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Protein

RING-box protein HRT1

Gene

HRT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. Recruits the E2 ubiquitin-conjugating enzyme CDC34/UBC3 to the complex and brings it into close proximity to the substrate. Also stimulates CDC34/UBC3 autoubiquitination and promotes the neddylation of CDC53 and RTT101. Component of the SCF(CDC4) ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor SIC1 and for the G1-to-S phase transition. Component of the RTT101(MMS1-MMS22) ubiquitin ligase that promotes fork progression through damaged DNA or natural pause sites. Component of the CRL3(ELA1) ubiquitin ligase required for ubiquitinaton of RPB1, the largest subunit of RNA polymerase II (Pol II), which targets Pol II for proteasomal degradation in DNA-damaged cells.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Zinc 1By similarity
Metal bindingi58 – 581Zinc 1By similarity
Metal bindingi66 – 661Zinc 2By similarity
Metal bindingi69 – 691Zinc 2By similarity
Metal bindingi81 – 811Zinc 2By similarity
Metal bindingi88 – 881Zinc 3By similarity
Metal bindingi90 – 901Zinc 3; via pros nitrogenBy similarity
Metal bindingi93 – 931Zinc 1; via pros nitrogenBy similarity
Metal bindingi95 – 951Zinc 2By similarity
Metal bindingi107 – 1071Zinc 3By similarity
Metal bindingi110 – 1101Zinc 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri55 – 11157RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • protein binding, bridging Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: SGD
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33528-MONOMER.
ReactomeiR-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SCE-5696394. DNA Damage Recognition in GG-NER.
R-SCE-5696395. Formation of Incision Complex in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
RING-box protein HRT1
Short name:
RING-box protein 1
Alternative name(s):
E3 ubiquitin-protein ligase complex SCF subunit HRT1
High level expression reduces Ty3 transposition protein 1
Regulator of cullins protein 1
Gene namesi
Name:HRT1
Synonyms:RBX1, ROC1
Ordered Locus Names:YOL133W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL133W.
SGDiS000005493. HRT1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: SGD
  • Cul8-RING ubiquitin ligase complex Source: SGD
  • cytoplasm Source: SGD
  • nucleus Source: SGD
  • SCF ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721K → R in RBX1-1; temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity; when associated with R-81.
Mutagenesisi81 – 811C → R in RBX1-1; temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity; when associated with R-72.
Mutagenesisi81 – 811C → Y in HRT1-C81Y; defects in ubiquitin ligase activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121RING-box protein HRT1PRO_0000056022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08273.
PeptideAtlasiQ08273.

PTM databases

iPTMnetiQ08273.

Interactioni

Subunit structurei

Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, a cullin, a linker protein, and one of many alternative substrate receptors. Component of SCF E3 ubiquitin ligase complexes containing the cullin CDC53, the linker protein SKP1/CBF3D, and substrate receptors containing F-box motifs like DAS1 or GRR1. Component of RTT101(MMS1) E3 ubiquitin ligase complexes containing the cullin RTT101, the linker protein MMS1, and substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor) like MMS22. Component of CRL3 E3 ubiquitin ligase complexes containing the cullin CUL3, the linker protein ELC1, and substrate receptors containing SOCS-box motifs like ELA1. Interacts with CDC53, CUL3, RTT101, CDC4 and CDC34/UBC3.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC4P078343EBI-31686,EBI-4434
CDC53Q120188EBI-31686,EBI-4321
SAF1P383522EBI-31686,EBI-21172
YAK1P146803EBI-31686,EBI-20777
YBP2P531693EBI-31686,EBI-23796
YIL001WP405604EBI-31686,EBI-24911

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi34242. 87 interactions.
DIPiDIP-1373N.
IntActiQ08273. 107 interactions.
MINTiMINT-401535.

Structurei

3D structure databases

ProteinModelPortaliQ08273.
SMRiQ08273. Positions 33-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity.

Sequence similaritiesi

Belongs to the RING-box family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri55 – 11157RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000017058.
HOGENOMiHOG000171951.
InParanoidiQ08273.
KOiK03868.
OMAiGDTEMAT.
OrthoDBiEOG73Z363.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08273-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNEVDRMDV DEDESQNIAQ SSNQSAPVET KKKRFEIKKW TAVAFWSWDI
60 70 80 90 100
AVDNCAICRN HIMEPCIECQ PKAMTDTDNE CVAAWGVCNH AFHLHCINKW
110 120
IKTRDACPLD NQPWQLARCG R
Length:121
Mass (Da):13,940
Last modified:November 1, 1996 - v1
Checksum:iA9C3193E48CAF881
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64737.1.
Z74876 Genomic DNA. Translation: CAA99155.1.
BK006948 Genomic DNA. Translation: DAA10651.1.
PIRiS66830.
RefSeqiNP_014508.1. NM_001183387.1.

Genome annotation databases

EnsemblFungiiYOL133W; YOL133W; YOL133W.
GeneIDi853986.
KEGGisce:YOL133W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95465 Genomic DNA. Translation: CAA64737.1.
Z74876 Genomic DNA. Translation: CAA99155.1.
BK006948 Genomic DNA. Translation: DAA10651.1.
PIRiS66830.
RefSeqiNP_014508.1. NM_001183387.1.

3D structure databases

ProteinModelPortaliQ08273.
SMRiQ08273. Positions 33-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34242. 87 interactions.
DIPiDIP-1373N.
IntActiQ08273. 107 interactions.
MINTiMINT-401535.

PTM databases

iPTMnetiQ08273.

Proteomic databases

MaxQBiQ08273.
PeptideAtlasiQ08273.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL133W; YOL133W; YOL133W.
GeneIDi853986.
KEGGisce:YOL133W.

Organism-specific databases

EuPathDBiFungiDB:YOL133W.
SGDiS000005493. HRT1.

Phylogenomic databases

GeneTreeiENSGT00390000017058.
HOGENOMiHOG000171951.
InParanoidiQ08273.
KOiK03868.
OMAiGDTEMAT.
OrthoDBiEOG73Z363.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-33528-MONOMER.
ReactomeiR-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SCE-5696394. DNA Damage Recognition in GG-NER.
R-SCE-5696395. Formation of Incision Complex in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6781823. Formation of TC-NER Pre-Incision Complex.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ08273.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 12 801 bp fragment of the left arm of yeast chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene for a possible glycophospholipid-anchored surface protein and six other open reading frames."
    Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L., Arino J., Herrero E.
    Yeast 12:1053-1058(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34."
    Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C., Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K., Shevchenko A., Deshaies R.J.
    Genes Dev. 13:1614-1626(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-31, FUNCTION, INTERACTION WITH CDC53; CDC4 AND CDC34/UBC3, IDENTIFICATION IN SCF COMPLEX.
  5. "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2."
    Kamura T., Conrad M.N., Yan Q., Conaway R.C., Conaway J.W.
    Genes Dev. 13:2928-2933(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
    Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
    Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC53; CUL3 AND RTT101.
  7. Cited for: FUNCTION, INTERACTION WITH CDC53 AND CDC4.
  8. "Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1."
    Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W., Elledge S.J., Harper J.W.
    Science 284:662-665(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SCF COMPLEX, INTERACTION WITH CDC34/UBC3 AND CDC4, MUTANT RBX1-1.
  9. "Isolation and characterization of HRT1 using a genetic screen for mutants unable to degrade Gic2p in Saccharomyces cerevisiae."
    Blondel M., Galan J.-M., Peter M.
    Genetics 155:1033-1044(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTANT HRT1-C81Y.
  10. "A role for Saccharomyces cerevisiae Cul8 ubiquitin ligase in proper anaphase progression."
    Michel J.J., McCarville J.F., Xiong Y.
    J. Biol. Chem. 278:22828-22837(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL3 AND RTT101.
  11. "ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells."
    Ribar B., Prakash L., Prakash S.
    Mol. Cell. Biol. 27:3211-3216(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRBX1_YEAST
AccessioniPrimary (citable) accession number: Q08273
Secondary accession number(s): D6W1T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-8 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.