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UniProtKB - Q08109 (HRD1_YEAST)

Entry version 168 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

ERAD-associated E3 ubiquitin-protein ligase HRD1

Gene

HRD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M.

13 Publications

Miscellaneous

Present with 2660 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri349 – 400RING-type; atypicalPROSITE-ProRule annotationAdd BLAST52

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.2.27, 984

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ERAD-associated E3 ubiquitin-protein ligase HRD1 (EC:2.3.2.27)
Alternative name(s):
HMG-CoA reductase degradation protein 1
RING-type E3 ubiquitin transferase HRD1Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HRD1
Synonyms:DER3
Ordered Locus Names:YOL013C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005373, HRD1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YOL013C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 8Cytoplasmic8
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei9 – 29Helical; Name=1Add BLAST21
Topological domaini30 – 45LumenalAdd BLAST16
Transmembranei46 – 66Helical; Name=2Add BLAST21
Topological domaini67 – 82CytoplasmicAdd BLAST16
Transmembranei83 – 103Helical; Name=3Add BLAST21
Topological domaini104Lumenal1
Transmembranei105 – 125Helical; Name=4Add BLAST21
Topological domaini126 – 144CytoplasmicAdd BLAST19
Transmembranei145 – 165Helical; Name=5Add BLAST21
Topological domaini166 – 184LumenalAdd BLAST19
Transmembranei185 – 205Helical; Name=6Add BLAST21
Topological domaini206 – 551CytoplasmicAdd BLAST346

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impaired degradation of proteins with misfolded intramembrane or lumenal domains.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi399C → S: Stabilizes HRD1. Reduced interaction with substrate. Formation of oligomer with or without USA1. 5 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002403671 – 551ERAD-associated E3 ubiquitin-protein ligase HRD1Add BLAST551

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q08109

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q08109

PRoteomics IDEntifications database

More...PRIDEi		Q08109

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q08109

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homooligomers in a USA1-dependent manner: HRD1 oligomerization appears to be important for ERAD-L function but less important for ERAD-M function, although the underlying molecular mechanisms are unclear.

Component of the HRD1 complex which contains HRD1, HRD3, USA1, DER1, YOS9, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the core membrane complex, consisting of the E3 ligase HRD1 and its cofactors HRD3, DER1 and USA1, the substrate recruiting factor YOS9, and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1.

Interacts with HRD3 and DER1. The complex interacts with the ERAD substrates HMG1 and HMG2.

Interacts with the associated E2 ubiquitin conjugating enzymes UBC1 and UBC7 with its membrane anchor CUE1.

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34391, 163 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3070, HRD1 ubiquitin ligase complex

Database of interacting proteins

More...DIPi		DIP-8850N

Protein interaction database and analysis system

More...IntActi		Q08109, 12 interactors

Molecular INTeraction database

More...MINTi		Q08109

STRING: functional protein association networks

More...STRINGi		4932.YOL013C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q08109, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q08109

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni226 – 256DisorderedSequence analysisAdd BLAST31
Regioni517 – 551Interaction with USA1Add BLAST35

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HRD1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri349 – 400RING-type; atypicalPROSITE-ProRule annotationAdd BLAST52

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0802, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000172216

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026577_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q08109

Identification of Orthologs from Complete Genome Data

More...OMAi		KNWMERS

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR032832, E3_lig_synoviolin/Hrd1
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD

The PANTHER Classification System

More...PANTHERi		PTHR22763:SF169, PTHR22763:SF169, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13639, zf-RING_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00184, RING, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50089, ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q08109-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVPENRRKQL AIFVVVTYLL TFYCVYSATK TSVSFLQVTL KLNEGFNLMV 
        60         70         80         90        100
LSIFILLNST LLWQLLTKLL FGELRLIEHE HIFERLPFTI INTLFMSSLF 
       110        120        130        140        150
HERYFFTVAF FGLLLLYLKV FHWILKDRLE ALLQSINDST TMKTLIFSRF 
       160        170        180        190        200
SFNLVLLAVV DYQIITRCIS SIYTNQKSDI ESTSLYLIQV MEFTMLLIDL 
       210        220        230        240        250
LNLFLQTCLN FWEFYRSQQS LSNENNHIVH GDPTDENTVE SDQSQPVLND 
       260        270        280        290        300
DDDDDDDDRQ FTGLEGKFMY EKAIDVFTRF LKTALHLSML IPFRMPMMLL 
       310        320        330        340        350
KDVVWDILAL YQSGTSLWKI WRNNKQLDDT LVTVTVEQLQ NSANDDNICI 
       360        370        380        390        400
ICMDELIHSP NQQTWKNKNK KPKRLPCGHI LHLSCLKNWM ERSQTCPICR 
       410        420        430        440        450
LPVFDEKGNV VQTTFTSNSD ITTQTTVTDS TGIATDQQGF ANEVDLLPTR 
       460        470        480        490        500
TTSPDIRIVP TQNIDTLAMR TRSTSTPSPT WYTFPLHKTG DNSVGSSRSA 
       510        520        530        540        550
YEFLITNSDE KENGIPVKLT IENHEVNSLH GDGGEQIAKK IVIPDKFIQH 

I
Length:551
Mass (Da):63,535
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCAA6341E7A94DB0B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z74755 Genomic DNA Translation: CAA99012.1
BK006948 Genomic DNA Translation: DAA10770.1

Protein sequence database of the Protein Information Resource

More...PIRi		S66695

NCBI Reference Sequences

More...RefSeqi		NP_014630.1, NM_001183267.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YOL013C_mRNA; YOL013C; YOL013C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854149

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YOL013C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74755 Genomic DNA Translation: CAA99012.1
BK006948 Genomic DNA Translation: DAA10770.1
PIRiS66695
RefSeqiNP_014630.1, NM_001183267.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5V6Pelectron microscopy4.10A/B1-407[»]
6VJYelectron microscopy4.30B1-430[»]
6VJZelectron microscopy4.30B1-480[»]
6VK0electron microscopy4.10B1-480[»]
6VK1electron microscopy3.90B1-480[»]
SMRiQ08109
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34391, 163 interactors
ComplexPortaliCPX-3070, HRD1 ubiquitin ligase complex
DIPiDIP-8850N
IntActiQ08109, 12 interactors
MINTiQ08109
STRINGi4932.YOL013C

Protein family/group databases

TCDBi3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family

PTM databases

iPTMnetiQ08109

Proteomic databases

MaxQBiQ08109
PaxDbiQ08109
PRIDEiQ08109

Genome annotation databases

EnsemblFungiiYOL013C_mRNA; YOL013C; YOL013C
GeneIDi854149
KEGGisce:YOL013C

Organism-specific databases

SGDiS000005373, HRD1
VEuPathDBiFungiDB:YOL013C

Phylogenomic databases

eggNOGiKOG0802, Eukaryota
GeneTreeiENSGT00940000172216
HOGENOMiCLU_026577_0_0_1
InParanoidiQ08109
OMAiKNWMERS

Enzyme and pathway databases

UniPathwayiUPA00143
BRENDAi2.3.2.27, 984

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q08109
RNActiQ08109, protein

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032832, E3_lig_synoviolin/Hrd1
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
PANTHERiPTHR22763:SF169, PTHR22763:SF169, 1 hit
PfamiView protein in Pfam
PF13639, zf-RING_2, 1 hit
SMARTiView protein in SMART
SM00184, RING, 1 hit
PROSITEiView protein in PROSITE
PS50089, ZF_RING_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHRD1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q08109
Secondary accession number(s): D6W254
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: June 2, 2021
This is version 168 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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