Full text data of RBX1
RBX1
(RNF75, ROC1)
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase RBX1; 6.3.2.- (Protein ZYP; RING finger protein 75; RING-box protein 1; Rbx1; Regulator of cullins 1; E3 ubiquitin-protein ligase RBX1, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase RBX1; 6.3.2.- (Protein ZYP; RING finger protein 75; RING-box protein 1; Rbx1; Regulator of cullins 1; E3 ubiquitin-protein ligase RBX1, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62877
ID RBX1_HUMAN Reviewed; 108 AA.
AC P62877; B2RDY1; Q8N6Z8; Q9D1S2; Q9WUK9; Q9Y254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase RBX1;
DE EC=6.3.2.-;
DE AltName: Full=Protein ZYP;
DE AltName: Full=RING finger protein 75;
DE AltName: Full=RING-box protein 1;
DE Short=Rbx1;
DE AltName: Full=Regulator of cullins 1;
DE Contains:
DE RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
GN Name=RBX1; Synonyms=RNF75, ROC1;
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], INTERACTION WITH CULLINS, AND MUTAGENESIS
RP OF CYS-53; CYS-56; CYS-75 AND HIS-77.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN CBC(VHL) COMPLEX.
RX PubMed=10213691; DOI=10.1126/science.284.5414.657;
RA Kamura T., Koepp D.M., Conrad M.N., Skowyra D., Moreland R.J.,
RA Iliopoulos O., Lane W.S., Kaelin W.G. Jr., Elledge S.J., Conaway R.C.,
RA Harper J.W., Conaway J.W.;
RT "Rbx1, a component of the VHL tumor suppressor complex and SCF
RT ubiquitin ligase.";
RL Science 284:657-661(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [8]
RP PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-108.
RC TISSUE=Brain;
RX PubMed=10643962;
RA Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L.,
RA Rieger F., Alliel P.M.;
RT "Genomic organization and expression of the ubiquitin-proteasome
RT complex-associated protein Rbx1/ROC1/Hrt1.";
RL Cell. Mol. Biol. 45:1131-1137(1999).
RN [10]
RP PROTEIN SEQUENCE OF 92-105, INTERACTION WITH CUL1, AND IDENTIFICATION
RP IN A COMPLEX WITH CUL1; SKP1 AND SKP2.
RC TISSUE=Cervix carcinoma;
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 [11]
RP FUNCTION.
RX PubMed=10579999; DOI=10.1101/gad.13.22.2928;
RA Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.;
RT "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1
RT modification of cullins Cdc53 and Cul2.";
RL Genes Dev. 13:2928-2933(1999).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11027288; DOI=10.1128/MCB.20.21.8185-8197.2000;
RA Furukawa M., Zhang Y., McCarville J., Ohta T., Xiong Y.;
RT "The CUL1 C-terminal sequence and ROC1 are required for efficient
RT nuclear accumulation, NEDD8 modification, and ubiquitin ligase
RT activity of CUL1.";
RL Mol. Cell. Biol. 20:8185-8197(2000).
RN [13]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MUF1, AND
RP IDENTIFICATION IN COMPLEXES WITH CUL5.
RX PubMed=11384984; DOI=10.1074/jbc.M103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that
RT can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [14]
RP INTERACTION WITH COPS6.
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 [15]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
RX PubMed=12149480; DOI=10.1073/pnas.162424199;
RA Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A.,
RA Stearman R., Klausner R.D., Malik S., Lane W.S., Sorokina I.,
RA Roeder R.G., Conaway J.W., Conaway R.C.;
RT "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein
RT that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002).
RN [16]
RP IDENTIFICATION IN SCF-LIKE COMPLEX, AND INTERACTION WITH CUL7.
RX PubMed=12481031; DOI=10.1073/pnas.252646399;
RA Dias D.C., Dolios G., Wang R., Pan Z.Q.;
RT "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to
RT form an SCF-like complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
RN [17]
RP IDENTIFICATION IN THE CSA COMPLEX WITH ERCC8; DDB1 AND CUL4A, AND
RP INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9
RP SIGNALOSOME.
RX PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M.,
RA Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [18]
RP IDENTIFICATION IN THE DCX DET1-COP1 COMPLEX WITH DDB1; CUL4A; COP1 AND
RP DET1.
RX PubMed=14739464; DOI=10.1126/science.1093549;
RA Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D.,
RA Deshaies R.J., Dixit V.M.;
RT "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin
RT ligase.";
RL Science 303:1371-1374(2004).
RN [19]
RP FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN
RP THE BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, AND
RP IDENTIFICATION IN THE BCR(GAN) COMPLEX.
RX PubMed=15983046; DOI=10.1074/jbc.M501279200;
RA Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
RT "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
RT Cul3, targets Keap1 for degradation by a proteasome-independent
RT pathway.";
RL J. Biol. Chem. 280:30091-30099(2005).
RN [20]
RP FUNCTION.
RX PubMed=16751180; DOI=10.1101/gad.378206;
RA Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T.,
RA Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y.;
RT "CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway
RT establishes a link between complementation factors of the Cockayne
RT syndrome.";
RL Genes Dev. 20:1429-1434(2006).
RN [21]
RP IDENTIFICATION IN COMPLEX WITH DDB1; DDB2; CUL4A AND CUL4B, 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
RT ligase facilitates cellular response to DNA damage.";
RL Mol. Cell 22:383-394(2006).
RN [22]
RP FUNCTION.
RX PubMed=18397884; DOI=10.1074/jbc.M802030200;
RA Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
RT "Regulation of TIP60 by ATF2 modulates ATM activation.";
RL J. Biol. Chem. 283:17605-17614(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP INTERACTION WITH CUL1; FBXO3; SKP1 AND PML.
RX PubMed=18809579; DOI=10.1128/MCB.00897-08;
RA Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P.,
RA Kitabayashi I.;
RT "PML activates transcription by protecting HIPK2 and p300 from
RT SCFFbx3-mediated degradation.";
RL Mol. Cell. Biol. 28:7126-7138(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND CDC34, AND
RP FUNCTION.
RX PubMed=19112177; DOI=10.1074/jbc.M804531200;
RA Cen B., Li H., Weinstein I.B.;
RT "Histidine triad nucleotide-binding protein 1 up-regulates cellular
RT levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.";
RL J. Biol. Chem. 284:5265-5276(2009).
RN [27]
RP INTERACTION WITH UBE2M.
RX PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
RA Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M.,
RA Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F.,
RA Schulman B.A.;
RT "E2-RING expansion of the NEDD8 cascade confers specificity to cullin
RT modification.";
RL Mol. Cell 33:483-495(2009).
RN [28]
RP FUNCTION, AND INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
RX PubMed=19679664; DOI=10.1074/jbc.M109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I.,
RA Oda T., Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [29]
RP IDENTIFICATION IN THE SCF(CYCLIN F) COMPLEX.
RX PubMed=20596027; DOI=10.1038/nature09140;
RA D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
RA Washburn M.P., Dynlacht B., Pagano M.;
RT "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity
RT through CP110 degradation.";
RL Nature 466:138-142(2010).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT THR-9, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776
RP OF CUL1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH
RP CUL1; 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).
CC -!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-
CC based E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, including proteins involved in cell cycle progression,
CC signal transduction, transcription and transcription-coupled
CC nucleotide excision repair. The functional specificity of the E3
CC ubiquitin-protein ligase complexes depends on the variable
CC substrate recognition components. As a component of the CSA
CC complex promotes the ubiquitination of ERCC6 resulting in
CC proteasomal degradation. Through the RING-type zinc finger, seems
CC to recruit the E2 ubiquitination enzyme, like CDC34, to the
CC complex and brings it into close proximity to the substrate.
CC Probably also stimulates CDC34 autoubiquitination. May be required
CC for histone H3 and histone H4 ubiquitination in response to
CC ultraviolet and for subsequent DNA repair. Promotes the
CC neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with
CC UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41.
CC In concert with ATF2 and CUL3, promotes degradation of KAT5
CC thereby attenuating its ability to acetylate and activate ATM.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and
CC SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1
CC and FBXW8. Part of CBC(VHL) complexes with elongin BC complex
CC (TCEB1 and TCEB2), CUL2 or CUL5 and VHL. Part of the CSA complex
CC (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex
CC containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts
CC with RNA polymerase II; upon UV irradiation it interacts with the
CC COP9 signalosome and preferentially with the hyperphosphorylated
CC form of RNA polymerase II. Part of multisubunit E3 ubiquitin
CC ligase complexes with elongin BC complex (TCEB1 and TCEB2), CUL2
CC and MED8; elongin BC complex (TCEB1 and TCEB2), CUL5 and MUF1.
CC Part of multisubunit complexes with elongin BC complex (TCEB1 and
CC TCEB2), elongin A/TCEB3 or SOCS1 or WSB1 and CUL5. Interacts
CC directly with CUL1 and probably also with CUL2, CUL3, CUL4A,
CC CUL4B, CUL5 and CUL7. Probably interacts with CDC34. Interacts
CC with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase
CC complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1.
CC Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and
CC CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex
CC consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts
CC with PML via FBXO3. Interacts with human adenovirus early E1A
CC protein; this interaction inhibits RBX1-CUL1-dependent elongation
CC reaction of ubiquitin chains by the SCF(FBW7) complex. Component
CC of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and
CC CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex together with HINT1 and CDC34. Component of
CC multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC formed of CUL3, RBX1 and a variable BTB domain-containing protein.
CC Part of the BCR(ENC1) complex containing ENC1. Part of the
CC BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex
CC containing KLHL41. Part of the BCR(KEAP1) complex containing
CC KEAP1.
CC -!- INTERACTION:
CC Q13616:CUL1; NbExp=12; IntAct=EBI-398523, EBI-359390;
CC Q13617:CUL2; NbExp=5; IntAct=EBI-398523, EBI-456179;
CC Q13620:CUL4B; NbExp=4; IntAct=EBI-398523, EBI-456067;
CC Q93034:CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139;
CC Q13309:SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for
CC ubiquitin ligase activity. It coordinates an additional third zinc
CC ion.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17370.2; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBX1ID42075ch22q13.html";
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DR EMBL; AF142059; AAD30146.1; -; mRNA.
DR EMBL; AF140598; AAD29715.1; -; mRNA.
DR EMBL; CR456560; CAG30446.1; -; mRNA.
DR EMBL; AK315722; BAG38078.1; -; mRNA.
DR EMBL; AL080242; CAB62925.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60403.1; -; Genomic_DNA.
DR EMBL; BC001466; AAH01466.1; -; mRNA.
DR EMBL; BC017370; AAH17370.2; ALT_INIT; mRNA.
DR EMBL; AY099360; AAM21718.1; -; mRNA.
DR PIR; T51146; T51146.
DR RefSeq; NP_055063.1; NM_014248.3.
DR UniGene; Hs.474949; -.
DR PDB; 1LDJ; X-ray; 3.00 A; B=19-108.
DR PDB; 1LDK; X-ray; 3.10 A; C=19-108.
DR PDB; 1U6G; X-ray; 3.10 A; B=1-108.
DR PDB; 2HYE; X-ray; 3.10 A; D=1-108.
DR PDB; 2LGV; NMR; -; A=12-108.
DR PDB; 3DPL; X-ray; 2.60 A; R=5-108.
DR PDB; 3DQV; X-ray; 3.00 A; R/Y=5-108.
DR PDB; 3RTR; X-ray; 3.21 A; B/D/F/H=5-108.
DR PDB; 4F52; X-ray; 3.00 A; B/D=5-108.
DR PDBsum; 1LDJ; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1U6G; -.
DR PDBsum; 2HYE; -.
DR PDBsum; 2LGV; -.
DR PDBsum; 3DPL; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 3RTR; -.
DR PDBsum; 4F52; -.
DR ProteinModelPortal; P62877; -.
DR SMR; P62877; 19-106.
DR DIP; DIP-17014N; -.
DR IntAct; P62877; 42.
DR MINT; MINT-235894; -.
DR STRING; 9606.ENSP00000216225; -.
DR PhosphoSite; P62877; -.
DR DMDM; 51338609; -.
DR PaxDb; P62877; -.
DR PRIDE; P62877; -.
DR DNASU; 9978; -.
DR Ensembl; ENST00000216225; ENSP00000216225; ENSG00000100387.
DR GeneID; 9978; -.
DR KEGG; hsa:9978; -.
DR UCSC; uc003azk.3; human.
DR CTD; 9978; -.
DR GeneCards; GC22P041347; -.
DR H-InvDB; HIX0016509; -.
DR HGNC; HGNC:9928; RBX1.
DR HPA; HPA003038; -.
DR MIM; 603814; gene.
DR neXtProt; NX_P62877; -.
DR PharmGKB; PA34299; -.
DR eggNOG; COG5194; -.
DR HOGENOM; HOG000171951; -.
DR HOVERGEN; HBG001507; -.
DR InParanoid; P62877; -.
DR KO; K03868; -.
DR OMA; ARSVCPL; -.
DR OrthoDB; EOG7CG721; -.
DR PhylomeDB; P62877; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P62877; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P62877; -.
DR GeneWiki; RBX1; -.
DR GenomeRNAi; 9978; -.
DR NextBio; 37682; -.
DR PRO; PR:P62877; -.
DR Bgee; P62877; -.
DR CleanEx; HS_RBX1; -.
DR Genevestigator; P62877; -.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030891; C:VCB complex; IEA:Ensembl.
DR GO; GO:0019788; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair;
KW Host-virus interaction; Ligase; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1 108 E3 ubiquitin-protein ligase RBX1.
FT /FTId=PRO_0000423264.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 108 E3 ubiquitin-protein ligase RBX1, N-
FT terminally processed.
FT /FTId=PRO_0000056013.
FT ZN_FING 53 98 RING-type.
FT METAL 42 42 Zinc 1.
FT METAL 45 45 Zinc 1.
FT METAL 53 53 Zinc 3.
FT METAL 56 56 Zinc 3.
FT METAL 68 68 Zinc 3.
FT METAL 75 75 Zinc 2.
FT METAL 77 77 Zinc 2.
FT METAL 80 80 Zinc 1.
FT METAL 82 82 Zinc 3.
FT METAL 83 83 Zinc 1.
FT METAL 94 94 Zinc 2.
FT METAL 97 97 Zinc 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylalanine; in E3 ubiquitin-protein
FT ligase RBX1, N-terminally processed.
FT MOD_RES 9 9 Phosphothreonine.
FT MUTAGEN 53 53 C->A: Strong reduction in ligase
FT activity; when associated with A-56.
FT MUTAGEN 56 56 C->A: Strong reduction in ligase
FT activity; when associated with A-53.
FT MUTAGEN 75 75 C->A: Strong reduction in ligase
FT activity; when associated with A-77.
FT MUTAGEN 77 77 H->A: Strong reduction in ligase
FT activity; when associated with A-75.
FT CONFLICT 18 18 G -> S (in Ref. 9; AAM21718).
FT STRAND 21 37
FT STRAND 39 41
FT STRAND 43 45
FT TURN 49 54
FT HELIX 56 59
FT TURN 63 67
FT STRAND 70 73
FT STRAND 74 76
FT STRAND 78 80
FT HELIX 81 88
FT STRAND 90 93
FT STRAND 95 97
FT STRAND 103 105
SQ SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
//
ID RBX1_HUMAN Reviewed; 108 AA.
AC P62877; B2RDY1; Q8N6Z8; Q9D1S2; Q9WUK9; Q9Y254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase RBX1;
DE EC=6.3.2.-;
DE AltName: Full=Protein ZYP;
DE AltName: Full=RING finger protein 75;
DE AltName: Full=RING-box protein 1;
DE Short=Rbx1;
DE AltName: Full=Regulator of cullins 1;
DE Contains:
DE RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
GN Name=RBX1; Synonyms=RNF75, ROC1;
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], INTERACTION WITH CULLINS, AND MUTAGENESIS
RP OF CYS-53; CYS-56; CYS-75 AND HIS-77.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN CBC(VHL) COMPLEX.
RX PubMed=10213691; DOI=10.1126/science.284.5414.657;
RA Kamura T., Koepp D.M., Conrad M.N., Skowyra D., Moreland R.J.,
RA Iliopoulos O., Lane W.S., Kaelin W.G. Jr., Elledge S.J., Conaway R.C.,
RA Harper J.W., Conaway J.W.;
RT "Rbx1, a component of the VHL tumor suppressor complex and SCF
RT ubiquitin ligase.";
RL Science 284:657-661(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [8]
RP PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-108.
RC TISSUE=Brain;
RX PubMed=10643962;
RA Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L.,
RA Rieger F., Alliel P.M.;
RT "Genomic organization and expression of the ubiquitin-proteasome
RT complex-associated protein Rbx1/ROC1/Hrt1.";
RL Cell. Mol. Biol. 45:1131-1137(1999).
RN [10]
RP PROTEIN SEQUENCE OF 92-105, INTERACTION WITH CUL1, AND IDENTIFICATION
RP IN A COMPLEX WITH CUL1; SKP1 AND SKP2.
RC TISSUE=Cervix carcinoma;
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 [11]
RP FUNCTION.
RX PubMed=10579999; DOI=10.1101/gad.13.22.2928;
RA Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.;
RT "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1
RT modification of cullins Cdc53 and Cul2.";
RL Genes Dev. 13:2928-2933(1999).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11027288; DOI=10.1128/MCB.20.21.8185-8197.2000;
RA Furukawa M., Zhang Y., McCarville J., Ohta T., Xiong Y.;
RT "The CUL1 C-terminal sequence and ROC1 are required for efficient
RT nuclear accumulation, NEDD8 modification, and ubiquitin ligase
RT activity of CUL1.";
RL Mol. Cell. Biol. 20:8185-8197(2000).
RN [13]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MUF1, AND
RP IDENTIFICATION IN COMPLEXES WITH CUL5.
RX PubMed=11384984; DOI=10.1074/jbc.M103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that
RT can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [14]
RP INTERACTION WITH COPS6.
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 [15]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
RX PubMed=12149480; DOI=10.1073/pnas.162424199;
RA Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A.,
RA Stearman R., Klausner R.D., Malik S., Lane W.S., Sorokina I.,
RA Roeder R.G., Conaway J.W., Conaway R.C.;
RT "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein
RT that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002).
RN [16]
RP IDENTIFICATION IN SCF-LIKE COMPLEX, AND INTERACTION WITH CUL7.
RX PubMed=12481031; DOI=10.1073/pnas.252646399;
RA Dias D.C., Dolios G., Wang R., Pan Z.Q.;
RT "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to
RT form an SCF-like complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
RN [17]
RP IDENTIFICATION IN THE CSA COMPLEX WITH ERCC8; DDB1 AND CUL4A, AND
RP INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9
RP SIGNALOSOME.
RX PubMed=12732143; DOI=10.1016/S0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M.,
RA Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [18]
RP IDENTIFICATION IN THE DCX DET1-COP1 COMPLEX WITH DDB1; CUL4A; COP1 AND
RP DET1.
RX PubMed=14739464; DOI=10.1126/science.1093549;
RA Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D.,
RA Deshaies R.J., Dixit V.M.;
RT "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin
RT ligase.";
RL Science 303:1371-1374(2004).
RN [19]
RP FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN
RP THE BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, AND
RP IDENTIFICATION IN THE BCR(GAN) COMPLEX.
RX PubMed=15983046; DOI=10.1074/jbc.M501279200;
RA Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
RT "Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
RT Cul3, targets Keap1 for degradation by a proteasome-independent
RT pathway.";
RL J. Biol. Chem. 280:30091-30099(2005).
RN [20]
RP FUNCTION.
RX PubMed=16751180; DOI=10.1101/gad.378206;
RA Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T.,
RA Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y.;
RT "CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway
RT establishes a link between complementation factors of the Cockayne
RT syndrome.";
RL Genes Dev. 20:1429-1434(2006).
RN [21]
RP IDENTIFICATION IN COMPLEX WITH DDB1; DDB2; CUL4A AND CUL4B, 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
RT ligase facilitates cellular response to DNA damage.";
RL Mol. Cell 22:383-394(2006).
RN [22]
RP FUNCTION.
RX PubMed=18397884; DOI=10.1074/jbc.M802030200;
RA Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
RT "Regulation of TIP60 by ATF2 modulates ATM activation.";
RL J. Biol. Chem. 283:17605-17614(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP INTERACTION WITH CUL1; FBXO3; SKP1 AND PML.
RX PubMed=18809579; DOI=10.1128/MCB.00897-08;
RA Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P.,
RA Kitabayashi I.;
RT "PML activates transcription by protecting HIPK2 and p300 from
RT SCFFbx3-mediated degradation.";
RL Mol. Cell. Biol. 28:7126-7138(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
RP IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND CDC34, AND
RP FUNCTION.
RX PubMed=19112177; DOI=10.1074/jbc.M804531200;
RA Cen B., Li H., Weinstein I.B.;
RT "Histidine triad nucleotide-binding protein 1 up-regulates cellular
RT levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.";
RL J. Biol. Chem. 284:5265-5276(2009).
RN [27]
RP INTERACTION WITH UBE2M.
RX PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
RA Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M.,
RA Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F.,
RA Schulman B.A.;
RT "E2-RING expansion of the NEDD8 cascade confers specificity to cullin
RT modification.";
RL Mol. Cell 33:483-495(2009).
RN [28]
RP FUNCTION, AND INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
RX PubMed=19679664; DOI=10.1074/jbc.M109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I.,
RA Oda T., Kitagawa M.;
RT "Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
RL J. Biol. Chem. 284:27766-27779(2009).
RN [29]
RP IDENTIFICATION IN THE SCF(CYCLIN F) COMPLEX.
RX PubMed=20596027; DOI=10.1038/nature09140;
RA D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
RA Washburn M.P., Dynlacht B., Pagano M.;
RT "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity
RT through CP110 degradation.";
RL Nature 466:138-142(2010).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT THR-9, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776
RP OF CUL1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH
RP CUL1; 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).
CC -!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-
CC based E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, including proteins involved in cell cycle progression,
CC signal transduction, transcription and transcription-coupled
CC nucleotide excision repair. The functional specificity of the E3
CC ubiquitin-protein ligase complexes depends on the variable
CC substrate recognition components. As a component of the CSA
CC complex promotes the ubiquitination of ERCC6 resulting in
CC proteasomal degradation. Through the RING-type zinc finger, seems
CC to recruit the E2 ubiquitination enzyme, like CDC34, to the
CC complex and brings it into close proximity to the substrate.
CC Probably also stimulates CDC34 autoubiquitination. May be required
CC for histone H3 and histone H4 ubiquitination in response to
CC ultraviolet and for subsequent DNA repair. Promotes the
CC neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with
CC UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41.
CC In concert with ATF2 and CUL3, promotes degradation of KAT5
CC thereby attenuating its ability to acetylate and activate ATM.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and
CC SKP2. Part of a SCF-like complex consisting of CUL7, RBX1, SKP1
CC and FBXW8. Part of CBC(VHL) complexes with elongin BC complex
CC (TCEB1 and TCEB2), CUL2 or CUL5 and VHL. Part of the CSA complex
CC (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex
CC containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts
CC with RNA polymerase II; upon UV irradiation it interacts with the
CC COP9 signalosome and preferentially with the hyperphosphorylated
CC form of RNA polymerase II. Part of multisubunit E3 ubiquitin
CC ligase complexes with elongin BC complex (TCEB1 and TCEB2), CUL2
CC and MED8; elongin BC complex (TCEB1 and TCEB2), CUL5 and MUF1.
CC Part of multisubunit complexes with elongin BC complex (TCEB1 and
CC TCEB2), elongin A/TCEB3 or SOCS1 or WSB1 and CUL5. Interacts
CC directly with CUL1 and probably also with CUL2, CUL3, CUL4A,
CC CUL4B, CUL5 and CUL7. Probably interacts with CDC34. Interacts
CC with COPS6. Component of the DCX DET1-COP1 ubiquitin ligase
CC complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1.
CC Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and
CC CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex
CC consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts
CC with PML via FBXO3. Interacts with human adenovirus early E1A
CC protein; this interaction inhibits RBX1-CUL1-dependent elongation
CC reaction of ubiquitin chains by the SCF(FBW7) complex. Component
CC of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and
CC CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex together with HINT1 and CDC34. Component of
CC multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC formed of CUL3, RBX1 and a variable BTB domain-containing protein.
CC Part of the BCR(ENC1) complex containing ENC1. Part of the
CC BCR(GAN) complex containing GAN. Part of the BCR(KLHL41) complex
CC containing KLHL41. Part of the BCR(KEAP1) complex containing
CC KEAP1.
CC -!- INTERACTION:
CC Q13616:CUL1; NbExp=12; IntAct=EBI-398523, EBI-359390;
CC Q13617:CUL2; NbExp=5; IntAct=EBI-398523, EBI-456179;
CC Q13620:CUL4B; NbExp=4; IntAct=EBI-398523, EBI-456067;
CC Q93034:CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139;
CC Q13309:SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for
CC ubiquitin ligase activity. It coordinates an additional third zinc
CC ion.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17370.2; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RBX1ID42075ch22q13.html";
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DR EMBL; AF142059; AAD30146.1; -; mRNA.
DR EMBL; AF140598; AAD29715.1; -; mRNA.
DR EMBL; CR456560; CAG30446.1; -; mRNA.
DR EMBL; AK315722; BAG38078.1; -; mRNA.
DR EMBL; AL080242; CAB62925.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60403.1; -; Genomic_DNA.
DR EMBL; BC001466; AAH01466.1; -; mRNA.
DR EMBL; BC017370; AAH17370.2; ALT_INIT; mRNA.
DR EMBL; AY099360; AAM21718.1; -; mRNA.
DR PIR; T51146; T51146.
DR RefSeq; NP_055063.1; NM_014248.3.
DR UniGene; Hs.474949; -.
DR PDB; 1LDJ; X-ray; 3.00 A; B=19-108.
DR PDB; 1LDK; X-ray; 3.10 A; C=19-108.
DR PDB; 1U6G; X-ray; 3.10 A; B=1-108.
DR PDB; 2HYE; X-ray; 3.10 A; D=1-108.
DR PDB; 2LGV; NMR; -; A=12-108.
DR PDB; 3DPL; X-ray; 2.60 A; R=5-108.
DR PDB; 3DQV; X-ray; 3.00 A; R/Y=5-108.
DR PDB; 3RTR; X-ray; 3.21 A; B/D/F/H=5-108.
DR PDB; 4F52; X-ray; 3.00 A; B/D=5-108.
DR PDBsum; 1LDJ; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1U6G; -.
DR PDBsum; 2HYE; -.
DR PDBsum; 2LGV; -.
DR PDBsum; 3DPL; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 3RTR; -.
DR PDBsum; 4F52; -.
DR ProteinModelPortal; P62877; -.
DR SMR; P62877; 19-106.
DR DIP; DIP-17014N; -.
DR IntAct; P62877; 42.
DR MINT; MINT-235894; -.
DR STRING; 9606.ENSP00000216225; -.
DR PhosphoSite; P62877; -.
DR DMDM; 51338609; -.
DR PaxDb; P62877; -.
DR PRIDE; P62877; -.
DR DNASU; 9978; -.
DR Ensembl; ENST00000216225; ENSP00000216225; ENSG00000100387.
DR GeneID; 9978; -.
DR KEGG; hsa:9978; -.
DR UCSC; uc003azk.3; human.
DR CTD; 9978; -.
DR GeneCards; GC22P041347; -.
DR H-InvDB; HIX0016509; -.
DR HGNC; HGNC:9928; RBX1.
DR HPA; HPA003038; -.
DR MIM; 603814; gene.
DR neXtProt; NX_P62877; -.
DR PharmGKB; PA34299; -.
DR eggNOG; COG5194; -.
DR HOGENOM; HOG000171951; -.
DR HOVERGEN; HBG001507; -.
DR InParanoid; P62877; -.
DR KO; K03868; -.
DR OMA; ARSVCPL; -.
DR OrthoDB; EOG7CG721; -.
DR PhylomeDB; P62877; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P62877; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P62877; -.
DR GeneWiki; RBX1; -.
DR GenomeRNAi; 9978; -.
DR NextBio; 37682; -.
DR PRO; PR:P62877; -.
DR Bgee; P62877; -.
DR CleanEx; HS_RBX1; -.
DR Genevestigator; P62877; -.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0030891; C:VCB complex; IEA:Ensembl.
DR GO; GO:0019788; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair;
KW Host-virus interaction; Ligase; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1 108 E3 ubiquitin-protein ligase RBX1.
FT /FTId=PRO_0000423264.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 108 E3 ubiquitin-protein ligase RBX1, N-
FT terminally processed.
FT /FTId=PRO_0000056013.
FT ZN_FING 53 98 RING-type.
FT METAL 42 42 Zinc 1.
FT METAL 45 45 Zinc 1.
FT METAL 53 53 Zinc 3.
FT METAL 56 56 Zinc 3.
FT METAL 68 68 Zinc 3.
FT METAL 75 75 Zinc 2.
FT METAL 77 77 Zinc 2.
FT METAL 80 80 Zinc 1.
FT METAL 82 82 Zinc 3.
FT METAL 83 83 Zinc 1.
FT METAL 94 94 Zinc 2.
FT METAL 97 97 Zinc 2.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylalanine; in E3 ubiquitin-protein
FT ligase RBX1, N-terminally processed.
FT MOD_RES 9 9 Phosphothreonine.
FT MUTAGEN 53 53 C->A: Strong reduction in ligase
FT activity; when associated with A-56.
FT MUTAGEN 56 56 C->A: Strong reduction in ligase
FT activity; when associated with A-53.
FT MUTAGEN 75 75 C->A: Strong reduction in ligase
FT activity; when associated with A-77.
FT MUTAGEN 77 77 H->A: Strong reduction in ligase
FT activity; when associated with A-75.
FT CONFLICT 18 18 G -> S (in Ref. 9; AAM21718).
FT STRAND 21 37
FT STRAND 39 41
FT STRAND 43 45
FT TURN 49 54
FT HELIX 56 59
FT TURN 63 67
FT STRAND 70 73
FT STRAND 74 76
FT STRAND 78 80
FT HELIX 81 88
FT STRAND 90 93
FT STRAND 95 97
FT STRAND 103 105
SQ SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
//
MIM
603814
*RECORD*
*FIELD* NO
603814
*FIELD* TI
*603814 RING-BOX 1; RBX1
;;REGULATOR OF CULLINS 1; ROC1
*FIELD* TX
CLONING
The VHL protein (VHL; 608537) is part of a complex that includes elongin
read moreB (600787), elongin C (600788), and cullin-2 (CUL2; 603135), proteins
associated with transcriptional elongation and ubiquitination.
Components of the VCB (VHL-elongin C/elongin B) complex share sequence
similarities with the E3 ubiquitin ligase complexes, SCF (SKP1
(601434)-CUL1 (603134)-F-box protein) and APC (anaphase promoting
complex, see 603462). F-box proteins, such as S. cerevisiae Cdc4 and
Grr1, are adaptor proteins that recruit different binding partners to
SCF (Tyers and Willems, 1999).
Kamura et al. (1999) purified the endogenous VHL complex from rat liver
and determined the partial protein sequence of a 16-kD protein
component. By searching an EST database with the peptide sequences,
these authors identified human and mouse cDNAs encoding a predicted
108-amino acid protein. They designated the protein RBX1 (RING-box
protein-1) because it contained a RING-H2 finger-like motif. The mouse
and human RBX1 proteins are identical, and there are RBX1 homologs in
Drosophila, C. elegans, and S. cerevisiae. Kamura et al. (1999)
demonstrated that RBX1 interacts with both CUL1 and CUL2. They found
that yeast Rbx1 is a subunit and a potent activator of the SCF-Cdc4
complex that is required for ubiquitination of the cyclin-dependent
kinase inhibitor Sic1 and for the G1-to-S cell cycle transition.
Mammalian RBX1 rescued the viability defect in yeast rbx1 mutants. The
authors concluded that the presence of RBX1 as a component of both the
VHL and SCF-Cdc4 complexes extends the structural similarity between
these 2 complexes and raises the possibility that the VHL complex may
function as a ubiquitin ligase for target proteins. Skowyra et al.
(1999) found that Rbx1 is part of the yeast SCF-Grr1 complex, which
ubiquitinates the phosphorylated G1 cyclin cln1.
Using mouse cullin-4A (603137) as bait in a yeast 2-hybrid screen of a
human HeLa pGAD cDNA library, Ohta et al. (1999) identified 2 highly
conserved RING finger proteins, which they referred to as ROC1 and ROC2
(603863), which are homologous to APC11 (ANAPC11; 614534), a subunit of
the APC. The ROC1 and ROC2 proteins commonly interact with all cullins.
Yeast ROC1 encodes an essential gene whose reduced expression resulted
in multiple, elongated buds and accumulation of Sic1 and Cln2 proteins.
ROC1 and APC11 immunocomplexes can catalyze isopeptide ligations to form
polyubiquitin chains in an E1 (314370)- and E2 (see 602961)-dependent
manner. ROC1 mutations completely abolished their ligase activity
without noticeable changes in associated proteins. Ubiquitination of
phosphorylated I-kappa-B-alpha (164008) can be catalyzed by the ROC1
immunocomplex in vitro. Hence, combinations of ROC/APC11 and cullin
proteins potentially constitute a wide variety of ubiquitin ligases.
GENE FUNCTION
Tan et al. (1999) showed that ROC1 is recruited by cullin-1 to form a
quaternary SCF(HOS)-ROC1 holoenzyme (with SKP1 and the BTRCP (603482)
homolog HOS). SCF(HOS)-ROC1 binds IKK-beta (603258)-phosphorylated
I-kappa-B-alpha and catalyzes its ubiquitination in the presence of
ubiquitin, E1, and CDC34 (116948). ROC1 plays a unique role in the
ubiquitination reaction by heterodimerizing with cullin-1 to catalyze
ubiquitin polymerization.
Wertz et al. (2004) reported that human DET1 (608727) promotes
ubiquitination and degradation of the protooncogenic transcription
factor c-Jun (165160) by assembling a multisubunit ubiquitin ligase
containing DNA damage-binding protein-1 (DDB1; 600045), cullin 4A
(CUL4A; 603137), ROC1, and constitutively photomorphogenic-1 (COP1;
608067). Ablation of any subunit by RNA interference stabilized c-Jun
and increased c-Jun-activated transcription. Wertz et al. (2004)
concluded that their findings characterized a c-Jun ubiquitin ligase and
define a specific function for DET1 in mammalian cells.
Dias et al. (2002) found that CUL7 (609577) assembled an SCF-ROC1-like
E3 ligase complex containing SKP1, CUL7, FBX29 (FBXW8; 609073), and ROC1
in human embryonic kidney cells. Immunoprecipitated CUL7-ROC1 complexes
converted monomeric ubiquitin into high molecular mass ubiquitin
conjugates when incubated with E1 and UBC5C (UBE2D3; 602963). Arai et
al. (2003) found that mouse Cul7 formed a specific SCF-like complex with
Skp1, Fbx29, Rbx1, and Fap68 (GLMN; 601749).
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the
CUL4-DDB1-ROC1 complex. Sequence alignment revealed that most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors. For example, inactivation of L2DTL (DTL;
610617), but not other WDR proteins, prevented CUL4-DDB1-dependent
proteolysis of CDT1 (605525) following gamma irradiation. Inactivation
of WDR5 (609012) or EED (605984), but not other WDR proteins, altered
the pattern of CUL4-DDB1-dependent histone H3 (see 602810) methylation.
BIOCHEMICAL FEATURES
Zheng et al. (2002) reported the crystal structure to 3.2-angstrom
resolution of the quaternary complex containing CUL1, RBX1, SKP1, and
the F box of SKP2 (601436), and the 3.0-angstrom structure of the
CUL1-RBX1 complex. CUL1 is an elongated protein that consists of a long
stalk and a globular domain. The globular domain binds the RING finger
protein RBX1 through an intermolecular beta-sheet, forming a 2-subunit
catalytic core that recruits the ubiquitin-conjugating enzyme. The long
stalk, which consists of 3 repeats of a novel 5-helix motif, binds the
SKP1-F box(SKP2) protein substrate recognition complex at its tip. CUL1
serves as a rigid scaffold that organizes the SKP1-F box(SKP2) and RBX1
subunits, holding them over 100 angstroms apart. The structure suggests
that CUL1 may contribute to catalysis through the positioning of the
substrate and the ubiquitin-conjugating enzyme, and that this model is
supported by CUL1 mutations designed to eliminate the rigidity of the
scaffold.
MAPPING
Hartz (2012) mapped the RBX1 gene to chromosome 22q13.2 based on an
alignment of the RBX1 sequence (GenBank GENBANK AF140598) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Arai, T.; Kasper, J. S.; Skaar, J. R.; Ali, S. H.; Takahashi, C.;
DeCaprio, J. A.: Targeted disruption of p185/Cul7 gene results in
abnormal vascular morphogenesis. Proc. Nat. Acad. Sci. 100: 9855-9860,
2003.
2. Dias, D. C.; Dolios, G.; Wang, R.; Pan, Z.-Q.: CUL7: A DOC domain-containing
cullin selectively binds Skp1-Fbx29 to form an SCF-like complex. Proc.
Nat. Acad. Sci. 99: 16601-16606, 2002.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/10/2012.
4. Higa, L. A.; Wu, M.; Ye, T.; Kobayashi, R.; Sun, H.; Zhang, H.
: CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
and regulates histone methylation. Nature Cell Biol. 8: 1277-1283,
2006.
5. Kamura, T.; Koepp, D. M.; Conrad, M. N.; Skowyra, D.; Moreland,
R. J.; Iliopoulos, O.; Lane, W. S.; Kaelin, W. G., Jr.; Elledge, S.
J.; Conaway, R. C.; Harper, J. W.; Conaway, J. W.: Rbx1, a component
of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284:
657-661, 1999.
6. Ohta, T.; Michel, J. J.; Schottelius, A. J.; Xiong, Y.: ROC1,
a homolog of APC11, represents a family of cullin partners with an
associated ubiquitin ligase activity. Molec. Cell 3: 535-541, 1999.
7. Skowyra, D.; Koepp, D. M.; Kamura, T.; Conrad, M. N.; Conaway,
R. C.; Conaway, J. W.; Elledge, S. J.; Harper, J. W.: Reconstitution
of G1 cyclin ubiquitination with complexes containing SCF(Grr1) and
Rbx1. Science 284: 662-665, 1999.
8. Tan, P.; Fuchs, S. Y.; Chen, A.; Wu, K.; Gomez, C.; Ronai, Z.;
Pan, Z.-Q.: Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and
HOS to catalyze the ubiquitination of I-kappa-B-alpha. Molec. Cell 3:
527-533, 1999.
9. Tyers, M.; Willems, A. R.: One ring to rule a superfamily of E3
ubiquitin ligases. Science 284: 602-604, 1999.
10. Wertz, I. E.; O'Rourke, K. M.; Zhang, Z.; Dornan, D.; Arnott,
D.; Deshaies, R. J.; Dixit, V. M.: Human de-etiolated-1 regulates
c-Jun by assembling a CUL4A ubiquitin ligase. Science 303: 1371-1374,
2004.
11. Zheng, N.; Schulman, B. A.; Song, L.; Miller, J. J.; Jeffrey,
P. D.; Wang, P.; Chu, C.; Koepp, D. M.; Elledge, S. J.; Pagano, M.;
Conaway, R. C.; Conaway, J. W.; Harper, J. W.; Pavletich, N. P.:
Structure of the Cul1-Rbx1-Skp1-F box-Skp2 SCF ubiquitin ligase complex. Nature 416:
703-709, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
Patricia A. Hartz - updated: 2/10/2012
Patricia A. Hartz - updated: 9/13/2005
Ada Hamosh - updated: 6/10/2004
Ada Hamosh - updated: 4/30/2002
Stylianos E. Antonarakis - updated: 6/2/1999
*FIELD* CD
Rebekah S. Rasooly: 5/17/1999
*FIELD* ED
mgross: 03/05/2013
mgross: 3/15/2012
terry: 2/10/2012
carol: 3/24/2006
mgross: 9/13/2005
alopez: 6/11/2004
terry: 6/10/2004
ckniffin: 3/23/2004
alopez: 4/30/2002
terry: 4/30/2002
mgross: 11/4/1999
kayiaros: 7/27/1999
mgross: 6/2/1999
alopez: 5/17/1999
*RECORD*
*FIELD* NO
603814
*FIELD* TI
*603814 RING-BOX 1; RBX1
;;REGULATOR OF CULLINS 1; ROC1
*FIELD* TX
CLONING
The VHL protein (VHL; 608537) is part of a complex that includes elongin
read moreB (600787), elongin C (600788), and cullin-2 (CUL2; 603135), proteins
associated with transcriptional elongation and ubiquitination.
Components of the VCB (VHL-elongin C/elongin B) complex share sequence
similarities with the E3 ubiquitin ligase complexes, SCF (SKP1
(601434)-CUL1 (603134)-F-box protein) and APC (anaphase promoting
complex, see 603462). F-box proteins, such as S. cerevisiae Cdc4 and
Grr1, are adaptor proteins that recruit different binding partners to
SCF (Tyers and Willems, 1999).
Kamura et al. (1999) purified the endogenous VHL complex from rat liver
and determined the partial protein sequence of a 16-kD protein
component. By searching an EST database with the peptide sequences,
these authors identified human and mouse cDNAs encoding a predicted
108-amino acid protein. They designated the protein RBX1 (RING-box
protein-1) because it contained a RING-H2 finger-like motif. The mouse
and human RBX1 proteins are identical, and there are RBX1 homologs in
Drosophila, C. elegans, and S. cerevisiae. Kamura et al. (1999)
demonstrated that RBX1 interacts with both CUL1 and CUL2. They found
that yeast Rbx1 is a subunit and a potent activator of the SCF-Cdc4
complex that is required for ubiquitination of the cyclin-dependent
kinase inhibitor Sic1 and for the G1-to-S cell cycle transition.
Mammalian RBX1 rescued the viability defect in yeast rbx1 mutants. The
authors concluded that the presence of RBX1 as a component of both the
VHL and SCF-Cdc4 complexes extends the structural similarity between
these 2 complexes and raises the possibility that the VHL complex may
function as a ubiquitin ligase for target proteins. Skowyra et al.
(1999) found that Rbx1 is part of the yeast SCF-Grr1 complex, which
ubiquitinates the phosphorylated G1 cyclin cln1.
Using mouse cullin-4A (603137) as bait in a yeast 2-hybrid screen of a
human HeLa pGAD cDNA library, Ohta et al. (1999) identified 2 highly
conserved RING finger proteins, which they referred to as ROC1 and ROC2
(603863), which are homologous to APC11 (ANAPC11; 614534), a subunit of
the APC. The ROC1 and ROC2 proteins commonly interact with all cullins.
Yeast ROC1 encodes an essential gene whose reduced expression resulted
in multiple, elongated buds and accumulation of Sic1 and Cln2 proteins.
ROC1 and APC11 immunocomplexes can catalyze isopeptide ligations to form
polyubiquitin chains in an E1 (314370)- and E2 (see 602961)-dependent
manner. ROC1 mutations completely abolished their ligase activity
without noticeable changes in associated proteins. Ubiquitination of
phosphorylated I-kappa-B-alpha (164008) can be catalyzed by the ROC1
immunocomplex in vitro. Hence, combinations of ROC/APC11 and cullin
proteins potentially constitute a wide variety of ubiquitin ligases.
GENE FUNCTION
Tan et al. (1999) showed that ROC1 is recruited by cullin-1 to form a
quaternary SCF(HOS)-ROC1 holoenzyme (with SKP1 and the BTRCP (603482)
homolog HOS). SCF(HOS)-ROC1 binds IKK-beta (603258)-phosphorylated
I-kappa-B-alpha and catalyzes its ubiquitination in the presence of
ubiquitin, E1, and CDC34 (116948). ROC1 plays a unique role in the
ubiquitination reaction by heterodimerizing with cullin-1 to catalyze
ubiquitin polymerization.
Wertz et al. (2004) reported that human DET1 (608727) promotes
ubiquitination and degradation of the protooncogenic transcription
factor c-Jun (165160) by assembling a multisubunit ubiquitin ligase
containing DNA damage-binding protein-1 (DDB1; 600045), cullin 4A
(CUL4A; 603137), ROC1, and constitutively photomorphogenic-1 (COP1;
608067). Ablation of any subunit by RNA interference stabilized c-Jun
and increased c-Jun-activated transcription. Wertz et al. (2004)
concluded that their findings characterized a c-Jun ubiquitin ligase and
define a specific function for DET1 in mammalian cells.
Dias et al. (2002) found that CUL7 (609577) assembled an SCF-ROC1-like
E3 ligase complex containing SKP1, CUL7, FBX29 (FBXW8; 609073), and ROC1
in human embryonic kidney cells. Immunoprecipitated CUL7-ROC1 complexes
converted monomeric ubiquitin into high molecular mass ubiquitin
conjugates when incubated with E1 and UBC5C (UBE2D3; 602963). Arai et
al. (2003) found that mouse Cul7 formed a specific SCF-like complex with
Skp1, Fbx29, Rbx1, and Fap68 (GLMN; 601749).
By mass spectrometric analysis, Higa et al. (2006) identified over 20
WD40 repeat-containing (WDR) proteins that interacted with the
CUL4-DDB1-ROC1 complex. Sequence alignment revealed that most of the
interacting WDR proteins had a centrally positioned WDxR/K submotif.
Knockdown studies suggested that the WDR proteins functioned as
substrate-specific adaptors. For example, inactivation of L2DTL (DTL;
610617), but not other WDR proteins, prevented CUL4-DDB1-dependent
proteolysis of CDT1 (605525) following gamma irradiation. Inactivation
of WDR5 (609012) or EED (605984), but not other WDR proteins, altered
the pattern of CUL4-DDB1-dependent histone H3 (see 602810) methylation.
BIOCHEMICAL FEATURES
Zheng et al. (2002) reported the crystal structure to 3.2-angstrom
resolution of the quaternary complex containing CUL1, RBX1, SKP1, and
the F box of SKP2 (601436), and the 3.0-angstrom structure of the
CUL1-RBX1 complex. CUL1 is an elongated protein that consists of a long
stalk and a globular domain. The globular domain binds the RING finger
protein RBX1 through an intermolecular beta-sheet, forming a 2-subunit
catalytic core that recruits the ubiquitin-conjugating enzyme. The long
stalk, which consists of 3 repeats of a novel 5-helix motif, binds the
SKP1-F box(SKP2) protein substrate recognition complex at its tip. CUL1
serves as a rigid scaffold that organizes the SKP1-F box(SKP2) and RBX1
subunits, holding them over 100 angstroms apart. The structure suggests
that CUL1 may contribute to catalysis through the positioning of the
substrate and the ubiquitin-conjugating enzyme, and that this model is
supported by CUL1 mutations designed to eliminate the rigidity of the
scaffold.
MAPPING
Hartz (2012) mapped the RBX1 gene to chromosome 22q13.2 based on an
alignment of the RBX1 sequence (GenBank GENBANK AF140598) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Arai, T.; Kasper, J. S.; Skaar, J. R.; Ali, S. H.; Takahashi, C.;
DeCaprio, J. A.: Targeted disruption of p185/Cul7 gene results in
abnormal vascular morphogenesis. Proc. Nat. Acad. Sci. 100: 9855-9860,
2003.
2. Dias, D. C.; Dolios, G.; Wang, R.; Pan, Z.-Q.: CUL7: A DOC domain-containing
cullin selectively binds Skp1-Fbx29 to form an SCF-like complex. Proc.
Nat. Acad. Sci. 99: 16601-16606, 2002.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/10/2012.
4. Higa, L. A.; Wu, M.; Ye, T.; Kobayashi, R.; Sun, H.; Zhang, H.
: CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
and regulates histone methylation. Nature Cell Biol. 8: 1277-1283,
2006.
5. Kamura, T.; Koepp, D. M.; Conrad, M. N.; Skowyra, D.; Moreland,
R. J.; Iliopoulos, O.; Lane, W. S.; Kaelin, W. G., Jr.; Elledge, S.
J.; Conaway, R. C.; Harper, J. W.; Conaway, J. W.: Rbx1, a component
of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284:
657-661, 1999.
6. Ohta, T.; Michel, J. J.; Schottelius, A. J.; Xiong, Y.: ROC1,
a homolog of APC11, represents a family of cullin partners with an
associated ubiquitin ligase activity. Molec. Cell 3: 535-541, 1999.
7. Skowyra, D.; Koepp, D. M.; Kamura, T.; Conrad, M. N.; Conaway,
R. C.; Conaway, J. W.; Elledge, S. J.; Harper, J. W.: Reconstitution
of G1 cyclin ubiquitination with complexes containing SCF(Grr1) and
Rbx1. Science 284: 662-665, 1999.
8. Tan, P.; Fuchs, S. Y.; Chen, A.; Wu, K.; Gomez, C.; Ronai, Z.;
Pan, Z.-Q.: Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and
HOS to catalyze the ubiquitination of I-kappa-B-alpha. Molec. Cell 3:
527-533, 1999.
9. Tyers, M.; Willems, A. R.: One ring to rule a superfamily of E3
ubiquitin ligases. Science 284: 602-604, 1999.
10. Wertz, I. E.; O'Rourke, K. M.; Zhang, Z.; Dornan, D.; Arnott,
D.; Deshaies, R. J.; Dixit, V. M.: Human de-etiolated-1 regulates
c-Jun by assembling a CUL4A ubiquitin ligase. Science 303: 1371-1374,
2004.
11. Zheng, N.; Schulman, B. A.; Song, L.; Miller, J. J.; Jeffrey,
P. D.; Wang, P.; Chu, C.; Koepp, D. M.; Elledge, S. J.; Pagano, M.;
Conaway, R. C.; Conaway, J. W.; Harper, J. W.; Pavletich, N. P.:
Structure of the Cul1-Rbx1-Skp1-F box-Skp2 SCF ubiquitin ligase complex. Nature 416:
703-709, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 03/05/2013
Patricia A. Hartz - updated: 2/10/2012
Patricia A. Hartz - updated: 9/13/2005
Ada Hamosh - updated: 6/10/2004
Ada Hamosh - updated: 4/30/2002
Stylianos E. Antonarakis - updated: 6/2/1999
*FIELD* CD
Rebekah S. Rasooly: 5/17/1999
*FIELD* ED
mgross: 03/05/2013
mgross: 3/15/2012
terry: 2/10/2012
carol: 3/24/2006
mgross: 9/13/2005
alopez: 6/11/2004
terry: 6/10/2004
ckniffin: 3/23/2004
alopez: 4/30/2002
terry: 4/30/2002
mgross: 11/4/1999
kayiaros: 7/27/1999
mgross: 6/2/1999
alopez: 5/17/1999