SDA1_HUMAN
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 03-AUG-2022, entry version 153.
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};
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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. [Q9NVU7-2]
DR AlphaFoldDB; Q9NVU7; -.
DR SMR; Q9NVU7; -.
DR BioGRID; 120456; 140.
DR IntAct; Q9NVU7; 34.
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; Q9NVU7; -.
DR PeptideAtlas; Q9NVU7; -.
DR PRIDE; Q9NVU7; -.
DR ProteomicsDB; 82860; -. [Q9NVU7-1]
DR ProteomicsDB; 82861; -. [Q9NVU7-2]
DR TopDownProteomics; Q9NVU7-1; -. [Q9NVU7-1]
DR Antibodypedia; 49727; 65 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 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; 426305at2759; -.
DR PhylomeDB; Q9NVU7; -.
DR TreeFam; TF105727; -.
DR PathwayCommons; Q9NVU7; -.
DR SignaLink; Q9NVU7; -.
DR BioGRID-ORCS; 55153; 698 hits in 1073 CRISPR screens.
DR ChiTaRS; SDAD1; human.
DR GeneWiki; SDAD1; -.
DR GenomeRNAi; 55153; -.
DR Pharos; Q9NVU7; Tdark.
DR PRO; PR:Q9NVU7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NVU7; protein.
DR Bgee; ENSG00000198301; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; Q9NVU7; baseline and differential.
DR Genevisible; Q9NVU7; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
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; IPR007949; SDA1_dom.
DR InterPro; IPR012977; Uncharacterised_NUC130/133_N.
DR PANTHER; PTHR12730; PTHR12730; 1.
DR Pfam; PF08158; NUC130_3NT; 1.
DR Pfam; PF05285; SDA1; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 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
