PYM1_HUMAN
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 03-AUG-2022, entry version 148.
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}.
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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; 144.
DR CORUM; Q9BRP8; -.
DR DIP; DIP-48413N; -.
DR IntAct; Q9BRP8; 45.
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; Q9BRP8; -.
DR PeptideAtlas; Q9BRP8; -.
DR PRIDE; Q9BRP8; -.
DR ProteomicsDB; 78798; -. [Q9BRP8-1]
DR ProteomicsDB; 78799; -. [Q9BRP8-2]
DR Antibodypedia; 48574; 218 antibodies from 19 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 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; 1545729at2759; -.
DR PhylomeDB; Q9BRP8; -.
DR TreeFam; TF324615; -.
DR PathwayCommons; Q9BRP8; -.
DR SignaLink; Q9BRP8; -.
DR BioGRID-ORCS; 84305; 318 hits in 1077 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 180 other tissues.
DR ExpressionAtlas; Q9BRP8; baseline and differential.
DR Genevisible; Q9BRP8; HS.
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; PTHR22959; 1.
DR Pfam; PF09282; Mago-bind; 1.
DR SMART; SM01273; Mago-bind; 1.
DR SUPFAM; SSF101931; SSF101931; 1.
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
