ID FXR2_HUMAN Reviewed; 673 AA. AC P51116; B2R9M2; D3DTQ1; Q86V09; Q8WUM2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 09-DEC-2015, entry version 145. DE RecName: Full=Fragile X mental retardation syndrome-related protein 2; GN Name=FXR2; Synonyms=FMR1L2; 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]. RC TISSUE=Brain; RX PubMed=7489725; RA Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A., RA Nussbaum R.L., Dreyfuss G.; RT "The fragile X mental retardation syndrome protein interacts with RT novel homologs FXR1 and FXR2."; RL EMBO J. 14:5358-5366(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-252. RC TISSUE=Lymph, PNS, and Skin; 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 [GENOMIC DNA] OF 1-27. RX PubMed=9437788; DOI=10.1016/S0039-128X(97)00087-1; RA Joseph D.R.; RT "The rat androgen-binding protein (ABP/SHBG) gene contains triplet RT repeats similar to unstable triplets: evidence that the ABP/SHBG and RT the fragile X-related 2 genes overlap."; RL Steroids 63:2-4(1998). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites RT from human T cells using immobilized metal affinity chromatography and RT tandem mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP INTERACTION WITH TDRD3. RX PubMed=18664458; DOI=10.1093/hmg/ddn219; RA Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., RA Meister G., Keidel E., Fischer U.; RT "Tdrd3 is a novel stress granule-associated protein interacting with RT the Fragile-X syndrome protein FMRP."; RL Hum. Mol. Genet. 17:3236-3246(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-533; SER-566; RP THR-598; SER-601 AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-601 AND RP SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND SER-603, AND 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598 AND SER-601, AND 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 13-136, AND DOMAINS TUDOR. RX PubMed=21072162; DOI=10.1371/journal.pone.0013559; RA Adams-Cioaba M.A., Guo Y., Bian C., Amaya M.F., Lam R., Wasney G.A., RA Vedadi M., Xu C., Min J.; RT "Structural studies of the tandem Tudor domains of fragile X mental RT retardation related proteins FXR1 and FXR2."; RL PLoS ONE 5:E13559-E13559(2010). CC -!- FUNCTION: RNA-binding protein. CC -!- SUBUNIT: Interacts with FMR1 and FXR1. Interacts with CYFIP2 but CC not with CYFIP1. Interacts with TDRD3. CC {ECO:0000269|PubMed:18664458}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-740459, EBI-740459; CC Q9BXS5:AP1M1; NbExp=4; IntAct=EBI-740459, EBI-541426; CC Q15041:ARL6IP1; NbExp=3; IntAct=EBI-740459, EBI-714543; CC Q9UIF8-2:BAZ2B; NbExp=3; IntAct=EBI-740459, EBI-10321972; CC Q13895:BYSL; NbExp=5; IntAct=EBI-740459, EBI-358049; CC Q5T681:C10orf62; NbExp=4; IntAct=EBI-740459, EBI-744052; CC Q13557:CAMK2D; NbExp=3; IntAct=EBI-740459, EBI-351018; CC Q8IVW4:CDKL3; NbExp=3; IntAct=EBI-740459, EBI-3919850; CC Q9C0F1:CEP44; NbExp=3; IntAct=EBI-740459, EBI-744115; CC D3DR37:CEP55; NbExp=3; IntAct=EBI-740459, EBI-10173536; CC Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-740459, EBI-6658203; CC Q06787-8:FMR1; NbExp=3; IntAct=EBI-740459, EBI-10224470; CC Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-740459, EBI-2549423; CC Q6NT76-2:HMBOX1; NbExp=3; IntAct=EBI-740459, EBI-10212206; CC Q14847:LASP1; NbExp=3; IntAct=EBI-740459, EBI-742828; CC Q9UIC8:LCMT1; NbExp=2; IntAct=EBI-740459, EBI-747632; CC Q13094:LCP2; NbExp=3; IntAct=EBI-740459, EBI-346946; CC O95751:LDOC1; NbExp=3; IntAct=EBI-740459, EBI-740738; CC Q9NS73:MBIP; NbExp=3; IntAct=EBI-740459, EBI-741953; CC Q9HAF1:MEAF6; NbExp=3; IntAct=EBI-740459, EBI-399266; CC P55081:MFAP1; NbExp=3; IntAct=EBI-740459, EBI-1048159; CC Q5JRA6-2:MIA3; NbExp=3; IntAct=EBI-740459, EBI-10244342; CC Q9BU76:MMTAG2; NbExp=3; IntAct=EBI-740459, EBI-742459; CC Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-740459, EBI-399246; CC Q8N983:MRPL43; NbExp=3; IntAct=EBI-740459, EBI-1043145; CC Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-740459, EBI-740897; CC P49902:NT5C2; NbExp=3; IntAct=EBI-740459, EBI-742084; CC Q8N7H5:PAF1; NbExp=4; IntAct=EBI-740459, EBI-2607770; CC P22234:PAICS; NbExp=3; IntAct=EBI-740459, EBI-712261; CC P61457:PCBD1; NbExp=4; IntAct=EBI-740459, EBI-740475; CC P11309:PIM1; NbExp=3; IntAct=EBI-740459, EBI-696621; CC Q96HA1:POM121; NbExp=4; IntAct=EBI-740459, EBI-739990; CC Q96QH2:PRAM1; NbExp=3; IntAct=EBI-740459, EBI-2860740; CC Q9UI14:RABAC1; NbExp=3; IntAct=EBI-740459, EBI-712367; CC O95171:SCEL; NbExp=3; IntAct=EBI-740459, EBI-7543896; CC P78362:SRPK2; NbExp=3; IntAct=EBI-740459, EBI-593303; CC Q5T7P8-2:SYT6; NbExp=3; IntAct=EBI-740459, EBI-10246152; CC Q96C24:SYTL4; NbExp=3; IntAct=EBI-740459, EBI-747142; CC Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-740459, EBI-8787464; CC P07947:YES1; NbExp=3; IntAct=EBI-740459, EBI-515331; CC O15209:ZBTB22; NbExp=3; IntAct=EBI-740459, EBI-723574; CC Q96NC0:ZMAT2; NbExp=3; IntAct=EBI-740459, EBI-2682299; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: The tandem Tudor domains preferentially recognize CC trimethylated histone peptides. {ECO:0000269|PubMed:21072162}. CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 Agenet-like domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 KH domains. {ECO:0000255|PROSITE- CC ProRule:PRU00117}. 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; U31501; AAC50292.1; -; mRNA. DR EMBL; BT009817; AAP88819.1; -; mRNA. DR EMBL; AK313836; BAG36569.1; -; mRNA. DR EMBL; CH471108; EAW90154.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90155.1; -; Genomic_DNA. DR EMBL; BC020090; AAH20090.1; -; mRNA. DR EMBL; BC051907; AAH51907.1; -; mRNA. DR EMBL; BC067272; AAH67272.1; -; mRNA. DR EMBL; AF044263; AAC03357.1; -; Genomic_DNA. DR CCDS; CCDS45604.1; -. DR PIR; S60173; S60173. DR RefSeq; NP_004851.2; NM_004860.3. DR UniGene; Hs.52788; -. DR PDB; 3H8Z; X-ray; 1.92 A; A=13-136. DR PDBsum; 3H8Z; -. DR ProteinModelPortal; P51116; -. DR SMR; P51116; 13-209, 222-369. DR BioGrid; 114890; 121. DR IntAct; P51116; 106. DR MINT; MINT-108243; -. DR STRING; 9606.ENSP00000250113; -. DR PhosphoSite; P51116; -. DR BioMuta; FXR2; -. DR DMDM; 90177782; -. DR MaxQB; P51116; -. DR PaxDb; P51116; -. DR PRIDE; P51116; -. DR DNASU; 9513; -. DR Ensembl; ENST00000250113; ENSP00000250113; ENSG00000129245. DR GeneID; 9513; -. DR KEGG; hsa:9513; -. DR UCSC; uc002gia.2; human. DR CTD; 9513; -. DR GeneCards; FXR2; -. DR HGNC; HGNC:4024; FXR2. DR HPA; CAB011205; -. DR HPA; HPA022997; -. DR MIM; 605339; gene. DR neXtProt; NX_P51116; -. DR PharmGKB; PA28440; -. DR eggNOG; ENOG410IF9J; Eukaryota. DR eggNOG; ENOG410ZDJG; LUCA. DR GeneTree; ENSGT00390000017033; -. DR HOGENOM; HOG000293377; -. DR HOVERGEN; HBG005739; -. DR InParanoid; P51116; -. DR KO; K15516; -. DR OMA; MHFRSIR; -. DR OrthoDB; EOG7NKKJT; -. DR PhylomeDB; P51116; -. DR TreeFam; TF105427; -. DR ChiTaRS; FXR2; human. DR EvolutionaryTrace; P51116; -. DR GeneWiki; FXR2; -. DR GenomeRNAi; 9513; -. DR NextBio; 35646; -. DR PRO; PR:P51116; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P51116; -. DR CleanEx; HS_FXR2; -. DR ExpressionAtlas; P51116; baseline and differential. DR Genevisible; P51116; HS. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; TAS:ProtInc. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005844; C:polysome; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; TAS:ProtInc. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:ParkinsonsUK-UCL. DR GO; GO:0098792; P:xenophagy; IMP:ParkinsonsUK-UCL. DR Gene3D; 3.30.1370.10; -; 2. DR InterPro; IPR008395; Agenet-like_dom. DR InterPro; IPR022034; FXMRP1_C_core. DR InterPro; IPR032172; FXR_C1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR Pfam; PF05641; Agenet; 1. DR Pfam; PF12235; FXMRP1_C_core; 1. DR Pfam; PF16096; FXR_C1; 1. DR Pfam; PF00013; KH_1; 2. DR SMART; SM00322; KH; 2. DR SUPFAM; SSF54791; SSF54791; 2. DR PROSITE; PS51641; AGENET_LIKE; 2. DR PROSITE; PS50084; KH_TYPE_1; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; RNA-binding. FT CHAIN 1 673 Fragile X mental retardation syndrome- FT related protein 2. FT /FTId=PRO_0000050110. FT DOMAIN 14 60 Agenet-like 1. FT DOMAIN 73 125 Agenet-like 2. FT DOMAIN 232 261 KH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT DOMAIN 295 324 KH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT COMPBIAS 414 418 Poly-Ser. FT COMPBIAS 544 552 Poly-Arg. FT COMPBIAS 584 594 Poly-Arg. FT MOD_RES 411 411 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 533 533 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 566 566 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 598 598 Phosphothreonine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 601 601 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 603 603 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT VARIANT 252 252 Q -> H (in dbSNP:rs17854734). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_067039. FT VARIANT 591 591 R -> P (in dbSNP:rs36013555). FT /FTId=VAR_055979. FT CONFLICT 625 626 RP -> SA (in Ref. 1; AAC50292). FT {ECO:0000305}. FT STRAND 15 19 {ECO:0000244|PDB:3H8Z}. FT STRAND 25 33 {ECO:0000244|PDB:3H8Z}. FT STRAND 35 42 {ECO:0000244|PDB:3H8Z}. FT STRAND 50 53 {ECO:0000244|PDB:3H8Z}. FT HELIX 54 56 {ECO:0000244|PDB:3H8Z}. FT STRAND 74 79 {ECO:0000244|PDB:3H8Z}. FT STRAND 88 98 {ECO:0000244|PDB:3H8Z}. FT STRAND 101 106 {ECO:0000244|PDB:3H8Z}. FT STRAND 115 117 {ECO:0000244|PDB:3H8Z}. FT HELIX 119 121 {ECO:0000244|PDB:3H8Z}. FT STRAND 122 124 {ECO:0000244|PDB:3H8Z}. SQ SEQUENCE 673 AA; 74223 MW; B8A498C3F634D41F CRC64; MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD ATYNEIVTLE RLRPVNPNPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT RENISNAQAL LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG SGGSDKAGYS TDESSSSSLH ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS TASETESEKR EEPNRAGPGD RDPPTRGEES RRRPTGGRGR GPPPAPRPTS RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP ASARRRRSRR RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP KGPSENGELS APLELGSMVN GVS //