RBX1_MOUSE
ID RBX1_MOUSE Reviewed; 108 AA.
AC P62878; Q8N6Z8; Q9D1S2; Q9WUK9; Q9Y254;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase RBX1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P62877};
DE EC=2.3.2.32 {ECO:0000250|UniProtKB:P62877};
DE AltName: Full=E3 ubiquitin-protein transferase RBX1 {ECO:0000305};
DE AltName: Full=RING finger protein 75;
DE AltName: Full=RING-box protein 1;
DE Short=Rbx1;
DE Contains:
DE RecName: Full=E3 ubiquitin-protein ligase RBX1, N-terminally processed;
GN Name=Rbx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN CBC(VHL) COMPLEX.
RX PubMed=10213691; DOI=10.1126/science.284.5414.657;
RA Kamura T., Koepp D.M., Conrad M.N., Skowyra D., Moreland R.J.,
RA Iliopoulos O., Lane W.S., Kaelin W.G. Jr., Elledge S.J., Conaway R.C.,
RA Harper J.W., Conaway J.W.;
RT "Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin
RT ligase.";
RL Science 284:657-661(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10643962;
RA Perin J.-P., Seddiqi N., Charbonnier F., Goudou D., Belkadi L., Rieger F.,
RA Alliel P.M.;
RT "Genomic organization and expression of the ubiquitin-proteasome complex-
RT associated protein Rbx1/ROC1/Hrt1.";
RL Cell. Mol. Biol. 45:1131-1137(1999).
RN [5]
RP IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEX WITH MUF1, AND IDENTIFICATION
RP IN COMPLEXES WITH CUL5.
RX PubMed=11384984; DOI=10.1074/jbc.m103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12140560; DOI=10.1038/nature00890;
RA Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y.,
RA Matsuoka K., Yoshida M., Tanaka K., Tai T.;
RT "E3 ubiquitin ligase that recognizes sugar chains.";
RL Nature 418:438-442(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 12-108 IN COMPLEXES WITH ZINC;
RP DDB1; CUL4B; CAND1 AND DAMAGED DNA, SUBUNIT, AND FUNCTION.
RX PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
RA Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M.,
RA Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H.,
RA Sugasawa K., Thoma N.H.;
RT "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
RT targeting, and activation.";
RL Cell 147:1024-1039(2011).
CC -!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-based
CC E3 ubiquitin-protein ligase (CRLs) complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, including proteins involved in cell cycle progression, signal
CC transduction, transcription and transcription-coupled nucleotide
CC excision repair (PubMed:22118460). CRLs complexes and ARIH1 collaborate
CC in tandem to mediate ubiquitination of target proteins, ARIH1 mediating
CC addition of the first ubiquitin on CRLs targets (By similarity). The
CC functional specificity of the E3 ubiquitin-protein ligase complexes
CC depends on the variable substrate recognition components (By
CC similarity). As a component of the CSA complex promotes the
CC ubiquitination of ERCC6 resulting in proteasomal degradation (By
CC similarity). Through the RING-type zinc finger, seems to recruit the E2
CC ubiquitination enzyme, like CDC34, to the complex and brings it into
CC close proximity to the substrate (By similarity). Probably also
CC stimulates CDC34 autoubiquitination (By similarity). May be required
CC for histone H3 and histone H4 ubiquitination in response to ultraviolet
CC and for subsequent DNA repair (By similarity). Promotes the neddylation
CC of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M (By
CC similarity). Involved in the ubiquitination of KEAP1, ENC1 and KLHL41
CC (By similarity). In concert with ATF2 and CUL3, promotes degradation of
CC KAT5 thereby attenuating its ability to acetylate and activate ATM (By
CC similarity). {ECO:0000250|UniProtKB:P62877,
CC ECO:0000269|PubMed:22118460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:P62877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine
CC + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine +
CC N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32;
CC Evidence={ECO:0000250|UniProtKB:P62877};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P62877}.
CC -!- SUBUNIT: Interacts with COPS6. Component of the DCX DET1-COP1 ubiquitin
CC ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1.
CC Part of an E3 ligase complex composed of RBX1, DDB1, DDB2 and CUL4A or
CC CUL4B (PubMed:22118460). Interacts with CAND1 (PubMed:22118460).
CC Interacts with UBE2M (By similarity). Part of a SCF complex consisting
CC of CUL1, RBX1, SKP1 and SKP2. Part of a SCF-like complex consisting of
CC CUL7, RBX1, SKP1 and FBXW8. Part of CBC(VHL) complexes with elongin BC
CC complex (ELOB and ELOC), CUL2 or CUL5 and VHL. Part of the CSA complex
CC (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex
CC containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with
CC RNA polymerase II; upon UV irradiation it interacts with the COP9
CC signalosome and preferentially with the hyperphosphorylated form of RNA
CC polymerase II (By similarity). Part of multisubunit E3 ubiquitin ligase
CC complexes with elongin BC complex (ELOB and ELOC), CUL2 and MED8;
CC elongin BC complex (ELOB and ELOC), CUL5 and MUF1. Part of multisubunit
CC complexes with elongin BC complex (ELOB and ELOC), elongin A/ELOA or
CC SOCS1 or WSB1 and CUL5. Interacts directly with CUL1 and probably also
CC with CUL2, CUL3, CUL4A, CUL4B, CUL5 and CUL7. Interacts with CDC34.
CC Interacts with GLMN. GLMN competes for the binding site of the E2
CC ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding. Part of
CC a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Part of a SCF
CC complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex
CC interacts with PML via FBXO3. Component of the SCF(Cyclin F) complex
CC consisting of CUL1, RBX1, SKP1 and CCNF. Identified in a SCF (SKP1-
CC CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and
CC CDC34 (By similarity). Component of multiple BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable
CC BTB domain-containing protein. Part of the BCR(ENC1) complex containing
CC ENC1. Part of the BCR(GAN) complex containing GAN. Part of the
CC BCR(KLHL41) complex containing KLHL41. Part of the BCR(KEAP1) complex
CC containing KEAP1 (By similarity). Interacts with SESN1 and SESN2 (By
CC similarity). Interacts with NOTCH2 (By similarity). Component of the
CC BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3,
CC KLHL22 and RBX1 (By similarity). Interacts with DCUN1D1, DCUN1D2,
CC DCUN1D3, DCUN1D4 and DCUN1D5 (By similarity). Component of a BCR3 (BTB-
CC CUL3-RBX1) E3 ubiquitin ligase complex, also named Cul3-RING ubiquitin
CC ligase complex CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and
CC KBTBD7 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P62877,
CC ECO:0000269|PubMed:22118460}.
CC -!- INTERACTION:
CC P62878; P58004: SESN2; Xeno; NbExp=3; IntAct=EBI-2507414, EBI-3939642;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62877}. Nucleus
CC {ECO:0000250|UniProtKB:P62877}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10643962}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity (By similarity). It coordinates an additional third
CC zinc ion (PubMed:22118460). {ECO:0000250|UniProtKB:P62877,
CC ECO:0000269|PubMed:22118460}.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
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DR EMBL; AF140599; AAD29716.1; -; mRNA.
DR EMBL; AK003159; BAB22612.1; -; mRNA.
DR EMBL; BC027396; AAH27396.1; -; mRNA.
DR EMBL; BC051473; AAH51473.1; -; mRNA.
DR EMBL; BC056992; AAH56992.1; -; mRNA.
DR CCDS; CCDS49676.1; -.
DR RefSeq; NP_062686.1; NM_019712.3.
DR PDB; 4A0C; X-ray; 3.80 A; D/F=12-108.
DR PDB; 4A0K; X-ray; 5.93 A; B=12-108.
DR PDB; 4A0L; X-ray; 7.40 A; F/I=12-108.
DR PDB; 7OPC; EM; 3.00 A; f=1-108.
DR PDB; 7OPD; EM; 3.00 A; f=1-108.
DR PDBsum; 4A0C; -.
DR PDBsum; 4A0K; -.
DR PDBsum; 4A0L; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; P62878; -.
DR SMR; P62878; -.
DR BioGRID; 207980; 65.
DR ComplexPortal; CPX-650; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant.
DR ComplexPortal; CPX-651; CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant.
DR CORUM; P62878; -.
DR IntAct; P62878; 12.
DR MINT; P62878; -.
DR STRING; 10090.ENSMUSP00000023036; -.
DR iPTMnet; P62878; -.
DR PhosphoSitePlus; P62878; -.
DR EPD; P62878; -.
DR MaxQB; P62878; -.
DR PaxDb; P62878; -.
DR PeptideAtlas; P62878; -.
DR PRIDE; P62878; -.
DR ProteomicsDB; 255051; -.
DR Antibodypedia; 295; 353 antibodies from 40 providers.
DR DNASU; 56438; -.
DR Ensembl; ENSMUST00000023036; ENSMUSP00000023036; ENSMUSG00000022400.
DR GeneID; 56438; -.
DR KEGG; mmu:56438; -.
DR UCSC; uc007wwq.1; mouse.
DR CTD; 9978; -.
DR MGI; MGI:1891829; Rbx1.
DR VEuPathDB; HostDB:ENSMUSG00000022400; -.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000155618; -.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; P62878; -.
DR OMA; RFDVKKW; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; P62878; -.
DR TreeFam; TF105503; -.
DR BioCyc; MetaCyc:ENSG00000100387-MON; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56438; 30 hits in 111 CRISPR screens.
DR ChiTaRS; Rbx1; mouse.
DR PRO; PR:P62878; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P62878; protein.
DR Bgee; ENSMUSG00000022400; Expressed in yolk sac and 266 other tissues.
DR ExpressionAtlas; P62878; baseline and differential.
DR Genevisible; P62878; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; TAS:UniProtKB.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
DR GO; GO:0030891; C:VCB complex; ISO:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; TAS:UniProtKB.
DR GO; GO:0061663; F:NEDD8 ligase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0034644; P:cellular response to UV; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:MGI.
DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
DR GO; GO:0045116; P:protein neddylation; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID50217; -.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; DNA damage; DNA repair;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..108
FT /note="E3 ubiquitin-protein ligase RBX1"
FT /id="PRO_0000423265"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62877"
FT CHAIN 2..108
FT /note="E3 ubiquitin-protein ligase RBX1, N-terminally
FT processed"
FT /id="PRO_0000056014"
FT ZN_FING 53..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22118460"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22118460"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62877"
FT MOD_RES 2
FT /note="N-acetylalanine; in E3 ubiquitin-protein ligase
FT RBX1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P62877"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62877"
FT CONFLICT 42
FT /note="C -> F (in Ref. 2; BAB22612)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7OPC"
SQ SEQUENCE 108 AA; 12274 MW; 30FC5ADF66096C0E CRC64;
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
