GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

E3 ubiquitin-protein ligase RBX1 (EC 2 3 2 27) (EC 2 3 2 32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)]

 RBX1_HUMAN              Reviewed;         108 AA.
P62877; B2RDY1; Q8N6Z8; Q9D1S2; Q9WUK9; Q9Y254;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
02-JUN-2021, entry version 183.
RecName: Full=E3 ubiquitin-protein ligase RBX1;
EC=2.3.2.27 {ECO:0000269|PubMed:11027288};
EC=2.3.2.32 {ECO:0000269|PubMed:11027288};
AltName: Full=E3 ubiquitin-protein transferase RBX1 {ECO:0000305};
AltName: Full=Protein ZYP;
AltName: Full=RING finger protein 75;
AltName: Full=RING-box protein 1;
Short=Rbx1;
AltName: Full=Regulator of cullins 1;
Short=ROC1 {ECO:0000303|PubMed:10230407};
Contains:
RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
AltName: Full=E3 ubiquitin-protein transferase RBX1, N-terminally processed {ECO:0000305};
Name=RBX1; Synonyms=RNF75, ROC1 {ECO:0000303|PubMed:10230407};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, INTERACTION WITH CULLINS,
DOMAIN, AND MUTAGENESIS OF CYS-53; CYS-56; CYS-75 AND HIS-77.
TISSUE=Cervix carcinoma;
PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
"ROC1, a homolog of APC11, represents a family of cullin partners with an
associated ubiquitin ligase activity.";
Mol. Cell 3:535-541(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN CBC(VHL) COMPLEX.
PubMed=10213691; DOI=10.1126/science.284.5414.657;
Kamura T., Koepp D.M., Conrad M.N., Skowyra D., Moreland R.J.,
Iliopoulos O., Lane W.S., Kaelin W.G. Jr., Elledge S.J., Conaway R.C.,
Harper J.W., Conaway J.W.;
"Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin
ligase.";
Science 284:657-661(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-108.
TISSUE=Brain;
PubMed=10643962;
Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L., Rieger F.,
Alliel P.M.;
"Genomic organization and expression of the ubiquitin-proteasome complex-
associated protein Rbx1/ROC1/Hrt1.";
Cell. Mol. Biol. 45:1131-1137(1999).
[10]
PROTEIN SEQUENCE OF 92-105, INTERACTION WITH CUL1, AND IDENTIFICATION IN A
COMPLEX WITH CUL1; SKP1 AND SKP2.
TISSUE=Cervix carcinoma;
PubMed=10230406; DOI=10.1016/s1097-2765(00)80481-5;
Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.;
"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze
the ubiquitination of I kappa B alpha.";
Mol. Cell 3:527-533(1999).
[11]
FUNCTION.
PubMed=10579999; DOI=10.1101/gad.13.22.2928;
Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.;
"The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1
modification of cullins Cdc53 and Cul2.";
Genes Dev. 13:2928-2933(1999).
[12]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
PubMed=11027288; DOI=10.1128/mcb.20.21.8185-8197.2000;
Furukawa M., Zhang Y., McCarville J., Ohta T., Xiong Y.;
"The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear
accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1.";
Mol. Cell. Biol. 20:8185-8197(2000).
[13]
IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MUF1, AND
IDENTIFICATION IN COMPLEXES WITH CUL5.
PubMed=11384984; DOI=10.1074/jbc.m103093200;
Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
"Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
J. Biol. Chem. 276:29748-29753(2001).
[14]
INTERACTION WITH COPS6.
PubMed=11337588; DOI=10.1126/science.1059780;
Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
Science 292:1382-1385(2001).
[15]
IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
PubMed=12149480; DOI=10.1073/pnas.162424199;
Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A., Stearman R.,
Klausner R.D., Malik S., Lane W.S., Sorokina I., Roeder R.G., Conaway J.W.,
Conaway R.C.;
"Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that
can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase.";
Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002).
[16]
IDENTIFICATION IN SCF-LIKE COMPLEX, AND INTERACTION WITH CUL7.
PubMed=12481031; DOI=10.1073/pnas.252646399;
Dias D.C., Dolios G., Wang R., Pan Z.Q.;
"CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form
an SCF-like complex.";
Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
[17]
IDENTIFICATION IN THE CSA COMPLEX WITH ERCC8; DDB1 AND CUL4A, AND
INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9
SIGNALOSOME.
PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
Kisselev A.F., Tanaka K., Nakatani Y.;
"The ubiquitin ligase activity in the DDB2 and CSA complexes is
differentially regulated by the COP9 signalosome in response to DNA
damage.";
Cell 113:357-367(2003).
[18]
IDENTIFICATION IN THE DCX DET1-COP1 COMPLEX WITH DDB1; CUL4A; COP1 AND
DET1.
PubMed=14739464; DOI=10.1126/science.1093549;
Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J.,
Dixit V.M.;
"Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin
ligase.";
Science 303:1371-1374(2004).
[19]
FUNCTION, IDENTIFICATION IN THE BCR(KLHL41) COMPLEX, IDENTIFICATION IN THE
BCR(ENC1) COMPLEX, IDENTIFICATION IN THE BCR(KEAP1) COMPLEX, AND
IDENTIFICATION IN THE BCR(GAN) COMPLEX.
PubMed=15983046; DOI=10.1074/jbc.m501279200;
Zhang D.D., Lo S.C., Sun Z., Habib G.M., Lieberman M.W., Hannink M.;
"Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3,
targets Keap1 for degradation by a proteasome-independent pathway.";
J. Biol. Chem. 280:30091-30099(2005).
[20]
FUNCTION.
PubMed=16751180; DOI=10.1101/gad.378206;
Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K.,
Kisselev A.F., Harel-Bellan A., Nakatani Y.;
"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway
establishes a link between complementation factors of the Cockayne
syndrome.";
Genes Dev. 20:1429-1434(2006).
[21]
IDENTIFICATION IN COMPLEX WITH DDB1; DDB2; CUL4A AND CUL4B, IDENTIFICATION
BY MASS SPECTROMETRY, AND FUNCTION.
PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
Tempst P., Xiong Y., Zhang Y.;
"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase
facilitates cellular response to DNA damage.";
Mol. Cell 22:383-394(2006).
[22]
FUNCTION.
PubMed=18397884; DOI=10.1074/jbc.m802030200;
Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
"Regulation of TIP60 by ATF2 modulates ATM activation.";
J. Biol. Chem. 283:17605-17614(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
INTERACTION WITH CUL1; FBXO3; SKP1 AND PML.
PubMed=18809579; DOI=10.1128/mcb.00897-08;
Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.;
"PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-
mediated degradation.";
Mol. Cell. Biol. 28:7126-7138(2008).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND CDC34, AND
FUNCTION.
PubMed=19112177; DOI=10.1074/jbc.m804531200;
Cen B., Li H., Weinstein I.B.;
"Histidine triad nucleotide-binding protein 1 up-regulates cellular levels
of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.";
J. Biol. Chem. 284:5265-5276(2009).
[27]
INTERACTION WITH UBE2M.
PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C.,
Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.;
"E2-RING expansion of the NEDD8 cascade confers specificity to cullin
modification.";
Mol. Cell 33:483-495(2009).
[28]
FUNCTION, AND INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
PubMed=19679664; DOI=10.1074/jbc.m109.006809;
Isobe T., Hattori T., Kitagawa K., Uchida C., Kotake Y., Kosugi I., Oda T.,
Kitagawa M.;
"Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.";
J. Biol. Chem. 284:27766-27779(2009).
[29]
IDENTIFICATION IN THE SCF(CYCLIN F) COMPLEX.
PubMed=20596027; DOI=10.1038/nature09140;
D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
Washburn M.P., Dynlacht B., Pagano M.;
"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through
CP110 degradation.";
Nature 466:138-142(2010).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ALA-2, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT THR-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[34]
INTERACTION WITH SESN1 AND SESN2.
PubMed=23274085; DOI=10.1016/j.cmet.2012.12.002;
Bae S.H., Sung S.H., Oh S.Y., Lim J.M., Lee S.K., Park Y.N., Lee H.E.,
Kang D., Rhee S.G.;
"Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation
of Keap1 and prevent oxidative liver damage.";
Cell Metab. 17:73-84(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
FUNCTION, AND IDENTIFICATION IN THE BCR(KLHL22) COMPLEX.
PubMed=23455478; DOI=10.1038/ncb2695;
Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H.,
Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.;
"Ubiquitylation-dependent localization of PLK1 in mitosis.";
Nat. Cell Biol. 15:430-439(2013).
[37]
INTERACTION WITH DCUN1D5.
PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
"Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
and nuclear localization.";
Clin. Cancer Res. 20:372-381(2014).
[38]
INTERACTION WITH DCUN1D3.
PubMed=25349211; DOI=10.1074/jbc.m114.585505;
Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E.,
Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
"SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of
SCCRO (DCUN1D1).";
J. Biol. Chem. 289:34728-34742(2014).
[39]
SUBUNIT.
PubMed=25684205; DOI=10.1016/j.molcel.2014.12.040;
Genau H.M., Huber J., Baschieri F., Akutsu M., Doetsch V., Farhan H.,
Rogov V., Behrends C.;
"CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to
spatially restrict TIAM1-RAC1 signaling.";
Mol. Cell 57:995-1010(2015).
[40]
FUNCTION.
PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L., Paulo J.A.,
de Jong A., Ovaa H., Alpi A.F., Harper J.W., Schulman B.A.;
"Two distinct types of E3 ligases work in unison to regulate substrate
ubiquitylation.";
Cell 166:1198-1214(2016).
[41]
INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
PubMed=26906416; DOI=10.1242/jcs.181784;
Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
"Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
J. Cell Sci. 129:1441-1454(2016).
[42]
INTERACTION WITH NOTCH2.
PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W., Inuzuka H.;
"NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
promote osteoporosis.";
Mol. Cell 68:645-658(2017).
[43]
FUNCTION.
PubMed=29769719; DOI=10.1038/s41586-018-0128-9;
Chen J., Ou Y., Yang Y., Li W., Xu Y., Xie Y., Liu Y.;
"KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
tumorigenesis and ageing.";
Nature 557:585-589(2018).
[44]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776 OF
CUL1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; SKP1
AND SKP2, FUNCTION, AND DOMAIN.
PubMed=11961546; DOI=10.1038/416703a;
Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W.,
Harper J.W., Pavletich N.P.;
"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
Nature 416:703-709(2002).
[45] {ECO:0007744|PDB:4F52}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 5-108 IN COMPLEX WITH CUL1; GLMN
AND ZINC, SUBUNIT, INTERACTION WITH CDC34 AND GLMN, FUNCTION, DOMAIN, AND
PATHWAY.
PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044;
Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J.,
Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.;
"Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase
through masking of its E2-binding surface.";
Mol. Cell 47:371-382(2012).
-!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-based
E3 ubiquitin-protein ligase (CRLs) complexes which mediate the
ubiquitination and subsequent proteasomal degradation of target
proteins, including proteins involved in cell cycle progression, signal
transduction, transcription and transcription-coupled nucleotide
excision repair (PubMed:10230407, PubMed:10579999, PubMed:15983046,
PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:23455478,
PubMed:27565346, PubMed:29769719, PubMed:11961546, PubMed:22748924).
CRLs complexes and ARIH1 collaborate in tandem to mediate
ubiquitination of target proteins, ARIH1 mediating addition of the
first ubiquitin on CRLs targets (PubMed:27565346). The functional
specificity of the E3 ubiquitin-protein ligase complexes depends on the
variable substrate recognition components. As a component of the CSA
complex promotes the ubiquitination of ERCC6 resulting in proteasomal
degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the
complex and brings it into close proximity to the substrate. Probably
also stimulates CDC34 autoubiquitination. May be required for histone
H3 and histone H4 ubiquitination in response to ultraviolet and for
subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and
CUL4 via its interaction with UBE2M. Involved in the ubiquitination of
KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes
degradation of KAT5 thereby attenuating its ability to acetylate and
activate ATM. {ECO:0000269|PubMed:10230407,
ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:11027288,
ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:15983046,
ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:16751180,
ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:19112177,
ECO:0000269|PubMed:19679664, ECO:0000269|PubMed:22748924,
ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:27565346,
ECO:0000269|PubMed:29769719}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
[acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11027288};
-!- CATALYTIC ACTIVITY:
Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine
+ [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine +
N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32;
Evidence={ECO:0000269|PubMed:11027288};
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11027288,
ECO:0000269|PubMed:22748924}.
-!- SUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and SKP2
(PubMed:11961546). Part of a SCF-like complex consisting of CUL7, RBX1,
SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC complex
(ELOB and ELOC), CUL2 or CUL5 and VHL. Part of the CSA complex
(DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex
containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with
RNA polymerase II; upon UV irradiation it interacts with the COP9
signalosome and preferentially with the hyperphosphorylated form of RNA
polymerase II. Part of multisubunit E3 ubiquitin ligase complexes with
elongin BC complex (ELOB and ELOC), CUL2 and MED8; elongin BC complex
(ELOB and ELOC), CUL5 and MUF1. Part of multisubunit complexes with
elongin BC complex (ELOB and ELOC), elongin A/ELOA or SOCS1 or WSB1 and
CUL5. Interacts directly with CUL1 and probably also with CUL2, CUL3,
CUL4A, CUL4B, CUL5 and CUL7. Interacts with CDC34 (PubMed:22748924).
Interacts with GLMN. GLMN competes for the binding site of the E2
ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding
(PubMed:22748924). Interacts with COPS6. Component of the DCX DET1-COP1
ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A
and COP1. Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and
CUL4A or CUL4B. Interacts with UBE2M. Part of a SCF complex consisting
of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via
FBXO3. Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1,
SKP1 and CCNF. Identified in a SCF (SKP1-CUL1-F-box protein) E3
ubiquitin ligase complex together with HINT1 and CDC34. Component of
multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
formed of CUL3, RBX1 and a variable BTB domain-containing protein. Part
of the BCR(ENC1) complex containing ENC1. Part of the BCR(GAN) complex
containing GAN. Part of the BCR(KLHL41) complex containing KLHL41. Part
of the BCR(KEAP1) complex containing KEAP1. Interacts with SESN1 and
SESN2 (PubMed:23274085). Interacts with NOTCH2 (PubMed:29149593).
Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least
composed of CUL3, KLHL22 and RBX1 (PubMed:23455478). Interacts with
DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:26906416,
PubMed:24192928, PubMed:25349211). Component of a BCR3 (BTB-CUL3-RBX1)
E3 ubiquitin ligase complex, also named Cul3-RING ubiquitin ligase
complex CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and KBTBD7
(PubMed:25684205). {ECO:0000269|PubMed:10213691,
ECO:0000269|PubMed:10230406, ECO:0000269|PubMed:10230407,
ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:11384984,
ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:12149480,
ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12732143,
ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15983046,
ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18809579,
ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:19250909,
ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:22748924,
ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:23455478,
ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:25349211,
ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:26906416,
ECO:0000269|PubMed:29149593}.
-!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5
protein E1A; this interaction inhibits RBX1-CUL1-dependent elongation
reaction of ubiquitin chains by the SCF(FBW7) complex.
{ECO:0000269|PubMed:19679664}.
-!- INTERACTION:
P62877; Q13616: CUL1; NbExp=28; IntAct=EBI-398523, EBI-359390;
P62877; Q13617: CUL2; NbExp=8; IntAct=EBI-398523, EBI-456179;
P62877; Q13620: CUL4B; NbExp=5; IntAct=EBI-398523, EBI-456067;
P62877; Q93034: CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139;
P62877; Q92990: GLMN; NbExp=6; IntAct=EBI-398523, EBI-726150;
P62877; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-398523, EBI-10176379;
P62877; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-398523, EBI-10302990;
P62877; P58004: SESN2; NbExp=3; IntAct=EBI-398523, EBI-3939642;
P62877; Q13309: SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291;
P62877; P61081: UBE2M; NbExp=7; IntAct=EBI-398523, EBI-1041660;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11027288}. Nucleus
{ECO:0000269|PubMed:11027288}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
ligase activity (PubMed:10230407). It coordinates an additional third
zinc ion (PubMed:11961546, PubMed:22748924).
{ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:11961546,
ECO:0000269|PubMed:22748924}.
-!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH17370.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RBX1ID42075ch22q13.html";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AF142059; AAD30146.1; -; mRNA.
EMBL; AF140598; AAD29715.1; -; mRNA.
EMBL; CR456560; CAG30446.1; -; mRNA.
EMBL; AK315722; BAG38078.1; -; mRNA.
EMBL; AL080242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60403.1; -; Genomic_DNA.
EMBL; BC001466; AAH01466.1; -; mRNA.
EMBL; BC017370; AAH17370.2; ALT_INIT; mRNA.
EMBL; AY099360; AAM21718.1; -; mRNA.
CCDS; CCDS14009.1; -.
PIR; T51146; T51146.
RefSeq; NP_055063.1; NM_014248.3.
PDB; 1LDJ; X-ray; 3.00 A; B=19-108.
PDB; 1LDK; X-ray; 3.10 A; C=19-108.
PDB; 1U6G; X-ray; 3.10 A; B=1-108.
PDB; 2HYE; X-ray; 3.10 A; D=1-108.
PDB; 2LGV; NMR; -; A=12-108.
PDB; 3DPL; X-ray; 2.60 A; R=5-108.
PDB; 3DQV; X-ray; 3.00 A; R/Y=5-108.
PDB; 3RTR; X-ray; 3.21 A; B/D/F/H=5-108.
PDB; 4F52; X-ray; 3.00 A; B/D=5-108.
PDB; 4P5O; X-ray; 3.11 A; B/D=5-108.
PDB; 5N4W; X-ray; 3.90 A; R=1-102.
PDB; 6R6H; EM; 8.40 A; R=17-102.
PDB; 6R7F; EM; 8.20 A; R=19-108.
PDB; 6R7H; EM; 8.80 A; R=19-108.
PDB; 6R7I; EM; 5.90 A; R=19-102.
PDB; 6R7N; EM; 6.50 A; R=17-102.
PDB; 6TTU; EM; 3.70 A; R=1-108.
PDB; 7B5L; EM; 3.80 A; R=1-108.
PDB; 7B5M; EM; 3.91 A; R=1-108.
PDB; 7B5N; EM; 3.60 A; R=1-108.
PDB; 7B5S; EM; 3.60 A; R=1-108.
PDBsum; 1LDJ; -.
PDBsum; 1LDK; -.
PDBsum; 1U6G; -.
PDBsum; 2HYE; -.
PDBsum; 2LGV; -.
PDBsum; 3DPL; -.
PDBsum; 3DQV; -.
PDBsum; 3RTR; -.
PDBsum; 4F52; -.
PDBsum; 4P5O; -.
PDBsum; 5N4W; -.
PDBsum; 6R6H; -.
PDBsum; 6R7F; -.
PDBsum; 6R7H; -.
PDBsum; 6R7I; -.
PDBsum; 6R7N; -.
PDBsum; 6TTU; -.
PDBsum; 7B5L; -.
PDBsum; 7B5M; -.
PDBsum; 7B5N; -.
PDBsum; 7B5S; -.
SMR; P62877; -.
BioGRID; 115301; 431.
ComplexPortal; CPX-477; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
ComplexPortal; CPX-648; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
CORUM; P62877; -.
DIP; DIP-17014N; -.
IntAct; P62877; 78.
MINT; P62877; -.
STRING; 9606.ENSP00000216225; -.
ChEMBL; CHEMBL3833061; -.
iPTMnet; P62877; -.
MetOSite; P62877; -.
PhosphoSitePlus; P62877; -.
SwissPalm; P62877; -.
BioMuta; RBX1; -.
DMDM; 51338609; -.
EPD; P62877; -.
jPOST; P62877; -.
MassIVE; P62877; -.
MaxQB; P62877; -.
PaxDb; P62877; -.
PeptideAtlas; P62877; -.
PRIDE; P62877; -.
ProteomicsDB; 57443; -.
TopDownProteomics; P62877; -.
Antibodypedia; 295; 341 antibodies.
DNASU; 9978; -.
Ensembl; ENST00000216225; ENSP00000216225; ENSG00000100387.
GeneID; 9978; -.
KEGG; hsa:9978; -.
UCSC; uc003azk.4; human.
CTD; 9978; -.
DisGeNET; 9978; -.
GeneCards; RBX1; -.
HGNC; HGNC:9928; RBX1.
HPA; ENSG00000100387; Low tissue specificity.
MIM; 603814; gene.
neXtProt; NX_P62877; -.
OpenTargets; ENSG00000100387; -.
PharmGKB; PA34299; -.
VEuPathDB; HostDB:ENSG00000100387.8; -.
eggNOG; KOG2930; Eukaryota.
GeneTree; ENSGT00940000155618; -.
HOGENOM; CLU_115512_2_1_1; -.
InParanoid; P62877; -.
OMA; IDKENCT; -.
OrthoDB; 1587140at2759; -.
PhylomeDB; P62877; -.
TreeFam; TF105503; -.
BRENDA; 2.3.2.27; 2681.
BRENDA; 2.3.2.32; 2681.
PathwayCommons; P62877; -.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P62877; -.
SIGNOR; P62877; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 9978; 610 hits in 998 CRISPR screens.
ChiTaRS; RBX1; human.
EvolutionaryTrace; P62877; -.
GeneWiki; RBX1; -.
GenomeRNAi; 9978; -.
Pharos; P62877; Tbio.
PRO; PR:P62877; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; P62877; protein.
Bgee; ENSG00000100387; Expressed in bone marrow and 241 other tissues.
Genevisible; P62877; HS.
GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0030891; C:VCB complex; IEA:Ensembl.
GO; GO:0097602; F:cullin family protein binding; IDA:MGI.
GO; GO:0061663; F:NEDD8 ligase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IPI:UniProtKB.
GO; GO:1902499; P:positive regulation of protein autoubiquitination; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0010265; P:SCF complex assembly; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
DisProt; DP01750; -.
Gene3D; 3.30.40.10; -; 1.
IDEAL; IID00059; -.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR024766; Znf_RING_H2.
Pfam; PF12678; zf-rbx1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
DNA damage; DNA repair; Host-virus interaction; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1..108
/note="E3 ubiquitin-protein ligase RBX1"
/id="PRO_0000423264"
INIT_MET 1
/note="Removed; alternate"
/evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378"
CHAIN 2..108
/note="E3 ubiquitin-protein ligase RBX1, N-terminally
processed"
/id="PRO_0000056013"
ZN_FING 53..98
/note="RING-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
METAL 42
/note="Zinc 1"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 45
/note="Zinc 1"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 53
/note="Zinc 2"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 56
/note="Zinc 2"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 68
/note="Zinc 2"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 75
/note="Zinc 3"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 77
/note="Zinc 3; via pros nitrogen"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 80
/note="Zinc 1; via pros nitrogen"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 82
/note="Zinc 2; via pros nitrogen"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 83
/note="Zinc 1"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR,
ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O"
METAL 94
/note="Zinc 3"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
METAL 97
/note="Zinc 3"
/evidence="ECO:0000269|PubMed:11961546,
ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK,
ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE,
ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV,
ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52,
ECO:0007744|PDB:4P5O"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:20068231"
MOD_RES 2
/note="N-acetylalanine; in E3 ubiquitin-protein ligase
RBX1, N-terminally processed"
/evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378"
MOD_RES 9
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MUTAGEN 53
/note="C->A: Strong reduction in ligase activity; when
associated with A-56."
/evidence="ECO:0000269|PubMed:10230407"
MUTAGEN 56
/note="C->A: Strong reduction in ligase activity; when
associated with A-53."
/evidence="ECO:0000269|PubMed:10230407"
MUTAGEN 75
/note="C->A: Strong reduction in ligase activity; when
associated with A-77."
/evidence="ECO:0000269|PubMed:10230407"
MUTAGEN 77
/note="H->A: Strong reduction in ligase activity; when
associated with A-75."
/evidence="ECO:0000269|PubMed:10230407"
CONFLICT 18
/note="G -> S (in Ref. 9; AAM21718)"
/evidence="ECO:0000305"
STRAND 21..37
/evidence="ECO:0007829|PDB:3DPL"
STRAND 39..41
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 43..45
/evidence="ECO:0007829|PDB:3DPL"
TURN 49..54
/evidence="ECO:0007829|PDB:1LDJ"
HELIX 56..59
/evidence="ECO:0007829|PDB:3DPL"
TURN 63..67
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 70..73
/evidence="ECO:0007829|PDB:3DPL"
STRAND 74..76
/evidence="ECO:0007829|PDB:1LDJ"
STRAND 78..80
/evidence="ECO:0007829|PDB:3DPL"
HELIX 81..88
/evidence="ECO:0007829|PDB:3DPL"
STRAND 90..93
/evidence="ECO:0007829|PDB:1LDK"
STRAND 95..97
/evidence="ECO:0007829|PDB:3DPL"
STRAND 103..105
/evidence="ECO:0007829|PDB:3DPL"
SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH


Related products :

Catalog number Product name Quantity
EIAAB34069 E3 ubiquitin-protein ligase RBX1,Homo sapiens,Human,Protein ZYP,Rbx1,RBX1,Regulator of cullins 1,RING finger protein 75,RING-box protein 1,RNF75,ROC1
EIAAB34070 E3 ubiquitin-protein ligase RBX1,Mouse,Mus musculus,Rbx1,Rbx1,RING finger protein 75,RING-box protein 1
CSB-EL019496MO Mouse E3 ubiquitin-protein ligase RBX1(RBX1) ELISA kit SpeciesMouse 96T
CSB-EL019496HU Human E3 ubiquitin-protein ligase RBX1(RBX1) ELISA kit SpeciesHuman 96T
CSB-EL019496HU Human E3 ubiquitin-protein ligase RBX1(RBX1) ELISA kit 96T
CSB-EL019496MO Mouse E3 ubiquitin-protein ligase RBX1(RBX1) ELISA kit 96T
RBX1_MOUSE ELISA Kit FOR E3 ubiquitin-protein ligase RBX1; organism: Mouse; gene name: Rbx1 96T
18-003-42898 RING-box protein 1 - Rbx1; Regulator of cullins 1; RING finger protein 75; Protein ZYP Polyclonal 0.1 mg Protein A
10-288-22026F RING-box protein 1 - Rbx1; Regulator of cullins 1; RING finger protein 75; Protein ZYP 0.1 mg
10-288-22026F RING-box protein 1 - Rbx1; Regulator of cullins 1; RING finger protein 75; Protein ZYP 0.05 mg
E1585m Human ELISA Kit FOR E3 ubiquitin-protein ligase RBX1 96T
18-272-196432 ROC1 prediluted - Rabbit polyclonal to ROC1 prediluted; Rbx1; Regulator of cullins 1; RING finger protein 75; Protein ZYP Polyclonal 7 ml
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
A1832 RBX1 Primary Antibody, RBX1, Species: Human Recombinant Protein Source: Rabbit Polyclonal 50ug
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35571 CARP-1,Caspase regulator CARP1,Caspases-8 and -10-associated RING finger protein 1,E3 ubiquitin-protein ligase RNF34,FYVE-RING finger protein Momo,Homo sapiens,hRFI,Human,Human RING finger homologous
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135
Pathways :
WP2199: Seed Development
WP211: BMP signaling pathway
WP2292: Chemokine signaling pathway
WP1678: Nucleotide excision repair
WP1672: Mismatch repair
WP1625: Base excision repair
WP1676: Non-homologous end-joining
WP1714: Tyrosine metabolism
WP1689: Porphyrin and chlorophyll metabolism
WP1371: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP35: G Protein Signaling Pathways
WP1657: Glycerolipid metabolism
WP2218: sGC
WP931: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1693: Purine metabolism
WP1566: Citrate cycle (TCA cycle)
WP1713: Two-component system
WP525: Mitochondrial Unfolded-Protein Response
WP1663: Homologous recombination
WP2324: AGE/RAGE pathway
WP1892: Protein folding
WP73: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways

Related Genes :
[RBX1 RNF75 ROC1] E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) (ROC1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed (E3 ubiquitin-protein transferase RBX1, N-terminally processed)]
[Rbx1] E3 ubiquitin-protein ligase RBX1 (EC 2.3.2.27) (EC 2.3.2.32) (E3 ubiquitin-protein transferase RBX1) (RING finger protein 75) (RING-box protein 1) (Rbx1) [Cleaved into: E3 ubiquitin-protein ligase RBX1, N-terminally processed]
[HRT1 RBX1 ROC1 YOL133W] RING-box protein HRT1 (RING-box protein 1) (E3 ubiquitin-protein ligase complex SCF subunit HRT1) (High level expression reduces Ty3 transposition protein 1) (Regulator of cullins protein 1)
[RBX1A ROC1 At5g20570 F7C8.160] RING-box protein 1a (At-Rbx1;1) (Protein RING of cullins 1) (RBX1-2) (RBX1a-At)
[rbx-1 ZK287.5] RING-box protein 1 (Rbx1) (Ce-rbx-1)
[COP1 RFWD2 RNF200] E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (hCOP1) (RING finger and WD repeat domain protein 2) (RING finger protein 200) (RING-type E3 ubiquitin transferase RFWD2)
[Cop1 Rfwd2 RNF200] E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (mCOP1) (RING finger and WD repeat domain protein 2) (RING-type E3 ubiquitin transferase RFWD2)
[RAG1 RNF74] V(D)J recombination-activating protein 1 (RAG-1) (RING finger protein 74) [Includes: Endonuclease RAG1 (EC 3.1.-.-); E3 ubiquitin-protein ligase RAG1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAG1)]
[Rag1] V(D)J recombination-activating protein 1 (RAG-1) [Includes: Endonuclease RAG1 (EC 3.1.-.-); E3 ubiquitin-protein ligase RAG1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAG1)]
[CDC34 UBCH3 UBE2R1] Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1)
[dsc1 SPBC947.10] DSC E3 ubiquitin ligase complex subunit 1 (EC 2.3.2.27) (Defective for SREBP cleavage protein 1) (RING-type E3 ubiquitin transferase DSC1)
[TUL1 YKL034W YKL247] Transmembrane E3 ubiquitin-protein ligase 1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TUL1)
[ubr-1 C32E8.11] E3 ubiquitin-protein ligase ubr-1 (EC 2.3.2.27) (N-recognin-1) (RING-type E3 ubiquitin transferase ubr-1) (Ubiquitin-protein ligase E3-alpha)
[Cdc34 Ubch3 Ube2r1] Ubiquitin-conjugating enzyme E2 R1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme R1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme R1) (Ubiquitin-conjugating enzyme E2-32 kDa complementing) (Ubiquitin-conjugating enzyme E2-CDC34) (Ubiquitin-protein ligase R1)
[Uhrf1 Np95] E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
[Sh3rf2 Posh3 Ppp1r39 Rnf158] E3 ubiquitin-protein ligase SH3RF2 (EC 2.3.2.27) (Protein phosphatase 1 regulatory subunit 39) (RING finger protein 158) (RING-type E3 ubiquitin transferase SH3RF2) (SH3 domain-containing RING finger protein 2)
[Rnf2 DinG Ring1b] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2)
[GRR1 CAT80 COT2 YJR090C J1885] SCF E3 ubiquitin ligase complex F-box protein GRR1 (F-box and leucine-rich repeat protein GRR1) (F-box/LRR-repeat protein GRR1)
[RNF8 KIAA0646] E3 ubiquitin-protein ligase RNF8 (hRNF8) (EC 2.3.2.27) (RING finger protein 8) (RING-type E3 ubiquitin transferase RNF8)
[RCHY1 ARNIP CHIMP PIRH2 RNF199 ZNF363] RING finger and CHY zinc finger domain-containing protein 1 (EC 2.3.2.27) (Androgen receptor N-terminal-interacting protein) (CH-rich-interacting match with PLAG1) (E3 ubiquitin-protein ligase Pirh2) (RING finger protein 199) (RING-type E3 ubiquitin transferase RCHY1) (Zinc finger protein 363) (p53-induced RING-H2 protein) (hPirh2)
[hrd1 SPBC17D11.02c] ERAD-associated E3 ubiquitin-protein ligase hrd1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase hrd1)
[Ubr3 Kiaa2024 Zfp650 Znf650] E3 ubiquitin-protein ligase UBR3 (EC 2.3.2.27) (N-recognin-3) (RING-type E3 ubiquitin transferase UBR3) (Ubiquitin-protein ligase E3-alpha-3) (Ubiquitin-protein ligase E3-alpha-III) (Zinc finger protein 650)
[Pias1 Ddxbp1] E3 SUMO-protein ligase PIAS1 (EC 2.3.2.27) (DEAD/H box-binding protein 1) (Protein inhibitor of activated STAT protein 1) (RING-type E3 ubiquitin transferase PIAS1)
[Trim8 Gerp Rnf27] E3 ubiquitin-protein ligase TRIM8 (EC 2.3.2.27) (Glioblastoma-expressed RING finger protein) (RING finger protein 27) (RING-type E3 ubiquitin transferase TRIM8) (Tripartite motif-containing protein 8)
[RNF2 BAP1 DING HIPI3 RING1B] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (Huntingtin-interacting protein 2-interacting protein 3) (HIP2-interacting protein 3) (Protein DinG) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING finger protein BAP-1) (RING-type E3 ubiquitin transferase RING2)
[Rnf40 Bre1b Kiaa0661] E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B)
[Mid1 Fxy Trim18] E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[SH3RF2 POSH3 POSHER PPP1R39 RNF158] E3 ubiquitin-protein ligase SH3RF2 (EC 2.3.2.27) (Heart protein phosphatase 1-binding protein) (HEPP1) (POSH-eliminating RING protein) (Protein phosphatase 1 regulatory subunit 39) (RING finger protein 158) (RING-type E3 ubiquitin transferase SH3RF2) (SH3 domain-containing RING finger protein 2)
[Rnf128 Grail Greul1 MNCb-3816] E3 ubiquitin-protein ligase RNF128 (EC 2.3.2.27) (Gene related to anergy in lymphocytes protein) (Goliath-related E3 ubiquitin-protein ligase 1) (RING finger protein 128) (RING-type E3 ubiquitin transferase RNF128)

Bibliography :