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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)DescriptionActionsGraphical viewLength
Metal bindingi55Zinc 1By similarity1
Metal bindingi58Zinc 1By similarity1
Metal bindingi66Zinc 2By similarity1
Metal bindingi69Zinc 2By similarity1
Metal bindingi81Zinc 2By similarity1
Metal bindingi88Zinc 3By similarity1
Metal bindingi90Zinc 3; via pros nitrogenBy similarity1
Metal bindingi93Zinc 1; via pros nitrogenBy similarity1
Metal bindingi95Zinc 2By similarity1
Metal bindingi107Zinc 3By similarity1
Metal bindingi110Zinc 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri55 – 111RING-typePROSITE-ProRule annotationAdd BLAST57

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • G1/S transition of mitotic cell cycle Source: SGD
  • protein neddylation Source: GO_Central
  • 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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
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

  • Cul2-RING ubiquitin ligase complex Source: GO_Central
  • Cul3-RING ubiquitin ligase complex Source: SGD
  • Cul4-RING E3 ubiquitin ligase complex Source: GO_Central
  • Cul7-RING ubiquitin ligase complex Source: GO_Central
  • Cul8-RING ubiquitin ligase complex Source: SGD
  • cytoplasm Source: SGD
  • nuclear SCF ubiquitin ligase complex Source: GO_Central
  • nucleus Source: SGD
  • SCF ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72K → R in RBX1-1; temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity; when associated with R-81. 1
Mutagenesisi81C → R in RBX1-1; temperature-sensitive allele. At 38 degrees Celsius induces defects in ubiquitin ligase activity; when associated with R-72. 1
Mutagenesisi81C → Y in HRT1-C81Y; defects in ubiquitin ligase activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560221 – 121RING-box protein HRT1Add BLAST121

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08273.
PRIDEiQ08273.

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

  • cullin family protein binding Source: GO_Central
  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi34242. 88 interactors.
DIPiDIP-1373N.
IntActiQ08273. 107 interactors.
MINTiMINT-401535.

Structurei

3D structure databases

ProteinModelPortaliQ08273.
SMRiQ08273.
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)DescriptionActionsGraphical viewLength
Zinc fingeri55 – 111RING-typePROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000017058.
HOGENOMiHOG000171951.
InParanoidiQ08273.
KOiK03868.
OMAiTVAWEDD.
OrthoDBiEOG092C4PUH.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34242. 88 interactors.
DIPiDIP-1373N.
IntActiQ08273. 107 interactors.
MINTiMINT-401535.

PTM databases

iPTMnetiQ08273.

Proteomic databases

MaxQBiQ08273.
PRIDEiQ08273.

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.
OMAiTVAWEDD.
OrthoDBiEOG092C4PUH.

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-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
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...

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: November 30, 2016
This is version 146 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.