ID PYM1_HUMAN Reviewed; 204 AA. AC Q9BRP8; B6ZDM5; Q8IXJ8; Q8N8E7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804}; DE AltName: Full=PYM homolog 1 exon junction complex-associated factor {ECO:0000312|HGNC:HGNC:30258}; DE AltName: Full=Protein wibg homolog; GN Name=PYM1 {ECO:0000312|HGNC:HGNC:30258}; Synonyms=PYM, WIBG; 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). RX PubMed=12438415; DOI=10.1083/jcb.200207128; RA Gatfield D., Izaurralde E.; RT "REF1/Aly and the additional exon junction complex proteins are dispensable RT for nuclear mRNA export."; RL J. Cell Biol. 159:579-588(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell, and Pancreas; 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 SUBCELLULAR LOCATION, INTERACTION WITH MAGOH AND RBM8A, AND RNA-BINDING. RX PubMed=14968132; DOI=10.1038/sj.embor.7400091; RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.; RT "Molecular insights into the interaction of PYM with the Mago-Y14 core of RT the exon junction complex."; RL EMBO Rep. 5:304-310(2004). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN EIF2A-LIKE, AND INTERACTION WITH RP MAGOH; RBM8A AND RIBOSOME. RX PubMed=18026120; DOI=10.1038/nsmb1321; RA Diem M.D., Chan C.C., Younis I., Dreyfuss G.; RT "PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance RT translation of spliced mRNAs."; RL Nat. Struct. Mol. Biol. 14:1173-1179(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-72, AND RP 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 [8] 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 [9] RP FUNCTION, AND INTERACTION WITH MAGOH; RBM8A AND RIBOSOME. RX PubMed=19410547; DOI=10.1016/j.cell.2009.02.042; RA Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.; RT "Disassembly of exon junction complexes by PYM."; RL Cell 137:536-548(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-117, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13] RP IDENTIFICATION BY 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). CC -!- FUNCTION: Key regulator of the exon junction complex (EJC), a CC multiprotein complex that associates immediately upstream of the exon- CC exon junction on mRNAs and serves as a positional landmark for the CC intron exon structure of genes and directs post-transcriptional CC processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA CC decay (NMD) or translation. Acts as an EJC disassembly factor, allowing CC translation-dependent EJC removal and recycling by disrupting mature CC EJC from spliced mRNAs. Its association with the 40S ribosomal subunit CC probably prevents a translation-independent disassembly of the EJC from CC spliced mRNAs, by restricting its activity to mRNAs that have been CC translated. Interferes with NMD and enhances translation of spliced CC mRNAs, probably by antagonizing EJC functions. May bind RNA; the CC relevance of RNA-binding remains unclear in vivo, RNA-binding was CC detected by PubMed:14968132, while PubMed:19410547 did not detect RNA- CC binding activity independently of the EJC. CC {ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19410547}. CC -!- SUBUNIT: Interacts (via N-terminus) with MAGOH and RBM8A; the CC interaction is direct. Associates (eIF2A-like region) with the 40S CC ribosomal subunit and the 48S preinitiation complex. CC {ECO:0000269|PubMed:14968132, ECO:0000269|PubMed:18026120, CC ECO:0000269|PubMed:19410547}. CC -!- INTERACTION: CC Q9BRP8; P61326: MAGOH; NbExp=16; IntAct=EBI-2352802, EBI-299134; CC Q9BRP8; Q9NUX5: POT1; NbExp=2; IntAct=EBI-2352802, EBI-752420; CC Q9BRP8; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-2352802, EBI-743502; CC Q9BRP8; B2R9Y1; NbExp=3; IntAct=EBI-2352802, EBI-10175746; CC Q9BRP8; Q68842: HCV core; Xeno; NbExp=2; IntAct=EBI-2352802, EBI-11687770; CC Q9BRP8; Q2HR75: ORF57; Xeno; NbExp=4; IntAct=EBI-2352802, EBI-6884751; CC Q9BRP8; PRO_0000045592 [Q99IB8]; Xeno; NbExp=4; IntAct=EBI-2352802, EBI-6858513; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14968132, CC ECO:0000269|PubMed:18026120}. Nucleus, nucleolus CC {ECO:0000269|PubMed:14968132}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:14968132}. Note=Shuttles between the nucleus and CC the cytoplasm (PubMed:14968132). Nuclear export is mediated by CC XPO1/CRM1 (PubMed:14968132). {ECO:0000269|PubMed:14968132}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BRP8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRP8-2; Sequence=VSP_025430; CC -!- DOMAIN: The eIF2A-like region shares sequence similarity with eIF2A and CC mediates the interaction with the 40S ribosomal subunit and the 48S CC preinitiation complex. {ECO:0000269|PubMed:18026120}. CC -!- SIMILARITY: Belongs to the pym 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; AJ459406; CAD30677.1; -; mRNA. DR EMBL; AK096922; BAC04897.1; -; mRNA. DR EMBL; AC023055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006135; AAH06135.1; -; mRNA. DR EMBL; BC014976; AAH14976.1; -; mRNA. DR CCDS; CCDS41795.1; -. [Q9BRP8-1] DR CCDS; CCDS44916.1; -. [Q9BRP8-2] DR RefSeq; NP_001137325.1; NM_001143853.1. [Q9BRP8-2] DR RefSeq; NP_115721.1; NM_032345.2. [Q9BRP8-1] DR AlphaFoldDB; Q9BRP8; -. DR SMR; Q9BRP8; -. DR BioGRID; 124031; 170. DR CORUM; Q9BRP8; -. DR DIP; DIP-48413N; -. DR IntAct; Q9BRP8; 46. DR MINT; Q9BRP8; -. DR STRING; 9606.ENSP00000386156; -. DR iPTMnet; Q9BRP8; -. DR MetOSite; Q9BRP8; -. DR PhosphoSitePlus; Q9BRP8; -. DR BioMuta; PYM1; -. DR EPD; Q9BRP8; -. DR jPOST; Q9BRP8; -. DR MassIVE; Q9BRP8; -. DR MaxQB; Q9BRP8; -. DR PaxDb; 9606-ENSP00000386156; -. DR PeptideAtlas; Q9BRP8; -. DR ProteomicsDB; 78798; -. [Q9BRP8-1] DR ProteomicsDB; 78799; -. [Q9BRP8-2] DR Pumba; Q9BRP8; -. DR Antibodypedia; 48574; 261 antibodies from 20 providers. DR DNASU; 84305; -. DR Ensembl; ENST00000398213.4; ENSP00000381271.4; ENSG00000170473.17. [Q9BRP8-2] DR Ensembl; ENST00000408946.7; ENSP00000386156.2; ENSG00000170473.17. [Q9BRP8-1] DR GeneID; 84305; -. DR KEGG; hsa:84305; -. DR MANE-Select; ENST00000408946.7; ENSP00000386156.2; NM_032345.3; NP_115721.1. DR UCSC; uc001sie.2; human. [Q9BRP8-1] DR AGR; HGNC:30258; -. DR CTD; 84305; -. DR DisGeNET; 84305; -. DR GeneCards; PYM1; -. DR HGNC; HGNC:30258; PYM1. DR HPA; ENSG00000170473; Low tissue specificity. DR MIM; 619753; gene. DR neXtProt; NX_Q9BRP8; -. DR OpenTargets; ENSG00000170473; -. DR PharmGKB; PA142670574; -. DR VEuPathDB; HostDB:ENSG00000170473; -. DR eggNOG; KOG4325; Eukaryota. DR GeneTree; ENSGT00730000111107; -. DR HOGENOM; CLU_074603_3_0_1; -. DR InParanoid; Q9BRP8; -. DR OMA; IPGCADS; -. DR OrthoDB; 1216579at2759; -. DR PhylomeDB; Q9BRP8; -. DR TreeFam; TF324615; -. DR PathwayCommons; Q9BRP8; -. DR SignaLink; Q9BRP8; -. DR BioGRID-ORCS; 84305; 335 hits in 1148 CRISPR screens. DR ChiTaRS; PYM1; human. DR GenomeRNAi; 84305; -. DR Pharos; Q9BRP8; Tbio. DR PRO; PR:Q9BRP8; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9BRP8; Protein. DR Bgee; ENSG00000170473; Expressed in lower esophagus mucosa and 182 other cell types or tissues. DR ExpressionAtlas; Q9BRP8; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:1903259; P:exon-exon junction complex disassembly; IDA:HGNC. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB. DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB. DR InterPro; IPR039333; PYM1. DR InterPro; IPR015362; WIBG_mago-bd. DR InterPro; IPR036348; WIBG_N_sf. DR PANTHER; PTHR22959:SF0; PARTNER OF Y14 AND MAGO; 1. DR PANTHER; PTHR22959; PYM PROTEIN; 1. DR Pfam; PF09282; Mago-bind; 1. DR SMART; SM01273; Mago-bind; 1. DR SUPFAM; SSF101931; Pym (Within the bgcn gene intron protein, WIBG), N-terminal domain; 1. DR Genevisible; Q9BRP8; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; Translation regulation. FT CHAIN 1..204 FT /note="Partner of Y14 and mago" FT /id="PRO_0000287285" FT REGION 1..33 FT /note="Required for interaction with MAGOH and RBM8A" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 55..151 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 152..204 FT /note="eIF2A-like" FT COILED 82..116 FT /evidence="ECO:0000255" FT COILED 145..204 FT /evidence="ECO:0000255" FT COMPBIAS 97..114 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 116..145 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 72 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..12 FT /note="MEAAGSPAATET -> MATPYVTDETG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025430" FT VARIANT 66 FT /note="E -> Q (in dbSNP:rs3802998)" FT /id="VAR_032297" FT CONFLICT 147 FT /note="T -> S (in Ref. 1; CAD30677)" FT /evidence="ECO:0000305" SQ SEQUENCE 204 AA; 22656 MW; 087B901279007C05 CRC64; MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGL //