR   EMBL; AK123688; BAG53936.1; -; mRNA.
DR   EMBL; AK299081; BAH12944.1; -; mRNA.
DR   EMBL; AK315037; BAG37520.1; -; mRNA.
DR   EMBL; BX537787; CAD97843.1; -; mRNA.
DR   EMBL; AC002476; AAB67315.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL451005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471107; EAX11877.1; -; Genomic_DNA.
DR   EMBL; BC036216; AAH36216.1; -; mRNA.
DR   EMBL; AB014595; BAA31670.2; -; mRNA.
DR   EMBL; U58091; AAC50548.1; -; mRNA.
DR   CCDS; CCDS35379.1; -. [Q13620-2]
DR   CCDS; CCDS43987.1; -. [Q13620-1]
DR   RefSeq; NP_001073341.1; NM_001079872.1. [Q13620-1]
DR   RefSeq; NP_003579.3; NM_003588.3. [Q13620-2]
DR   RefSeq; XP_011529702.1; XM_011531400.2.
DR   PDB; 2DO7; NMR; -; A=826-913.
DR   PDB; 4A0C; X-ray; 3.80 A; C/E=192-913.
DR   PDB; 4A0L; X-ray; 7.40 A; E/H=192-913.
DR   PDB; 4A64; X-ray; 2.57 A; A/B/C/D=206-557.
DR   PDBsum; 2DO7; -.
DR   PDBsum; 4A0C; -.
DR   PDBsum; 4A0L; -.
DR   PDBsum; 4A64; -.
DR   SMR; Q13620; -.
DR   BioGRID; 114028; 599.
DR   ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR   CORUM; Q13620; -.
DR   DIP; DIP-31609N; -.
DR   IntAct; Q13620; 294.
DR   MINT; Q13620; -.
DR   STRING; 9606.ENSP00000384109; -.
DR   GlyGen; Q13620; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q13620; -.
DR   PhosphoSitePlus; Q13620; -.
DR   SwissPalm; Q13620; -.
DR   BioMuta; CUL4B; -.
DR   DMDM; 296439468; -.
DR   EPD; Q13620; -.
DR   jPOST; Q13620; -.
DR   MassIVE; Q13620; -.
DR   PaxDb; Q13620; -.
DR   PeptideAtlas; Q13620; -.
DR   PRIDE; Q13620; -.
DR   ProteomicsDB; 59611; -. [Q13620-2]
DR   ProteomicsDB; 59612; -. [Q13620-1]
DR   ProteomicsDB; 59613; -. [Q13620-3]
DR   Antibodypedia; 531; 409 antibodies.
DR   DNASU; 8450; -.
DR   Ensembl; ENST00000371322; ENSP00000360373; ENSG00000158290. [Q13620-1]
DR   Ensembl; ENST00000371323; ENSP00000360374; ENSG00000158290. [Q13620-3]
DR   Ensembl; ENST00000404115; ENSP00000384109; ENSG00000158290. [Q13620-2]
DR   GeneID; 8450; -.
DR   KEGG; hsa:8450; -.
DR   UCSC; uc004esv.4; human. [Q13620-2]
DR   CTD; 8450; -.
DR   DisGeNET; 8450; -.
DR   GeneCards; CUL4B; -.
DR   HGNC; HGNC:2555; CUL4B.
DR   HPA; ENSG00000158290; Low tissue specificity.
DR   MalaCards; CUL4B; -.
DR   MIM; 300304; gene.
DR   MIM; 300354; phenotype.
DR   neXtProt; NX_Q13620; -.
DR   OpenTargets; ENSG00000158290; -.
DR   Orphanet; 85293; X-linked intellectual disability, Cabezas type.
DR   PharmGKB; PA27051; -.
DR   VEuPathDB; HostDB:ENSG00000158290.16; -.
DR   eggNOG; KOG2167; Eukaryota.
DR   GeneTree; ENSGT00940000155339; -.
DR   HOGENOM; CLU_004747_7_2_1; -.
DR   InParanoid; Q13620; -.
DR   OMA; PKYRVKI; -.
DR   OrthoDB; 1040292at2759; -.
DR   PhylomeDB; Q13620; -.
DR   TreeFam; TF101153; -.
DR   PathwayCommons; Q13620; -.
DR   Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR   Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   SIGNOR; Q13620; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 8450; 16 hits in 627 CRISPR screens.
DR   ChiTaRS; CUL4B; human.
DR   EvolutionaryTrace; Q13620; -.
DR   GeneWiki; CUL4B; -.
DR   GenomeRNAi; 8450; -.
DR   Pharos; Q13620; Tbio.
DR   PRO; PR:Q13620; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q13620; protein.
DR   Bgee; ENSG00000158290; Expressed in testis and 244 other tissues.
DR   ExpressionAtlas; Q13620; baseline and differential.
DR   Genevisible; Q13620; HS.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:UniProtKB.
DR   GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR   GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
DR   GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
DR   GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
DR   GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
DR   GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   GO; GO:0070914; P:UV-damage excision repair; IDA:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR033044; CUL4B.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11932:SF66; PTHR11932:SF66; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF74788; SSF74788; 1.
DR   SUPFAM; SSF75632; SSF75632; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW   Disease variant; DNA damage; DNA repair; Dwarfism; Isopeptide bond;
KW   Mental retardation; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..913
FT                   /note="Cullin-4B"
FT                   /id="PRO_0000393946"
FT   MOTIF           55..58
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   COMPBIAS        3..193
FT                   /note="Ser-rich"
FT   MOD_RES         49
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13619"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         148
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:A2A432"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13619"
FT   CROSSLNK        859
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
FT   VAR_SEQ         1..196
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039084"
FT   VAR_SEQ         1..22
FT                   /note="MMSQSSGSGDGNDDEATTSKDG -> MFPT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14578910,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_039085"
FT   VAR_SEQ         197..203
FT                   /note="LVIKNFK -> MIDPDFA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039086"
FT   VARIANT         103
FT                   /note="L -> P (in dbSNP:rs61759504)"
FT                   /evidence="ECO:0000269|PubMed:17236139"
FT                   /id="VAR_032272"
FT   VARIANT         213
FT                   /note="T -> I (in MRXS15; uncertain pathological
FT                   significance; dbSNP:rs763692058)"
FT                   /evidence="ECO:0000269|PubMed:17236139,
FT                   ECO:0000269|PubMed:19377476"
FT                   /id="VAR_032273"
FT   VARIANT         572
FT                   /note="R -> C (in MRXS15; dbSNP:rs121434615)"
FT                   /evidence="ECO:0000269|PubMed:17236139,
FT                   ECO:0000269|PubMed:19377476"
FT                   /id="VAR_032274"
FT   VARIANT         745
FT                   /note="V -> A (in MRXS15)"
FT                   /evidence="ECO:0000269|PubMed:17236139,
FT                   ECO:0000269|PubMed:19377476"
FT                   /id="VAR_032275"
FT   MUTAGEN         55..58
FT                   /note="Missing: Distributed in cytoplasm. Fails to promote
FT                   cell proliferation. No binding to KPNA2, KPNA4 and KPNA1."
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   MUTAGEN         55
FT                   /note="K->A: No impairment in nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   MUTAGEN         56
FT                   /note="K->A: Disrupts nuclear localization and does not
FT                   bind KPNA2, KPNA4, KPNA1; when associated with A-57.
FT                   Disrupts nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   MUTAGEN         57
FT                   /note="R->A: Disrupts nuclear localization and does not
FT                   bind KPNA2, KPNA4, KPNA1; when associated with A-56.
FT                   Disrupts nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   MUTAGEN         58
FT                   /note="K->A: No impairment in nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:19801544"
FT   CONFLICT        69
FT                   /note="S -> R (in Ref. 3; BAG53936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="E -> G (in Ref. 4; CAD97843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="S -> P (in Ref. 3; BAG53936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="K -> N (in Ref. 2; AAK16812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="E -> G (in Ref. 3; BAG53936)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="I -> M (in Ref. 2; AAK16812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        485
FT                   /note="G -> D (in Ref. 4; CAD97843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        664
FT                   /note="Q -> QVK (in Ref. 2; AAK16812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        727
FT                   /note="L -> I (in Ref. 1; AAR13073 and 7; AAH36216)"
FT                   /evidence="ECO:0000305"
FT   STRAND          210..212
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           215..228
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           237..250
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           253..270
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           271..276
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           282..306
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           308..312
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   TURN            315..317
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           324..335
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   TURN            336..338
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           340..358
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           365..377
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           381..384
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           386..407
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           410..430
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           434..436
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           437..448
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           450..452
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           453..466
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           470..480
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           486..507
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   STRAND          511..513
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           515..533
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           538..549
FT                   /evidence="ECO:0007744|PDB:4A64"
FT   HELIX           841..860
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   STRAND          861..865
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   HELIX           866..876
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   HELIX           883..895
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   STRAND          898..901
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   STRAND          908..911
FT                   /evidence="ECO:0007744|PDB:2DO7"
FT   MOD_RES         Q13620-1:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q13620-1:8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q13620-1:10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
SQ   SEQUENCE   913 AA;  103982 MW;  3E58C5868FDF0700 CRC64;
     MMSQSSGSGD GNDDEATTSK DGGFSSPSPS AAAAAQEVRS ATDGNTSTTP PTSAKKRKLN
     SSSSSSSNSS NEREDFDSTS SSSSTPPLQP RDSASPSTSS FCLGVSVAAS SHVPIQKKLR
     FEDTLEFVGF DAKMAEESSS SSSSSSPTAA TSQQQQLKNK SILISSVASV HHANGLAKSS
     TTVSSFANSK PGSAKKLVIK NFKDKPKLPE NYTDETWQKL KEAVEAIQNS TSIKYNLEEL
     YQAVENLCSY KISANLYKQL RQICEDHIKA QIHQFREDSL DSVLFLKKID RCWQNHCRQM
     IMIRSIFLFL DRTYVLQNSM LPSIWDMGLE LFRAHIISDQ KVQNKTIDGI LLLIERERNG
     EAIDRSLLRS LLSMLSDLQI YQDSFEQRFL EETNRLYAAE GQKLMQEREV PEYLHHVNKR
     LEEEADRLIT YLDQTTQKSL IATVEKQLLG EHLTAILQKG LNNLLDENRI QDLSLLYQLF
     SRVRGGVQVL LQQWIEYIKA FGSTIVINPE KDKTMVQELL DFKDKVDHII DICFLKNEKF
     INAMKEAFET FINKRPNKPA ELIAKYVDSK LRAGNKEATD EELEKMLDKI MIIFRFIYGK
     DVFEAFYKKD LAKRLLVGKS ASVDAEKSML SKLKHECGAA FTSKLEGMFK DMELSKDIMI
     QFKQYMQNQN VPGNIELTVN ILTMGYWPTY VPMEVHLPPE MVKLQEIFKT FYLGKHSGRK
     LQWQSTLGHC VLKAEFKEGK KELQVSLFQT LVLLMFNEGE EFSLEEIKQA TGIEDGELRR
     TLQSLACGKA RVLAKNPKGK DIEDGDKFIC NDDFKHKLFR IKINQIQMKE TVEEQASTTE
     RVFQDRQYQI DAAIVRIMKM RKTLSHNLLV SEVYNQLKFP VKPADLKKRI ESLIDRDYME
     RDKENPNQYN YIA
//
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