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E3 ubiquitin-protein ligase RBX1 (EC 6.3.2.-) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1) [Cleaved into: E3 ubiquitin-protein ligase 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.
22-NOV-2017, entry version 154.
RecName: Full=E3 ubiquitin-protein ligase RBX1;
EC=6.3.2.-;
AltName: Full=Protein ZYP;
AltName: Full=RING finger protein 75;
AltName: Full=RING-box protein 1;
Short=Rbx1;
AltName: Full=Regulator of cullins 1;
Contains:
RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
Name=RBX1; Synonyms=RNF75, ROC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CULLINS, 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, AND SUBCELLULAR LOCATION.
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.
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]
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).
[37]
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).
[38]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-108 IN COMPLEX WITH 17-776
OF CUL1, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH
CUL1; SKP1 AND SKP2.
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).
-!- 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. 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. Through the RING-type zinc finger, seems
to recruit the E2 ubiquitination enzyme, like 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:10579999, ECO:0000269|PubMed:11027288,
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:27565346}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a SCF complex consisting of CUL1, RBX1, SKP1 and
SKP2. 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. Probably interacts with CDC34. 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. Interacts
with human adenovirus 5 E1A protein; this interaction inhibits
RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the
SCF(FBW7) complex (PubMed:19679664). 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
DCUN1D3. Interacts with SESN1 and SESN2 (PubMed:23274085).
{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:19679664,
ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:23274085,
ECO:0000269|PubMed:25349211}.
-!- INTERACTION:
Q13616:CUL1; NbExp=24; IntAct=EBI-398523, EBI-359390;
Q13617:CUL2; NbExp=7; IntAct=EBI-398523, EBI-456179;
Q13620:CUL4B; NbExp=5; IntAct=EBI-398523, EBI-456067;
Q93034:CUL5; NbExp=3; IntAct=EBI-398523, EBI-1057139;
P59991:KRTAP12-2; NbExp=4; IntAct=EBI-398523, EBI-10176379;
Q13309:SKP2; NbExp=3; IntAct=EBI-398523, EBI-456291;
P61081:UBE2M; NbExp=4; 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. It coordinates an additional third zinc
ion.
-!- 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";
-----------------------------------------------------------------------
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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.
UniGene; Hs.474949; -.
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.
PDBsum; 1LDJ; -.
PDBsum; 1LDK; -.
PDBsum; 1U6G; -.
PDBsum; 2HYE; -.
PDBsum; 2LGV; -.
PDBsum; 3DPL; -.
PDBsum; 3DQV; -.
PDBsum; 3RTR; -.
PDBsum; 4F52; -.
PDBsum; 4P5O; -.
PDBsum; 5N4W; -.
ProteinModelPortal; P62877; -.
SMR; P62877; -.
BioGrid; 115301; 183.
CORUM; P62877; -.
DIP; DIP-17014N; -.
IntAct; P62877; 74.
MINT; MINT-235894; -.
STRING; 9606.ENSP00000216225; -.
ChEMBL; CHEMBL3833061; -.
iPTMnet; P62877; -.
PhosphoSitePlus; P62877; -.
BioMuta; RBX1; -.
DMDM; 51338609; -.
EPD; P62877; -.
MaxQB; P62877; -.
PaxDb; P62877; -.
PeptideAtlas; P62877; -.
PRIDE; P62877; -.
TopDownProteomics; P62877; -.
DNASU; 9978; -.
Ensembl; ENST00000216225; ENSP00000216225; ENSG00000100387.
GeneID; 9978; -.
KEGG; hsa:9978; -.
UCSC; uc003azk.4; human.
CTD; 9978; -.
DisGeNET; 9978; -.
EuPathDB; HostDB:ENSG00000100387.8; -.
GeneCards; RBX1; -.
H-InvDB; HIX0016509; -.
HGNC; HGNC:9928; RBX1.
HPA; HPA003038; -.
MIM; 603814; gene.
neXtProt; NX_P62877; -.
OpenTargets; ENSG00000100387; -.
PharmGKB; PA34299; -.
eggNOG; KOG2930; Eukaryota.
eggNOG; COG5194; LUCA.
GeneTree; ENSGT00390000017058; -.
HOGENOM; HOG000171951; -.
HOVERGEN; HBG001507; -.
InParanoid; P62877; -.
KO; K03868; -.
OMA; KWTAVAF; -.
OrthoDB; EOG091G0TA5; -.
PhylomeDB; P62877; -.
TreeFam; TF105503; -.
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-446652; Interleukin-1 family signaling.
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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P62877; -.
SIGNOR; P62877; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; P62877; -.
GeneWiki; RBX1; -.
GenomeRNAi; 9978; -.
PRO; PR:P62877; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100387; -.
CleanEx; HS_RBX1; -.
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:0043224; C:nuclear SCF ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0019788; F:NEDD8 transferase activity; IDA:UniProtKB.
GO; GO:0032403; F:protein 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:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
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: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:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
Gene3D; 3.30.40.10; -; 1.
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; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair;
Host-virus interaction; Ligase; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 108 E3 ubiquitin-protein ligase RBX1.
/FTId=PRO_0000423264.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 108 E3 ubiquitin-protein ligase RBX1, N-
terminally processed.
/FTId=PRO_0000056013.
ZN_FING 53 98 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
METAL 42 42 Zinc 1. {ECO:0000269|PubMed:11961546}.
METAL 45 45 Zinc 1. {ECO:0000269|PubMed:11961546}.
METAL 53 53 Zinc 2. {ECO:0000269|PubMed:11961546}.
METAL 56 56 Zinc 2. {ECO:0000269|PubMed:11961546}.
METAL 68 68 Zinc 2. {ECO:0000269|PubMed:11961546}.
METAL 75 75 Zinc 3. {ECO:0000269|PubMed:11961546}.
METAL 77 77 Zinc 3; via pros nitrogen.
{ECO:0000269|PubMed:11961546}.
METAL 80 80 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:11961546}.
METAL 82 82 Zinc 2. {ECO:0000269|PubMed:11961546}.
METAL 83 83 Zinc 1. {ECO:0000269|PubMed:11961546}.
METAL 94 94 Zinc 3. {ECO:0000269|PubMed:11961546}.
METAL 97 97 Zinc 3. {ECO:0000269|PubMed:11961546}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2 2 N-acetylalanine; in E3 ubiquitin-protein
ligase RBX1, N-terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MUTAGEN 53 53 C->A: Strong reduction in ligase
activity; when associated with A-56.
{ECO:0000269|PubMed:10230407}.
MUTAGEN 56 56 C->A: Strong reduction in ligase
activity; when associated with A-53.
{ECO:0000269|PubMed:10230407}.
MUTAGEN 75 75 C->A: Strong reduction in ligase
activity; when associated with A-77.
{ECO:0000269|PubMed:10230407}.
MUTAGEN 77 77 H->A: Strong reduction in ligase
activity; when associated with A-75.
{ECO:0000269|PubMed:10230407}.
CONFLICT 18 18 G -> S (in Ref. 9; AAM21718).
{ECO:0000305}.
STRAND 21 37 {ECO:0000244|PDB:3DPL}.
STRAND 39 41 {ECO:0000244|PDB:1LDJ}.
STRAND 43 45 {ECO:0000244|PDB:3DPL}.
TURN 49 54 {ECO:0000244|PDB:1LDJ}.
HELIX 56 59 {ECO:0000244|PDB:3DPL}.
TURN 63 67 {ECO:0000244|PDB:1LDJ}.
STRAND 70 73 {ECO:0000244|PDB:3DPL}.
STRAND 74 76 {ECO:0000244|PDB:1LDJ}.
STRAND 78 80 {ECO:0000244|PDB:3DPL}.
HELIX 81 88 {ECO:0000244|PDB:3DPL}.
STRAND 90 93 {ECO:0000244|PDB:1LDK}.
STRAND 95 97 {ECO:0000244|PDB:3DPL}.
STRAND 103 105 {ECO:0000244|PDB:3DPL}.
SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH


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EIAAB38244 E3 ubiquitin-protein ligase SH3RF1,Homo sapiens,Human,KIAA1494,Plenty of SH3s,POSH,Protein POSH,RING finger protein 142,RNF142,SH3 domain-containing RING finger protein 1,SH3 multiple domains protein
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
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
EIAAB35482 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Gametogenesis-expressed protein GEG-154,Geg-154,Mouse,Mus musculus,RING finger protein 19A,Rnf19,Rnf19a,UBCM4-interacting protein 1
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


 

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