GenomeNet

Database: UniProt
Entry: P62878
LinkDB: P62878
Original site: P62878 
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   07-APR-2021, entry version 153.
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). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P62877, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; 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   PDBsum; 4A0C; -.
DR   PDBsum; 4A0K; -.
DR   PDBsum; 4A0L; -.
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; 341 antibodies.
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   eggNOG; KOG2930; Eukaryota.
DR   GeneTree; ENSGT00940000155618; -.
DR   HOGENOM; CLU_115512_2_1_1; -.
DR   InParanoid; P62878; -.
DR   OMA; IDKENCT; -.
DR   OrthoDB; 1587140at2759; -.
DR   PhylomeDB; P62878; -.
DR   TreeFam; TF105503; -.
DR   BioCyc; MetaCyc:ENSG00000100387-MONOMER; -.
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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 56438; 23 hits in 54 CRISPR screens.
DR   ChiTaRS; Rbx1; mouse.
DR   PRO; PR:P62878; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P62878; protein.
DR   Bgee; ENSMUSG00000022400; Expressed in dentate gyrus of hippocampal formation and 314 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; IEA:Ensembl.
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; IEA:Ensembl.
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; TAS:Reactome.
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:0008134; F:transcription factor binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:1902499; P:positive regulation of protein autoubiquitination; IEA:Ensembl.
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: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   METAL           42
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           45
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           53
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           56
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           68
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           75
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           77
FT                   /note="Zinc 3; via pros nitrogen"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           80
FT                   /note="Zinc 1; via pros nitrogen"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           82
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           94
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000269|PubMed:22118460"
FT   METAL           97
FT                   /note="Zinc 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"
SQ   SEQUENCE   108 AA;  12274 MW;  30FC5ADF66096C0E CRC64;
     MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
     ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
//
DBGET integrated database retrieval system