SMG8_HUMAN
ID SMG8_HUMAN Reviewed; 991 AA.
AC Q8ND04; Q8N5U5; Q8TDN0; Q9H5P5; Q9NVQ1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG8 {ECO:0000312|HGNC:HGNC:25551};
DE AltName: Full=Amplified in breast cancer gene 2 protein {ECO:0000303|Ref.1};
DE AltName: Full=Protein smg-8 homolog;
GN Name=SMG8; Synonyms=ABC2, C17orf71;
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 2).
RA Wu G.G., Couch F.J.;
RT "Cloning and characterization of three novel amplified and overexpressed
RT genes from breast cancer.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
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 MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-991 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-991 (ISOFORM 3).
RC TISSUE=Brain, and Colon;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, 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 [8]
RP FUNCTION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE SMG1C COMPLEX.
RX PubMed=19417104; DOI=10.1101/gad.1767209;
RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y.,
RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H.,
RA Anderson P., Ohno S.;
RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA
RT decay.";
RL Genes Dev. 23:1091-1105(2009).
RN [9]
RP 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 [10]
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 [11]
RP INTERACTION WITH SMG1 AND SMG9, AND ELECTRON MICROSCOPY OF THE SMG1C
RP COMPLEX.
RX PubMed=21245168; DOI=10.1101/gad.606911;
RA Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y.,
RA Izumi N., Ohno S., Llorca O.;
RT "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale
RT conformational changes controlled by SMG-8.";
RL Genes Dev. 25:153-164(2011).
RN [12]
RP SUBUNIT.
RX PubMed=20817927; DOI=10.1093/nar/gkq749;
RA Fernandez I.S., Yamashita A., Arias-Palomo E., Bamba Y., Bartolome R.A.,
RA Canales M.A., Teixido J., Ohno S., Llorca O.;
RT "Characterization of SMG-9, an essential component of the nonsense-mediated
RT mRNA decay SMG1C complex.";
RL Nucleic Acids Res. 39:347-358(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-668; SER-742 AND
RP SER-895, AND 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 [15]
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).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-898, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17]
RP INTERACTION WITH SMG1.
RX PubMed=33205750; DOI=10.7554/elife.63042;
RA Lopez-Perrote A., Hug N., Gonzalez-Corpas A., Rodriguez C.F., Serna M.,
RA Garcia-Martin C., Boskovic J., Fernandez-Leiro R., Caceres J.F., Llorca O.;
RT "Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA
RT decay factor DHX34, as evidenced by Cryo-EM.";
RL Elife 9:0-0(2020).
RN [18]
RP VARIANTS ALKUS ARG-208 AND 839-ARG--GLN-991 DEL, AND INVOLVEMENT IN ALKUS.
RX PubMed=33242396; DOI=10.1016/j.ajhg.2020.11.007;
RA Alzahrani F., Kuwahara H., Long Y., Al-Owain M., Tohary M., AlSayed M.,
RA Mahnashi M., Fathi L., Alnemer M., Al-Hamed M.H., Lemire G., Boycott K.M.,
RA Hashem M., Han W., Al-Maawali A., Al Mahrizi F., Al-Thihli K., Gao X.,
RA Alkuraya F.S.;
RT "Recessive, deleterious variants in SMG8 expand the role of nonsense-
RT mediated decay in developmental disorders in humans.";
RL Am. J. Hum. Genet. 107:1178-1185(2020).
CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing
CC premature stop codons. Is recruited by release factors to stalled
CC ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase
CC complex) and, in the SMG1C complex, is required to mediate the
CC recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1
CC kinase activity until the ribosome:SURF complex locates the exon
CC junction complex (EJC). Acts as a regulator of kinase activity.
CC {ECO:0000269|PubMed:19417104}.
CC -!- SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and
CC SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large
CC conformational change in the SMG1 C-terminal head domain containing the
CC catalytic domain (PubMed:33205750). Forms heterodimers with SMG9; this
CC assembly form may represent a SMG1C intermediate form.
CC {ECO:0000269|PubMed:19417104, ECO:0000269|PubMed:20817927,
CC ECO:0000269|PubMed:33205750}.
CC -!- INTERACTION:
CC Q8ND04; Q9H0W8: SMG9; NbExp=6; IntAct=EBI-3903643, EBI-2872322;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8ND04-1; Sequence=Displayed;
CC Name=2; Synonyms=ABC2;
CC IsoId=Q8ND04-2; Sequence=VSP_028166;
CC Name=3;
CC IsoId=Q8ND04-3; Sequence=VSP_028164, VSP_028165;
CC -!- PTM: Phosphorylated by SMG1. {ECO:0000269|PubMed:19417104}.
CC -!- DISEASE: Alzahrani-Kuwahara syndrome (ALKUS) [MIM:619268]: An autosomal
CC recessive disorder characterized by severe global developmental delay,
CC impaired intellectual function, poor or absent speech, microcephaly,
CC and facial dysmorphism. Additional variable features include early-
CC onset cataracts, hypotonia, lower limb spasticity, and congenital heart
CC malformations. {ECO:0000269|PubMed:33242396}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SMG8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91699.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF349467; AAL83913.1; -; mRNA.
DR EMBL; AK001449; BAA91699.1; ALT_INIT; mRNA.
DR EMBL; AK026858; BAB15576.1; -; mRNA.
DR EMBL; AL834490; CAD39148.1; -; mRNA.
DR EMBL; AC099850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94415.1; -; Genomic_DNA.
DR EMBL; BC020957; AAH20957.1; ALT_INIT; mRNA.
DR EMBL; BC031604; AAH31604.1; -; mRNA.
DR CCDS; CCDS11615.1; -. [Q8ND04-1]
DR RefSeq; NP_060619.4; NM_018149.6. [Q8ND04-1]
DR PDB; 6L54; EM; 3.43 A; B=1-991.
DR PDB; 6SYT; EM; 3.45 A; B=1-991.
DR PDB; 6Z3R; EM; 2.97 A; B=1-991.
DR PDB; 7PW4; EM; 3.27 A; B=1-991.
DR PDB; 7PW5; EM; 3.40 A; B=1-991.
DR PDB; 7PW8; EM; 2.82 A; B=1-991.
DR PDBsum; 6L54; -.
DR PDBsum; 6SYT; -.
DR PDBsum; 6Z3R; -.
DR PDBsum; 7PW4; -.
DR PDBsum; 7PW5; -.
DR PDBsum; 7PW8; -.
DR AlphaFoldDB; Q8ND04; -.
DR SMR; Q8ND04; -.
DR BioGRID; 120480; 120.
DR IntAct; Q8ND04; 24.
DR STRING; 9606.ENSP00000438748; -.
DR iPTMnet; Q8ND04; -.
DR PhosphoSitePlus; Q8ND04; -.
DR BioMuta; SMG8; -.
DR DMDM; 74715258; -.
DR EPD; Q8ND04; -.
DR jPOST; Q8ND04; -.
DR MassIVE; Q8ND04; -.
DR MaxQB; Q8ND04; -.
DR PaxDb; Q8ND04; -.
DR PeptideAtlas; Q8ND04; -.
DR PRIDE; Q8ND04; -.
DR ProteomicsDB; 72968; -. [Q8ND04-1]
DR ProteomicsDB; 72969; -. [Q8ND04-2]
DR ProteomicsDB; 72970; -. [Q8ND04-3]
DR Antibodypedia; 31075; 55 antibodies from 18 providers.
DR DNASU; 55181; -.
DR Ensembl; ENST00000300917.10; ENSP00000300917.4; ENSG00000167447.13. [Q8ND04-1]
DR Ensembl; ENST00000543872.6; ENSP00000438748.2; ENSG00000167447.13. [Q8ND04-1]
DR Ensembl; ENST00000578922.1; ENSP00000462119.1; ENSG00000167447.13. [Q8ND04-3]
DR GeneID; 55181; -.
DR KEGG; hsa:55181; -.
DR MANE-Select; ENST00000300917.10; ENSP00000300917.4; NM_018149.7; NP_060619.4.
DR UCSC; uc002ixi.4; human. [Q8ND04-1]
DR CTD; 55181; -.
DR DisGeNET; 55181; -.
DR GeneCards; SMG8; -.
DR HGNC; HGNC:25551; SMG8.
DR HPA; ENSG00000167447; Low tissue specificity.
DR MIM; 613175; gene.
DR MIM; 619268; phenotype.
DR neXtProt; NX_Q8ND04; -.
DR OpenTargets; ENSG00000167447; -.
DR PharmGKB; PA142672219; -.
DR VEuPathDB; HostDB:ENSG00000167447; -.
DR eggNOG; KOG3692; Eukaryota.
DR GeneTree; ENSGT00390000018533; -.
DR HOGENOM; CLU_008116_0_0_1; -.
DR InParanoid; Q8ND04; -.
DR OMA; HCTVKDS; -.
DR OrthoDB; 645776at2759; -.
DR PhylomeDB; Q8ND04; -.
DR TreeFam; TF323445; -.
DR PathwayCommons; Q8ND04; -.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q8ND04; -.
DR BioGRID-ORCS; 55181; 82 hits in 1086 CRISPR screens.
DR ChiTaRS; SMG8; human.
DR GenomeRNAi; 55181; -.
DR Pharos; Q8ND04; Tdark.
DR PRO; PR:Q8ND04; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8ND04; protein.
DR Bgee; ENSG00000167447; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q8ND04; baseline and differential.
DR Genevisible; Q8ND04; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; IMP:UniProtKB.
DR InterPro; IPR028802; SMG8.
DR InterPro; IPR019354; SMG8/SMG9.
DR PANTHER; PTHR13091; PTHR13091; 1.
DR Pfam; PF10220; Smg8_Smg9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cataract; Disease variant;
KW Intellectual disability; Methylation; Nonsense-mediated mRNA decay;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..991
FT /note="Nonsense-mediated mRNA decay factor SMG8"
FT /id="PRO_0000304974"
FT REGION 16..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 898
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 588
FT /note="E -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028164"
FT VAR_SEQ 589..991
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028165"
FT VAR_SEQ 945
FT /note="T -> TLPPDGLWVLRFPYAYGLREDLVSPXGKKQEIP (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028166"
FT VARIANT 208
FT /note="H -> R (in ALKUS)"
FT /evidence="ECO:0000269|PubMed:33242396"
FT /id="VAR_085550"
FT VARIANT 280
FT /note="P -> L (in dbSNP:rs8068240)"
FT /id="VAR_035137"
FT VARIANT 839..991
FT /note="Missing (in ALKUS)"
FT /evidence="ECO:0000269|PubMed:33242396"
FT /id="VAR_085551"
FT CONFLICT 278
FT /note="E -> V (in Ref. 2; BAB15576)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="R -> W (in Ref. 2; BAB15576)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="F -> L (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="I -> F (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="T -> P (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="T -> P (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="T -> P (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="L -> R (in Ref. 1; AAL83913)"
FT /evidence="ECO:0000305"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6Z3R"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6Z3R"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:7PW8"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 182..203
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:7PW8"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6SYT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 445..457
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 478..482
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:6L54"
FT HELIX 489..508
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 524..538
FT /evidence="ECO:0007829|PDB:7PW8"
FT HELIX 544..557
FT /evidence="ECO:0007829|PDB:7PW8"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 626..630
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 632..638
FT /evidence="ECO:0007829|PDB:7PW5"
FT TURN 639..644
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 743..749
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:7PW5"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 796..801
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 839..841
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 842..853
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 872..874
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 879..883
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 887..892
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 898..901
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 904..914
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 916..923
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 927..931
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 940..942
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 944..946
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 948..955
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 958..962
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:7PW5"
FT HELIX 976..978
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:7PW5"
FT STRAND 985..990
FT /evidence="ECO:0007829|PDB:7PW5"
SQ SEQUENCE 991 AA; 109684 MW; 9D8168B171179CFF CRC64;
MAGPVSLRDL LMGASAWMGS ESPGGSPTEG GGSAAGGPEP PWREDEICVV GIFGKTALRL
NSEKFSLVNT VCDRQVFPLF RHQDPGDPGP GIRTEAGAVG EAGGAEDPGA AAGGSVRGSG
AVAEGNRTEA GSQDYSLLQA YYSQESKVLY LLLTSICDNS QLLRACRALQ SGEAGGGLSL
PHAEAHEFWK HQEKLQCLSL LYLFSVCHIL LLVHPTCSFD ITYDRVFRAL DGLRQKVLPL
LKTAIKDCPV GKDWKLNCRP CPPRLLFLFQ LNGALKVEPP RNQDPAHPDK PKKHSPKRRL
QHALEDQIYR IFRKSRVLTN QSINCLFTVP ANQAFVYIVP GSQEEDPVGM LLDQLRSHCT
VKDPESLLVP APLSGPRRYQ VMRQHSRQQL SFHIDSSSSS SSGQLVDFTL REFLWQHVEL
VLSKKGFDDS VGRNPQPSHF ELPTYQKWIS AASKLYEVAI DGKEEDLGSP TGELTSKILS
SIKVLEGFLD IDTKFSENRC QKALPMAHSA YQSNLPHNYT MTVHKNQLAQ ALRVYSQHAR
GPAFHKYAMQ LHEDCYKFWS NGHQLCEERS LTDQHCVHKF HSLPKSGEKP EADRNPPVLY
HNSRARSTGA CNCGRKQAPR DDPFDIKAAN YDFYQLLEEK CCGKLDHINF PVFEPSTPDP
APAKNESSPA PPDSDADKLK EKEPQTQGES TSLSLALSLG QSTDSLGTYP ADPQAGGDNP
EVHGQVEVKT EKRPNFVDRQ ASTVEYLPGM LHSNCPKGLL PKFSSWSLVK LGPAKSYNFH
TGLDQQGFIP GTNYLMPWDI VIRTRAEDEG DLDTNSWPAP NKAIPGKRSA VVMGRGRRRD
DIARAFVGFE YEDSRGRRFM CSGPDKVMKV MGSGPKESAL KALNSDMPLY ILSSSQGRGL
KPHYAQLMRL FVVVPDAPLQ IILMPQVQPG PPPCPVFYPE KQEITLPPDG LWVLRFPYAY
VTERGPCFPP KENVQLMSYK VLRGVLKAVT Q
