ID SDA1_HUMAN Reviewed; 687 AA. AC Q9NVU7; Q32Q11; Q68D52; Q7Z5U4; Q9H831; Q9H9P6; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-MAR-2024, entry version 162. DE RecName: Full=Protein SDA1 homolog; DE AltName: Full=Nucleolar protein 130; DE AltName: Full=SDA1 domain-containing protein 1; DE Short=hSDA; GN Name=SDAD1; Synonyms=NUC130; 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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT CYS-575. RC TISSUE=Rectum tumor; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-277 (ISOFORM 1). RC TISSUE=PNS, and Uterus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-687 (ISOFORM 1), AND VARIANT RP CYS-575. 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 [5] RP SUBCELLULAR LOCATION. RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9; RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., RA Mann M., Lamond A.I.; RT "Directed proteomic analysis of the human nucleolus."; RL Curr. Biol. 12:1-11(2002). RN [6] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=14976432; RA Babbio F., Farinacci M., Saracino F., Carbone M.L., Privitera E.; RT "Expression and localization studies of hSDA, the human ortholog of the RT yeast SDA1 gene."; RL Cell Cycle 3:486-490(2004). RN [7] RP TISSUE SPECIFICITY. RX PubMed=15607425; DOI=10.1016/j.ygeno.2004.10.003; RA Fox M., Urano J., Reijo Pera R.A.; RT "Identification and characterization of RNA sequences to which human RT PUMILIO-2 (PUM2) and deleted in Azoospermia-like (DAZL) bind."; RL Genomics 85:92-105(2005). RN [8] RP POLYMORPHISM. RX PubMed=15753903; DOI=10.1016/j.jaci.2004.11.034; RA Zhang J., Noguchi E., Migita O., Yokouchi Y., Nakayama J., Shibasaki M., RA Arinami T.; RT "Association of a haplotype block spanning SDAD1 gene and CXC chemokine RT genes with allergic rhinitis."; RL J. Allergy Clin. Immunol. 115:548-554(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY RP 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY RP 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY RP 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 the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-234; SER-236 AND RP SER-585, AND 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 [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., 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY RP 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585 AND SER-595, AND RP IDENTIFICATION 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., 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-552 AND SER-585, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY RP 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: Required for 60S pre-ribosomal subunits export to the CC cytoplasm. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, CC ECO:0000269|PubMed:14976432}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NVU7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NVU7-2; Sequence=VSP_025505; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, kidney, spleen, brain CC and fetal tissues. Also expressed at lower level in heart, lung, liver, CC small intestine, ovary, uterus, mammary gland and placenta. CC {ECO:0000269|PubMed:14976432, ECO:0000269|PubMed:15607425}. CC -!- POLYMORPHISM: Variations in SDAD1 may be a cause of susceptibility to CC seasonal allergic rhinitis (SAR). SAR is a common allergic disorder CC characterized by episodes of sneezing, rhinorrhea, and swelling of the CC nasal mucosa. {ECO:0000269|PubMed:15753903}. CC -!- MISCELLANEOUS: DAZL and PUM2 bind its 3'-UTR mRNA, suggesting that CC these proteins may regulate its translation. CC -!- SIMILARITY: Belongs to the SDA1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI07896.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA91648.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB14177.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; CR749574; CAH18368.1; -; mRNA. DR EMBL; AC110615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC115628; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC054040; AAH54040.1; -; mRNA. DR EMBL; BC063797; AAH63797.1; -; mRNA. DR EMBL; BC107895; AAI07896.1; ALT_SEQ; mRNA. DR EMBL; AK001360; BAA91648.1; ALT_FRAME; mRNA. DR EMBL; AK022683; BAB14177.1; ALT_INIT; mRNA. DR EMBL; AK024031; BAB14790.1; ALT_INIT; mRNA. DR CCDS; CCDS3573.2; -. [Q9NVU7-1] DR RefSeq; NP_001275912.1; NM_001288983.1. DR RefSeq; NP_001275913.1; NM_001288984.1. [Q9NVU7-2] DR RefSeq; NP_060585.2; NM_018115.3. [Q9NVU7-1] DR RefSeq; XP_005263162.1; XM_005263105.4. DR PDB; 8FL2; EM; 2.67 A; NT=1-687. DR PDB; 8FL3; EM; 2.53 A; NT=1-687. DR PDB; 8FL4; EM; 2.89 A; NT=1-687. DR PDB; 8IDY; EM; 3.00 A; u=1-687. DR PDB; 8INF; EM; 3.00 A; f=1-687. DR PDB; 8INK; EM; 3.20 A; N=1-687. DR PDB; 8IPY; EM; 3.20 A; N=1-687. DR PDBsum; 8FL2; -. DR PDBsum; 8FL3; -. DR PDBsum; 8FL4; -. DR PDBsum; 8IDY; -. DR PDBsum; 8INF; -. DR PDBsum; 8INK; -. DR PDBsum; 8IPY; -. DR AlphaFoldDB; Q9NVU7; -. DR EMDB; EMD-29265; -. DR EMDB; EMD-29266; -. DR EMDB; EMD-29267; -. DR EMDB; EMD-35371; -. DR EMDB; EMD-35597; -. DR EMDB; EMD-35599; -. DR EMDB; EMD-35651; -. DR SMR; Q9NVU7; -. DR BioGRID; 120456; 171. DR IntAct; Q9NVU7; 36. DR MINT; Q9NVU7; -. DR STRING; 9606.ENSP00000348596; -. DR GlyGen; Q9NVU7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NVU7; -. DR PhosphoSitePlus; Q9NVU7; -. DR SwissPalm; Q9NVU7; -. DR BioMuta; SDAD1; -. DR DMDM; 296452964; -. DR EPD; Q9NVU7; -. DR jPOST; Q9NVU7; -. DR MassIVE; Q9NVU7; -. DR MaxQB; Q9NVU7; -. DR PaxDb; 9606-ENSP00000348596; -. DR PeptideAtlas; Q9NVU7; -. DR ProteomicsDB; 82860; -. [Q9NVU7-1] DR ProteomicsDB; 82861; -. [Q9NVU7-2] DR Pumba; Q9NVU7; -. DR TopDownProteomics; Q9NVU7-1; -. [Q9NVU7-1] DR Antibodypedia; 49727; 70 antibodies from 15 providers. DR DNASU; 55153; -. DR Ensembl; ENST00000356260.10; ENSP00000348596.5; ENSG00000198301.12. [Q9NVU7-1] DR GeneID; 55153; -. DR KEGG; hsa:55153; -. DR MANE-Select; ENST00000356260.10; ENSP00000348596.5; NM_018115.4; NP_060585.2. DR UCSC; uc003hje.6; human. [Q9NVU7-1] DR AGR; HGNC:25537; -. DR CTD; 55153; -. DR DisGeNET; 55153; -. DR GeneCards; SDAD1; -. DR HGNC; HGNC:25537; SDAD1. DR HPA; ENSG00000198301; Low tissue specificity. DR neXtProt; NX_Q9NVU7; -. DR OpenTargets; ENSG00000198301; -. DR PharmGKB; PA134961441; -. DR VEuPathDB; HostDB:ENSG00000198301; -. DR eggNOG; KOG2229; Eukaryota. DR GeneTree; ENSGT00390000010355; -. DR HOGENOM; CLU_009161_3_1_1; -. DR InParanoid; Q9NVU7; -. DR OMA; AMYKTYK; -. DR OrthoDB; 5482564at2759; -. DR PhylomeDB; Q9NVU7; -. DR TreeFam; TF105727; -. DR PathwayCommons; Q9NVU7; -. DR SignaLink; Q9NVU7; -. DR BioGRID-ORCS; 55153; 736 hits in 1154 CRISPR screens. DR ChiTaRS; SDAD1; human. DR GeneWiki; SDAD1; -. DR GenomeRNAi; 55153; -. DR Pharos; Q9NVU7; Tbio. DR PRO; PR:Q9NVU7; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9NVU7; Protein. DR Bgee; ENSG00000198301; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 209 other cell types or tissues. DR ExpressionAtlas; Q9NVU7; baseline and differential. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB. DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR027312; Sda1. DR InterPro; IPR048292; SDA1_C. DR InterPro; IPR007949; SDA1_MD. DR InterPro; IPR012977; SDA1_N. DR PANTHER; PTHR12730; HSDA/SDA1-RELATED; 1. DR PANTHER; PTHR12730:SF1; PROTEIN SDA1 HOMOLOG; 1. DR Pfam; PF21638; SDA1_C; 1. DR Pfam; PF05285; SDA1_dom; 1. DR Pfam; PF08158; SDA1_HEAT; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q9NVU7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein; KW Protein transport; Reference proteome; Ribosome biogenesis; Transport. FT CHAIN 1..687 FT /note="Protein SDA1 homolog" FT /id="PRO_0000287482" FT REGION 483..525 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 604..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 253..315 FT /evidence="ECO:0000255" FT COMPBIAS 486..511 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 604..632 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 234 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 552 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 585 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 595 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT VAR_SEQ 1..97 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_025505" FT VARIANT 258 FT /note="K -> Q (in dbSNP:rs15481)" FT /id="VAR_032312" FT VARIANT 490 FT /note="A -> D (in dbSNP:rs34627298)" FT /id="VAR_032313" FT VARIANT 575 FT /note="S -> C (in dbSNP:rs2242471)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005" FT /id="VAR_032314" FT VARIANT 660 FT /note="V -> I (in dbSNP:rs17001276)" FT /id="VAR_032315" FT CONFLICT 186 FT /note="E -> G (in Ref. 1; CAH18368)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="H -> L (in Ref. 4; BAA91648)" FT /evidence="ECO:0000305" FT CONFLICT 319 FT /note="N -> S (in Ref. 1; CAH18368)" FT /evidence="ECO:0000305" FT CONFLICT 396 FT /note="N -> S (in Ref. 1; CAH18368)" FT /evidence="ECO:0000305" FT CONFLICT 617 FT /note="A -> S (in Ref. 4; BAB14177)" FT /evidence="ECO:0000305" FT CONFLICT 634 FT /note="T -> A (in Ref. 1; CAH18368)" FT /evidence="ECO:0000305" FT CONFLICT 651 FT /note="F -> L (in Ref. 1; CAH18368)" FT /evidence="ECO:0000305" SQ SEQUENCE 687 AA; 79871 MW; B01EE09383EA959C CRC64; MSNRNNNKLP SNLPQLQNLI KRDPPAYIEE FLQQYNHYKS NVEIFKLQPN KPSKELAELV MFMAQISHCY PEYLSNFPQE VKDLLSCNHT VLDPDLRMTF CKALILLRNK NLINPSSLLE LFFELFRCHD KLLRKTLYTH IVTDIKNINA KHKNNKVNVV LQNFMYTMLR DSNATAAKMS LDVMIELYRR NIWNDAKTVN VITTACFSKV TKILVAALTF FLGKDEDEKQ DSDSESEDDG PTARDLLVQY ATGKKSSKNK KKLEKAMKVL KKQKKKKKPE VFNFSAIHLI HDPQDFAEKL LKQLECCKER FEVKMMLMNL ISRLVGIHEL FLFNFYPFLQ RFLQPHQREV TKILLFAAQA SHHLVPPEII QSLLMTVANN FVTDKNSGEV MTVGINAIKE ITARCPLAMT EELLQDLAQY KTHKDKNVMM SARTLIHLFR TLNPQMLQKK FRGKPTEASI EARVQEYGEL DAKDYIPGAE VLEVEKEENA ENDEDGWEST SLSEEEDADG EWIDVQHSSD EEQQEISKKL NSMPMEERKA KAAAISTSRV LTQEDFQKIR MAQMRKELDA APGKSQKRKY IEIDSDEEPR GELLSLRDIE RLHKKPKSDK ETRLATAMAG KTDRKEFVRK KTKTNPFSSS TNKEKKKQKN FMMMRYSQNV RSKNKRSFRE KQLALRDALL KKRKRMK //