CUL4B_HUMAN
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 03-AUG-2022, entry version 205.
DE RecName: Full=Cullin-4B {ECO:0000305};
DE Short=CUL-4B {ECO:0000303|PubMed:14578910};
GN Name=CUL4B {ECO:0000303|PubMed:14578910, ECO:0000312|HGNC:HGNC:2555};
GN Synonyms=KIAA0695 {ECO:0000303|PubMed:9734811};
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), AND FUNCTION.
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, AND PATHWAY.
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, FUNCTION, AND PATHWAY.
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 MRXSC.
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, PATHWAY, 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 INVOLVEMENT IN MRXSC.
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 FUNCTION, AND PATHWAY.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [36]
RP FUNCTION, AND PATHWAY.
RX PubMed=30166453; DOI=10.15252/embj.201797508;
RA Chen S.H., Jang G.M., Huettenhain R., Gordon D.E., Du D., Newton B.W.,
RA Johnson J.R., Hiatt J., Hultquist J.F., Johnson T.L., Liu Y.L.,
RA Burton L.A., Ye J., Reichermeier K.M., Stroud R.M., Marson A., Debnath J.,
RA Gross J.D., Krogan N.J.;
RT "CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to
RT modulate CRL5 signaling.";
RL EMBO J. 37:0-0(2018).
RN [37]
RP FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN
RP LIGASE COMPLEX, AND PATHWAY.
RX PubMed=33854232; DOI=10.1038/s41586-021-03422-5;
RA Maiani E., Milletti G., Nazio F., Holdgaard S.G., Bartkova J., Rizza S.,
RA Cianfanelli V., Lorente M., Simoneschi D., Di Marco M., D'Acunzo P.,
RA Di Leo L., Rasmussen R., Montagna C., Raciti M., De Stefanis C.,
RA Gabicagogeascoa E., Rona G., Salvador N., Pupo E., Merchut-Maya J.M.,
RA Daniel C.J., Carinci M., Cesarini V., O'sullivan A., Jeong Y.T., Bordi M.,
RA Russo F., Campello S., Gallo A., Filomeni G., Lanzetti L., Sears R.C.,
RA Hamerlik P., Bartolazzi A., Hynds R.E., Pearce D.R., Swanton C., Pagano M.,
RA Velasco G., Papaleo E., De Zio D., Maya-Mendoza A., Locatelli F.,
RA Bartek J., Cecconi F.;
RT "AMBRA1 regulates cyclin D to guard S-phase entry and genomic integrity.";
RL Nature 592:799-803(2021).
RN [38]
RP FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN
RP LIGASE COMPLEX, AND PATHWAY.
RX PubMed=33854239; DOI=10.1038/s41586-021-03474-7;
RA Chaikovsky A.C., Li C., Jeng E.E., Loebell S., Lee M.C., Murray C.W.,
RA Cheng R., Demeter J., Swaney D.L., Chen S.H., Newton B.W., Johnson J.R.,
RA Drainas A.P., Shue Y.T., Seoane J.A., Srinivasan P., He A., Yoshida A.,
RA Hipkins S.Q., McCrea E., Poltorack C.D., Krogan N.J., Diehl J.A., Kong C.,
RA Jackson P.K., Curtis C., Petrov D.A., Bassik M.C., Winslow M.M., Sage J.;
RT "The AMBRA1 E3 ligase adaptor regulates the stability of cyclin D.";
RL Nature 592:794-798(2021).
RN [39]
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 [40]
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 [41]
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 [42]
RP VARIANTS MRXSC 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 [43]
RP VARIANTS MRXSC 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 (PubMed:14578910,
CC PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:29779948,
CC PubMed:30166453, PubMed:33854232, PubMed:33854239, PubMed:22118460).
CC The functional specificity of the E3 ubiquitin-protein ligase complex
CC depends on the variable substrate recognition subunit (PubMed:14578910,
CC PubMed:16678110, PubMed:18593899, PubMed:29779948, PubMed:22118460).
CC CUL4B may act within the complex as a scaffold protein, contributing to
CC catalysis through positioning of the substrate and the ubiquitin-
CC conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899,
CC PubMed:22118460). Plays a role as part of the E3 ubiquitin-protein
CC ligase complex in polyubiquitination of CDT1, histone H2A, histone H3
CC and histone H4 in response to radiation-induced DNA damage
CC (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV
CC damaged chromatin by DDB2 and may be important for DNA repair and DNA
CC replication (PubMed:16678110). A number of DCX complexes (containing
CC either TRPC4AP or DCAF12 as substrate-recognition component) are part
CC of the DesCEND (destruction via C-end degrons) pathway, which
CC recognizes a C-degron located at the extreme C terminus of target
CC proteins, leading to their ubiquitination and degradation
CC (PubMed:29779948). The DCX(AMBRA1) complex is a master regulator of the
CC transition from G1 to S cell phase by mediating ubiquitination of
CC phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232,
CC PubMed:33854239). The DCX(AMBRA1) complex also acts as a regulator of
CC Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating
CC ubiquitination and degradation of Elongin-C (ELOC) component of CRL5
CC complexes (PubMed:30166453). Required for ubiquitination of cyclin E
CC (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression
CC (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-
CC rapamycin (mTOR) pathway involved in control of cell growth, size and
CC metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-
CC mediated pathway is dependent upon 26S proteasome function and requires
CC interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A,
CC contributes to ribosome biogenesis (PubMed:26711351).
CC {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693,
CC ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18235224,
CC ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544,
CC ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:26711351,
CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453,
CC ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:16678110,
CC ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:29779948,
CC ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33854232,
CC ECO:0000269|PubMed:33854239}.
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 (PubMed:18593899, PubMed:10230407, PubMed:16678110, PubMed:17041588).
CC Component of the DCX(DTL) complex with the putative substrate
CC recognition component DTL (PubMed:17041588). Component of the DCX(DDB2)
CC complex with the putative substrate recognition component DDB2
CC (PubMed:16678110). Component of DCX complexes part of the DesCEND
CC (destruction via C-end degrons) pathway, which contain either TRPC4AP
CC or DCAF12 as substrate-recognition component (PubMed:29779948).
CC Component of the DCX(AMBRA1) complex with the substrate recognition
CC component AMBRA1 (PubMed:30166453, PubMed:33854232, PubMed:33854239).
CC Part of a complex with RBX1 and TIP120A/CAND1 (PubMed:12609982,
CC PubMed:22118460). Interacts with RBX1, GRWD1, MLST8, SMU1, TLE2, TLE3,
CC DCAF1, DDA1, DCAF6, DCAF17, DDB2, DCAF8, TIP120A/CAND1 and TMEM113
CC (PubMed:17041588, PubMed:16949367, PubMed:18235224). Interacts with
CC cyclin E (CCNE1 or CCNE2) and with importins alpha-1 (KPNA2), alpha-3
CC (KPNA4), alpha-5 (KPNA1) and beta-1 (KPNB1) (PubMed:16322693,
CC PubMed:19801544). May interact with WDR26, WDR51B, SNRNP40, WDR61,
CC WDR76 and WDR5 (PubMed:17041588). Interacts (unneddylated form) with
CC DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions
CC promote the cullin neddylation (PubMed:23201271, PubMed:26906416).
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:12609982,
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 ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453,
CC ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}.
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; Q93009: USP7; NbExp=2; IntAct=EBI-456067, EBI-302474;
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: Intellectual developmental disorder, X-linked, syndromic,
CC Cabezas type (MRXSC) [MIM:300354]: A syndromic form of X-linked
CC intellectual disability characterized by severe intellectual deficit
CC associated with short stature, craniofacial dysmorphism, small testes,
CC muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes
CC cavus, small feet, and abnormalities of the toes. Additional neurologic
CC manifestations include speech delay and impairment, tremor, seizures,
CC gait ataxia, 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 AlphaFoldDB; Q13620; -.
DR SMR; Q13620; -.
DR BioGRID; 114028; 682.
DR ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR CORUM; Q13620; -.
DR DIP; DIP-31609N; -.
DR IntAct; Q13620; 301.
DR MINT; Q13620; -.
DR STRING; 9606.ENSP00000384109; -.
DR ChEMBL; CHEMBL4523287; -.
DR GlyGen; Q13620; 6 sites, 2 O-linked glycans (6 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 MaxQB; 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; 441 antibodies from 35 providers.
DR DNASU; 8450; -.
DR Ensembl; ENST00000371322.11; ENSP00000360373.5; ENSG00000158290.19. [Q13620-1]
DR Ensembl; ENST00000371323.3; ENSP00000360374.3; ENSG00000158290.19. [Q13620-3]
DR Ensembl; ENST00000680673.1; ENSP00000505084.1; ENSG00000158290.19. [Q13620-2]
DR Ensembl; ENST00000681253.1; ENSP00000506259.1; ENSG00000158290.19. [Q13620-2]
DR Ensembl; ENST00000681652.1; ENSP00000505176.1; ENSG00000158290.19. [Q13620-2]
DR GeneID; 8450; -.
DR KEGG; hsa:8450; -.
DR MANE-Select; ENST00000371322.11; ENSP00000360373.5; NM_001079872.2; NP_001073341.1. [Q13620-1]
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; -.
DR eggNOG; KOG2167; Eukaryota.
DR GeneTree; ENSGT00940000155339; -.
DR HOGENOM; CLU_004747_7_2_1; -.
DR InParanoid; Q13620; -.
DR OMA; WPTYPVM; -.
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 SignaLink; Q13620; -.
DR SIGNOR; Q13620; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8450; 20 hits in 752 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 sperm and 205 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:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IC:ComplexPortal.
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:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
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:0070914; P:UV-damage excision repair; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR033044; CUL4B.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR 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; Intellectual disability;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..913
FT /note="Cullin-4B"
FT /id="PRO_0000393946"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 55..58
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:19801544"
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 MRXSC; unknown pathological significance;
FT 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 MRXSC; 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 MRXSC)"
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:0007829|PDB:4A64"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 253..270
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 282..306
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:4A64"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:4A64"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 386..407
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 410..430
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 453..466
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 486..507
FT /evidence="ECO:0007829|PDB:4A64"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 515..533
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 538..549
FT /evidence="ECO:0007829|PDB:4A64"
FT HELIX 841..860
FT /evidence="ECO:0007829|PDB:2DO7"
FT STRAND 861..865
FT /evidence="ECO:0007829|PDB:2DO7"
FT HELIX 866..876
FT /evidence="ECO:0007829|PDB:2DO7"
FT HELIX 883..895
FT /evidence="ECO:0007829|PDB:2DO7"
FT STRAND 898..901
FT /evidence="ECO:0007829|PDB:2DO7"
FT STRAND 908..911
FT /evidence="ECO:0007829|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
