ID UBAC2_HUMAN Reviewed; 344 AA. AC Q8NBM4; B3KNV7; Q0VAB5; Q5W0W6; Q5W0W9; Q6GQR2; Q6P4B0; Q8N2E8; Q96NW2; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 10-JUN-2026, entry version 177. DE RecName: Full=Ubiquitin-associated domain-containing protein 2; DE Short=UBA domain-containing protein 2; DE AltName: Full=Phosphoglycerate dehydrogenase-like protein 1; DE Flags: Precursor; GN Name=UBAC2; Synonyms=PHGDHL1; ORFNames=PSEC0110; 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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Brain; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo, and Placenta; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 54-344 (ISOFORM 1). RC TISSUE=Blood, and Placenta; 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 [5] RP FUNCTION, INTERACTION WITH FAF2, AND SUBCELLULAR LOCATION. RX PubMed=23297223; DOI=10.1073/pnas.1213738110; RA Olzmann J.A., Richter C.M., Kopito R.R.; RT "Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid RT droplet turnover."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1345-1350(2013). RN [6] RP FUNCTION, AND INTERACTION WITH LMBR1L. RX PubMed=31073040; DOI=10.1126/science.aau0812; RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J., RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M., RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y., RA Beutler B.; RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling."; RL Science 364:0-0(2019). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GABARAP; MAP1LC3A; RP MAP1LC3B; MAP1LC3C; ATG16L1; LAMP1 AND WIPI2, SUBUNIT, MOTIF LIR, RP PHOSPHORYLATION AT SER-223, PROTEOLYTIC DEGRDATION, AND MUTAGENESIS OF RP SER-223; TRP-275 AND LEU-278. RX PubMed=39284914; DOI=10.1038/s44318-024-00232-z; RA He X., He H., Hou Z., Wang Z., Shi Q., Zhou T., Wu Y., Qin Y., Wang J., RA Cai Z., Cui J., Jin S.; RT "ER-phagy restrains inflammatory responses through its receptor UBAC2."; RL EMBO J. 43:5057-5084(2024). CC -!- FUNCTION: Acts as an ER-phagy receptor required for the selective CC autophagic degradation of endoplasmic reticulum (ER) fragments to CC maintain ER homeostasis and restrain ER stress-induced inflammatory CC responses (PubMed:39284914). Its function depends on phosphorylation- CC induced dimerization, which enhances interaction with GABARAP and CC facilitates recruitment of ER fragments to autophagosomes CC (PubMed:39284914). Restricts trafficking of FAF2 from the endoplasmic CC reticulum to lipid droplets (PubMed:23297223). In association with CC LMBR1L and E3 ubiquitin-protein ligase AMFR, negatively regulates the CC canonical Wnt signaling pathway in the lymphocytes by promoting the CC ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and CC LRP6 (PubMed:31073040). {ECO:0000269|PubMed:23297223, CC ECO:0000269|PubMed:31073040, ECO:0000269|PubMed:39284914}. CC -!- SUBUNIT: Homodimer; phosphorylation promotes dimerization CC (PubMed:39284914). Interacts with FAF2; the interaction restricts CC trafficking of FAF2 from the endoplasmic reticulum to lipid droplets CC (PubMed:23297223). Interacts with LMBR1L (PubMed:31073040). Interacts CC with AMFR and VCP (By similarity). The Ser-223 phosphorylated form CC interacts (via the LIR motif) with GABARAP (PubMed:39284914). Interacts CC with MAP1LC3A, MAP1LC3B and MAP1LC3C (PubMed:39284914). Interacts with CC ATG16L1, LAMP1 and WIPI2; interaction increases upon the activation of CC starvation-induced autophagy (PubMed:39284914). CC {ECO:0000250|UniProtKB:Q8R1K1, ECO:0000269|PubMed:23297223, CC ECO:0000269|PubMed:39284914, ECO:0000305|PubMed:31073040}. CC -!- INTERACTION: CC Q8NBM4; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-724045, EBI-739580; CC Q8NBM4; Q96CS3: FAF2; NbExp=8; IntAct=EBI-724045, EBI-1055805; CC Q8NBM4-4; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25840976, EBI-25840379; CC Q8NBM4-4; P04792: HSPB1; NbExp=3; IntAct=EBI-25840976, EBI-352682; CC Q8NBM4-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25840976, EBI-10975473; CC Q8NBM4-4; O60260-5: PRKN; NbExp=3; IntAct=EBI-25840976, EBI-21251460; CC Q8NBM4-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25840976, EBI-396669; CC Q8NBM4-4; O76024: WFS1; NbExp=3; IntAct=EBI-25840976, EBI-720609; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:23297223, ECO:0000269|PubMed:39284914}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8NBM4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NBM4-2; Sequence=VSP_023911, VSP_023912; CC Name=3; CC IsoId=Q8NBM4-3; Sequence=VSP_023910; CC Name=4; CC IsoId=Q8NBM4-4; Sequence=VSP_023909; CC Name=5; CC IsoId=Q8NBM4-5; Sequence=VSP_023913, VSP_023914; CC -!- PTM: Phosphorylation at Ser-223 by MARK2 upon ER stress or autophagy CC induction promotes UBAC2 dimerization and interaction with GABARAP, CC which is essential for ER-phagy. {ECO:0000269|PubMed:39284914}. CC -!- PTM: Undergoes autophagic proteolytic degradation upon nutrient CC deprivation or ER stress-induced autophagic conditions. CC {ECO:0000269|PubMed:39284914}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH72674.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI21139.1; 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; AK054563; BAB70757.1; -; mRNA. DR EMBL; AK055110; BAG51469.1; -; mRNA. DR EMBL; AK075419; BAC11609.1; -; mRNA. DR EMBL; AK075516; BAC11665.1; -; mRNA. DR EMBL; AL136961; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL159981; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL160155; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063559; AAH63559.1; -; mRNA. DR EMBL; BC072674; AAH72674.1; ALT_INIT; mRNA. DR EMBL; BC121138; AAI21139.1; ALT_INIT; mRNA. DR EMBL; BC121139; AAI21140.1; -; mRNA. DR CCDS; CCDS45064.1; -. [Q8NBM4-1] DR CCDS; CCDS9490.1; -. [Q8NBM4-2] DR RefSeq; NP_001137544.1; NM_001144072.2. [Q8NBM4-1] DR RefSeq; NP_808882.1; NM_177967.4. [Q8NBM4-2] DR RefSeq; XP_047286242.1; XM_047430286.1. [Q8NBM4-3] DR RefSeq; XP_054230464.1; XM_054374489.1. [Q8NBM4-3] DR AlphaFoldDB; Q8NBM4; -. DR SMR; Q8NBM4; -. DR BioGRID; 130617; 254. DR FunCoup; Q8NBM4; 1490. DR IntAct; Q8NBM4; 154. DR MINT; Q8NBM4; -. DR STRING; 9606.ENSP00000383911; -. DR GlyCosmos; Q8NBM4; 1 site, No reported glycans. DR GlyGen; Q8NBM4; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q8NBM4; -. DR PhosphoSitePlus; Q8NBM4; -. DR SwissPalm; Q8NBM4; -. DR BioMuta; UBAC2; -. DR DMDM; 74751173; -. DR jPOST; Q8NBM4; -. DR MassIVE; Q8NBM4; -. DR PaxDb; 9606-ENSP00000383911; -. DR PeptideAtlas; Q8NBM4; -. DR ProteomicsDB; 72792; -. [Q8NBM4-1] DR ProteomicsDB; 72793; -. [Q8NBM4-2] DR ProteomicsDB; 72794; -. [Q8NBM4-3] DR ProteomicsDB; 72795; -. [Q8NBM4-4] DR ProteomicsDB; 72796; -. [Q8NBM4-5] DR Pumba; Q8NBM4; -. DR Antibodypedia; 10857; 99 antibodies from 20 providers. DR DNASU; 337867; -. DR Ensembl; ENST00000376440.6; ENSP00000365623.2; ENSG00000134882.17. [Q8NBM4-2] DR Ensembl; ENST00000403766.8; ENSP00000383911.3; ENSG00000134882.17. [Q8NBM4-1] DR GeneID; 337867; -. DR KEGG; hsa:337867; -. DR MANE-Select; ENST00000403766.8; ENSP00000383911.3; NM_001144072.2; NP_001137544.1. DR UCSC; uc001voa.5; human. [Q8NBM4-1] DR AGR; HGNC:20486; -. DR ClinPGx; PA162407839; -. DR CTD; 337867; -. DR DisGeNET; 337867; -. DR GeneCards; UBAC2; -. DR HGNC; HGNC:20486; UBAC2. DR HPA; ENSG00000134882; Low tissue specificity. DR MalaCards; UBAC2; -. DR MIM; 621399; gene. DR OpenTargets; ENSG00000134882; -. DR Orphanet; 117; Behcet disease. DR VEuPathDB; HostDB:ENSG00000134882; -. DR eggNOG; KOG4463; Eukaryota. DR GeneTree; ENSGT00950000182999; -. DR HOGENOM; CLU_057710_0_0_1; -. DR InParanoid; Q8NBM4; -. DR OMA; NYQDHRP; -. DR OrthoDB; 272778at2759; -. DR PAN-GO; Q8NBM4; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q8NBM4; -. DR PathwayCommons; Q8NBM4; -. DR SignaLink; Q8NBM4; -. DR Agora; ENSG00000134882; -. DR BioGRID-ORCS; 337867; 17 hits in 1154 CRISPR screens. DR ChiTaRS; UBAC2; human. DR GenomeRNAi; 337867; -. DR Pharos; Q8NBM4; Tbio. DR PRO; PR:Q8NBM4; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q8NBM4; protein. DR Bgee; ENSG00000134882; Expressed in lower esophagus mucosa and 171 other cell types or tissues. DR ExpressionAtlas; Q8NBM4; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IDA:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd14305; UBA_UBAC2; 1. DR FunFam; 1.20.1540.10:FF:000021; UBA domain containing 2; 1. DR FunFam; 1.10.8.10:FF:000074; Ubiquitin-associated domain-containing protein 2; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 1.20.1540.10; Rhomboid-like; 1. DR InterPro; IPR035952; Rhomboid-like_sf. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR041928; UBA_UBAC2. DR PANTHER; PTHR43066; RHOMBOID-RELATED PROTEIN; 1. DR PANTHER; PTHR43066:SF21; UBIQUITIN-ASSOCIATED DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF00627; UBA; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF144091; Rhomboid-like; 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW Alternative splicing; Autophagy; Endoplasmic reticulum; Glycoprotein; KW Membrane; Phosphoprotein; Proteomics identification; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT CHAIN 36..344 FT /note="Ubiquitin-associated domain-containing protein 2" FT /id="PRO_0000280754" FT TOPO_DOM 36..91 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 92..112 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 113..125 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 147..163 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 185..344 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 304..344 FT /note="UBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT MOTIF 275..278 FT /note="LIR" FT /evidence="ECO:0000269|PubMed:39284914" FT MOD_RES 223 FT /note="Phosphoserine; by MARK2" FT /evidence="ECO:0000269|PubMed:39284914" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..187 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_023909" FT VAR_SEQ 1..113 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023910" FT VAR_SEQ 1..35 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023911" FT VAR_SEQ 36..130 FT /note="HCQKLFVYDLHAVKNDFQIWRLICGRIICLDLKDTFCSSLLIYNFRIFERRY FT GSRKFASFLLGSWVLSALFDFLLIEAMQYFFGITAASNLPSGF -> MCFFFSLQEEFL FT DKHTLMRVLSSGGKLGSRGEGAQLCCWMLLFSWRVSGGQQTRRLCRRAFCWSPVPSPSC FT SPSSCLTARSSLCMTFTQSRTTSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023912" FT VAR_SEQ 54..141 FT /note="IWRLICGRIICLDLKDTFCSSLLIYNFRIFERRYGSRKFASFLLGSWVLSAL FT FDFLLIEAMQYFFGITAASNLPSGFLAPVFALFVPF -> PGTCVCSVCTILLLHTKSP FT SGTNSGSVVHHKQDIDLYIGTAAFHLWFLHLDCSHKWTYVRSVLRQQNVPGASGALHPQ FT LDGKILFLDT (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_023913" FT VAR_SEQ 142..344 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_023914" FT MUTAGEN 223 FT /note="S->A: Loss of phosphorylation leading to reduced FT dimerization, decreased GABARAP interaction, and impaired FT ER-phagy." FT /evidence="ECO:0000269|PubMed:39284914" FT MUTAGEN 223 FT /note="S->D: Phosphomimetic mutant. Increased dimerization FT and interaction with GABARAP and enhanced ER-phagy." FT /evidence="ECO:0000269|PubMed:39284914" FT MUTAGEN 275 FT /note="W->A: Loss of interaction with GABARAP; when FT associated with A-278." FT /evidence="ECO:0000269|PubMed:39284914" FT MUTAGEN 278 FT /note="L->A: Loss of interaction with GABARAP; when FT associated with A-275." FT /evidence="ECO:0000269|PubMed:39284914" SQ SEQUENCE 344 AA; 38964 MW; A8C5D4D68B64CEB3 CRC64; MFTSTGSSGL YKAPLSKSLL LVPSALSLLL ALLLPHCQKL FVYDLHAVKN DFQIWRLICG RIICLDLKDT FCSSLLIYNF RIFERRYGSR KFASFLLGSW VLSALFDFLL IEAMQYFFGI TAASNLPSGF LAPVFALFVP FYCSIPRVQV AQILGPLSIT NKTLIYILGL QLFTSGSYIW IVAISGLMSG LCYDSKMFQV HQVLCIPSWM AKFFSWTLEP IFSSSEPTSE ARIGMGATLD IQRQQRMELL DRQLMFSQFA QGRRQRQQQG GMINWNRLFP PLRQRQNVNY QGGRQSEPAA PPLEVSEEQV ARLMEMGFSR GDALEALRAS NNDLNVATNF LLQH //