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ERAD-associated E3 ubiquitin-protein ligase HRD1 (EC 2.3.2.27) (HMG-CoA reductase degradation protein 1) (RING-type E3 ubiquitin transferase HRD1)

 HRD1_YEAST              Reviewed;         551 AA.
Q08109; D6W254;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-MAY-2022, entry version 171.
RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1;
EC=2.3.2.27;
AltName: Full=HMG-CoA reductase degradation protein 1;
AltName: Full=RING-type E3 ubiquitin transferase HRD1 {ECO:0000305};
Name=HRD1; Synonyms=DER3; OrderedLocusNames=YOL013C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=8970163; DOI=10.1091/mbc.7.12.2029;
Hampton R.Y., Gardner R.G., Rine J.;
"Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-
methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane
protein.";
Mol. Biol. Cell 7:2029-2044(1996).
[4]
FUNCTION.
PubMed=9437001; DOI=10.1091/mbc.9.1.209;
Bordallo J., Plemper R.K., Finger A., Wolf D.H.;
"Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation
of misfolded lumenal and integral membrane proteins.";
Mol. Biol. Cell 9:209-222(1998).
[5]
FUNCTION.
PubMed=10218484; DOI=10.1016/s0014-5793(99)00362-2;
Bordallo J., Wolf D.H.;
"A RING-H2 finger motif is essential for the function of Der3/Hrd1 in
endoplasmic reticulum associated protein degradation in the yeast
Saccharomyces cerevisiae.";
FEBS Lett. 448:244-248(1999).
[6]
FUNCTION.
PubMed=10547371; DOI=10.1242/jcs.112.22.4123;
Plemper R.K., Bordallo J., Deak P.M., Taxis C., Hitt R., Wolf D.H.;
"Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-
translocation complex mediating protein transport for ER degradation.";
J. Cell Sci. 112:4123-4134(1999).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HRD3, TOPOLOGY, AND
MUTAGENESIS OF CYS-399.
PubMed=11018054; DOI=10.1083/jcb.151.1.69;
Gardner R.G., Swarbrick G.M., Bays N.W., Cronin S.R., Wilhovsky S.,
Seelig L.P., Kim C., Hampton R.Y.;
"Endoplasmic reticulum degradation requires lumen to cytosol signaling.
Transmembrane control of Hrd1p by Hrd3p.";
J. Cell Biol. 151:69-82(2000).
[8]
FUNCTION.
PubMed=10793145; DOI=10.1091/mbc.11.5.1697;
Wilhovsky S., Gardner R.G., Hampton R.Y.;
"HRD gene dependence of endoplasmic reticulum-associated degradation.";
Mol. Biol. Cell 11:1697-1708(2000).
[9]
FUNCTION, MUTAGENESIS OF CYS-399, AND TOPOLOGY.
PubMed=11139575; DOI=10.1074/jbc.m008608200;
Deak P.M., Wolf D.H.;
"Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase
(E3) involved in endoplasmic reticulum degradation.";
J. Biol. Chem. 276:10663-10669(2001).
[10]
FUNCTION, AND INTERACTION WITH HMG1 AND HMG2.
PubMed=11390656; DOI=10.1128/mcb.21.13.4276-4291.2001;
Gardner R.G., Shearer A.G., Hampton R.Y.;
"In vivo action of the HRD ubiquitin ligase complex: mechanisms of
endoplasmic reticulum quality control and sterol regulation.";
Mol. Cell. Biol. 21:4276-4291(2001).
[11]
FUNCTION, INTERACTION WITH UBC1 AND UBC7, AND MUTAGENESIS OF CYS-399.
PubMed=11146622; DOI=10.1038/35050524;
Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
"Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
associated degradation.";
Nat. Cell Biol. 3:24-29(2001).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION, IDENTIFICATION IN THE HRD1 COMPLEX, AND DISRUPTION PHENOTYPE.
PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
Carvalho P., Goder V., Rapoport T.A.;
"Distinct ubiquitin-ligase complexes define convergent pathways for the
degradation of ER proteins.";
Cell 126:361-373(2006).
[15]
FUNCTION, AND INTERACTION WITH CDC48 AND DER1.
PubMed=16619026; DOI=10.1038/sj.emboj.7601088;
Gauss R., Sommer T., Jarosch E.;
"The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate
selection and Cdc48p recruitment.";
EMBO J. 25:1827-1835(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
FUNCTION, SUBUNIT, INTERACTION WITH DER1 AND USA1, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF CYS-399.
PubMed=20005842; DOI=10.1016/j.molcel.2009.10.015;
Horn S.C., Hanna J., Hirsch C., Volkwein C., Schutz A., Heinemann U.,
Sommer T., Jarosch E.;
"Usa1 functions as a scaffold of the HRD-ubiquitin ligase.";
Mol. Cell 36:782-793(2009).
[19]
FUNCTION, SUBUNIT, INTERACTION WITH USA1, AND MUTAGENESIS OF CYS-399.
PubMed=21074049; DOI=10.1016/j.cell.2010.10.028;
Carvalho P., Stanley A.M., Rapoport T.A.;
"Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-
ligase Hrd1p.";
Cell 143:579-591(2010).
[20] {ECO:0007744|PDB:5V6P}
STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF 1-407 IN COMPLEX WITH
HRD3.
PubMed=28682307; DOI=10.1038/nature23314;
Schoebel S., Mi W., Stein A., Ovchinnikov S., Pavlovicz R., DiMaio F.,
Baker D., Chambers M.G., Su H., Li D., Rapoport T.A., Liao M.;
"Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex
with Hrd3.";
Nature 548:352-355(2017).
[21] {ECO:0007744|PDB:6VJY, ECO:0007744|PDB:6VJZ, ECO:0007744|PDB:6VK0, ECO:0007744|PDB:6VK1}
STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 1-480 IN COMPLEX WITH
DER1; HRD3 AND USA1, FUNCTION, SUBUNIT, AND TRANSMEMBRANE DOMAINS.
PubMed=32327568; DOI=10.1126/science.aaz2449;
Wu X., Siggel M., Ovchinnikov S., Mi W., Svetlov V., Nudler E., Liao M.,
Hummer G., Rapoport T.A.;
"Structural basis of ER-associated protein degradation mediated by the Hrd1
ubiquitin ligase complex.";
Science 368:0-0(2020).
-!- FUNCTION: 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). In
ERAD-L, facilitates retrotranslocation of misfolded proteins from the
ER lumen through the ER membrane in conjunction with DER1
(PubMed:32327568). Both proteins have lateral gates facing each other
which form a channel through the ER membrane and which distort the
membrane region between the lateral gates, making it much thinner than
a normal phospholipid bilayer (PubMed:32327568). Substrates insert into
the membrane as a hairpin loop with one strand interacting with DER1
and the other with HRD1. 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 CDC48-NPL4-UFD1 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. {ECO:0000269|PubMed:10218484, ECO:0000269|PubMed:10547371,
ECO:0000269|PubMed:10793145, ECO:0000269|PubMed:11018054,
ECO:0000269|PubMed:11139575, ECO:0000269|PubMed:11146622,
ECO:0000269|PubMed:11390656, ECO:0000269|PubMed:16619026,
ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:20005842,
ECO:0000269|PubMed:21074049, ECO:0000269|PubMed:32327568,
ECO:0000269|PubMed:8970163, ECO:0000269|PubMed:9437001}.
-!- CATALYTIC ACTIVITY:
Reaction=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;
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Monomer (PubMed:32327568). Has also been shown to form
homodimers (PubMed:28682307). However, dimer assembly is likely to be
non-physiological (PubMed:32327568). Forms homooligomers in a USA1-
dependent manner (PubMed:20005842, PubMed:21074049). However, can
function as a monomer in ERAD-L so the role of USA1-dependent
oligomerization remains unclear (PubMed:32327568). Component of the
HRD1 ubiquitin ligase complex which contains the E3 ligase HRD1, its
cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and
CDC48-binding protein UBX2 (PubMed:16873066). Within the complex,
interacts directly with HRD3 and USA1 and indirectly with DER1
(PubMed:11018054, PubMed:16619026, PubMed:20005842, PubMed:21074049,
PubMed:28682307). In ERAD-L, HRD3 and YOS9 jointly bind misfolded
glycoproteins in the endoplasmic reticulum (ER) lumen
(PubMed:32327568). Movement of ERAD-L substrates through the ER
membrane is facilitated by HRD1 and DER1 which have lateral gates
facing each other and which distort the membrane region between the
lateral gates, making it much thinner than a normal phospholipid
bilayer (PubMed:32327568). Substrates insert into the membrane as a
hairpin loop with one strand interacting with DER1 and the other with
HRD1 (PubMed:32327568). The HRD1 complex interacts with the
heterotrimeric CDC48-NPL4-UFD1 ATPase complex which is recruited by
UBX2 via its interaction with CDC48 and which moves ubiquitinated
substrates to the cytosol for targeting to the proteasome
(PubMed:16873066, PubMed:16619026). The HRD1 complex interacts with the
ERAD substrates HMG1 and HMG2 (PubMed:11390656). Interacts with the
associated E2 ubiquitin conjugating enzymes UBC1 and UBC7 with its
membrane anchor CUE1 (PubMed:11146622). {ECO:0000269|PubMed:11018054,
ECO:0000269|PubMed:11146622, ECO:0000269|PubMed:11390656,
ECO:0000269|PubMed:16619026, ECO:0000269|PubMed:16873066,
ECO:0000269|PubMed:20005842, ECO:0000269|PubMed:21074049,
ECO:0000269|PubMed:28682307, ECO:0000269|PubMed:32327568}.
-!- INTERACTION:
Q08109; P25694: CDC48; NbExp=8; IntAct=EBI-37613, EBI-4308;
Q08109; P38307: DER1; NbExp=5; IntAct=EBI-37613, EBI-5761;
Q08109; Q08109: HRD1; NbExp=5; IntAct=EBI-37613, EBI-37613;
Q08109; Q05787: HRD3; NbExp=11; IntAct=EBI-37613, EBI-31647;
Q08109; P00729: PRC1; NbExp=11; IntAct=EBI-37613, EBI-4153;
Q08109; Q04228: UBX2; NbExp=7; IntAct=EBI-37613, EBI-27730;
Q08109; Q99220: YOS9; NbExp=6; IntAct=EBI-37613, EBI-34938;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11018054, ECO:0000269|PubMed:14562095}; Multi-pass
membrane protein {ECO:0000269|PubMed:11018054,
ECO:0000269|PubMed:14562095}.
-!- DISRUPTION PHENOTYPE: Impaired degradation of proteins with misfolded
intramembrane or lumenal domains. {ECO:0000269|PubMed:16873066,
ECO:0000269|PubMed:20005842}.
-!- MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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EMBL; Z74755; CAA99012.1; -; Genomic_DNA.
EMBL; BK006948; DAA10770.1; -; Genomic_DNA.
PIR; S66695; S66695.
RefSeq; NP_014630.1; NM_001183267.1.
PDB; 5V6P; EM; 4.10 A; A/B=1-407.
PDB; 6VJY; EM; 4.30 A; B=1-430.
PDB; 6VJZ; EM; 4.30 A; B=1-480.
PDB; 6VK0; EM; 4.10 A; B=1-480.
PDB; 6VK1; EM; 3.90 A; B=1-480.
PDBsum; 5V6P; -.
PDBsum; 6VJY; -.
PDBsum; 6VJZ; -.
PDBsum; 6VK0; -.
PDBsum; 6VK1; -.
AlphaFoldDB; Q08109; -.
SMR; Q08109; -.
BioGRID; 34391; 178.
ComplexPortal; CPX-3070; HRD1 ubiquitin ligase complex.
DIP; DIP-8850N; -.
IntAct; Q08109; 13.
MINT; Q08109; -.
STRING; 4932.YOL013C; -.
TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
iPTMnet; Q08109; -.
MaxQB; Q08109; -.
PaxDb; Q08109; -.
PRIDE; Q08109; -.
EnsemblFungi; YOL013C_mRNA; YOL013C; YOL013C.
GeneID; 854149; -.
KEGG; sce:YOL013C; -.
SGD; S000005373; HRD1.
VEuPathDB; FungiDB:YOL013C; -.
eggNOG; KOG0802; Eukaryota.
GeneTree; ENSGT00940000172216; -.
HOGENOM; CLU_026577_0_0_1; -.
InParanoid; Q08109; -.
OMA; MEFTMLL; -.
BRENDA; 2.3.2.27; 984.
Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
UniPathway; UPA00143; -.
PRO; PR:Q08109; -.
Proteomes; UP000002311; Chromosome XV.
RNAct; Q08109; protein.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; IPI:ComplexPortal.
GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
GO; GO:0000838; C:Hrd1p ubiquitin ligase ERAD-M complex; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
GO; GO:0051865; P:protein autoubiquitination; IDA:SGD.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:SGD.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR032832; E3_lig_synoviolin/Hrd1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR22763:SF169; PTHR22763:SF169; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Endoplasmic reticulum; Membrane; Metal-binding;
Reference proteome; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1..551
/note="ERAD-associated E3 ubiquitin-protein ligase HRD1"
/id="PRO_0000240367"
TOPO_DOM 1..8
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 9..30
/note="Helical; Name=1"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 31..43
/note="Lumenal"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 44..71
/note="Helical; Name=2"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 72..84
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 85..101
/note="Helical; Name=3"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 102..103
/note="Lumenal"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 104..126
/note="Helical; Name=4"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 127..147
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 148..169
/note="Helical; Name=5"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 170..183
/note="Lumenal"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 184..208
/note="Helical; Name=6"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 209..271
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 272..292
/note="Helical; Name=7"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 293..296
/note="Lumenal"
/evidence="ECO:0000269|PubMed:32327568"
TRANSMEM 297..314
/note="Helical; Name=8"
/evidence="ECO:0000269|PubMed:32327568"
TOPO_DOM 315..551
/note="Cytoplasmic"
/evidence="ECO:0000269|PubMed:32327568"
ZN_FING 349..400
/note="RING-type; atypical"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
REGION 226..256
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 517..551
/note="Interaction with USA1"
MUTAGEN 399
/note="C->S: Stabilizes HRD1. Reduced interaction with
substrate. Formation of oligomer with or without USA1."
/evidence="ECO:0000269|PubMed:11018054,
ECO:0000269|PubMed:11139575, ECO:0000269|PubMed:11146622,
ECO:0000269|PubMed:20005842, ECO:0000269|PubMed:21074049"
SEQUENCE 551 AA; 63535 MW; CAA6341E7A94DB0B CRC64;
MVPENRRKQL AIFVVVTYLL TFYCVYSATK TSVSFLQVTL KLNEGFNLMV LSIFILLNST
LLWQLLTKLL FGELRLIEHE HIFERLPFTI INTLFMSSLF HERYFFTVAF FGLLLLYLKV
FHWILKDRLE ALLQSINDST TMKTLIFSRF SFNLVLLAVV DYQIITRCIS SIYTNQKSDI
ESTSLYLIQV MEFTMLLIDL LNLFLQTCLN FWEFYRSQQS LSNENNHIVH GDPTDENTVE
SDQSQPVLND DDDDDDDDRQ FTGLEGKFMY EKAIDVFTRF LKTALHLSML IPFRMPMMLL
KDVVWDILAL YQSGTSLWKI WRNNKQLDDT LVTVTVEQLQ NSANDDNICI ICMDELIHSP
NQQTWKNKNK KPKRLPCGHI LHLSCLKNWM ERSQTCPICR LPVFDEKGNV VQTTFTSNSD
ITTQTTVTDS TGIATDQQGF ANEVDLLPTR TTSPDIRIVP TQNIDTLAMR TRSTSTPSPT
WYTFPLHKTG DNSVGSSRSA YEFLITNSDE KENGIPVKLT IENHEVNSLH GDGGEQIAKK
IVIPDKFIQH I


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25-845 HACE1 contains 6 ANK repeats and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. HACE1 is an E3 ubiquitin-protein ligase that may function in cellular proteins degradation. 0.05 mg
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
27-508 RNF12 is a RING-H2 zinc finger protein. It has been shown to be a ubiquitin protein ligase that targets LIM domain binding 1 (LDB1_CLIM), and causes proteasome-dependent degradation of LDB1. This prot 0.05 mg
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135
EIAAB35497 E3 ubiquitin-protein ligase RNF216,Mouse,Mus musculus,RING finger protein 216,Rnf216,Triad domain-containing protein 3,Triad3,Ubce7ip1,UbcM4-interacting protein 83,Ubiquitin-conjugating enzyme 7-inter
EIAAB35496 E3 ubiquitin-protein ligase RNF216,Homo sapiens,Human,RING finger protein 216,RNF216,Triad domain-containing protein 3,TRIAD3,UBCE7IP1,Ubiquitin-conjugating enzyme 7-interacting protein 1,ZIN,Zinc fin
EIAAB45297 E3 ubiquitin-protein ligase UHRF1,Mouse,Mus musculus,Np95,Nuclear protein 95,Nuclear zinc finger protein Np95,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing P
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
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EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
EIAAB44908 Cell proliferation-inducing gene 50 protein,Homo sapiens,HSPC150,Human,PIG50,UBE2T,Ubiquitin carrier protein T,Ubiquitin-conjugating enzyme E2 T,Ubiquitin-protein ligase T
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU