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 27-MAR-2024, entry version 196. 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 {ECO:0000312|HGNC:HGNC:9928}; GN 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 FUNCTION, AND IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH ELONGIN BC; RP ELONGIN A/ELOA AND CUL5. RX PubMed=19920177; DOI=10.1073/pnas.0907052106; RA Harreman M., Taschner M., Sigurdsson S., Anindya R., Reid J., Somesh B., RA Kong S.E., Banks C.A., Conaway R.C., Conaway J.W., Svejstrup J.Q.; RT "Distinct ubiquitin ligases act sequentially for RNA polymerase II RT polyubiquitylation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20705-20710(2009). RN [30] 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 [31] 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 [32] 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 [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=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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] {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). RN [47] {ECO:0007744|PDB:7PLO} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH REPLISOME RP AND DNA POLYMERASE EPSILON, AND SUBUNIT. RX PubMed=34700328; DOI=10.1038/s41586-021-04145-3; RA Jenkyn-Bedford M., Jones M.L., Baris Y., Labib K.P.M., Cannone G., RA Yeeles J.T.P., Deegan T.D.; RT "A conserved mechanism for regulating replisome disassembly in RT eukaryotes."; RL Nature 600:743-747(2021). 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. As part of a multisubunit complex composed of elongin BC CC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; CC polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177). CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10579999, CC ECO:0000269|PubMed:11027288, ECO:0000269|PubMed:11961546, CC ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, CC ECO:0000269|PubMed:16751180, ECO:0000269|PubMed:18397884, CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19679664, CC ECO:0000269|PubMed:19920177, 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:10230406, PubMed:11961546). Part of a SCF-like complex CC consisting of CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes CC with elongin BC complex (ELOB and ELOC), CUL2 or CUL5 and VHL CC (PubMed:10213691). Part of the CSA complex (DCX(ERCC8) complex), a DCX CC E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CC CUL4A; the CSA complex interacts with RNA polymerase II; upon UV CC irradiation it interacts with the COP9 signalosome and preferentially CC with the hyperphosphorylated form of RNA polymerase II CC (PubMed:12732143). Part of multisubunit E3 ubiquitin ligase complexes CC with elongin BC complex (ELOB and ELOC), CUL2 and MED8; elongin BC CC complex (ELOB and ELOC), CUL5 and MUF1 (PubMed:11384984, CC PubMed:12149480). Part of multisubunit complexes with elongin BC CC complex (ELOB and ELOC), SOCS1 or WSB1 and CUL5. Part of a multisubunit CC ubiquitin ligase complex consisting of elongin BC complex (ELOB and CC ELOC), elongin A/ELOA, RBX1 and CUL5 (PubMed:19920177). Interacts CC directly with CUL1 and probably also with CUL2, CUL3, CUL4A, CUL4B, CC CUL5 and CUL7 (PubMed:10230407, PubMed:12481031). Interacts with CDC34 CC (PubMed:22748924). Interacts with GLMN. GLMN competes for the binding CC site of the E2 ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 CC binding (PubMed:22748924). Interacts with COPS6 (PubMed:11337588). CC Component of the DCX DET1-COP1 ubiquitin ligase complex at least CC composed of RBX1, DET1, DDB1, CUL4A and COP1 (PubMed:14739464). Part of CC an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or CUL4B CC (PubMed:16678110). Interacts with UBE2M (PubMed:19250909). Part of a CC SCF complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex CC interacts with PML via FBXO3 (PubMed:18809579). Component of the CC SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF CC (PubMed:20596027). Identified in a SCF (SKP1-CUL1-F-box protein) E3 CC ubiquitin ligase complex together with HINT1 and CDC34 CC (PubMed:19112177). Component of multiple BCR (BTB-CUL3-RBX1) E3 CC ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable CC BTB domain-containing protein (PubMed:15983046). Part of the BCR(ENC1) CC complex containing ENC1 (PubMed:15983046). Part of the BCR(GAN) complex CC containing GAN (PubMed:15983046). Part of the BCR(KLHL41) complex CC containing KLHL41 (PubMed:15983046). Part of the BCR(KEAP1) complex CC containing KEAP1 (PubMed:15983046). Interacts with SESN1 and SESN2 CC (PubMed:23274085). Interacts with NOTCH2 (PubMed:29149593). Component CC of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CC CUL3, KLHL22 and RBX1 (PubMed:23455478). Interacts with DCUN1D1, CC 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). Component of the ECS(LRR1) complex with the CC substrate recognition component LRR1 (PubMed:34700328). CC {ECO:0000269|PubMed:10213691, ECO:0000269|PubMed:10230406, CC ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11337588, CC ECO:0000269|PubMed:11384984, ECO:0000269|PubMed:11961546, CC ECO:0000269|PubMed:12149480, ECO:0000269|PubMed:12481031, CC ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14739464, CC ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16678110, CC ECO:0000269|PubMed:18809579, ECO:0000269|PubMed:19112177, CC ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:20596027, CC ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:23274085, CC ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:24192928, CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:25684205, CC ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:29149593, CC ECO:0000269|PubMed:34700328}. 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=30; IntAct=EBI-398523, EBI-359390; CC P62877; Q13617: CUL2; NbExp=8; IntAct=EBI-398523, EBI-456179; CC P62877; Q13618: CUL3; NbExp=4; IntAct=EBI-398523, EBI-456129; CC P62877; Q13620: CUL4B; NbExp=7; 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; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42075/RBX1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7Z8B; EM; 2.80 A; R=1-108. DR PDB; 7Z8R; EM; 2.70 A; R=5-108. DR PDB; 7Z8T; EM; 3.00 A; R=5-108. DR PDB; 7Z8V; EM; 2.70 A; R=5-108. DR PDB; 7ZBW; EM; 3.50 A; R=5-108. DR PDB; 8B3I; EM; 3.50 A; R=1-108. DR PDB; 8CDJ; EM; 3.40 A; R=5-108. DR PDB; 8CDK; EM; 3.32 A; R=5-108. DR PDB; 8GQ6; EM; 3.96 A; D/E=1-108. DR PDB; 8H33; EM; 7.86 A; D/E/K/L=1-108. DR PDB; 8H34; EM; 7.99 A; D/E/K/L/Q/R=1-108. DR PDB; 8H35; EM; 7.41 A; D/E/K/L/Q/R/W/X=1-108. DR PDB; 8H36; EM; 4.60 A; D/E=1-108. DR PDB; 8H37; EM; 7.52 A; D/E/Q/R=1-108. DR PDB; 8H38; EM; 4.25 A; R=1-108. DR PDB; 8H3A; EM; 7.51 A; R=1-108. DR PDB; 8H3F; EM; 6.73 A; R=1-108. DR PDB; 8H3Q; EM; 3.76 A; E=1-108. DR PDB; 8H3R; EM; 6.36 A; D/E=1-108. DR PDB; 8JAQ; EM; 3.26 A; R/V=1-108. DR PDB; 8JAS; EM; 3.54 A; R/V=1-108. DR PDB; 8JAV; EM; 3.44 A; R/V=1-108. DR PDB; 8OR0; EM; 3.10 A; B=1-108. DR PDB; 8OR2; EM; 3.20 A; B=1-108. DR PDB; 8OR3; EM; 2.90 A; B=1-108. DR PDB; 8OR4; EM; 3.80 A; B=1-108. DR PDB; 8QU8; EM; 3.50 A; E=2-108. 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 PDBsum; 7Z8B; -. DR PDBsum; 7Z8R; -. DR PDBsum; 7Z8T; -. DR PDBsum; 7Z8V; -. DR PDBsum; 7ZBW; -. DR PDBsum; 8B3I; -. DR PDBsum; 8CDJ; -. DR PDBsum; 8CDK; -. DR PDBsum; 8GQ6; -. DR PDBsum; 8H33; -. DR PDBsum; 8H34; -. DR PDBsum; 8H35; -. DR PDBsum; 8H36; -. DR PDBsum; 8H37; -. DR PDBsum; 8H38; -. DR PDBsum; 8H3A; -. DR PDBsum; 8H3F; -. DR PDBsum; 8H3Q; -. DR PDBsum; 8H3R; -. DR PDBsum; 8JAQ; -. DR PDBsum; 8JAS; -. DR PDBsum; 8JAV; -. DR PDBsum; 8OR0; -. DR PDBsum; 8OR2; -. DR PDBsum; 8OR3; -. DR PDBsum; 8OR4; -. DR PDBsum; 8QU8; -. DR AlphaFoldDB; P62877; -. DR EMDB; EMD-10585; -. DR EMDB; EMD-12037; -. DR EMDB; EMD-12040; -. DR EMDB; EMD-12041; -. DR EMDB; EMD-12050; -. DR EMDB; EMD-12964; -. DR EMDB; EMD-13494; -. DR EMDB; EMD-14547; -. DR EMDB; EMD-14561; -. DR EMDB; EMD-14563; -. DR EMDB; EMD-14564; -. DR EMDB; EMD-14594; -. DR EMDB; EMD-14597; -. DR EMDB; EMD-15829; -. DR EMDB; EMD-16575; -. DR EMDB; EMD-16576; -. DR EMDB; EMD-17114; -. DR EMDB; EMD-17115; -. DR EMDB; EMD-17116; -. DR EMDB; EMD-17117; -. DR EMDB; EMD-3401; -. DR EMDB; EMD-34199; -. DR EMDB; EMD-34449; -. DR EMDB; EMD-34450; -. DR EMDB; EMD-34451; -. DR EMDB; EMD-34452; -. DR EMDB; EMD-34453; -. DR EMDB; EMD-34455; -. DR EMDB; EMD-34462; -. DR EMDB; EMD-34467; -. DR EMDB; EMD-34473; -. DR EMDB; EMD-34474; -. DR EMDB; EMD-36131; -. DR EMDB; EMD-36133; -. DR EMDB; EMD-36135; -. DR EMDB; EMD-4736; -. DR EMDB; EMD-4739; -. DR EMDB; EMD-4741; -. DR EMDB; EMD-4742; -. DR EMDB; EMD-4744; -. DR SMR; P62877; -. DR BioGRID; 115301; 573. DR ComplexPortal; CPX-2214; LRR1-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2217; FEM1A-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2218; FEB1B-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2219; FEB1C-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2220; ZYG11B-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2221; APPBP2-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2222; ZER1-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2223; KLHDC10-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2226; KLHDC2-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2228; KLHDC3-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2229; PRAME-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2239; SCF E3 ubiquitin ligase complex, FBXL5 variant. DR ComplexPortal; CPX-2241; SCF E3 ubiquitin ligase complex, FBXL13 variant. DR ComplexPortal; CPX-2250; VHL-Elongin C-Elongin B E3 ubiquitin ligase complex. DR ComplexPortal; CPX-2319; SCF E3 ubiquitin ligase complex, FBXL14 variant. DR ComplexPortal; CPX-2343; SCF E3 ubiquitin ligase complex, FBXL16 variant. DR ComplexPortal; CPX-2365; SCF E3 ubiquitin ligase complex, BTRC variant. DR ComplexPortal; CPX-2399; CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2403; CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2404; CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2405; CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2406; CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2407; CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2411; CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2412; CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2413; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2414; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2415; CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2416; CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2438; SCF E3 ubiquitin ligase complex, FBXL8 variant. DR ComplexPortal; CPX-2489; SCF E3 ubiquitin ligase complex, FBXL22 variant. DR ComplexPortal; CPX-2492; SCF E3 ubiquitin ligase complex, FBXL15 variant. DR ComplexPortal; CPX-2512; SCF E3 ubiquitin ligase complex, FBXL4 variant. DR ComplexPortal; CPX-2516; SCF E3 ubiquitin ligase complex, FBXL6 variant. DR ComplexPortal; CPX-2538; SCF E3 ubiquitin ligase complex, KDM2A variant. DR ComplexPortal; CPX-2553; SCF E3 ubiquitin ligase complex, FBXL18 variant. DR ComplexPortal; CPX-2554; SCF E3 ubiquitin ligase complex, FBXL19 variant. DR ComplexPortal; CPX-2658; SCF E3 ubiquitin ligase complex, FBXL12 variant. DR ComplexPortal; CPX-2683; SCF E3 ubiquitin ligase complex, FBXL7 variant. DR ComplexPortal; CPX-2748; SCF E3 ubiquitin ligase complex, FBXL21 variant. DR ComplexPortal; CPX-2757; CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2758; CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2759; CRL4-CRBN E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2762; CRL4-CRBN E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2765; CRL4-DCAF15 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2766; CRL4-DCAF15 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2769; CRL4-DCAF1 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2770; CRL4-DCAF1 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2773; SCF E3 ubiquitin ligase complex, FBXL17 variant. DR ComplexPortal; CPX-2777; CRL4-CDT2 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2778; CRL4-AMBRA1 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2782; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2783; CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2784; CRL4-DCAF6 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2785; CRL4-DCAF7 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2786; CRL4-DCAF7 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2787; CRL4-DCAF9 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2795; CRL4-CDT2 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2797; CRL4-AMBRA1 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2799; CRL4-DCAF4 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2804; CRL4-DCAF6 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2809; CRL4-DCAF9 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2816; CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2817; CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2818; CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4A variant. DR ComplexPortal; CPX-2819; CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2832; SCF E3 ubiquitin ligase complex, KDM2B variant. DR ComplexPortal; CPX-2859; CRL4-DCAF4 E3 ubiquitin ligase complex, CUL4B variant. DR ComplexPortal; CPX-2873; SCF E3 ubiquitin ligase complex, FBXL20 variant. DR ComplexPortal; CPX-3291; SCF E3 ubiquitin ligase complex, FBXL3 variant. DR ComplexPortal; CPX-3292; SCF E3 ubiquitin ligase complex, FBXL2 variant. DR ComplexPortal; CPX-3295; SCF E3 ubiquitin ligase complex, SKP2 variant. 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 ComplexPortal; CPX-7747; SCF E3 ubiquitin ligase complex, FBXW2 variant. DR ComplexPortal; CPX-7761; SCF E3 ubiquitin ligase complex, FBXW4 variant. DR ComplexPortal; CPX-7762; SCF E3 ubiquitin ligase complex, FBXW5 variant. DR ComplexPortal; CPX-7763; SCF E3 ubiquitin ligase complex, FBXW7 variant. DR ComplexPortal; CPX-7784; SCF E3 ubiquitin ligase complex, FBXW8-CUL7 variant. DR ComplexPortal; CPX-7785; SCF E3 ubiquitin ligase complex, FBXW9 variant. DR ComplexPortal; CPX-7786; SCF E3 ubiquitin ligase complex, FBXW10 variant. DR ComplexPortal; CPX-7821; SCF E3 ubiquitin ligase complex, FBXW11 variant. DR ComplexPortal; CPX-7822; SCF E3 ubiquitin ligase complex, FBXW12 variant. DR ComplexPortal; CPX-7846; SCF E3 ubiquitin ligase complex, CCNF variant. DR ComplexPortal; CPX-7847; SCF E3 ubiquitin ligase complex, FBXO2 variant. DR ComplexPortal; CPX-7881; SCF E3 ubiquitin ligase complex, FBXO3 variant. DR ComplexPortal; CPX-7882; SCF E3 ubiquitin ligase complex, FBXO4 variant. DR ComplexPortal; CPX-7904; SCF E3 ubiquitin ligase complex, FBXO5 variant. DR ComplexPortal; CPX-7905; SCF E3 ubiquitin ligase complex, FBXO6 variant. DR ComplexPortal; CPX-7906; SCF E3 ubiquitin ligase complex, FBXO7 variant. DR ComplexPortal; CPX-7921; SCF E3 ubiquitin ligase complex, FBXO8 variant. DR ComplexPortal; CPX-7922; SCF E3 ubiquitin ligase complex, FBXO9 variant. DR ComplexPortal; CPX-7923; SCF E3 ubiquitin ligase complex, FBXO10 variant. DR ComplexPortal; CPX-7924; SCF E3 ubiquitin ligase complex, FBXO11 variant. DR ComplexPortal; CPX-7925; SCF E3 ubiquitin ligase complex, FBXO15 variant. DR ComplexPortal; CPX-7926; SCF E3 ubiquitin ligase complex, FBXO16 variant. DR ComplexPortal; CPX-7927; SCF E3 ubiquitin ligase complex, FBXO17 variant. DR ComplexPortal; CPX-7928; SCF E3 ubiquitin ligase complex, FBH1 variant. DR ComplexPortal; CPX-7929; SCF E3 ubiquitin ligase complex, LMO7 variant. DR ComplexPortal; CPX-7930; SCF E3 ubiquitin ligase complex, FBXO21 variant. DR ComplexPortal; CPX-7962; SCF E3 ubiquitin ligase complex, FBXO22 variant. DR ComplexPortal; CPX-7963; SCF E3 ubiquitin ligase complex, FBXO24 variant. DR ComplexPortal; CPX-7965; SCF E3 ubiquitin ligase complex, FBXO25 variant. DR ComplexPortal; CPX-7966; SCF E3 ubiquitin ligase complex, FBXO27 variant. DR ComplexPortal; CPX-7967; SCF E3 ubiquitin ligase complex, FBXO28 variant. DR ComplexPortal; CPX-7968; SCF E3 ubiquitin ligase complex, FBXO30 variant. DR ComplexPortal; CPX-7971; SCF E3 ubiquitin ligase complex, FBXO31 variant. DR ComplexPortal; CPX-7972; SCF E3 ubiquitin ligase complex, FBXO32 variant. DR ComplexPortal; CPX-7973; SCF E3 ubiquitin ligase complex, FBXO33 variant. DR ComplexPortal; CPX-7975; SCF E3 ubiquitin ligase complex, FBXO34 variant. DR ComplexPortal; CPX-7976; SCF E3 ubiquitin ligase complex, FBXO36 variant. DR ComplexPortal; CPX-7977; SCF E3 ubiquitin ligase complex, FBXO38 variant. DR ComplexPortal; CPX-7979; SCF E3 ubiquitin ligase complex, FBXO39 variant. DR ComplexPortal; CPX-7981; SCF E3 ubiquitin ligase complex, FBXO40 variant. DR ComplexPortal; CPX-7982; SCF E3 ubiquitin ligase complex, FBXO41 variant. DR ComplexPortal; CPX-7983; SCF E3 ubiquitin ligase complex, FBXO42 variant. DR ComplexPortal; CPX-8002; SCF E3 ubiquitin ligase complex, FBXO43 variant. DR ComplexPortal; CPX-8003; SCF E3 ubiquitin ligase complex, FBXO44 variant. DR ComplexPortal; CPX-8005; SCF E3 ubiquitin ligase complex, FBXO46 variant. DR ComplexPortal; CPX-8006; SCF E3 ubiquitin ligase complex, FBXO47 variant. DR ComplexPortal; CPX-8007; CRL3 E3 ubiquitin ligase complex, KLHL1 variant. DR ComplexPortal; CPX-8025; CRL3 E3 ubiquitin ligase complex, KLHL2 variant. DR ComplexPortal; CPX-8041; CRL3 E3 ubiquitin ligase complex, KLHL3 variant. DR ComplexPortal; CPX-8061; CRL3 E3 ubiquitin ligase complex, KLHL4 variant. DR ComplexPortal; CPX-8063; CRL3 E3 ubiquitin ligase complex, KLHL5 variant. DR ComplexPortal; CPX-8064; CRL3 E3 ubiquitin ligase complex, KLHL6 variant. DR ComplexPortal; CPX-8083; CRL3 E3 ubiquitin ligase complex, KLHL9 variant. DR ComplexPortal; CPX-8084; CRL3 E3 ubiquitin ligase complex, KLHL7 variant. DR ComplexPortal; CPX-8085; CRL3 E3 ubiquitin ligase complex, KLHL8 variant. DR ComplexPortal; CPX-8087; CRL3 E3 ubiquitin ligase complex, KLHL10 variant. DR ComplexPortal; CPX-8088; CRL3 E3 ubiquitin ligase complex, KLHL11 variant. DR ComplexPortal; CPX-8089; CRL3 E3 ubiquitin ligase complex, KLHL12 variant. DR ComplexPortal; CPX-8090; CRL3 E3 ubiquitin ligase complex, KLHL13 variant. DR ComplexPortal; CPX-8091; CRL3 E3 ubiquitin ligase complex, KLHL14 variant. DR ComplexPortal; CPX-8097; CRL3 E3 ubiquitin ligase complex, KLHL15 variant. DR ComplexPortal; CPX-8102; CRL3 E3 ubiquitin ligase complex, KLHL16 variant. DR ComplexPortal; CPX-8103; CRL3 E3 ubiquitin ligase complex, KLHL17 variant. DR ComplexPortal; CPX-8106; CRL3 E3 ubiquitin ligase complex, KLHL18 variant. DR ComplexPortal; CPX-8107; CRL3 E3 ubiquitin ligase complex, KEAP1 variant. DR ComplexPortal; CPX-8108; SCF E3 ubiquitin ligase complex, TSPAN17 variant. DR ComplexPortal; CPX-8109; CRL3 E3 ubiquitin ligase complex, KLHL20 variant. DR ComplexPortal; CPX-8110; CRL3 E3 ubiquitin ligase complex, KLHL21 variant. DR ComplexPortal; CPX-8122; CRL3 E3 ubiquitin ligase complex, KLHL22 variant. DR ComplexPortal; CPX-8123; CRL3 E3 ubiquitin ligase complex, KLHL23 variant. DR ComplexPortal; CPX-8125; CRL3 E3 ubiquitin ligase complex, KLHL24 variant. DR ComplexPortal; CPX-8126; CRL3 E3 ubiquitin ligase complex, KLHL25 variant. DR ComplexPortal; CPX-8130; CRL3 E3 ubiquitin ligase complex, KLHL26 variant. DR ComplexPortal; CPX-8131; CRL3 E3 ubiquitin ligase complex, IPP variant. DR ComplexPortal; CPX-8135; CRL3 E3 ubiquitin ligase complex, KLHL28 variant. DR ComplexPortal; CPX-8147; CRL3 E3 ubiquitin ligase complex, KLHL29 variant. DR ComplexPortal; CPX-8150; CRL3 E3 ubiquitin ligase complex, KLHL30 variant. DR ComplexPortal; CPX-8151; CRL3 E3 ubiquitin ligase complex, KLHL31 variant. DR ComplexPortal; CPX-8201; CRL3 E3 ubiquitin ligase complex, KLHL32 variant. DR ComplexPortal; CPX-8202; CRL3 E3 ubiquitin ligase complex, KLHL34 variant. DR ComplexPortal; CPX-8221; CRL3 E3 ubiquitin ligase complex, KLHL35 variant. DR ComplexPortal; CPX-8222; CRL3 E3 ubiquitin ligase complex, KLHL36 variant. DR ComplexPortal; CPX-8241; CRL3 E3 ubiquitin ligase complex, ENC1 variant. DR ComplexPortal; CPX-8242; CRL3 E3 ubiquitin ligase complex, KLHL38 variant. DR ComplexPortal; CPX-8261; CRL3 E3 ubiquitin ligase complex, KLHL40 variant. DR ComplexPortal; CPX-8262; CRL3 E3 ubiquitin ligase complex, KLHL41 variant. DR ComplexPortal; CPX-8263; CRL3 E3 ubiquitin ligase complex, KLHL42 variant. DR CORUM; P62877; -. DR DIP; DIP-17014N; -. DR IntAct; P62877; 83. DR MINT; P62877; -. DR STRING; 9606.ENSP00000216225; -. DR BindingDB; P62877; -. 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; 9606-ENSP00000216225; -. DR PeptideAtlas; P62877; -. DR ProteomicsDB; 57443; -. DR Pumba; P62877; -. DR TopDownProteomics; P62877; -. DR Antibodypedia; 295; 399 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 AGR; HGNC:9928; -. 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; NACPLDN; -. DR OrthoDB; 3546417at2759; -. 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; 663 hits in 1209 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 210 other cell types or tissues. 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:0005737; C:cytoplasm; IDA:UniProt. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProt. 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:0060090; F:molecular adaptor activity; EXP:DisProt. 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:0071230; P:cellular response to amino acid stimulus; IDA:UniProt. DR GO; GO:0062197; P:cellular response to chemical stress; TAS:Reactome. DR GO; GO:0034644; P:cellular response to UV; EXP:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; EXP: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:0032480; P:negative regulation of type I interferon production; IDA:UniProt. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProt. 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:0045732; P:positive regulation of protein catabolic process; IDA:UniProt. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProt. 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:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IDA:UniProt. DR GO; GO:0042110; P:T cell activation; IDA:UniProt. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProt. DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProt. DR CDD; cd16485; mRING-H2-C3H2C2D_RBX1; 1. DR DisProt; DP01750; -. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; IID00059; -. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR024766; Znf_RING_H2. DR PANTHER; PTHR11210:SF2; E3 UBIQUITIN-PROTEIN LIGASE RBX1; 1. DR PANTHER; PTHR11210; RING BOX; 1. DR Pfam; PF12678; zf-rbx1; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; P62877; HS. 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 STRAND 47..51 FT /evidence="ECO:0007829|PDB:7Z8B" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:3DPL" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:8OR2" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:7Z8R" 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 //