RBX1_HUMAN
ID RBX1_HUMAN Reviewed; 108 AA.
AC P62877; B2RDY1; Q8N6Z8; Q9D1S2; Q9WUK9; Q9Y254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=E3 ubiquitin-protein ligase RBX1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:11027288};
DE EC=2.3.2.32 {ECO:0000269|PubMed:11027288};
DE AltName: Full=E3 ubiquitin-protein transferase RBX1 {ECO:0000305};
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 Short=ROC1 {ECO:0000303|PubMed:10230407};
DE Contains:
DE RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
DE AltName: Full=E3 ubiquitin-protein transferase RBX1, N-terminally processed {ECO:0000305};
GN Name=RBX1; Synonyms=RNF75, ROC1 {ECO:0000303|PubMed:10230407};
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], FUNCTION, PATHWAY, INTERACTION WITH CULLINS,
RP DOMAIN, AND MUTAGENESIS 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 an
RT 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 ubiquitin
RT 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., 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 [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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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., 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 (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY 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., Rieger F.,
RA Alliel P.M.;
RT "Genomic organization and expression of the ubiquitin-proteasome complex-
RT 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 IN A
RP 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 catalyze
RT 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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
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 nuclear
RT accumulation, NEDD8 modification, and ubiquitin ligase 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 can
RT 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., Stearman R.,
RA Klausner R.D., Malik S., Lane W.S., Sorokina I., Roeder R.G., Conaway J.W.,
RA Conaway R.C.;
RT "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that
RT can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin 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 form
RT 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., Drapkin R.,
RA 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., Deshaies R.J.,
RA 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 THE
RP 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 Cul3,
RT targets Keap1 for degradation by a proteasome-independent 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., Tanaka K.,
RA 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, IDENTIFICATION
RP BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
RA Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
RA Tempst P., Xiong Y., Zhang Y.;
RT "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase
RT facilitates cellular response to DNA damage.";
RL Mol. Cell 22:383-394(2006).
RN [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 the
RT 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., Kitabayashi I.;
RT "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-
RT mediated degradation.";
RL Mol. Cell. Biol. 28:7126-7138(2008).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [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 levels
RT 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., Scott D.C.,
RA Borg L.A., Neale G., Murray P.J., Roussel M.F., 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 HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=19679664; DOI=10.1074/jbc.m109.006809;
RA Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T.,
RA 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 through
RT 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, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [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., 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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [34]
RP INTERACTION WITH SESN1 AND SESN2.
RX PubMed=23274085; DOI=10.1016/j.cmet.2012.12.002;
RA Bae S.H., Sung S.H., Oh S.Y., Lim J.M., Lee S.K., Park Y.N., Lee H.E.,
RA Kang D., Rhee S.G.;
RT "Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation
RT of Keap1 and prevent oxidative liver damage.";
RL Cell Metab. 17:73-84(2013).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS
RP 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 [36]
RP FUNCTION, AND IDENTIFICATION IN THE BCR(KLHL22) COMPLEX.
RX PubMed=23455478; DOI=10.1038/ncb2695;
RA Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H.,
RA Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.;
RT "Ubiquitylation-dependent localization of PLK1 in mitosis.";
RL Nat. Cell Biol. 15:430-439(2013).
RN [37]
RP INTERACTION WITH DCUN1D5.
RX PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
RA Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
RA Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
RT "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
RT and nuclear localization.";
RL Clin. Cancer Res. 20:372-381(2014).
RN [38]
RP INTERACTION WITH DCUN1D3.
RX PubMed=25349211; DOI=10.1074/jbc.m114.585505;
RA Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E.,
RA Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of
RT SCCRO (DCUN1D1).";
RL J. Biol. Chem. 289:34728-34742(2014).
RN [39]
RP SUBUNIT.
RX PubMed=25684205; DOI=10.1016/j.molcel.2014.12.040;
RA Genau H.M., Huber J., Baschieri F., Akutsu M., Doetsch V., Farhan H.,
RA Rogov V., Behrends C.;
RT "CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to
RT spatially restrict TIAM1-RAC1 signaling.";
RL Mol. Cell 57:995-1010(2015).
RN [40]
RP FUNCTION.
RX PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
RA Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L., Paulo J.A.,
RA de Jong A., Ovaa H., Alpi A.F., Harper J.W., Schulman B.A.;
RT "Two distinct types of E3 ligases work in unison to regulate substrate
RT ubiquitylation.";
RL Cell 166:1198-1214(2016).
RN [41]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 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 [42]
RP INTERACTION WITH NOTCH2.
RX PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
RA Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
RA Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
RA Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W., Inuzuka H.;
RT "NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
RT promote osteoporosis.";
RL Mol. Cell 68:645-658(2017).
RN [43]
RP FUNCTION.
RX PubMed=29769719; DOI=10.1038/s41586-018-0128-9;
RA Chen J., Ou Y., Yang Y., Li W., Xu Y., Xie Y., Liu Y.;
RT "KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
RT tumorigenesis and ageing.";
RL Nature 557:585-589(2018).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776 OF
RP CUL1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; SKP1
RP AND SKP2, FUNCTION, AND DOMAIN.
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., Conaway J.W.,
RA Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
RL Nature 416:703-709(2002).
RN [45] {ECO:0007744|PDB:4F52}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 5-108 IN COMPLEX WITH CUL1; GLMN
RP AND ZINC, SUBUNIT, INTERACTION WITH CDC34 AND GLMN, FUNCTION, DOMAIN, AND
RP PATHWAY.
RX PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044;
RA Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J.,
RA Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.;
RT "Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase
RT through masking of its E2-binding surface.";
RL Mol. Cell 47:371-382(2012).
CC -!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-based
CC E3 ubiquitin-protein ligase (CRLs) complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, including proteins involved in cell cycle progression, signal
CC transduction, transcription and transcription-coupled nucleotide
CC excision repair (PubMed:10230407, PubMed:10579999, PubMed:15983046,
CC PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:23455478,
CC PubMed:27565346, PubMed:29769719, PubMed:11961546, PubMed:22748924).
CC CRLs complexes and ARIH1 collaborate in tandem to mediate
CC ubiquitination of target proteins, ARIH1 mediating addition of the
CC first ubiquitin on CRLs targets (PubMed:27565346). The functional
CC specificity of the E3 ubiquitin-protein ligase complexes depends on the
CC variable substrate recognition components. As a component of the CSA
CC complex promotes the ubiquitination of ERCC6 resulting in proteasomal
CC degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the
CC complex and brings it into close proximity to the substrate. Probably
CC also stimulates CDC34 autoubiquitination. May be required for histone
CC H3 and histone H4 ubiquitination in response to ultraviolet and for
CC subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and
CC CUL4 via its interaction with UBE2M. Involved in the ubiquitination of
CC KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes
CC degradation of KAT5 thereby attenuating its ability to acetylate and
CC activate ATM. {ECO:0000269|PubMed:10230407,
CC ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:11027288,
CC ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:15983046,
CC ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16751180,
CC ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19112177,
CC ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:22748924,
CC ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:27565346,
CC ECO:0000269|PubMed:29769719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11027288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine
CC + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine +
CC N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32;
CC Evidence={ECO:0000269|PubMed:11027288};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11027288,
CC ECO:0000269|PubMed:22748924}.
CC -!- SUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2
CC (PubMed:11961546). Part of a SCF-like complex consisting of CUL7, RBX1,
CC SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex
CC (ELOB and ELOC), 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 with
CC RNA polymerase II; upon UV irradiation it interacts with the COP9
CC signalosome and preferentially with the hyperphosphorylated form of RNA
CC polymerase II. Part of multisubunit E3 ubiquitin ligase complexes with
CC elongin BC complex (ELOB and ELOC), CUL2 and MED8; elongin BC complex
CC (ELOB and ELOC), CUL5 and MUF1. Part of multisubunit complexes with
CC elongin BC complex (ELOB and ELOC), elongin A/ELOA or SOCS1 or WSB1 and
CC CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3,
CC CUL4A, CUL4B, CUL5 and CUL7. Interacts with CDC34 (PubMed:22748924).
CC Interacts with GLMN. GLMN competes for the binding site of the E2
CC ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding
CC (PubMed:22748924). Interacts with COPS6. Component of the DCX DET1-COP1
CC ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A
CC and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and
CC CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex consisting
CC of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via
CC FBXO3. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1,
CC SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin 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. Part
CC of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex
CC containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part
CC of the BCR(KEAP1) complex containing KEAP1. Interacts with SESN1 and
CC SESN2 (PubMed:23274085). Interacts with NOTCH2 (PubMed:29149593).
CC Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least
CC composed of CUL3, KLHL22 and RBX1 (PubMed:23455478). Interacts with
CC DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:26906416,
CC PubMed:24192928, PubMed:25349211). Component of a BCR3 (BTB-CUL3-RBX1)
CC E3 ubiquitin ligase complex, also named Cul3-RING ubiquitin ligase
CC complex CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and KBTBD7
CC (PubMed:25684205). {ECO:0000269|PubMed:10213691,
CC ECO:0000269|PubMed:10230406, ECO:0000269|PubMed:10230407,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:11384984,
CC ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:12149480,
CC ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15983046,
CC ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18809579,
CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19250909,
CC ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22748924,
CC ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:23455478,
CC ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:25349211,
CC ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:26906416,
CC ECO:0000269|PubMed:29149593}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5
CC protein E1A; this interaction inhibits RBX1-CUL1-dependent elongation
CC reaction of ubiquitin chains by the SCF(FBW7) complex.
CC {ECO:0000269|PubMed:19679664}.
CC -!- INTERACTION:
CC P62877; Q13616: CUL1; NbExp=28; IntAct=EBI-398523, EBI-359390;
CC P62877; Q13617: CUL2; NbExp=8; IntAct=EBI-398523, EBI-456179;
CC P62877; Q13620: CUL4B; NbExp=5; IntAct=EBI-398523, EBI-456067;
CC P62877; Q93034: CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139;
CC P62877; Q92990: GLMN; NbExp=6; IntAct=EBI-398523, EBI-726150;
CC P62877; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-398523, EBI-10176379;
CC P62877; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-398523, EBI-10302990;
CC P62877; P58004: SESN2; NbExp=3; IntAct=EBI-398523, EBI-3939642;
CC P62877; Q13309: SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291;
CC P62877; P61081: UBE2M; NbExp=7; IntAct=EBI-398523, EBI-1041660;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11027288}. Nucleus
CC {ECO:0000269|PubMed:11027288}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity (PubMed:10230407). It coordinates an additional third
CC zinc ion (PubMed:11961546, PubMed:22748924).
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11961546,
CC ECO:0000269|PubMed:22748924}.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17370.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS14009.1; -.
DR PIR; T51146; T51146.
DR RefSeq; NP_055063.1; NM_014248.3.
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 PDB; 4P5O; X-ray; 3.11 A; B/D=5-108.
DR PDB; 5N4W; X-ray; 3.90 A; R=1-102.
DR PDB; 6R6H; EM; 8.40 A; R=17-102.
DR PDB; 6R7F; EM; 8.20 A; R=19-108.
DR PDB; 6R7H; EM; 8.80 A; R=19-108.
DR PDB; 6R7I; EM; 5.90 A; R=19-102.
DR PDB; 6R7N; EM; 6.50 A; R=17-102.
DR PDB; 6TTU; EM; 3.70 A; R=1-108.
DR PDB; 7B5L; EM; 3.80 A; R=1-108.
DR PDB; 7B5M; EM; 3.91 A; R=1-108.
DR PDB; 7B5N; EM; 3.60 A; R=1-108.
DR PDB; 7B5S; EM; 3.60 A; R=1-108.
DR PDB; 7OKQ; EM; 8.40 A; D/H/L/P=2-108.
DR PDB; 7PLO; EM; 2.80 A; T=1-108.
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 PDBsum; 4P5O; -.
DR PDBsum; 5N4W; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR PDBsum; 6TTU; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5N; -.
DR PDBsum; 7B5S; -.
DR PDBsum; 7OKQ; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; P62877; -.
DR SMR; P62877; -.
DR BioGRID; 115301; 517.
DR ComplexPortal; CPX-477; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
DR ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR CORUM; P62877; -.
DR DIP; DIP-17014N; -.
DR IntAct; P62877; 79.
DR MINT; P62877; -.
DR STRING; 9606.ENSP00000216225; -.
DR ChEMBL; CHEMBL3833061; -.
DR GlyGen; P62877; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62877; -.
DR MetOSite; P62877; -.
DR PhosphoSitePlus; P62877; -.
DR SwissPalm; P62877; -.
DR BioMuta; RBX1; -.
DR DMDM; 51338609; -.
DR EPD; P62877; -.
DR jPOST; P62877; -.
DR MassIVE; P62877; -.
DR MaxQB; P62877; -.
DR PaxDb; P62877; -.
DR PeptideAtlas; P62877; -.
DR PRIDE; P62877; -.
DR ProteomicsDB; 57443; -.
DR TopDownProteomics; P62877; -.
DR Antibodypedia; 295; 353 antibodies from 40 providers.
DR DNASU; 9978; -.
DR Ensembl; ENST00000216225.9; ENSP00000216225.8; ENSG00000100387.9.
DR GeneID; 9978; -.
DR KEGG; hsa:9978; -.
DR MANE-Select; ENST00000216225.9; ENSP00000216225.8; NM_014248.4; NP_055063.1.
DR UCSC; uc003azk.4; human.
DR CTD; 9978; -.
DR DisGeNET; 9978; -.
DR GeneCards; RBX1; -.
DR HGNC; HGNC:9928; RBX1.
DR HPA; ENSG00000100387; Low tissue specificity.
DR MIM; 603814; gene.
DR neXtProt; NX_P62877; -.
DR OpenTargets; ENSG00000100387; -.
DR PharmGKB; PA34299; -.
DR VEuPathDB; HostDB:ENSG00000100387; -.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000155618; -.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; P62877; -.
DR OMA; RFDVKKW; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; P62877; -.
DR TreeFam; TF105503; -.
DR BRENDA; 2.3.2.27; 2681.
DR BRENDA; 2.3.2.32; 2681.
DR PathwayCommons; P62877; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
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-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P62877; -.
DR SIGNOR; P62877; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9978; 626 hits in 1124 CRISPR screens.
DR ChiTaRS; RBX1; human.
DR EvolutionaryTrace; P62877; -.
DR GeneWiki; RBX1; -.
DR GenomeRNAi; 9978; -.
DR Pharos; P62877; Tbio.
DR PRO; PR:P62877; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P62877; protein.
DR Bgee; ENSG00000100387; Expressed in periodontal ligament and 208 other tissues.
DR Genevisible; P62877; HS.
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 E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0097602; F:cullin family protein binding; IDA:MGI.
DR GO; GO:0061663; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0019788; F:NEDD8 transferase activity; TAS:Reactome.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IPI:UniProtKB.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IMP:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; TAS:Reactome.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR DisProt; DP01750; -.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00059; -.
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 PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; Host-virus interaction; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..108
FT /note="E3 ubiquitin-protein ligase RBX1"
FT /id="PRO_0000423264"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..108
FT /note="E3 ubiquitin-protein ligase RBX1, N-terminally
FT processed"
FT /id="PRO_0000056013"
FT ZN_FING 53..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR,
FT ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11961546,
FT ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
FT ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
FT ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
FT ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
FT ECO:0007744|PDB:4P5O"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2
FT /note="N-acetylalanine; in E3 ubiquitin-protein ligase
FT RBX1, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MUTAGEN 53
FT /note="C->A: Strong reduction in ligase activity; when
FT associated with A-56."
FT /evidence="ECO:0000269|PubMed:10230407"
FT MUTAGEN 56
FT /note="C->A: Strong reduction in ligase activity; when
FT associated with A-53."
FT /evidence="ECO:0000269|PubMed:10230407"
FT MUTAGEN 75
FT /note="C->A: Strong reduction in ligase activity; when
FT associated with A-77."
FT /evidence="ECO:0000269|PubMed:10230407"
FT MUTAGEN 77
FT /note="H->A: Strong reduction in ligase activity; when
FT associated with A-75."
FT /evidence="ECO:0000269|PubMed:10230407"
FT CONFLICT 18
FT /note="G -> S (in Ref. 9; AAM21718)"
FT /evidence="ECO:0000305"
FT STRAND 21..37
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3DPL"
FT TURN 49..54
FT /evidence="ECO:0007829|PDB:1LDJ"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:3DPL"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1LDJ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3DPL"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1LDK"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3DPL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3DPL"
SQ SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
