HYOU1_HUMAN
ID HYOU1_HUMAN Reviewed; 999 AA.
AC Q9Y4L1; A8C1Z0; B7Z909; Q2I204; Q53H25;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Hypoxia up-regulated protein 1;
DE AltName: Full=150 kDa oxygen-regulated protein;
DE Short=ORP-150;
DE AltName: Full=170 kDa glucose-regulated protein;
DE Short=GRP-170;
DE Flags: Precursor;
GN Name=HYOU1; Synonyms=GRP170, ORP150;
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=Astrocytoma;
RX PubMed=9020069; DOI=10.1006/bbrc.1996.5890;
RA Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T., Matsumoto M.,
RA Yura T., Yanagi H.;
RT "Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated
RT protein, ORP150.";
RL Biochem. Biophys. Res. Commun. 230:94-99(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10965054; DOI=10.1093/oxfordjournals.jbchem.a022783;
RA Kaneda S., Yura T., Yanagi H.;
RT "Production of three distinct mRNAs of 150 kDa oxygen-regulated protein
RT (ORP150) by alternative promoters: preferential induction of one species
RT under stress conditions.";
RL J. Biochem. 128:529-538(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=17131193; DOI=10.1007/s10930-006-9038-z;
RA Takeuchi S.;
RT "Molecular cloning, sequence, function and structural basis of human heart
RT 150 kDa oxygen-regulated protein, an ER chaperone.";
RL Protein J. 25:517-528(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Trachea;
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 MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
RP PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION.
RX PubMed=10037731; DOI=10.1074/jbc.274.10.6397;
RA Ozawa K., Kuwabara K., Tamatani M., Takatsuji K., Tsukamoto Y., Kaneda S.,
RA Yanagi H., Stern D.M., Eguchi Y., Tsujimoto Y., Ogawa S., Tohyama M.;
RT "150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced
RT apoptotic cell death.";
RL J. Biol. Chem. 274:6397-6404(1999).
RN [10]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [11]
RP GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND
RP ASN-931.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830; ASN-862
RP AND ASN-931.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER THR-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INVOLVEMENT IN IMD59, AND VARIANTS IMD59 HIS-231 AND PRO-419.
RX PubMed=27913302; DOI=10.1016/j.jaci.2016.09.050;
RA Haapaniemi E.M., Fogarty C.L., Keskitalo S., Katayama S., Vihinen H.,
RA Ilander M., Mustjoki S., Krjutskov K., Lehto M., Hautala T., Eriksson O.,
RA Jokitalo E., Velagapudi V., Varjosalo M., Seppaenen M., Kere J.;
RT "Combined immunodeficiency and hypoglycemia associated with mutations in
RT hypoxia upregulated 1.";
RL J. Allergy Clin. Immunol. 139:1391-1393(2017).
CC -!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
CC triggered by oxygen deprivation. May play a role as a molecular
CC chaperone and participate in protein folding.
CC {ECO:0000269|PubMed:10037731}.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX.
CC -!- INTERACTION:
CC Q9Y4L1; P11021: HSPA5; NbExp=2; IntAct=EBI-1054186, EBI-354921;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4L1-2; Sequence=VSP_056364, VSP_056365, VSP_056366;
CC -!- TISSUE SPECIFICITY: Highly expressed in tissues that contain well-
CC developed endoplasmic reticulum and synthesize large amounts of
CC secretory proteins. Highly expressed in liver and pancreas and lower
CC expression in brain and kidney. Also expressed in macrophages within
CC aortic atherosclerotic plaques, and in breast cancers.
CC -!- INDUCTION: By hypoxia and also by 2-deoxyglucose or tunicamycin.
CC -!- DISEASE: Immunodeficiency 59 and hypoglycemia (IMD59) [MIM:233600]: An
CC autosomal recessive primary immunologic disorder characterized by
CC combined immunodeficiency, granulocytopenia, B-cell and dendritic cell
CC deficiency, recurrent septic infections of the respiratory tract, skin
CC and mucous membranes, and disturbed glucose metabolism.
CC {ECO:0000269|PubMed:27913302}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U65785; AAC50947.1; -; mRNA.
DR EMBL; AB009979; BAF80348.1; -; Genomic_DNA.
DR EMBL; DQ350134; ABC75106.1; -; mRNA.
DR EMBL; DQ372932; ABD14370.1; -; mRNA.
DR EMBL; AK304264; BAH14145.1; -; mRNA.
DR EMBL; AK314178; BAG36860.1; -; mRNA.
DR EMBL; AK222756; BAD96476.1; -; mRNA.
DR EMBL; EF444986; ACA06002.1; -; Genomic_DNA.
DR EMBL; AP003392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS8408.1; -. [Q9Y4L1-1]
DR PIR; JC5278; JC5278.
DR RefSeq; NP_001124463.1; NM_001130991.2. [Q9Y4L1-1]
DR RefSeq; NP_006380.1; NM_006389.4. [Q9Y4L1-1]
DR RefSeq; XP_016872585.1; XM_017017096.1. [Q9Y4L1-1]
DR RefSeq; XP_016872586.1; XM_017017097.1. [Q9Y4L1-1]
DR AlphaFoldDB; Q9Y4L1; -.
DR SMR; Q9Y4L1; -.
DR BioGRID; 115780; 244.
DR IntAct; Q9Y4L1; 77.
DR MINT; Q9Y4L1; -.
DR STRING; 9606.ENSP00000480150; -.
DR ChEMBL; CHEMBL2216741; -.
DR TCDB; 3.A.16.1.4; the endoplasmic reticular retrotranslocon (er-rt) family.
DR CarbonylDB; Q9Y4L1; -.
DR GlyConnect; 1383; 47 N-Linked glycans (8 sites).
DR GlyGen; Q9Y4L1; 15 sites, 57 N-linked glycans (8 sites), 3 O-linked glycans (4 sites).
DR iPTMnet; Q9Y4L1; -.
DR MetOSite; Q9Y4L1; -.
DR PhosphoSitePlus; Q9Y4L1; -.
DR SwissPalm; Q9Y4L1; -.
DR BioMuta; HYOU1; -.
DR DMDM; 10720185; -.
DR REPRODUCTION-2DPAGE; IPI00000877; -.
DR CPTAC; CPTAC-2220; -.
DR CPTAC; CPTAC-2599; -.
DR EPD; Q9Y4L1; -.
DR jPOST; Q9Y4L1; -.
DR MassIVE; Q9Y4L1; -.
DR MaxQB; Q9Y4L1; -.
DR PaxDb; Q9Y4L1; -.
DR PeptideAtlas; Q9Y4L1; -.
DR PRIDE; Q9Y4L1; -.
DR ProteomicsDB; 6996; -.
DR ProteomicsDB; 86227; -. [Q9Y4L1-1]
DR Antibodypedia; 32575; 518 antibodies from 38 providers.
DR DNASU; 10525; -.
DR Ensembl; ENST00000617285.5; ENSP00000480150.1; ENSG00000149428.20. [Q9Y4L1-1]
DR Ensembl; ENST00000630669.3; ENSP00000486825.1; ENSG00000280682.3. [Q9Y4L1-1]
DR GeneID; 10525; -.
DR KEGG; hsa:10525; -.
DR MANE-Select; ENST00000617285.5; ENSP00000480150.1; NM_006389.5; NP_006380.1.
DR UCSC; uc031yhc.2; human. [Q9Y4L1-1]
DR CTD; 10525; -.
DR DisGeNET; 10525; -.
DR GeneCards; HYOU1; -.
DR HGNC; HGNC:16931; HYOU1.
DR HPA; ENSG00000149428; Tissue enhanced (liver).
DR MalaCards; HYOU1; -.
DR MIM; 233600; phenotype.
DR MIM; 601746; gene.
DR neXtProt; NX_Q9Y4L1; -.
DR OpenTargets; ENSG00000149428; -.
DR PharmGKB; PA38427; -.
DR VEuPathDB; HostDB:ENSG00000149428; -.
DR eggNOG; KOG0104; Eukaryota.
DR GeneTree; ENSGT00940000157686; -.
DR InParanoid; Q9Y4L1; -.
DR OrthoDB; 708294at2759; -.
DR PhylomeDB; Q9Y4L1; -.
DR TreeFam; TF105048; -.
DR PathwayCommons; Q9Y4L1; -.
DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q9Y4L1; -.
DR SIGNOR; Q9Y4L1; -.
DR BioGRID-ORCS; 10525; 542 hits in 1092 CRISPR screens.
DR ChiTaRS; HYOU1; human.
DR GeneWiki; HYOU1; -.
DR GenomeRNAi; 10525; -.
DR Pharos; Q9Y4L1; Tbio.
DR PRO; PR:Q9Y4L1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y4L1; protein.
DR Bgee; ENSG00000149428; Expressed in islet of Langerhans and 96 other tissues.
DR ExpressionAtlas; Q9Y4L1; baseline and differential.
DR Genevisible; Q9Y4L1; HS.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; NAS:ParkinsonsUK-UCL.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; ISS:FlyBase.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:ParkinsonsUK-UCL.
DR GO; GO:0002931; P:response to ischemia; ISS:ParkinsonsUK-UCL.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Signal; Stress response.
FT SIGNAL 1..32
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 33..999
FT /note="Hypoxia up-regulated protein 1"
FT /id="PRO_0000013538"
FT REGION 578..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 996..999
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 578..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 883
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKR6"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056364"
FT VAR_SEQ 603..646
FT /note="EEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKGDAT -> MLFL
FT CPARLPQSKQAIDRFHTAVTCMEPPWGRRCRARPAWRLCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056365"
FT VAR_SEQ 647..999
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056366"
FT VARIANT 231
FT /note="Y -> H (in IMD59; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27913302"
FT /id="VAR_081773"
FT VARIANT 419
FT /note="A -> P (in IMD59; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27913302"
FT /id="VAR_081774"
FT CONFLICT 75
FT /note="K -> E (in Ref. 5; BAD96476)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="N -> D (in Ref. 5; BAD96476)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="M -> T (in Ref. 5; BAD96476)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="V -> A (in Ref. 5; BAD96476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 111335 MW; FCE0F292466AFAB9 CRC64;
MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF
PEHELTFDPQ RQTVHFQISS QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC
TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP
GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGIH SLKHNKRVLF SRMGPYPQRK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE KATEKENGDK
SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG VELVVLDLPD LPEDKLAQSV
QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST
WLEDEGVGAT TVMLKEKLAE LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR
LIPEMDQIFT EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED AEPISEPEKV
ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL
