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Protein

E3 ubiquitin-protein ligase hrd-1

Gene

sel-11

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradation (ERAD) system, involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins. Protects cells from ER stress-induced apoptosis. Thought to play a role together with hsp-3 in developmental growth and function of intestinal cells and to play a role together with hsp-4 in gonad formation.2 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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri292 – 333RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

GO - Biological processi

  • endoplasmic reticulum unfolded protein response Source: GO_Central
  • ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
  • multicellular organism growth Source: WormBase
  • protein polyubiquitination Source: GO_Central
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  • regulation of gene expression Source: WormBase
  • regulation of Notch signaling pathway Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CEL-5358346. Hedgehog ligand biogenesis.
R-CEL-901032. ER Quality Control Compartment (ERQC).
SignaLinkiQ20798.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase hrd-1
Alternative name(s):
Suppressor/enhancer of lin-12 (EC:6.3.2.-)
Gene namesi
Name:sel-11
Synonyms:hrd-1
ORF Names:F55A11.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiF55A11.3; CE05945; WBGene00004768; sel-11.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 41LumenalSequence analysisAdd BLAST18
Transmembranei42 – 62HelicalSequence analysisAdd BLAST21
Topological domaini63 – 99CytoplasmicSequence analysisAdd BLAST37
Transmembranei100 – 120HelicalSequence analysisAdd BLAST21
Topological domaini121 – 144LumenalSequence analysisAdd BLAST24
Transmembranei145 – 165HelicalSequence analysisAdd BLAST21
Topological domaini166 – 170CytoplasmicSequence analysis5
Transmembranei171 – 191HelicalSequence analysisAdd BLAST21
Topological domaini192 – 215LumenalSequence analysisAdd BLAST24
Transmembranei216 – 236HelicalSequence analysisAdd BLAST21
Topological domaini237 – 610CytoplasmicSequence analysisAdd BLAST374

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Reduced growth rate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000028055324 – 610E3 ubiquitin-protein ligase hrd-1Add BLAST587

Proteomic databases

EPDiQ20798.
PaxDbiQ20798.
PeptideAtlasiQ20798.
PRIDEiQ20798.

PTM databases

iPTMnetiQ20798.

Expressioni

Gene expression databases

BgeeiWBGene00004768.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi44637. 6 interactors.
DIPiDIP-26690N.
IntActiQ20798. 4 interactors.
MINTiMINT-212290.
STRINGi6239.F55A11.3.1.

Structurei

3D structure databases

ProteinModelPortaliQ20798.
SMRiQ20798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi371 – 467Pro-richAdd BLAST97

Domaini

The RING-type zinc finger is required for E3 ligase activity.By similarity

Sequence similaritiesi

Belongs to the HRD1 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri292 – 333RING-type; atypicalPROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000294196.
InParanoidiQ20798.
KOiK10601.
OMAiAMEGHQR.
OrthoDBiEOG091G13IJ.
PhylomeDBiQ20798.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032832. E3_lig_synoviolin/Hrd1.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22763:SF25. PTHR22763:SF25. 2 hits.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q20798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVSAGLMIG GSCVATAATI LNAFLINKQF YPSIVYLSKS NASMAVIYVQ
60 70 80 90 100
GIVLVYLMFQ LLKSILFGDL RAAEAEHLSE RTWHAVLETC LAFTVFRDDF
110 120 130 140 150
SAIFVMQFIG LLFIKCFHWL ADDRVDMMER SPVITLRFHL RMMTVLAALG
160 170 180 190 200
FADSYFVSSA YFTTITRGAS AQIVFGFEYA ILLALVLHVT IKYLLHMHDL
210 220 230 240 250
RNPQSWDNKA VYLLYAELFI NLIRCLLYGF FAVVMLRVHT FPLFSVRPFY
260 270 280 290 300
QSVRALHKAF LDVILSRRAI NAMNSQFPVV SAEDLAAMDA TCIICREEMT
310 320 330 340 350
VDASPKRLPC SHVFHAHCLR SWFQRQQTCP TCRTDIWQGR NGAAAGGNAA
360 370 380 390 400
DAAANVADAN VAGAQIGAGM PPFLPFLGHQ FGFPQQPAGA GGAQPGAAQA
410 420 430 440 450
GGQPGPFPHQ IFYAPAPANR PEFMNLIPPP PLPMAGPPGM FPMMPPPPLP
460 470 480 490 500
QVNTTQGTSS ETPPVNPSYS QLSTEELRRM EGESREALLA RLQAMDNIMV
510 520 530 540 550
LLESAQMQMI QLATVTPIRP RPVVPSDESE QEAPGPSTDQ VTSEEQEIPA
560 570 580 590 600
TSSAPSIFRT ESPSTSSTAP STSSPVTASS TPTTSSTRTP EAEEVRQRRL
610
ARLLGENANQ
Length:610
Mass (Da):66,814
Last modified:November 1, 1996 - v1
Checksum:i42BE294F4A554F50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72511 Genomic DNA. Translation: CAA96657.1.
PIRiT22687.
RefSeqiNP_505969.1. NM_073568.4.
UniGeneiCel.23482.

Genome annotation databases

EnsemblMetazoaiF55A11.3; F55A11.3; WBGene00004768.
GeneIDi179612.
KEGGicel:CELE_F55A11.3.
UCSCiF55A11.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72511 Genomic DNA. Translation: CAA96657.1.
PIRiT22687.
RefSeqiNP_505969.1. NM_073568.4.
UniGeneiCel.23482.

3D structure databases

ProteinModelPortaliQ20798.
SMRiQ20798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44637. 6 interactors.
DIPiDIP-26690N.
IntActiQ20798. 4 interactors.
MINTiMINT-212290.
STRINGi6239.F55A11.3.1.

PTM databases

iPTMnetiQ20798.

Proteomic databases

EPDiQ20798.
PaxDbiQ20798.
PeptideAtlasiQ20798.
PRIDEiQ20798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF55A11.3; F55A11.3; WBGene00004768.
GeneIDi179612.
KEGGicel:CELE_F55A11.3.
UCSCiF55A11.3. c. elegans.

Organism-specific databases

CTDi179612.
WormBaseiF55A11.3; CE05945; WBGene00004768; sel-11.

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00530000062938.
HOGENOMiHOG000294196.
InParanoidiQ20798.
KOiK10601.
OMAiAMEGHQR.
OrthoDBiEOG091G13IJ.
PhylomeDBiQ20798.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-CEL-5358346. Hedgehog ligand biogenesis.
R-CEL-901032. ER Quality Control Compartment (ERQC).
SignaLinkiQ20798.

Miscellaneous databases

PROiQ20798.

Gene expression databases

BgeeiWBGene00004768.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032832. E3_lig_synoviolin/Hrd1.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR22763:SF25. PTHR22763:SF25. 2 hits.
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHRD1_CAEEL
AccessioniPrimary (citable) accession number: Q20798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.