ID DDX20_HUMAN Reviewed; 824 AA. AC Q9UHI6; Q96F72; Q9NVM3; Q9UF59; Q9UIY0; Q9Y659; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 31-OCT-2012, entry version 140. DE RecName: Full=Probable ATP-dependent RNA helicase DDX20; DE EC=3.6.4.13; DE AltName: Full=Component of gems 3; DE AltName: Full=DEAD box protein 20; DE AltName: Full=DEAD box protein DP 103; DE AltName: Full=Gemin-3; GN Name=DDX20; Synonyms=DP103, GEMIN3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE CORE SMN COMPLEX, RP INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, AND MASS SPECTROMETRY. RX MEDLINE=20069784; PubMed=10601333; DOI=10.1083/jcb.147.6.1181; RA Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M., RA Dreyfuss G.; RT "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal RT muscular atrophy gene product, and a component of gems."; RL J. Cell Biol. 147:1181-1194(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH EBV EBNA2 AND EBV RP EBNA3C. RX MEDLINE=99315855; PubMed=10383418; DOI=10.1074/jbc.274.27.19136; RA Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., RA Atz J., Mueller-Lantzsch N., Schubach W.H., Grasser F.A.; RT "Characterization of DP103, a novel DEAD box protein that binds to the RT Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C."; RL J. Biol. Chem. 274:19136-19144(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-636. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275. 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP INTERACTION WITH SNUPN; SMN1 AND SNRPB. RX MEDLINE=22090571; PubMed=12095920; DOI=10.1093/hmg/11.15.1785; RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.; RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP RT complex with snurportin1 and importin beta."; RL Hum. Mol. Genet. 11:1785-1795(2002). RN [8] 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 RT complex and enhances the temporal localisation of snRNPs."; RL J. Cell Sci. 116:1905-1913(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-705 AND SER-714, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). RN [10] RP INTERACTION WITH FOXL2. RX PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184; RA Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y., RA Bae J.; RT "Transcriptional factor FOXL2 interacts with DP103 and induces RT apoptosis."; RL Biochem. Biophys. Res. Commun. 336:876-881(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18187866; DOI=10.2116/analsci.24.161; RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; RT "Automated phosphoproteome analysis for cultured cancer cells by two- RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; RL Anal. Sci. 24:161-166(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-187; THR-552; RP SER-677; SER-678; THR-705 AND SER-714, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532; RP THR-552; SER-649; SER-652; SER-654; SER-656; SER-672; SER-677; RP SER-678; SER-703; THR-705 AND SER-714, AND MASS SPECTROMETRY. 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678; SER-703; RP THR-705 AND SER-714, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677; SER-678 AND RP SER-703, AND MASS SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] 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., RA Buerckstuemmer T., 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 [19] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP, RP AND ADP-BINDING. RX PubMed=20510246; DOI=10.1016/j.jmb.2010.05.046; RA Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., RA Flores A., Schuler H.; RT "Crystal structure of human RNA helicase A (DHX9): structural basis RT for unselective nucleotide base binding in a DEAD-box variant RT protein."; RL J. Mol. Biol. 400:768-782(2010). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268. RX PubMed=20941364; DOI=10.1371/journal.pone.0012791; RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., RA Hogbom M., Holmberg-Schiavone L., Tempel W., Park H.W., RA Hammarstrom M., Moche M., Thorsell A.G., Schuler H.; RT "Comparative structural analysis of human DEAD-box RNA helicases."; RL PLoS ONE 5:0-0(2010). CC -!- FUNCTION: The SMN complex plays an essential role in spliceosomal CC snRNP assembly in the cytoplasm and is required for pre-mRNA CC splicing in the nucleus. It may also play a role in the metabolism CC of snoRNPs. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 CC and STRAP/UNRIP. Interacts directly with SMN1 and with several CC spliceosomal snRNP core Sm proteins, including SNUPN, SNRPB, CC SNRPD2 and SNRPD3. Interacts with PPP4R2. Interacts with EBV EBNA2 CC and EBNA3C. Interacts with FOXL2. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in CC subnuclear structures next to coiled bodies, called Gemini of CC Cajal bodies (Gems). CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20 CC subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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; AF171063; AAF14544.1; -; mRNA. DR EMBL; AF106019; AAD42744.1; -; mRNA. DR EMBL; AK001506; BAA91727.1; -; mRNA. DR EMBL; AL049557; CAB55686.2; -; Genomic_DNA. DR EMBL; BC011556; AAH11556.1; -; mRNA. DR EMBL; AL133598; CAB63734.2; -; mRNA. DR IPI; IPI00005904; -. DR PIR; T43476; T43476. DR RefSeq; NP_009135.4; NM_007204.4. DR UniGene; Hs.591405; -. DR PDB; 2OXC; X-ray; 1.30 A; A/B=41-268. DR PDB; 3B7G; X-ray; 1.90 A; A/B=41-268. DR PDBsum; 2OXC; -. DR PDBsum; 3B7G; -. DR ProteinModelPortal; Q9UHI6; -. DR SMR; Q9UHI6; 62-441. DR DIP; DIP-32606N; -. DR IntAct; Q9UHI6; 13. DR MINT; MINT-96973; -. DR STRING; Q9UHI6; -. DR PhosphoSite; Q9UHI6; -. DR DMDM; 12643886; -. DR PeptideAtlas; Q9UHI6; -. DR PRIDE; Q9UHI6; -. DR DNASU; 11218; -. DR Ensembl; ENST00000369702; ENSP00000358716; ENSG00000064703. DR GeneID; 11218; -. DR KEGG; hsa:11218; -. DR UCSC; uc001ebs.3; human. DR CTD; 11218; -. DR GeneCards; GC01P112298; -. DR HGNC; HGNC:2743; DDX20. DR HPA; CAB015427; -. DR HPA; HPA005516; -. DR HPA; HPA023541; -. DR MIM; 606168; gene. DR neXtProt; NX_Q9UHI6; -. DR PharmGKB; PA27209; -. DR eggNOG; COG0513; -. DR HOGENOM; HOG000112184; -. DR HOVERGEN; HBG051330; -. DR InParanoid; Q9UHI6; -. DR KO; K13131; -. DR OMA; DYLNPGS; -. DR OrthoDB; EOG4SF95N; -. DR PhylomeDB; Q9UHI6; -. DR Reactome; REACT_21257; Metabolism of RNA. DR Reactome; REACT_71; Gene Expression. DR EvolutionaryTrace; Q9UHI6; -. DR GenomeRNAi; 11218; -. DR NextBio; 42699; -. DR ArrayExpress; Q9UHI6; -. DR Bgee; Q9UHI6; -. DR CleanEx; HS_DDX20; -. DR Genevestigator; Q9UHI6; -. DR GermOnline; ENSG00000064703; Homo sapiens. DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. DR GO; GO:0017053; C:transcriptional repressor complex; IEA:Compara. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000244; P:assembly of spliceosomal tri-snRNP; TAS:ProtInc. DR GO; GO:0006917; P:induction of apoptosis; IEA:Compara. DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; DNA-binding; KW Helicase; Hydrolase; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Spliceosome. FT CHAIN 1 824 Probable ATP-dependent RNA helicase FT DDX20. FT /FTId=PRO_0000055025. FT DOMAIN 93 264 Helicase ATP-binding. FT DOMAIN 299 448 Helicase C-terminal. FT NP_BIND 109 114 ATP. FT REGION 456 548 SMN interacting. FT MOTIF 62 90 Q motif. FT MOTIF 211 214 DEAD box. FT BINDING 84 84 ATP; via carbonyl oxygen. FT BINDING 89 89 ATP. FT MOD_RES 48 48 Phosphoserine. FT MOD_RES 187 187 Phosphoserine. FT MOD_RES 500 500 Phosphoserine. FT MOD_RES 532 532 Phosphoserine. FT MOD_RES 552 552 Phosphothreonine. FT MOD_RES 649 649 Phosphoserine. FT MOD_RES 652 652 Phosphoserine. FT MOD_RES 654 654 Phosphoserine. FT MOD_RES 656 656 Phosphoserine. FT MOD_RES 672 672 Phosphoserine. FT MOD_RES 677 677 Phosphoserine. FT MOD_RES 678 678 Phosphoserine. FT MOD_RES 703 703 Phosphoserine. FT MOD_RES 705 705 Phosphothreonine. FT MOD_RES 714 714 Phosphoserine. FT VARIANT 636 636 I -> T (in dbSNP:rs197412). FT /FTId=VAR_057231. FT VARIANT 693 693 R -> S (in dbSNP:rs197414). FT /FTId=VAR_057232. FT VARIANT 762 762 I -> T (in dbSNP:rs85276). FT /FTId=VAR_057233. FT CONFLICT 5 5 F -> V (in Ref. 2; AAD42744). FT CONFLICT 279 279 Y -> C (in Ref. 3; BAA91727). FT CONFLICT 639 639 R -> K (in Ref. 1; AAF14544). FT CONFLICT 659 659 Y -> H (in Ref. 2; AAD42744). FT CONFLICT 676 676 G -> S (in Ref. 1; AAF14544). FT CONFLICT 703 703 S -> T (in Ref. 1; AAF14544). FT HELIX 64 67 FT HELIX 71 79 FT HELIX 87 97 FT STRAND 102 105 FT HELIX 112 123 FT STRAND 133 136 FT HELIX 140 153 FT TURN 154 156 FT STRAND 162 165 FT HELIX 171 177 FT STRAND 182 186 FT HELIX 188 196 FT HELIX 202 204 FT STRAND 207 212 FT HELIX 213 217 FT HELIX 223 232 FT STRAND 238 244 FT HELIX 248 254 FT TURN 255 257 FT STRAND 262 264 SQ SEQUENCE 824 AA; 92241 MW; 76712F014B2A0CF2 CRC64; MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR TRTGDVLLAE PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL DLIVQAKSGT GKTCVFSTIA LDSLVLENLS TQILILAPTR EIAVQIHSVI TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK CHIAVGSPGR IKQLIELDYL NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML AVSATYPEFL ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD AMAKLKHFHC RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA GRFGTLGLTV TYCCRGEEEN MMMRIAQKCN INLLPLPDPI PSGLMEECVD WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE RTLQIQKAHG DHMASSRNNS VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR QSEEQMKNSV QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG DSESDSDSYS SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP NGSDTPNPEK YQESPGIQMK TRLKEGASQR AKQSRRNLPR RSSFRLQTEA QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY YRAWQEYYAA ASHSYYWNAQ RHPSWMAAYH MNTIYLQEMM HSNQ //