AUP1
entrez
550
canonical
uniprot
Q9Y679
canonical
ensembl
ENSG00000115307
resolver
ensp
ENSP00000366748
resolver
genesymbol
AUP1
resolver
hgnc
HGNC:891
resolver
uniprot
C0H5W8
resolver
uniprot
Q9H866
resolver
uniprot
Q9UNQ6
resolver
uniprot
Q9Y685
resolver
uniprot_entry
AUP1_HUMAN
resolver
uniprot_sec
C0H5W8
resolver
uniprot_sec
Q9H866
resolver
uniprot_sec
Q9UNQ6
resolver
uniprot_sec
Q9Y685
resolver
amino_acid_sequence
MELPSGPGPERLFDSHRLPGDCFLLLVLLLYAPVGFCLLVLRLFLGIHVFLVSCALPDSVLRRFVVRTMCAVLGLVARQEDSGLRDHSVRVLISNHVTPFDHNIVNLLTTCSTPLLNSPPSFVCWSRGFMEMNGRGELVESLKRFCASTRLPPTPLLLFPEEEATNGREGLLRFSSWPFSIQDVVQPLTLQVQRPLVSVTVSDASWVSELLWSLFVPFTVYQVRWLRPVHRQLGEANEEFALRVQQLVAKELGQTGTRLTPADKAEHMKRQRHPRLRPQSAQSSFPPSPGPSPDVQLATLAQRVKEVLPHVPLGVIQRDLAKTGCVDLTITNLLEGAVAFMPEDITKGTQSLPTASASKFPSSGPVTPQPTALTFAKSSWARQESLQERKQALYEYARRRFTERRAQEAD
uniprot
proteins
function
FUNCTION: Plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome (PubMed:18711132, PubMed:21857022). Plays a role in lipid droplet formation (PubMed:21857022). Induces lipid droplet clustering (PubMed:24039768). Recruits ubiquitin-conjugating enzyme UBE2G2 to lipid droplets which facilitates its interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading to sterol-induced ubiquitination of HMGCR and its subsequent proteasomal degradation (PubMed:21127063, PubMed:23223569). Also required for the degradation of INSIG1, SREBF1 and SREBF2 (PubMed:23223569). Plays a role in regulating assembly and secretion of very low density lipoprotein particles and stability of apolipoprotein APOB (PubMed:28183703). {ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:24039768, ECO:0000269|PubMed:28183703}.; FUNCTION: (Microbial infection) Following Dengue virus infection, required for induction of lipophagy which facilitates production of virus progeny particles. {ECO:0000269|PubMed:29902443}.
uniprot
proteins
mass_dalton
45787
uniprot
proteins
mutagenesis
MUTAGEN 33..35; /note="PVG->LLL: Disrupts topology with the N-terminus in the lumen instead of the cytoplasm. Abolishes lipid droplet localization and lipid droplet clustering."; /evidence="ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:24039768"; MUTAGEN 42; /note="R->I: Abolishes lipid droplet localization."; /evidence="ECO:0000269|PubMed:23197321"; MUTAGEN 58; /note="D->I: Does not affect lipid droplet localization."; /evidence="ECO:0000269|PubMed:23197321"; MUTAGEN 62..63; /note="RR->FF: Abolishes lipid droplet localization."; /evidence="ECO:0000269|PubMed:23197321"; MUTAGEN 96; /note="H->A: Reduced formation of lipid droplets."; /evidence="ECO:0000269|PubMed:21857022"; MUTAGEN 306..308; /note="EVL->KAA: Reduced interaction with ER quality control machinery and misfolded substrates; when associated with 333-L-L-334 Del."; /evidence="ECO:0000269|PubMed:21857022"; MUTAGEN 307..309; /note="VLP->GGR: Reduced lipid droplet clustering."; /evidence="ECO:0000269|PubMed:24039768"; MUTAGEN 316; /note="I->R: Reduced lipid droplet clustering; when associated with 319-V-E-320 and 333-E-D-334."; /evidence="ECO:0000269|PubMed:24039768"; MUTAGEN 319..320; /note="DL->VE: Reduced lipid droplet clustering; when associated with R-316 and 333-E-D-334."; /evidence="ECO:0000269|PubMed:24039768"; MUTAGEN 329..330; /note="TI->AD: Reduced lipid droplet clustering."; /evidence="ECO:0000269|PubMed:24039768"; MUTAGEN 333..334; /note="LL->ED: Reduced lipid droplet clustering; when associated with R-316 and 319-V-E-320."; /evidence="ECO:0000269|PubMed:24039768"; MUTAGEN 333..334; /note="Missing: Reduced interaction with ER quality control machinery and misfolded substrates; when associated with 306-K--A-308."; /evidence="ECO:0000269|PubMed:21857022"; MUTAGEN 382; /note="R->A: Significantly reduced interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 383; /note="Q->A: Significantly reduced interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 384; /note="E->A: No effect on interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 386; /note="L->A: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 388; /note="E->A: No effect on interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 389; /note="R->A: Significantly reduced interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 390; /note="K->A: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 393; /note="L->A: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 397..402; /note="ARRRFT->EGREDA: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:21127063"; MUTAGEN 398; /note="R->A: Significantly reduced interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 399; /note="R->A: No effect on interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 400; /note="R->A: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 404; /note="R->A: Abolishes interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 408; /note="E->A: Significantly reduced interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569"; MUTAGEN 410; /note="D->A: No effect on interaction with UBE2G2."; /evidence="ECO:0000269|PubMed:23223569
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated and diubiquitinated. {ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:24039768, ECO:0000269|PubMed:29902443}.; PTM: (Microbial infection) Not ubiquitinated following Dengue virus infection. {ECO:0000269|PubMed:29902443}.
uniprot
proteins
protein_family
AUP1 family
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
12042322
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18711132
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21127063
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21857022
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23197321
uniprot
proteins
pubmed
23223569
uniprot
proteins
pubmed
24039768
uniprot
proteins
pubmed
28183703
uniprot
proteins
pubmed
29902443
uniprot
proteins
sequence_length
410
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569}; Peripheral membrane protein {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:23197321}. Lipid droplet {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:28183703, ECO:0000269|PubMed:29902443}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:29902443}. Note=(Microbial infection) Upon Dengue virus infection, relocates from lipid droplets to autophagosomes. {ECO:0000269|PubMed:29902443}.
uniprot
proteins