RBX1_YEAST
ID RBX1_YEAST Reviewed; 121 AA.
AC Q08273; D6W1T5;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=RING-box protein HRT1;
DE Short=RING-box protein 1;
DE AltName: Full=E3 ubiquitin-protein ligase complex SCF subunit HRT1;
DE AltName: Full=High level expression reduces Ty3 transposition protein 1;
DE AltName: Full=Regulator of cullins protein 1;
GN Name=HRT1; Synonyms=RBX1, ROC1; OrderedLocusNames=YOL133W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896270;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1053::aid-yea993>3.0.co;2-s;
RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast
RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene
RT for a possible glycophospholipid-anchored surface protein and six other
RT open reading frames.";
RL Yeast 12:1053-1058(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 8-31, FUNCTION, INTERACTION WITH CDC53; CDC4 AND
RP CDC34/UBC3, AND IDENTIFICATION IN SCF COMPLEX.
RX PubMed=10385629; DOI=10.1101/gad.13.12.1614;
RA Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C.,
RA Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K.,
RA Shevchenko A., Deshaies R.J.;
RT "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a
RT ubiquitin ligase module that activates the E2 enzyme Cdc34.";
RL Genes Dev. 13:1614-1626(1999).
RN [5]
RP FUNCTION.
RX PubMed=10579999; DOI=10.1101/gad.13.22.2928;
RA Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.;
RT "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1
RT modification of cullins Cdc53 and Cul2.";
RL Genes Dev. 13:2928-2933(1999).
RN [6]
RP INTERACTION WITH CDC53; CUL3 AND RTT101.
RX PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with an
RT associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH CDC53 AND CDC4.
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 [8]
RP IDENTIFICATION IN SCF COMPLEX, INTERACTION WITH CDC34/UBC3 AND CDC4, AND
RP MUTANT RBX1-1.
RX PubMed=10213692; DOI=10.1126/science.284.5414.662;
RA Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W.,
RA Elledge S.J., Harper J.W.;
RT "Reconstitution of G1 cyclin ubiquitination with complexes containing
RT SCFGrr1 and Rbx1.";
RL Science 284:662-665(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTANT HRT1-C81Y.
RX PubMed=10880467; DOI=10.1093/genetics/155.3.1033;
RA Blondel M., Galan J.-M., Peter M.;
RT "Isolation and characterization of HRT1 using a genetic screen for mutants
RT unable to degrade Gic2p in Saccharomyces cerevisiae.";
RL Genetics 155:1033-1044(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH CUL3 AND RTT101.
RX PubMed=12676951; DOI=10.1074/jbc.m210358200;
RA Michel J.J., McCarville J.F., Xiong Y.;
RT "A role for Saccharomyces cerevisiae Cul8 ubiquitin ligase in proper
RT anaphase progression.";
RL J. Biol. Chem. 278:22828-22837(2003).
RN [11]
RP FUNCTION.
RX PubMed=17296727; DOI=10.1128/mcb.00091-07;
RA Ribar B., Prakash L., Prakash S.;
RT "ELA1 and CUL3 are required along with ELC1 for RNA polymerase II
RT polyubiquitylation and degradation in DNA-damaged yeast cells.";
RL Mol. Cell. Biol. 27:3211-3216(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-
CC protein ligase complexes (CRLs), which mediate the ubiquitination of
CC target proteins. Recruits the E2 ubiquitin-conjugating enzyme
CC CDC34/UBC3 to the complex and brings it into close proximity to the
CC substrate. Also stimulates CDC34/UBC3 autoubiquitination and promotes
CC the neddylation of CDC53 and RTT101. Component of the SCF(CDC4)
CC ubiquitin ligase required for ubiquitination of the cyclin-dependent
CC kinase inhibitor SIC1 and for the G1-to-S phase transition. Component
CC of the RTT101(MMS1-MMS22) ubiquitin ligase that promotes fork
CC progression through damaged DNA or natural pause sites. Component of
CC the CRL3(ELA1) ubiquitin ligase required for ubiquitination of RPB1,
CC the largest subunit of RNA polymerase II (Pol II), which targets Pol II
CC for proteasomal degradation in DNA-damaged cells.
CC {ECO:0000269|PubMed:10213691, ECO:0000269|PubMed:10385629,
CC ECO:0000269|PubMed:10579999, ECO:0000269|PubMed:12676951,
CC ECO:0000269|PubMed:17296727}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple cullin-RING ligases (CRLs) composed of 4
CC subunits: the RING protein HRT1, a cullin, a linker protein, and one of
CC many alternative substrate receptors. Component of SCF E3 ubiquitin
CC ligase complexes containing the cullin CDC53, the linker protein
CC SKP1/CBF3D, and substrate receptors containing F-box motifs like DAS1
CC or GRR1. Component of RTT101(MMS1) E3 ubiquitin ligase complexes
CC containing the cullin RTT101, the linker protein MMS1, and substrate
CC receptors belonging to a protein family described as DCAF (DDB1- and
CC CUL4-associated factor) like MMS22. Component of CRL3 E3 ubiquitin
CC ligase complexes containing the cullin CUL3, the linker protein ELC1,
CC and substrate receptors containing SOCS-box motifs like ELA1. Interacts
CC with CDC53, CUL3, RTT101, CDC4 and CDC34/UBC3.
CC {ECO:0000269|PubMed:10213691, ECO:0000269|PubMed:10213692,
CC ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10385629,
CC ECO:0000269|PubMed:12676951}.
CC -!- INTERACTION:
CC Q08273; P07834: CDC4; NbExp=3; IntAct=EBI-31686, EBI-4434;
CC Q08273; Q12018: CDC53; NbExp=9; IntAct=EBI-31686, EBI-4321;
CC Q08273; Q06211: MMS1; NbExp=3; IntAct=EBI-31686, EBI-38894;
CC Q08273; P47050: RTT101; NbExp=3; IntAct=EBI-31686, EBI-25861;
CC Q08273; P38352: SAF1; NbExp=2; IntAct=EBI-31686, EBI-21172;
CC Q08273; P14680: YAK1; NbExp=3; IntAct=EBI-31686, EBI-20777;
CC Q08273; P53169: YBP2; NbExp=3; IntAct=EBI-31686, EBI-23796;
CC Q08273; P40560: YIL001W; NbExp=4; IntAct=EBI-31686, EBI-24911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880467}. Nucleus
CC {ECO:0000269|PubMed:10880467}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X95465; CAA64737.1; -; Genomic_DNA.
DR EMBL; Z74876; CAA99155.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10651.1; -; Genomic_DNA.
DR PIR; S66830; S66830.
DR RefSeq; NP_014508.1; NM_001183387.1.
DR AlphaFoldDB; Q08273; -.
DR SMR; Q08273; -.
DR BioGRID; 34242; 96.
DR ComplexPortal; CPX-1157; CUL8-MMS1-MMS22-ESC4 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1165; CUL8-MMS1-MMS22-CTF4 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1166; CUL8-MMS1-ESC2 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1167; CUL8-MMS1-ORC5 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1837; CUL3-HRT1/ELC1/ELA1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3234; SCF-Cdc4 ubiquitin ligase complex.
DR ComplexPortal; CPX-3241; SCF-Grr1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3242; SCF-Mdm30 ubiquitin ligase complex.
DR ComplexPortal; CPX-3243; SCF-Ufo1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3244; SCF-Das1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3249; SCF-Met30 ubiquitin ligase complex.
DR ComplexPortal; CPX-3250; SCF-Dia2 ubiquitin ligase complex.
DR ComplexPortal; CPX-3253; SCF-Ylr352w ubiquitin ligase complex.
DR ComplexPortal; CPX-3254; SCF-Saf1 ubiquitin ligase complex.
DR ComplexPortal; CPX-3255; SCF-Hrt3 ubiquitin ligase complex.
DR ComplexPortal; CPX-3681; SCF-Ydr131c ubiquitin ligase complex.
DR DIP; DIP-1373N; -.
DR IntAct; Q08273; 160.
DR MINT; Q08273; -.
DR STRING; 4932.YOL133W; -.
DR iPTMnet; Q08273; -.
DR MaxQB; Q08273; -.
DR PaxDb; Q08273; -.
DR PRIDE; Q08273; -.
DR EnsemblFungi; YOL133W_mRNA; YOL133W; YOL133W.
DR GeneID; 853986; -.
DR KEGG; sce:YOL133W; -.
DR SGD; S000005493; HRT1.
DR VEuPathDB; FungiDB:YOL133W; -.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000168153; -.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; Q08273; -.
DR OMA; GHEYHTH; -.
DR BioCyc; YEAST:G3O-33528-MON; -.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q08273; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08273; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071406; P:cellular response to methylmercury; IC:ComplexPortal.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0008053; P:mitochondrial fusion; IC:ComplexPortal.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006289; P:nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IC:ComplexPortal.
DR GO; GO:0019222; P:regulation of metabolic process; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IC:ComplexPortal.
DR GO; GO:0000409; P:regulation of transcription by galactose; IC:ComplexPortal.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:SGD.
DR Gene3D; 3.30.40.10; -; 1.
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 Cell cycle; Cell division; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..121
FT /note="RING-box protein HRT1"
FT /id="PRO_0000056022"
FT ZN_FING 55..111
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 72
FT /note="K->R: In RBX1-1; temperature-sensitive allele. At 38
FT degrees Celsius induces defects in ubiquitin ligase
FT activity; when associated with R-81."
FT MUTAGEN 81
FT /note="C->R: In RBX1-1; temperature-sensitive allele. At 38
FT degrees Celsius induces defects in ubiquitin ligase
FT activity; when associated with R-72."
FT MUTAGEN 81
FT /note="C->Y: In HRT1-C81Y; defects in ubiquitin ligase
FT activity."
SQ SEQUENCE 121 AA; 13940 MW; A9C3193E48CAF881 CRC64;
MSNEVDRMDV DEDESQNIAQ SSNQSAPVET KKKRFEIKKW TAVAFWSWDI AVDNCAICRN
HIMEPCIECQ PKAMTDTDNE CVAAWGVCNH AFHLHCINKW IKTRDACPLD NQPWQLARCG
R
