Q08109

PR
Gene name
HRD1 (DER3, YOL013C)
Protein name
ERAD-associated E3 ubiquitin-protein ligase HRD1
Names
HMG-CoA reductase degradation protein 1, RING-type E3 ubiquitin transferase HRD1
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YOL013C
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

409-490 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

6 structures for Q08109

Entry ID Method Resolution Chain Position Source
5V6P EM 410 A A/B 1-407 PDB
6VJY EM 430 A B 1-430 PDB
6VJZ EM 430 A B 1-480 PDB
6VK0 EM 410 A B 1-480 PDB
6VK1 EM 390 A B 1-480 PDB
AF-Q08109-F1 Predicted AlphaFoldDB

10 variants for Q08109

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-303001 12 I>M No SGRP
s15-302114 308 L>S No SGRP
s15-302018 340 Q>R No SGRP
s15-301680 453 S>P No SGRP
s15-301662 459 V>M No SGRP
s15-301659 460 P>S No SGRP
s15-301632 469 M>V No SGRP
s15-301622 472 R>T No SGRP
s15-301569 490 G>S No SGRP
s15-301494 515 I>L No SGRP

No associated diseases with Q08109

1 regional properties for Q08109

Type Name Position InterPro Accession
domain Zinc finger, RING-type 348 - 400 IPR001841

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
Hrd1p ubiquitin ligase complex A multiprotein complex that recognizes and ubiquitinates proteins with misfolded luminal and membrane domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p. In mammals, this complex contains the ubiquitin ligase HRD1 (Synoviolin) or AMFR (gp78).
Hrd1p ubiquitin ligase ERAD-L complex A multiprotein complex that recognizes and ubiquitinates proteins with misfolded luminal domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p.
Hrd1p ubiquitin ligase ERAD-M complex A multiprotein complex that recognizes and ubiquitinates proteins with misfolded membrane domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

4 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

7 GO annotations of biological process

Name Definition
endoplasmic reticulum unfolded protein response The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
fungal-type cell wall organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
protein autoubiquitination The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
protein K48-linked ubiquitination A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation.
retrograde protein transport, ER to cytosol The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVPENRRKQL AIFVVVTYLL TFYCVYSATK TSVSFLQVTL KLNEGFNLMV LSIFILLNST
70 80 90 100 110 120
LLWQLLTKLL FGELRLIEHE HIFERLPFTI INTLFMSSLF HERYFFTVAF FGLLLLYLKV
130 140 150 160 170 180
FHWILKDRLE ALLQSINDST TMKTLIFSRF SFNLVLLAVV DYQIITRCIS SIYTNQKSDI
190 200 210 220 230 240
ESTSLYLIQV MEFTMLLIDL LNLFLQTCLN FWEFYRSQQS LSNENNHIVH GDPTDENTVE
250 260 270 280 290 300
SDQSQPVLND DDDDDDDDRQ FTGLEGKFMY EKAIDVFTRF LKTALHLSML IPFRMPMMLL
310 320 330 340 350 360
KDVVWDILAL YQSGTSLWKI WRNNKQLDDT LVTVTVEQLQ NSANDDNICI ICMDELIHSP
370 380 390 400 410 420
NQQTWKNKNK KPKRLPCGHI LHLSCLKNWM ERSQTCPICR LPVFDEKGNV VQTTFTSNSD
430 440 450 460 470 480
ITTQTTVTDS TGIATDQQGF ANEVDLLPTR TTSPDIRIVP TQNIDTLAMR TRSTSTPSPT
490 500 510 520 530 540
WYTFPLHKTG DNSVGSSRSA YEFLITNSDE KENGIPVKLT IENHEVNSLH GDGGEQIAKK
550
IVIPDKFIQH I