ID UFD1_HUMAN Reviewed; 307 AA. AC Q92890; A8MW31; Q9Y5N0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 3. DT 28-JAN-2026, entry version 198. DE RecName: Full=Ubiquitin recognition factor in ER-associated degradation protein 1 {ECO:0000312|HGNC:HGNC:12520}; DE AltName: Full=Ubiquitin fusion degradation protein 1; DE Short=UB fusion protein 1; GN Name=UFD1 {ECO:0000312|HGNC:HGNC:12520}; Synonyms=UFD1L; 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] (ISOFORMS LONG AND SHORT), AND VARIANT ALA-130. RC TISSUE=Brain; RX PubMed=9063746; DOI=10.1093/hmg/6.2.259; RA Pizzuti A., Novelli G., Ratti A., Amati F., Mari A., Calabrese G., RA Nicolis S., Silani V., Marino B., Scarlato G., Ottolenghi S., RA Dallapiccola B.; RT "UFD1L, a developmentally expressed ubiquitination gene, is deleted in RT CATCH 22 syndrome."; RL Hum. Mol. Genet. 6:259-265(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RC TISSUE=Heart; RA Gong L., Yeh E.T.H.; RT "Characterization of human UFD1, a ubiquitin fusion-degradation protein."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC TISSUE=Brain, 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 INTERACTION WITH NPLOC4. RX PubMed=11574150; DOI=10.1016/s0378-1119(01)00649-7; RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B., Novelli G.; RT "Cloning and characterization of the gene encoding human NPL4, a protein RT interacting with the ubiquitin fusion-degradation protein (UFD1L)."; RL Gene 275:39-46(2001). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-245; SER-247 AND RP SER-299, AND IDENTIFICATION BY 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 [12] 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 [13] RP INTERACTION WITH USP13. RX PubMed=21571647; DOI=10.1073/pnas.1100028108; RA Chen M., Gutierrez G.J., Ronai Z.A.; RT "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) RT stress response to cell cycle control."; RL Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-231; SER-245; RP SER-247 AND SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [16] RP INTERACTION WITH ZFAND2B. RX PubMed=24160817; DOI=10.1042/bj20130710; RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S., RA Edelmann M.J., Kessler B.M., Stanhill A.; RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL RT complex."; RL Biochem. J. 457:253-261(2014). RN [17] RP FUNCTION, AND INTERACTION WITH NPLOC4 AND VCP. RX PubMed=26471729; DOI=10.15252/embj.201591888; RA Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X., RA Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.; RT "A non-canonical role of the p97 complex in RIG-I antiviral signaling."; RL EMBO J. 34:2903-2920(2015). RN [18] RP STRUCTURE BY NMR OF 11-193. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of human ubiquitin fusion degradation protein 1 homolog RT UFD1."; RL Submitted (APR-2008) to the PDB data bank. CC -!- FUNCTION: Essential component of the ubiquitin-dependent proteolytic CC pathway which degrades ubiquitin fusion proteins. The ternary complex CC containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is CC necessary for the export of misfolded proteins from the ER to the CC cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1- CC VCP complex regulates spindle disassembly at the end of mitosis and is CC necessary for the formation of a closed nuclear envelope. It may be CC involved in the development of some ectoderm-derived structures (By CC similarity). Acts as a negative regulator of type I interferon CC production via the complex formed with VCP and NPLOC4, which binds to CC RIGI and recruits RNF125 to promote ubiquitination and degradation of CC RIGI (PubMed:26471729). {ECO:0000250|UniProtKB:Q9ES53, CC ECO:0000269|PubMed:26471729}. CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway. CC {ECO:0000250|UniProtKB:Q9ES53}. CC -!- SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and CC inhibits Golgi membrane fusion (PubMed:11574150, PubMed:26471729). CC Interacts with USP13 (PubMed:21571647). Interacts with ZFAND2B; CC probably through VCP (PubMed:24160817). {ECO:0000269|PubMed:11574150, CC ECO:0000269|PubMed:21571647, ECO:0000269|PubMed:24160817, CC ECO:0000269|PubMed:26471729}. CC -!- INTERACTION: CC Q92890; P42858: HTT; NbExp=7; IntAct=EBI-1994090, EBI-466029; CC Q92890; Q8TAT6: NPLOC4; NbExp=10; IntAct=EBI-1994090, EBI-1994109; CC Q92890; P55072: VCP; NbExp=10; IntAct=EBI-1994090, EBI-355164; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ES53}. CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES53}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Short; CC IsoId=Q92890-2; Sequence=Displayed; CC Name=Long; CC IsoId=Q92890-1; Sequence=VSP_006707; CC Name=3; CC IsoId=Q92890-3; Sequence=VSP_045044; CC -!- TISSUE SPECIFICITY: Found in adult heart, skeletal muscle and pancreas, CC and in fetal liver and kidney. CC -!- MISCELLANEOUS: [Isoform Short]: Major isoform. CC -!- SIMILARITY: Belongs to the UFD1 family. {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; U64444; AAD08720.1; -; mRNA. DR EMBL; AF141201; AAD28788.1; -; mRNA. DR EMBL; CR456607; CAG30493.1; -; mRNA. DR EMBL; AK225877; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC000068; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC000087; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001049; AAH01049.1; -; mRNA. DR EMBL; BC005087; AAH05087.1; -; mRNA. DR CCDS; CCDS13761.1; -. [Q92890-2] DR CCDS; CCDS33600.2; -. [Q92890-3] DR RefSeq; NP_001030324.2; NM_001035247.3. [Q92890-3] DR RefSeq; NP_005650.2; NM_005659.6. [Q92890-2] DR PDB; 2YUJ; NMR; -; A=11-193. DR PDB; 5B6C; X-ray; 1.55 A; B=225-235. DR PDB; 5C1B; X-ray; 3.08 A; U/V=221-241. DR PDB; 7WWQ; X-ray; 2.72 A; B=258-273. DR PDBsum; 2YUJ; -. DR PDBsum; 5B6C; -. DR PDBsum; 5C1B; -. DR PDBsum; 7WWQ; -. DR AlphaFoldDB; Q92890; -. DR SMR; Q92890; -. DR BioGRID; 113200; 178. DR ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex. DR ComplexPortal; CPX-8096; VCP-NPL4-UFD1-FAF1 AAA ATPase complex. DR ComplexPortal; CPX-8101; VCP-NPL4-UFD1-UBXN7 AAA ATPase complex. DR ComplexPortal; CPX-8104; VCP-NPL4-UFD1-FAF2 AAA ATPase complex. DR ComplexPortal; CPX-8105; VCP-NPL4-UFD1-UBXN1 AAA ATPase complex. DR CORUM; Q92890; -. DR DIP; DIP-45954N; -. DR FunCoup; Q92890; 4246. DR IntAct; Q92890; 73. DR MINT; Q92890; -. DR STRING; 9606.ENSP00000263202; -. DR MoonDB; Q92890; Predicted. DR GlyGen; Q92890; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q92890; -. DR PhosphoSitePlus; Q92890; -. DR BioMuta; UFD1; -. DR DMDM; 160332310; -. DR OGP; Q92890; -. DR jPOST; Q92890; -. DR MassIVE; Q92890; -. DR PaxDb; 9606-ENSP00000263202; -. DR PeptideAtlas; Q92890; -. DR ProteomicsDB; 2220; -. DR ProteomicsDB; 75576; -. [Q92890-2] DR ProteomicsDB; 75577; -. [Q92890-1] DR Pumba; Q92890; -. DR Antibodypedia; 22930; 393 antibodies from 33 providers. DR DNASU; 7353; -. DR Ensembl; ENST00000263202.15; ENSP00000263202.9; ENSG00000070010.20. [Q92890-2] DR Ensembl; ENST00000399523.5; ENSP00000382439.1; ENSG00000070010.20. [Q92890-3] DR GeneID; 7353; -. DR KEGG; hsa:7353; -. DR MANE-Select; ENST00000263202.15; ENSP00000263202.9; NM_005659.7; NP_005650.2. DR UCSC; uc002zpm.3; human. [Q92890-2] DR AGR; HGNC:12520; -. DR ClinPGx; PA37167; -. DR CTD; 7353; -. DR DisGeNET; 7353; -. DR GeneCards; UFD1; -. DR HGNC; HGNC:12520; UFD1. DR HPA; ENSG00000070010; Low tissue specificity. DR MalaCards; UFD1; -. DR MIM; 601754; gene. DR OpenTargets; ENSG00000070010; -. DR Orphanet; 567; 22q11.2 deletion syndrome. DR VEuPathDB; HostDB:ENSG00000070010; -. DR eggNOG; KOG1816; Eukaryota. DR GeneTree; ENSGT00390000002408; -. DR HOGENOM; CLU_037790_2_0_1; -. DR InParanoid; Q92890; -. DR OMA; WMMQQLC; -. DR OrthoDB; 422728at2759; -. DR PAN-GO; Q92890; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q92890; -. DR PathwayCommons; Q92890; -. DR Reactome; R-HSA-110320; Translesion Synthesis by POLH. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway. DR SignaLink; Q92890; -. DR SIGNOR; Q92890; -. DR UniPathway; UPA00144; -. DR Agora; ENSG00000070010; -. DR BioGRID-ORCS; 7353; 797 hits in 1175 CRISPR screens. DR ChiTaRS; UFD1L; human. DR EvolutionaryTrace; Q92890; -. DR GeneWiki; UFD1L; -. DR GenomeRNAi; 7353; -. DR Pharos; Q92890; Tbio. DR PRO; PR:Q92890; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q92890; protein. DR Bgee; ENSG00000070010; Expressed in tendon of biceps brachii and 213 other cell types or tissues. DR ExpressionAtlas; Q92890; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0036501; C:UFD1-NPL4 complex; IPI:ParkinsonsUK-UCL. DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; TAS:ProtInc. DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central. DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:ParkinsonsUK-UCL. DR GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:UniProtKB. DR GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR FunFam; 2.40.40.50:FF:000001; Ubiquitin fusion degradation protein 1 homolog; 1. DR FunFam; 3.10.330.10:FF:000002; ubiquitin fusion degradation protein 1 homolog; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 2.40.40.50; Ubiquitin fusion degradation protein UFD1, N-terminal domain; 1. DR InterPro; IPR004854; Ufd1-like. DR InterPro; IPR042299; Ufd1-like_Nn. DR InterPro; IPR055417; UFD1_N1. DR InterPro; IPR055418; UFD1_N2. DR PANTHER; PTHR12555; UBIQUITIN FUSION DEGRADATON PROTEIN 1; 1. DR PANTHER; PTHR12555:SF13; UBIQUITIN RECOGNITION FACTOR IN ER-ASSOCIATED DEGRADATION PROTEIN 1; 1. DR Pfam; PF03152; UFD1_N1; 1. DR Pfam; PF24842; UFD1_N2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..307 FT /note="Ubiquitin recognition factor in ER-associated FT degradation protein 1" FT /id="PRO_0000194984" FT REGION 231..256 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 288..307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 245 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 106 FT /note="E -> EDGLVQLETVNLQVATYSKSKFCYLPHWMMQNLLLEE (in FT isoform Long)" FT /evidence="ECO:0000303|PubMed:9063746" FT /id="VSP_006707" FT VAR_SEQ 267..307 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_045044" FT VARIANT 130 FT /note="P -> A (in dbSNP:rs17744624)" FT /evidence="ECO:0000269|PubMed:9063746" FT /id="VAR_052436" FT CONFLICT 25 FT /note="C -> R (in Ref. 4; AK225877)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="G -> W (in Ref. 1; AAD08720)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="I -> H (in Ref. 1; AAD08720)" FT /evidence="ECO:0000305" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 20..26 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:2YUJ" FT TURN 39..44 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:2YUJ" FT HELIX 50..58 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:2YUJ" FT TURN 72..75 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 76..84 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:2YUJ" FT HELIX 97..102 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:2YUJ" FT HELIX 130..134 FT /evidence="ECO:0007829|PDB:2YUJ" FT HELIX 138..146 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 166..181 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:2YUJ" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:7WWQ" SQ SEQUENCE 307 AA; 34500 MW; FC69860002C042C6 CRC64; MFSFNMFDHP IPRVFQNRFS TQYRCFSVSM LAGPNDRSDV EKGGKIIMPP SALDQLSRLN ITYPMLFKLT NKNSDRMTHC GVLEFVADEG ICYLPHWMMQ NLLLEEGGLV QVESVNLQVA TYSKFQPQSP DFLDITNPKA VLENALRNFA CLTTGDVIAI NYNEKIYELR VMETKPDKAV SIIECDMNVD FDAPLGYKEP ERQVQHEEST EGEADHSGYA GELGFRAFSG SGNRLDGKKK GVEPSPSPIK PGDIKRGIPN YEFKLGKITF IRNSRPLVKK VEEDEAGGRF VAFSGEGQSL RKKGRKP //