ID   SFSWA_HUMAN             Reviewed;         951 AA.
AC   Q12872; B2RN45; B7ZM97; F5H6B8; Q6PJF7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 3.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Splicing factor, suppressor of white-apricot homolog;
DE   AltName: Full=Splicing factor, arginine/serine-rich 8;
DE   AltName: Full=Suppressor of white apricot protein homolog;
GN   Name=SFSWAP; Synonyms=SFRS8, SWAP;
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] (ISOFORM 1), AND VARIANTS GLN-52; PHE-136 AND
RP   PRO-421.
RC   TISSUE=Placenta;
RX   PubMed=8206918; DOI=10.1016/s0021-9258(17)33989-3;
RA   Denhez F., Lafyatis R.;
RT   "Conservation of regulated alternative splicing and identification of
RT   functional domains in vertebrate homologs to the Drosophila splicing
RT   regulator, suppressor-of-white-apricot.";
RL   J. Biol. Chem. 269:16170-16179(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-421.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   PRO-421.
RC   TISSUE=Brain, 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=8940107; DOI=10.1074/jbc.271.49.31106;
RA   Sarkissian M., Winne A., Lafyatis R.;
RT   "The mammalian homolog of suppressor-of-white-apricot regulates alternative
RT   mRNA splicing of CD45 exon 4 and fibronectin IIICS.";
RL   J. Biol. Chem. 271:31106-31114(1996).
RN   [6]
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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-604 AND SER-909, AND
RP   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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-909, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-832; SER-834 AND
RP   SER-909, AND 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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).
RN   [16]
RP   STRUCTURE BY NMR OF 189-282 AND 434-522.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SURP1 and SURP2 domain in splicing factor,
RT   arginine/serine-rich 8.";
RL   Submitted (JUN-2007) to the PDB data bank.
CC   -!- FUNCTION: Plays a role as an alternative splicing regulator. Regulate
CC       its own expression at the level of RNA processing. Also regulates the
CC       splicing of fibronectin and CD45 genes. May act, at least in part, by
CC       interaction with other R/S-containing splicing factors. Represses the
CC       splicing of MAPT/Tau exon 10. {ECO:0000269|PubMed:8940107}.
CC   -!- INTERACTION:
CC       Q12872; Q15637: SF1; NbExp=2; IntAct=EBI-1055938, EBI-744603;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q12872-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12872-2; Sequence=VSP_044786;
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DR   EMBL; U08377; AAA19604.1; -; mRNA.
DR   EMBL; AC117500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW98526.1; -; Genomic_DNA.
DR   EMBL; BC008707; AAH08707.1; -; mRNA.
DR   EMBL; BC015953; AAH15953.1; -; mRNA.
DR   EMBL; BC136678; AAI36679.1; -; mRNA.
DR   EMBL; BC144364; AAI44365.1; -; mRNA.
DR   CCDS; CCDS58290.1; -. [Q12872-2]
DR   CCDS; CCDS9273.1; -. [Q12872-1]
DR   PIR; A54037; A54037.
DR   PIR; B54037; B54037.
DR   PIR; C54037; C54037.
DR   RefSeq; NP_001248340.1; NM_001261411.1. [Q12872-2]
DR   RefSeq; NP_004583.2; NM_004592.3. [Q12872-1]
DR   PDB; 2E5Z; NMR; -; A=440-522.
DR   PDB; 2E60; NMR; -; A=189-282.
DR   PDBsum; 2E5Z; -.
DR   PDBsum; 2E60; -.
DR   AlphaFoldDB; Q12872; -.
DR   SMR; Q12872; -.
DR   BioGRID; 112331; 102.
DR   IntAct; Q12872; 18.
DR   MINT; Q12872; -.
DR   STRING; 9606.ENSP00000437738; -.
DR   GlyGen; Q12872; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q12872; -.
DR   PhosphoSitePlus; Q12872; -.
DR   BioMuta; SFSWAP; -.
DR   DMDM; 292495067; -.
DR   EPD; Q12872; -.
DR   jPOST; Q12872; -.
DR   MassIVE; Q12872; -.
DR   MaxQB; Q12872; -.
DR   PaxDb; 9606-ENSP00000437738; -.
DR   PeptideAtlas; Q12872; -.
DR   ProteomicsDB; 27138; -.
DR   ProteomicsDB; 58994; -. [Q12872-1]
DR   Pumba; Q12872; -.
DR   Antibodypedia; 19429; 216 antibodies from 27 providers.
DR   DNASU; 6433; -.
DR   Ensembl; ENST00000261674.9; ENSP00000261674.4; ENSG00000061936.10. [Q12872-1]
DR   Ensembl; ENST00000541286.5; ENSP00000437738.1; ENSG00000061936.10. [Q12872-2]
DR   GeneID; 6433; -.
DR   KEGG; hsa:6433; -.
DR   MANE-Select; ENST00000261674.9; ENSP00000261674.4; NM_004592.4; NP_004583.2.
DR   UCSC; uc001uja.3; human. [Q12872-1]
DR   AGR; HGNC:10790; -.
DR   CTD; 6433; -.
DR   DisGeNET; 6433; -.
DR   GeneCards; SFSWAP; -.
DR   HGNC; HGNC:10790; SFSWAP.
DR   HPA; ENSG00000061936; Low tissue specificity.
DR   MIM; 601945; gene.
DR   neXtProt; NX_Q12872; -.
DR   OpenTargets; ENSG00000061936; -.
DR   PharmGKB; PA35706; -.
DR   VEuPathDB; HostDB:ENSG00000061936; -.
DR   eggNOG; KOG1847; Eukaryota.
DR   GeneTree; ENSGT00940000153892; -.
DR   HOGENOM; CLU_015459_0_0_1; -.
DR   InParanoid; Q12872; -.
DR   OMA; IDMATYY; -.
DR   OrthoDB; 76580at2759; -.
DR   PhylomeDB; Q12872; -.
DR   TreeFam; TF106264; -.
DR   PathwayCommons; Q12872; -.
DR   SignaLink; Q12872; -.
DR   BioGRID-ORCS; 6433; 606 hits in 1161 CRISPR screens.
DR   ChiTaRS; SFSWAP; human.
DR   EvolutionaryTrace; Q12872; -.
DR   GenomeRNAi; 6433; -.
DR   Pharos; Q12872; Tbio.
DR   PRO; PR:Q12872; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q12872; Protein.
DR   Bgee; ENSG00000061936; Expressed in sural nerve and 207 other cell types or tissues.
DR   ExpressionAtlas; Q12872; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   Gene3D; 1.10.10.790; Surp module; 2.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR040397; SWAP.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   InterPro; IPR019147; SWAP_N_domain.
DR   PANTHER; PTHR13161; SPLICING FACTOR SUPPRESSOR OF WHITE APRICOT; 1.
DR   PANTHER; PTHR13161:SF15; SPLICING FACTOR, SUPPRESSOR OF WHITE-APRICOT HOMOLOG; 1.
DR   Pfam; PF09750; DRY_EERY; 1.
DR   Pfam; PF01805; Surp; 2.
DR   SMART; SM01141; DRY_EERY; 1.
DR   SMART; SM00648; SWAP; 2.
DR   SUPFAM; SSF109905; Surp module (SWAP domain); 2.
DR   PROSITE; PS50128; SURP; 2.
DR   Genevisible; Q12872; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..951
FT                   /note="Splicing factor, suppressor of white-apricot
FT                   homolog"
FT                   /id="PRO_0000081934"
FT   REPEAT          211..253
FT                   /note="SURP motif 1"
FT   REPEAT          459..499
FT                   /note="SURP motif 2"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..423
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..814
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..862
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         315
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         604
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         642
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         832
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         834
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3USH5"
FT   MOD_RES         909
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         801
FT                   /note="R -> RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAASTTTRFDSASSFE
FT                   GKPGKT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_044786"
FT   VARIANT         52
FT                   /note="L -> Q (in dbSNP:rs1051207)"
FT                   /evidence="ECO:0000269|PubMed:8206918"
FT                   /id="VAR_046442"
FT   VARIANT         122
FT                   /note="L -> F (in dbSNP:rs1051314)"
FT                   /id="VAR_046443"
FT   VARIANT         136
FT                   /note="L -> F (in dbSNP:rs1131564)"
FT                   /evidence="ECO:0000269|PubMed:8206918"
FT                   /id="VAR_046444"
FT   VARIANT         421
FT                   /note="L -> P (in dbSNP:rs1982528)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8206918, ECO:0000269|Ref.3"
FT                   /id="VAR_021789"
FT   VARIANT         512
FT                   /note="G -> S (in dbSNP:rs34541796)"
FT                   /id="VAR_057248"
FT   VARIANT         538
FT                   /note="E -> G (in dbSNP:rs34744641)"
FT                   /id="VAR_057249"
FT   VARIANT         887
FT                   /note="A -> E (in dbSNP:rs34729193)"
FT                   /id="VAR_057250"
FT   CONFLICT        236
FT                   /note="R -> P (in Ref. 1; AAA19604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="H -> Y (in Ref. 1; AAA19604)"
FT                   /evidence="ECO:0000305"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   HELIX           206..221
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   HELIX           224..233
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   HELIX           249..262
FT                   /evidence="ECO:0007829|PDB:2E60"
FT   TURN            454..456
FT                   /evidence="ECO:0007829|PDB:2E5Z"
FT   HELIX           457..469
FT                   /evidence="ECO:0007829|PDB:2E5Z"
FT   HELIX           472..481
FT                   /evidence="ECO:0007829|PDB:2E5Z"
FT   HELIX           484..486
FT                   /evidence="ECO:0007829|PDB:2E5Z"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:2E5Z"
FT   HELIX           496..509
FT                   /evidence="ECO:0007829|PDB:2E5Z"
SQ   SEQUENCE   951 AA;  104822 MW;  A942D589F4B6BF47 CRC64;
     MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER ALAQEQGQHL
     IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS EEEARIEALC DEERYLALHT
     DLLEEEARQE EEYKRLSEAL AEDGSYNAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN
     LEENEEPFVA PLGLSVPSDV ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF
     DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS
     LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV QPSQVEYTAD
     STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV TVSNSPGVTT TAPPPPGTTP
     LPPPTTAETS SGATSTTTTT SALAPVAAII PPPPDVQPVI DKLAEYVARN GLKFETSVRA
     KNDQRFEFLQ PWHQYNAYYE FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG
     APEDAAEVGA RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL
     DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ AKQKLEDRLA
     AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE AEAGKIEESP FSVEESSTTP
     CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS
     RSRSHSKAKH SLPSAYRTVR RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK
     RTRSRSPHEK KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS
     SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA S
//