ID AUP1_HUMAN Reviewed; 410 AA. AC Q9Y679; C0H5W8; Q9H866; Q9UNQ6; Q9Y685; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 2. DT 27-MAR-2024, entry version 189. DE RecName: Full=Lipid droplet-regulating VLDL assembly factor AUP1 {ECO:0000312|HGNC:HGNC:891}; DE AltName: Full=Ancient ubiquitous protein 1 {ECO:0000303|PubMed:12042322}; GN Name=AUP1 {ECO:0000312|HGNC:HGNC:891}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Pituitary; RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human ancient ubiquitous protein AUP1 isoform gene."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hematopoietic stem cell; RA Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Zhou J., Wang Y., Huang C., RA Ren S., Tu Y., Chen Z.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Eye, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP SUBCELLULAR LOCATION, INTERACTION WITH ITGA2B; ITGA1; ITGA2; ITGA5; ITGAV RP AND ITGAM, AND TISSUE SPECIFICITY. RX PubMed=12042322; DOI=10.1074/jbc.m204340200; RA Kato A., Kawamata N., Tamayose K., Egashira M., Miura R., Fujimura T., RA Murayama K., Oshimi K.; RT "Ancient ubiquitous protein 1 binds to the conserved membrane-proximal RT sequence of the cytoplasmic tail of the integrin alpha subunits that plays RT a crucial role in the inside-out signaling of alpha IIbbeta 3."; RL J. Biol. Chem. 277:28934-28941(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND THR-367, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-292; SER-363 AND RP THR-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION IN A COMPLEX WITH SEL1L, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=18711132; DOI=10.1073/pnas.0805371105; RA Mueller B., Klemm E.J., Spooner E., Claessen J.H., Ploegh H.L.; RT "SEL1L nucleates a protein complex required for dislocation of misfolded RT glycoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12325-12330(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP FUNCTION, INTERACTION WITH UBE2G2, SUBCELLULAR LOCATION, TOPOLOGY, AND RP MUTAGENESIS OF 397-ALA--THR-402. RX PubMed=21127063; DOI=10.1074/jbc.m110.190785; RA Spandl J., Lohmann D., Kuerschner L., Moessinger C., Thiele C.; RT "Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds RT the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region."; RL J. Biol. Chem. 286:5599-5606(2011). RN [15] RP FUNCTION, INTERACTION WITH UBE2G2, SUBCELLULAR LOCATION, DOMAIN, RP UBIQUITINATION, AND MUTAGENESIS OF HIS-96; 306-GLU--LEU-308 AND RP 333-LEU-LEU-334. RX PubMed=21857022; DOI=10.1074/jbc.m111.284794; RA Klemm E.J., Spooner E., Ploegh H.L.; RT "Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet RT accumulation and endoplasmic reticulum (ER) protein quality control."; RL J. Biol. Chem. 286:37602-37614(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF 33-PRO--GLY-35; ARG-42; RP ASP-58 AND 62-ARG-ARG-63. RX PubMed=23197321; DOI=10.1194/jlr.m033852; RA Stevanovic A., Thiele C.; RT "Monotopic topology is required for lipid droplet targeting of ancient RT ubiquitous protein 1."; RL J. Lipid Res. 54:503-513(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-288 AND THR-367, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP FUNCTION, INTERACTION WITH AMFR; RNF139 AND UBE2G2, SUBCELLULAR LOCATION, RP DOMAIN, AND MUTAGENESIS OF ARG-382; GLN-383; GLU-384; LEU-386; GLU-388; RP ARG-389; LYS-390; LEU-393; ARG-398; ARG-399; ARG-400; ARG-404; GLU-408 AND RP ASP-410. RX PubMed=23223569; DOI=10.1091/mbc.e12-07-0564; RA Jo Y., Hartman I.Z., DeBose-Boyd R.A.; RT "Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3- RT hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated RT endoplasmic reticulum membranes."; RL Mol. Biol. Cell 24:169-183(2013). RN [21] RP FUNCTION, DOMAIN, UBIQUITINATION, AND MUTAGENESIS OF 33-PRO--GLY-35; RP 307-VAL--PRO-309; ILE-316; 319-ASP-LEU-320; 329-THR-ILE-330 AND RP 333-LEU-LEU-334. RX PubMed=24039768; DOI=10.1371/journal.pone.0072453; RA Lohmann D., Spandl J., Stevanovic A., Schoene M., Philippou-Massier J., RA Thiele C.; RT "Monoubiquitination of ancient ubiquitous protein 1 promotes lipid droplet RT clustering."; RL PLoS ONE 8:e72453-e72453(2013). RN [22] RP FUNCTION, INTERACTION WITH APOB, AND SUBCELLULAR LOCATION. RX PubMed=28183703; DOI=10.1161/atvbaha.117.309000; RA Zhang J., Zamani M., Thiele C., Taher J., Amir Alipour M., Yao Z., RA Adeli K.; RT "AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of Hepatic Very- RT Low-Density Lipoprotein Assembly and Secretion."; RL Arterioscler. Thromb. Vasc. Biol. 37:633-642(2017). RN [23] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH DENV NS4A, SUBCELLULAR RP LOCATION, INDUCTION (MICROBIAL INFECTION), UBIQUITINATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=29902443; DOI=10.1016/j.chom.2018.05.005; RA Zhang J., Lan Y., Li M.Y., Lamers M.M., Fusade-Boyer M., Klemm E., RA Thiele C., Ashour J., Sanyal S.; RT "Flaviviruses Exploit the Lipid Droplet Protein AUP1 to Trigger Lipophagy RT and Drive Virus Production."; RL Cell Host Microbe 23:819-831.e5(2018). RN [24] RP STRUCTURE BY NMR OF 292-345. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-075, a human CUE domain."; RL Submitted (SEP-2007) to the PDB data bank. CC -!- FUNCTION: Plays a role in the translocation of terminally misfolded CC proteins from the endoplasmic reticulum lumen to the cytoplasm and CC their degradation by the proteasome (PubMed:18711132, PubMed:21857022). CC Plays a role in lipid droplet formation (PubMed:21857022). Induces CC lipid droplet clustering (PubMed:24039768). Recruits ubiquitin- CC conjugating enzyme UBE2G2 to lipid droplets which facilitates its CC interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading CC to sterol-induced ubiquitination of HMGCR and its subsequent CC proteasomal degradation (PubMed:23223569, PubMed:21127063). Also CC required for the degradation of INSIG1, SREBF1 and SREBF2 CC (PubMed:23223569). Plays a role in regulating assembly and secretion of CC very low density lipoprotein particles and stability of apolipoprotein CC APOB (PubMed:28183703). {ECO:0000269|PubMed:18711132, CC ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:24039768, CC ECO:0000269|PubMed:28183703}. CC -!- FUNCTION: (Microbial infection) Following Dengue virus infection, CC required for induction of lipophagy which facilitates production of CC virus progeny particles. {ECO:0000269|PubMed:29902443}. CC -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8, CC UBE2J1/UBC6E and AUP1 (PubMed:18711132). Interacts with the cytoplasmic CC tail of ITGA2B, ITGA1, ITGA2, ITGA5, ITGAV and ITGAM (PubMed:12042322). CC Interacts (via C-terminus) with ubiquitin-conjugating enzyme UBE2G2; CC the interaction recruits UBE2G2 to lipid droplets (PubMed:21127063, CC PubMed:23223569). Interacts with ubiquitin ligases AMFR/gp78 and CC RNF139/TRC8; this promotes interaction of UBE2G2 with AMFR and RNF139 CC (PubMed:23223569). Interacts with apolipoprotein APOB CC (PubMed:28183703). {ECO:0000269|PubMed:12042322, CC ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:21127063, CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:28183703}. CC -!- SUBUNIT: (Microbial infection) Interacts with Dengue virus NS4A; the CC interaction occurs in the presence of Dengue virus NS4B and induces CC lipophagy which facilitates production of virus progeny. CC {ECO:0000269|PubMed:29902443}. CC -!- INTERACTION: CC Q9Y679; P35372: OPRM1; NbExp=4; IntAct=EBI-1058701, EBI-2624570; CC Q9Y679; P60604: UBE2G2; NbExp=6; IntAct=EBI-1058701, EBI-1051028; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132, CC ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, CC ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569}; Peripheral CC membrane protein {ECO:0000269|PubMed:21127063, CC ECO:0000269|PubMed:23197321}. Lipid droplet CC {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022, CC ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569, CC ECO:0000269|PubMed:28183703, ECO:0000269|PubMed:29902443}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome CC {ECO:0000269|PubMed:29902443}. Note=(Microbial infection) Upon Dengue CC virus infection, relocates from lipid droplets to autophagosomes. CC {ECO:0000269|PubMed:29902443}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y679-2; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y679-3; Sequence=VSP_059683, VSP_059684; CC -!- TISSUE SPECIFICITY: Detected in blood platelets and leukocytes (at CC protein level). Ubiquitous. Highly expressed in placenta, liver, CC kidney, skeletal muscle, heart and brain. CC {ECO:0000269|PubMed:12042322}. CC -!- INDUCTION: (Microbial infection) By Dengue virus infection (at protein CC level). {ECO:0000269|PubMed:29902443}. CC -!- DOMAIN: The CUE domain is required for interaction with the ER quality CC control machinery and misfolded substrates, ubiquitination, lipid CC clustering and interaction with AMFR but is not required for CC localization to lipid droplets. {ECO:0000269|PubMed:21857022, CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:24039768}. CC -!- PTM: Monoubiquitinated and diubiquitinated. CC {ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:24039768, CC ECO:0000269|PubMed:29902443}. CC -!- PTM: (Microbial infection) Not ubiquitinated following Dengue virus CC infection. {ECO:0000269|PubMed:29902443}. CC -!- SIMILARITY: Belongs to the AUP1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD43018.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH33646.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF100754; AAD43018.1; ALT_FRAME; mRNA. DR EMBL; AF100753; AAD43017.1; -; mRNA. DR EMBL; AF100746; AAD43010.1; -; mRNA. DR EMBL; AF165515; AAF86645.1; -; mRNA. DR EMBL; AK023983; BAB14753.1; -; mRNA. DR EMBL; CH471053; EAW99623.1; -; Genomic_DNA. DR EMBL; BC001658; AAH01658.1; -; mRNA. DR EMBL; BC033646; AAH33646.2; ALT_INIT; mRNA. DR CCDS; CCDS42702.1; -. [Q9Y679-2] DR RefSeq; NP_853553.1; NM_181575.4. [Q9Y679-2] DR PDB; 2EKF; NMR; -; A=292-345. DR PDB; 7LEW; X-ray; 1.74 A; B=379-410. DR PDBsum; 2EKF; -. DR PDBsum; 7LEW; -. DR AlphaFoldDB; Q9Y679; -. DR SMR; Q9Y679; -. DR BioGRID; 107031; 272. DR CORUM; Q9Y679; -. DR IntAct; Q9Y679; 60. DR MINT; Q9Y679; -. DR STRING; 9606.ENSP00000366748; -. DR iPTMnet; Q9Y679; -. DR PhosphoSitePlus; Q9Y679; -. DR SwissPalm; Q9Y679; -. DR BioMuta; AUP1; -. DR DMDM; 12643958; -. DR EPD; Q9Y679; -. DR jPOST; Q9Y679; -. DR MassIVE; Q9Y679; -. DR MaxQB; Q9Y679; -. DR PaxDb; 9606-ENSP00000366748; -. DR PeptideAtlas; Q9Y679; -. DR ProteomicsDB; 86617; -. [Q9Y679-2] DR ProteomicsDB; 86618; -. [Q9Y679-3] DR Pumba; Q9Y679; -. DR Antibodypedia; 2357; 214 antibodies from 27 providers. DR DNASU; 550; -. DR Ensembl; ENST00000377526.4; ENSP00000366748.3; ENSG00000115307.17. [Q9Y679-2] DR Ensembl; ENST00000425118.5; ENSP00000403430.1; ENSG00000115307.17. [Q9Y679-3] DR GeneID; 550; -. DR KEGG; hsa:550; -. DR MANE-Select; ENST00000377526.4; ENSP00000366748.3; NM_181575.5; NP_853553.1. DR UCSC; uc002smf.4; human. [Q9Y679-2] DR AGR; HGNC:891; -. DR CTD; 550; -. DR DisGeNET; 550; -. DR GeneCards; AUP1; -. DR HGNC; HGNC:891; AUP1. DR HPA; ENSG00000115307; Low tissue specificity. DR MIM; 602434; gene. DR neXtProt; NX_Q9Y679; -. DR OpenTargets; ENSG00000115307; -. DR PharmGKB; PA25182; -. DR VEuPathDB; HostDB:ENSG00000115307; -. DR GeneTree; ENSGT00390000016110; -. DR HOGENOM; CLU_045696_0_0_1; -. DR InParanoid; Q9Y679; -. DR OMA; KFNSWPF; -. DR OrthoDB; 2907518at2759; -. DR PhylomeDB; Q9Y679; -. DR TreeFam; TF313372; -. DR PathwayCommons; Q9Y679; -. DR SignaLink; Q9Y679; -. DR BioGRID-ORCS; 550; 63 hits in 1162 CRISPR screens. DR ChiTaRS; AUP1; human. DR EvolutionaryTrace; Q9Y679; -. DR GeneWiki; AUP1; -. DR GenomeRNAi; 550; -. DR Pharos; Q9Y679; Tbio. DR PRO; PR:Q9Y679; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9Y679; Protein. DR Bgee; ENSG00000115307; Expressed in granulocyte and 200 other cell types or tissues. DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB. DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB. DR GO; GO:0034389; P:lipid droplet organization; IDA:UniProtKB. DR GO; GO:0061724; P:lipophagy; IMP:UniProtKB. DR GO; GO:1990044; P:protein localization to lipid droplet; IDA:UniProtKB. DR GO; GO:0009615; P:response to virus; IMP:UniProtKB. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB. DR CDD; cd14420; CUE_AUP1; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR048056; AUP1_CUE. DR InterPro; IPR003892; CUE. DR PANTHER; PTHR15486; ANCIENT UBIQUITOUS PROTEIN; 1. DR PANTHER; PTHR15486:SF49; LIPID DROPLET-REGULATING VLDL ASSEMBLY FACTOR AUP1; 1. DR Pfam; PF02845; CUE; 1. DR SMART; SM00546; CUE; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. DR PROSITE; PS51140; CUE; 1. DR Genevisible; Q9Y679; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle; KW Endoplasmic reticulum; Host-virus interaction; Lipid droplet; Membrane; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..410 FT /note="Lipid droplet-regulating VLDL assembly factor AUP1" FT /id="PRO_0000020765" FT TOPO_DOM 1..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:21127063, FT ECO:0000305|PubMed:23197321" FT INTRAMEM 21..41 FT /evidence="ECO:0000305|PubMed:21127063, FT ECO:0000305|PubMed:23197321" FT TOPO_DOM 42..410 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:21127063, FT ECO:0000305|PubMed:23197321" FT DOMAIN 296..338 FT /note="CUE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468" FT REGION 255..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 350..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 367 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT VAR_SEQ 360..373 FT /note="FPSSGPVTPQPTAL -> AFDACLMMMTPQAL (in isoform 2)" FT /id="VSP_059683" FT VAR_SEQ 374..410 FT /note="Missing (in isoform 2)" FT /id="VSP_059684" FT MUTAGEN 33..35 FT /note="PVG->LLL: Disrupts topology with the N-terminus in FT the lumen instead of the cytoplasm. Abolishes lipid droplet FT localization and lipid droplet clustering." FT /evidence="ECO:0000269|PubMed:23197321, FT ECO:0000269|PubMed:24039768" FT MUTAGEN 42 FT /note="R->I: Abolishes lipid droplet localization." FT /evidence="ECO:0000269|PubMed:23197321" FT MUTAGEN 58 FT /note="D->I: Does not affect lipid droplet localization." FT /evidence="ECO:0000269|PubMed:23197321" FT MUTAGEN 62..63 FT /note="RR->FF: Abolishes lipid droplet localization." FT /evidence="ECO:0000269|PubMed:23197321" FT MUTAGEN 96 FT /note="H->A: Reduced formation of lipid droplets." FT /evidence="ECO:0000269|PubMed:21857022" FT MUTAGEN 306..308 FT /note="EVL->KAA: Reduced interaction with ER quality FT control machinery and misfolded substrates; when associated FT with 333-L-L-334 Del." FT /evidence="ECO:0000269|PubMed:21857022" FT MUTAGEN 307..309 FT /note="VLP->GGR: Reduced lipid droplet clustering." FT /evidence="ECO:0000269|PubMed:24039768" FT MUTAGEN 316 FT /note="I->R: Reduced lipid droplet clustering; when FT associated with 319-V-E-320 and 333-E-D-334." FT /evidence="ECO:0000269|PubMed:24039768" FT MUTAGEN 319..320 FT /note="DL->VE: Reduced lipid droplet clustering; when FT associated with R-316 and 333-E-D-334." FT /evidence="ECO:0000269|PubMed:24039768" FT MUTAGEN 329..330 FT /note="TI->AD: Reduced lipid droplet clustering." FT /evidence="ECO:0000269|PubMed:24039768" FT MUTAGEN 333..334 FT /note="LL->ED: Reduced lipid droplet clustering; when FT associated with R-316 and 319-V-E-320." FT /evidence="ECO:0000269|PubMed:24039768" FT MUTAGEN 333..334 FT /note="Missing: Reduced interaction with ER quality control FT machinery and misfolded substrates; when associated with FT 306-K--A-308." FT /evidence="ECO:0000269|PubMed:21857022" FT MUTAGEN 382 FT /note="R->A: Significantly reduced interaction with FT UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 383 FT /note="Q->A: Significantly reduced interaction with FT UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 384 FT /note="E->A: No effect on interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 386 FT /note="L->A: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 388 FT /note="E->A: No effect on interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 389 FT /note="R->A: Significantly reduced interaction with FT UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 390 FT /note="K->A: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 393 FT /note="L->A: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 397..402 FT /note="ARRRFT->EGREDA: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:21127063" FT MUTAGEN 398 FT /note="R->A: Significantly reduced interaction with FT UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 399 FT /note="R->A: No effect on interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 400 FT /note="R->A: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 404 FT /note="R->A: Abolishes interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 408 FT /note="E->A: Significantly reduced interaction with FT UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT MUTAGEN 410 FT /note="D->A: No effect on interaction with UBE2G2." FT /evidence="ECO:0000269|PubMed:23223569" FT CONFLICT 288 FT /note="S -> P (in Ref. 3; AAD43010)" FT /evidence="ECO:0000305" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:2EKF" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:2EKF" FT HELIX 313..321 FT /evidence="ECO:0007829|PDB:2EKF" FT HELIX 326..334 FT /evidence="ECO:0007829|PDB:2EKF" FT HELIX 379..402 FT /evidence="ECO:0007829|PDB:7LEW" SQ SEQUENCE 410 AA; 45787 MW; 1A06476225C5DFDC CRC64; MELPSGPGPE RLFDSHRLPG DCFLLLVLLL YAPVGFCLLV LRLFLGIHVF LVSCALPDSV LRRFVVRTMC AVLGLVARQE DSGLRDHSVR VLISNHVTPF DHNIVNLLTT CSTPLLNSPP SFVCWSRGFM EMNGRGELVE SLKRFCASTR LPPTPLLLFP EEEATNGREG LLRFSSWPFS IQDVVQPLTL QVQRPLVSVT VSDASWVSEL LWSLFVPFTV YQVRWLRPVH RQLGEANEEF ALRVQQLVAK ELGQTGTRLT PADKAEHMKR QRHPRLRPQS AQSSFPPSPG PSPDVQLATL AQRVKEVLPH VPLGVIQRDL AKTGCVDLTI TNLLEGAVAF MPEDITKGTQ SLPTASASKF PSSGPVTPQP TALTFAKSSW ARQESLQERK QALYEYARRR FTERRAQEAD //