GEMI4_HUMAN
ID GEMI4_HUMAN Reviewed; 1058 AA.
AC P57678; Q9NZS7; Q9UG32; Q9Y4Q2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Gem-associated protein 4;
DE Short=Gemin-4;
DE AltName: Full=Component of gems 4;
DE AltName: Full=p97;
GN Name=GEMIN4;
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], AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10725331; DOI=10.1083/jcb.148.6.1177;
RA Charroux B., Pellizzoni L., Perkinson R.A., Yong J., Shevchenko A.,
RA Mann M., Dreyfuss G.;
RT "Gemin4: a novel component of the SMN complex that is found in both gems
RT and nucleoli.";
RL J. Cell Biol. 148:1177-1186(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-1058.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP INTERACTION WITH PPP4R2.
RX PubMed=12668731; DOI=10.1242/jcs.00409;
RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
RA Philp A., Lamond A.I., Cohen P.T.W.;
RT "Protein phosphatase 4 interacts with the survival of motor neurons complex
RT and enhances the temporal localisation of snRNPs.";
RL J. Cell Sci. 116:1905-1913(2003).
RN [5]
RP IDENTIFICATION IN THE SMN COMPLEX, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005;
RA Golembe T.J., Yong J., Dreyfuss G.;
RT "Specific sequence features, recognized by the SMN complex, identify snRNAs
RT and determine their fate as snRNPs.";
RL Mol. Cell. Biol. 25:10989-11004(2005).
RN [6]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN3 AND GEMIN8.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [7]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, 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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP INTERACTION WITH GEMIN5.
RX PubMed=33963192; DOI=10.1038/s41467-021-22627-w;
RA Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S.,
RA Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J.,
RA Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K.,
RA Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P.,
RA Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C.,
RA Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N.,
RA Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S.,
RA Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A.,
RA Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M.,
RA Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J.,
RA Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y.,
RA Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S.,
RA Senderek J., Pandey U.B.;
RT "Loss of function mutations in GEMIN5 cause a neurodevelopmental
RT disorder.";
RL Nat. Commun. 12:2558-2558(2021).
RN [13]
RP VARIANT NEDMCR ARG-818, AND INVOLVEMENT IN NEDMCR.
RX PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
RA Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
RA Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
RA Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y., Sogaty S.,
RA Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F., Alshahwan S.A.,
RA Seidahmed M.Z., Alhadid A.A., Aldhalaan H., Alqallaf F., Kurdi W.,
RA Alfadhel M., Babay Z., Alsogheer M., Kaya N., Al-Hassnan Z.N.,
RA Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F., El Khashab H.Y., Bohlega S.,
RA Jia X., Nguyen H.C., Hammami R., Adly N., Mohamed J.Y., Abdulwahab F.,
RA Ibrahim N., Naim E.A., Al-Younes B., Meyer B.F., Hashem M., Shaheen R.,
RA Xiong Y., Abouelhoda M., Aldeeri A.A., Monies D.M., Alkuraya F.S.;
RT "Accelerating novel candidate gene discovery in neurogenetic disorders via
RT whole-exome sequencing of prescreened multiplex consanguineous families.";
RL Cell Rep. 10:148-161(2015).
RN [14]
RP VARIANT NEDMCR LEU-105.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP.
CC {ECO:0000269|PubMed:18984161}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (PubMed:18984161, PubMed:16314521, PubMed:17178713). Part of the SMN-Sm
CC complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5,
CC GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1,
CC SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:18984161,
CC PubMed:16314521). Interacts with GEMIN3; the interaction is direct
CC (PubMed:18984161, PubMed:17178713). Interacts with GEMIN5
CC (PubMed:33963192). Interacts with GEMIN8; the interaction is direct
CC (PubMed:17178713). Interacts with several snRNP SM core proteins,
CC including SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE (PubMed:18984161).
CC Interacts with PPP4R2 (PubMed:12668731). {ECO:0000269|PubMed:12668731,
CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:17178713,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:33963192}.
CC -!- INTERACTION:
CC P57678; P05187: ALPP; NbExp=3; IntAct=EBI-356700, EBI-1211484;
CC P57678; Q8N715: CCDC185; NbExp=3; IntAct=EBI-356700, EBI-740814;
CC P57678; P49368: CCT3; NbExp=3; IntAct=EBI-356700, EBI-356673;
CC P57678; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-356700, EBI-11983537;
CC P57678; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-356700, EBI-12261896;
CC P57678; P27918: CFP; NbExp=3; IntAct=EBI-356700, EBI-9038570;
CC P57678; Q9UHI6: DDX20; NbExp=7; IntAct=EBI-356700, EBI-347658;
CC P57678; Q9NXK8: FBXL12; NbExp=3; IntAct=EBI-356700, EBI-719790;
CC P57678; O43593: HR; NbExp=3; IntAct=EBI-356700, EBI-2880706;
CC P57678; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-356700, EBI-2556193;
CC P57678; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-356700, EBI-11953846;
CC P57678; Q3LI77: KRTAP13-4; NbExp=3; IntAct=EBI-356700, EBI-11953996;
CC P57678; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-356700, EBI-11992140;
CC P57678; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-356700, EBI-14065470;
CC P57678; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-356700, EBI-1044640;
CC P57678; O95711: LY86; NbExp=3; IntAct=EBI-356700, EBI-12203791;
CC P57678; P16860: NPPB; NbExp=3; IntAct=EBI-356700, EBI-747044;
CC P57678; P20618: PSMB1; NbExp=3; IntAct=EBI-356700, EBI-372273;
CC P57678; O75127: PTCD1; NbExp=3; IntAct=EBI-356700, EBI-2560233;
CC P57678; O75771: RAD51D; NbExp=3; IntAct=EBI-356700, EBI-1055693;
CC P57678; O95977: S1PR4; NbExp=3; IntAct=EBI-356700, EBI-12194739;
CC P57678; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-356700, EBI-742688;
CC P57678; O43609: SPRY1; NbExp=4; IntAct=EBI-356700, EBI-3866665;
CC P57678; Q03518: TAP1; NbExp=3; IntAct=EBI-356700, EBI-747259;
CC P57678; Q9Y3C8: UFC1; NbExp=3; IntAct=EBI-356700, EBI-1045733;
CC P57678; Q9Y4E8-2: USP15; NbExp=3; IntAct=EBI-356700, EBI-12041225;
CC P57678; O75604: USP2; NbExp=3; IntAct=EBI-356700, EBI-743272;
CC P57678; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-356700, EBI-2560158;
CC P57678; P13682: ZNF35; NbExp=3; IntAct=EBI-356700, EBI-11041653;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus,
CC gem. Note=Localized in subnuclear structures next to coiled bodies,
CC called gems, which are highly enriched in spliceosomal snRNPs and in
CC the nucleolus.
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly, cataracts, and
CC renal abnormalities (NEDMCR) [MIM:617913]: An autosomal recessive,
CC severe neurodevelopmental disorder characterized by global
CC developmental delay since infancy, microcephaly, poor or absent speech,
CC and inability to walk or spasticity. Additional features include renal
CC abnormalities, congenital cataracts, gastroesophageal reflux disease,
CC seizures with onset in infancy or childhood, hyporeflexia, and non-
CC specific white matter abnormalities on brain imaging.
CC {ECO:0000269|PubMed:25558065, ECO:0000269|PubMed:30237576}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AF173856; AAF35283.1; -; mRNA.
DR EMBL; AC087392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL080150; CAB45743.3; -; mRNA.
DR EMBL; AL080167; CAB45755.1; -; mRNA.
DR CCDS; CCDS45559.1; -.
DR PIR; T12535; T12535.
DR RefSeq; NP_056536.2; NM_015721.2.
DR AlphaFoldDB; P57678; -.
DR BioGRID; 119102; 246.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; P57678; -.
DR IntAct; P57678; 91.
DR MINT; P57678; -.
DR STRING; 9606.ENSP00000321706; -.
DR GlyGen; P57678; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P57678; -.
DR PhosphoSitePlus; P57678; -.
DR SwissPalm; P57678; -.
DR BioMuta; GEMIN4; -.
DR DMDM; 322510030; -.
DR EPD; P57678; -.
DR jPOST; P57678; -.
DR MassIVE; P57678; -.
DR MaxQB; P57678; -.
DR PaxDb; P57678; -.
DR PeptideAtlas; P57678; -.
DR PRIDE; P57678; -.
DR ProteomicsDB; 57005; -.
DR Antibodypedia; 22646; 216 antibodies from 27 providers.
DR DNASU; 50628; -.
DR Ensembl; ENST00000319004.6; ENSP00000321706.5; ENSG00000179409.11.
DR GeneID; 50628; -.
DR KEGG; hsa:50628; -.
DR MANE-Select; ENST00000319004.6; ENSP00000321706.5; NM_015721.3; NP_056536.2.
DR UCSC; uc002frs.2; human.
DR CTD; 50628; -.
DR DisGeNET; 50628; -.
DR GeneCards; GEMIN4; -.
DR HGNC; HGNC:15717; GEMIN4.
DR HPA; ENSG00000179409; Low tissue specificity.
DR MalaCards; GEMIN4; -.
DR MIM; 606969; gene.
DR MIM; 617913; phenotype.
DR neXtProt; NX_P57678; -.
DR OpenTargets; ENSG00000179409; -.
DR VEuPathDB; HostDB:ENSG00000179409; -.
DR eggNOG; ENOG502QRX9; Eukaryota.
DR GeneTree; ENSGT00390000012296; -.
DR InParanoid; P57678; -.
DR OMA; SCHNWLP; -.
DR OrthoDB; 426377at2759; -.
DR PhylomeDB; P57678; -.
DR TreeFam; TF329445; -.
DR PathwayCommons; P57678; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; P57678; -.
DR SIGNOR; P57678; -.
DR BioGRID-ORCS; 50628; 615 hits in 1081 CRISPR screens.
DR ChiTaRS; GEMIN4; human.
DR GeneWiki; GEMIN4; -.
DR GenomeRNAi; 50628; -.
DR Pharos; P57678; Tbio.
DR PRO; PR:P57678; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P57678; protein.
DR Bgee; ENSG00000179409; Expressed in sperm and 177 other tissues.
DR ExpressionAtlas; P57678; baseline and differential.
DR Genevisible; P57678; HS.
DR GO; GO:0015030; C:Cajal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
DR GO; GO:0006364; P:rRNA processing; TAS:ProtInc.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR InterPro; IPR033265; GEMIN4.
DR PANTHER; PTHR15571; PTHR15571; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Disease variant; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1058
FT /note="Gem-associated protein 4"
FT /id="PRO_0000087459"
FT REGION 714..735
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 105
FT /note="P -> L (in NEDMCR; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30237576"
FT /id="VAR_082144"
FT VARIANT 182
FT /note="F -> L (in dbSNP:rs34604548)"
FT /id="VAR_056891"
FT VARIANT 502
FT /note="I -> V (in dbSNP:rs34616851)"
FT /id="VAR_056892"
FT VARIANT 579
FT /note="A -> G (in dbSNP:rs910925)"
FT /id="VAR_024317"
FT VARIANT 684
FT /note="R -> Q (in dbSNP:rs3744741)"
FT /id="VAR_021971"
FT VARIANT 739
FT /note="I -> T (in dbSNP:rs1062923)"
FT /id="VAR_056893"
FT VARIANT 749
FT /note="P -> L (in dbSNP:rs8078660)"
FT /id="VAR_056894"
FT VARIANT 782
FT /note="F -> L (in dbSNP:rs34452716)"
FT /id="VAR_056895"
FT VARIANT 818
FT /note="W -> R (in NEDMCR; unknown pathological
FT significance; dbSNP:rs730882219)"
FT /evidence="ECO:0000269|PubMed:25558065"
FT /id="VAR_080610"
FT VARIANT 824
FT /note="V -> F (in dbSNP:rs34936176)"
FT /id="VAR_056896"
FT VARIANT 913
FT /note="V -> I (in dbSNP:rs34610323)"
FT /id="VAR_056897"
FT VARIANT 1033
FT /note="R -> C (in dbSNP:rs7813)"
FT /id="VAR_020390"
FT CONFLICT 163
FT /note="V -> I (in Ref. 1; AAF35283)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="Q -> E (in Ref. 1; AAF35283 and 3; CAB45743)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> V (in Ref. 1; AAF35283 and 3; CAB45743)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="Q -> P (in Ref. 1; AAF35283)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="D -> N (in Ref. 1; AAF35283 and 3; CAB45755/
FT CAB45743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1058 AA; 120037 MW; ACEC60EC19EF5081 CRC64;
MDLGPLNICE EMTILHGGFL LAEQLFHPKA LAELTKSDWE RVGRPIVEAL REISSAAAHS
QPFAWKKKAL IIIWAKVLQP HPVTPSDTET RWQEDLFFSV GNMIPTINHT ILFELLKSLE
ASGLFIQLLM ALPTTICHAE LERFLEHVTV DTSAEDVAFF LDVWWEVMKH KGHPQDPLLS
QFSAMAHKYL PALDEFPHPP KRLRSDPDAC PTMPLLAMLL RGLTQIQSRI LGPGRKCCAL
ANLADMLTVF ALTEDDPQEV SATVYLDKLA TVISVWNSDT QNPYHQQALA EKVKEAERDV
SLTSLAKLPS ETIFVGCEFL HHLLREWGEE LQAVLRSSQG TSYDSYRLCD SLTSFSQNAT
LYLNRTSLSK EDRQVVSELA ECVRDFLRKT STVLKNRALE DITASIAMAV IQQKMDRHME
VCYIFASEKK WAFSDEWVAC LGSNRALFRQ PDLVLRLLET VIDVSTADRA IPESQIRQVI
HLILECYADL SLPGKNKVLA GILRSWGRKG LSEKLLAYVE GFQEDLNTTF NQLTQSASEQ
GLAKAVASVA RLVIVHPEVT VKKMCSLAVV NLGTHKFLAQ ILTAFPALRF VEEQGPNSSA
TFMVSCLKET VWMKFSTPKE EKQFLELLNC LMSPVKPQGI PVAALLEPDE VLKEFVLPFL
RLDVEEVDLS LRIFIQTLEA NACREEYWLQ TCSPFPLLFS LCQLLDRFSK YWQLPKEKRC
LSLDRKDLAI HILELLCEIV SANAETFSPD VWIKSLSWLH RKLEQLDWTV GLRLKSFFEG
HFKCEVPATL FEICKLSEDE WTSQAHPGYG AGTGLLAWME CCCVSSGISE RMLSLLVVDV
GNPEEVRLFS KGFLVALVQV MPWCSPQEWQ RLHQLTRRLL EKQLLHVPYS LEYIQFVPLL
NLKPFAQELQ LSVLFLRTFQ FLCSHSCRDW LPLEGWNHVV KLLCGSLTRL LDSVRAIQAA
GPWVQGPEQD LTQEALFVYT QVFCHALHIM AMLHPEVCEP LYVLALETLT CYETLSKTNP
SVSSLLQRAH EQRFLKSIAE GIGPEERRQT LLQKMSSF
