UFD1_HUMAN
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 03-AUG-2022, entry version 181.
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 DDX58/RIG-I and recruits RNF125 to promote ubiquitination and
CC degradation of DDX58/RIG-I (PubMed:26471729).
CC {ECO:0000250|UniProtKB:Q9ES53, 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=8; IntAct=EBI-1994090, EBI-1994109;
CC Q92890; P55072: VCP; NbExp=5; 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}.
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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_001035247.2. [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 PDBsum; 2YUJ; -.
DR PDBsum; 5B6C; -.
DR PDBsum; 5C1B; -.
DR AlphaFoldDB; Q92890; -.
DR SMR; Q92890; -.
DR BioGRID; 113200; 144.
DR ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex.
DR CORUM; Q92890; -.
DR DIP; DIP-45954N; -.
DR IntAct; Q92890; 43.
DR MINT; Q92890; -.
DR STRING; 9606.ENSP00000263202; -.
DR MoonDB; Q92890; Predicted.
DR GlyGen; Q92890; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92890; -.
DR PhosphoSitePlus; Q92890; -.
DR BioMuta; UFD1; -.
DR DMDM; 160332310; -.
DR OGP; Q92890; -.
DR EPD; Q92890; -.
DR jPOST; Q92890; -.
DR MassIVE; Q92890; -.
DR MaxQB; Q92890; -.
DR PaxDb; Q92890; -.
DR PeptideAtlas; Q92890; -.
DR PRIDE; Q92890; -.
DR ProteomicsDB; 2220; -.
DR ProteomicsDB; 75576; -. [Q92890-2]
DR ProteomicsDB; 75577; -. [Q92890-1]
DR Antibodypedia; 22930; 377 antibodies from 32 providers.
DR DNASU; 7353; -.
DR Ensembl; ENST00000263202.15; ENSP00000263202.9; ENSG00000070010.19. [Q92890-2]
DR Ensembl; ENST00000399523.5; ENSP00000382439.1; ENSG00000070010.19. [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 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 neXtProt; NX_Q92890; -.
DR OpenTargets; ENSG00000070010; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA37167; -.
DR VEuPathDB; HostDB:ENSG00000070010; -.
DR eggNOG; KOG1816; Eukaryota.
DR GeneTree; ENSGT00390000002408; -.
DR HOGENOM; CLU_037790_2_0_1; -.
DR InParanoid; Q92890; -.
DR OMA; NIEYPMI; -.
DR PhylomeDB; Q92890; -.
DR TreeFam; TF314581; -.
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 BioGRID-ORCS; 7353; 784 hits in 1092 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 211 other tissues.
DR ExpressionAtlas; Q92890; baseline and differential.
DR Genevisible; Q92890; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0071712; P:ER-associated misfolded protein catabolic process; 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:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 2.40.40.50; -; 1.
DR InterPro; IPR004854; Ufd1-like.
DR InterPro; IPR042299; Ufd1-like_Nn.
DR PANTHER; PTHR12555; PTHR12555; 1.
DR Pfam; PF03152; UFD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; 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..258
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"
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
