ID   SCAF4_HUMAN             Reviewed;        1147 AA.
AC   O95104; C9JLZ0; Q0P5W8; Q6P1M5; Q8N3I8; Q9UFM1; Q9ULP8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=SR-related and CTD-associated factor 4 {ECO:0000303|PubMed:31104839};
DE   AltName: Full=CTD-binding SR-like protein RA4 {ECO:0000305};
DE   AltName: Full=Splicing factor, arginine/serine-rich 15 {ECO:0000305};
GN   Name=SCAF4 {ECO:0000303|PubMed:31104839, ECO:0000312|HGNC:HGNC:19304};
GN   Synonyms=KIAA1172 {ECO:0000303|PubMed:10574461}, SFRS15
GN   {ECO:0000312|HGNC:HGNC:19304};
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).
RA   Tassone F., Villard L., Gardiner K.;
RT   "Sequence, genomic organization and map localization of the human SR
RT   protein gene rA4.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Trachea;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Melanoma, and 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., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1147 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP   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-154, AND IDENTIFICATION BY
RP   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-49, 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   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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-1004, 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POLR2A.
RX   PubMed=31104839; DOI=10.1016/j.cell.2019.04.038;
RA   Gregersen L.H., Mitter R., Ugalde A.P., Nojima T., Proudfoot N.J.,
RA   Agami R., Stewart A., Svejstrup J.Q.;
RT   "SCAF4 and SCAF8, mRNA anti-terminator proteins.";
RL   Cell 0:0-0(2019).
CC   -!- FUNCTION: Anti-terminator protein required to prevent early mRNA
CC       termination during transcription (PubMed:31104839). Together with
CC       SCAF8, acts by suppressing the use of early, alternative poly(A) sites,
CC       thereby preventing the accumulation of non-functional truncated
CC       proteins (PubMed:31104839). Mechanistically, associates with the
CC       phosphorylated C-terminal heptapeptide repeat domain (CTD) of the
CC       largest RNA polymerase II subunit (POLR2A), and subsequently binds
CC       nascent RNA upstream of early polyadenylation sites to prevent
CC       premature mRNA transcript cleavage and polyadenylation
CC       (PubMed:31104839). Independently of SCAF8, also acts as a suppressor of
CC       transcriptional readthrough (PubMed:31104839).
CC       {ECO:0000269|PubMed:31104839}.
CC   -!- SUBUNIT: Interacts with POLR2A; via C-terminal heptapeptide repeat
CC       domain (CTD) phosphorylated at 'Ser-2' and 'Ser-5'.
CC       {ECO:0000269|PubMed:31104839}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31104839}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O95104-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95104-2; Sequence=VSP_005879;
CC       Name=3;
CC         IsoId=O95104-3; Sequence=VSP_047351;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD09327.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF023142; AAD09327.1; ALT_INIT; mRNA.
DR   EMBL; AK308406; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL834304; CAD38974.2; -; mRNA.
DR   EMBL; AL117417; CAB55911.1; ALT_SEQ; mRNA.
DR   EMBL; AP001711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014921; AAH14921.1; -; mRNA.
DR   EMBL; BC052286; AAH52286.1; -; mRNA.
DR   EMBL; BC064990; AAH64990.1; -; mRNA.
DR   EMBL; AB032998; BAA86486.1; -; mRNA.
DR   CCDS; CCDS33537.1; -. [O95104-1]
DR   CCDS; CCDS46644.1; -. [O95104-2]
DR   CCDS; CCDS54482.1; -. [O95104-3]
DR   RefSeq; NP_001138916.1; NM_001145444.1. [O95104-3]
DR   RefSeq; NP_001138917.1; NM_001145445.1. [O95104-2]
DR   RefSeq; NP_065757.1; NM_020706.2. [O95104-1]
DR   PDB; 6XKB; X-ray; 1.60 A; A/B/C/D/E=1-139.
DR   PDBsum; 6XKB; -.
DR   AlphaFoldDB; O95104; -.
DR   SMR; O95104; -.
DR   BioGRID; 121536; 131.
DR   IntAct; O95104; 23.
DR   MINT; O95104; -.
DR   STRING; 9606.ENSP00000286835; -.
DR   GlyCosmos; O95104; 1 site, 1 glycan.
DR   GlyGen; O95104; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O95104; -.
DR   PhosphoSitePlus; O95104; -.
DR   BioMuta; SCAF4; -.
DR   EPD; O95104; -.
DR   jPOST; O95104; -.
DR   MassIVE; O95104; -.
DR   MaxQB; O95104; -.
DR   PaxDb; 9606-ENSP00000286835; -.
DR   PeptideAtlas; O95104; -.
DR   ProteomicsDB; 10774; -.
DR   ProteomicsDB; 50653; -. [O95104-1]
DR   ProteomicsDB; 50654; -. [O95104-2]
DR   Pumba; O95104; -.
DR   Antibodypedia; 6761; 127 antibodies from 24 providers.
DR   DNASU; 57466; -.
DR   Ensembl; ENST00000286835.12; ENSP00000286835.7; ENSG00000156304.15. [O95104-1]
DR   Ensembl; ENST00000399804.5; ENSP00000382703.1; ENSG00000156304.15. [O95104-2]
DR   Ensembl; ENST00000434667.3; ENSP00000402377.2; ENSG00000156304.15. [O95104-3]
DR   GeneID; 57466; -.
DR   KEGG; hsa:57466; -.
DR   MANE-Select; ENST00000286835.12; ENSP00000286835.7; NM_020706.2; NP_065757.1.
DR   UCSC; uc002ypd.3; human. [O95104-1]
DR   AGR; HGNC:19304; -.
DR   CTD; 57466; -.
DR   DisGeNET; 57466; -.
DR   GeneCards; SCAF4; -.
DR   HGNC; HGNC:19304; SCAF4.
DR   HPA; ENSG00000156304; Low tissue specificity.
DR   MalaCards; SCAF4; -.
DR   MIM; 616023; gene.
DR   neXtProt; NX_O95104; -.
DR   OpenTargets; ENSG00000156304; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA134903281; -.
DR   VEuPathDB; HostDB:ENSG00000156304; -.
DR   eggNOG; KOG0132; Eukaryota.
DR   GeneTree; ENSGT00530000063946; -.
DR   HOGENOM; CLU_005263_0_1_1; -.
DR   InParanoid; O95104; -.
DR   OMA; DSREKMT; -.
DR   OrthoDB; 5406494at2759; -.
DR   PhylomeDB; O95104; -.
DR   TreeFam; TF324527; -.
DR   PathwayCommons; O95104; -.
DR   SignaLink; O95104; -.
DR   BioGRID-ORCS; 57466; 114 hits in 1169 CRISPR screens.
DR   ChiTaRS; SCAF4; human.
DR   GenomeRNAi; 57466; -.
DR   Pharos; O95104; Tbio.
DR   PRO; PR:O95104; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; O95104; Protein.
DR   Bgee; ENSG00000156304; Expressed in tendon of biceps brachii and 181 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:UniProtKB.
DR   GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:UniProtKB.
DR   CDD; cd17005; CID_SFRS15_SCAF4; 1.
DR   CDD; cd12461; RRM_SCAF4; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034369; SCAF4_RRM.
DR   PANTHER; PTHR23140; RNA PROCESSING PROTEIN LD23810P; 1.
DR   PANTHER; PTHR23140:SF3; SR-RELATED AND CTD-ASSOCIATED FACTOR 4; 1.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; O95104; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..1147
FT                   /note="SR-related and CTD-associated factor 4"
FT                   /id="PRO_0000081943"
FT   DOMAIN          1..139
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   DOMAIN          508..582
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          145..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..477
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..917
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..976
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1087
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         656
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         1004
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         38..52
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047351"
FT   VAR_SEQ         766..788
FT                   /note="STIAGINEDTTKDLSIGNPIPTV -> L (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10574461,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_005879"
FT   VARIANT         846
FT                   /note="S -> Y (in dbSNP:rs12152067)"
FT                   /id="VAR_052234"
FT   CONFLICT        1
FT                   /note="M -> W (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260..264
FT                   /note="Missing (in Ref. 3; CAB55911)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="T -> I (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="T -> A (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="T -> A (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="V -> L (in Ref. 6; BAA86486)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="H -> Y (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="L -> V (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="N -> T (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        598..600
FT                   /note="GVT -> CVI (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        604..606
FT                   /note="WDK -> CDN (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        612
FT                   /note="L -> M (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="C -> Y (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="D -> N (in Ref. 3; AK308406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        808..826
FT                   /note="AVPPAAPTNLPTPPVTQPV -> TCCTHESAHPSCNPACLPC (in Ref.
FT                   1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        844
FT                   /note="A -> E (in Ref. 1; AAD09327)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1139
FT                   /note="S -> G (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1..12
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           13..16
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           23..35
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           40..53
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           92..99
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:6XKB"
FT   HELIX           125..134
FT                   /evidence="ECO:0007829|PDB:6XKB"
SQ   SEQUENCE   1147 AA;  125869 MW;  DED5EEAB45DB4B83 CRC64;
     MDAVNAFNQE LFSLMDMKPP ISRAKMILIT KAAIKAIKLY KHVVQIVEKF IKKCKPEYKV
     PGLYVIDSIV RQSRHQFGTD KDVFGPRFSK NITATFQYLY LCPSEDKSKI VRVLNLWQKN
     GVFKIEIIQP LLDMAAGTSN AAPVAENVTN NEGSPPPPVK VSSEPPTQAT PNSVPAVPQL
     PSSDAFAAVA QLFQTTQGQQ LQQILQTFQQ PPKPQSPALD NAVMAQVQAI TAQLKTTPTQ
     PSEQKAAFPP PEQKTAFDKK LLDRFDYDDE PEAVEESKKE DTTAVTTTAP AAAVPPAPTA
     TVPAAAAPAA ASPPPPQAPF GFPGDGMQQP AYTQHQNMDQ FQPRMMGIQQ DPMHHQVPLP
     PNGQMPGFGL LPTPPFPPMA QPVIPPTPPV QQPFQASFQA QNEPLTQKPH QQEMEVEQPC
     IQEVKRHMSD NRKSRSRSAS RSPKRRRSRS GSRSRRSRHR RSRSRSRDRR RHSPRSRSQE
     RRDREKERER RQKGLPQVKP ETASVCSTTL WVGQLDKRTT QQDVASLLEE FGPIESINMI
     PPRGCAYIVM VHRQDAYRAL QKLSRGNYKV NQKSIKIAWA LNKGIKADYK QYWDVELGVT
     YIPWDKVKPE ELESFCEGGM LDSDTLNPDW KGIPKKPENE VAQNGGAETS HTEPVSPIPK
     PLPVPVPPIP VPAPITVPPP QVPPHQPGPP VVGALQPPAF TPPLGIPPPG FGPGVPPPPP
     PPPFLRPGFN PMHLPPGFLP PGPPPPITPP VSIPPPHTPP ISIPNSTIAG INEDTTKDLS
     IGNPIPTVVS GARGNAESGD SVKMYGSAVP PAAPTNLPTP PVTQPVSLLG TQGVAPGPVI
     GLQAPSTGLL GARPGLIPLQ RPPGMPPPHL QRFPLMPPRP MPPHMMHRGP PPGPGGFAMP
     PPHGMKGPFP PHGPFVRPGG MPGLGGPGPG PGGPEDRDGR QQPPQQPQQQ PQPQAPQQPQ
     QQQQQQPPPS QQPPPTQQQP QQFRNDNRQQ FNSGRDQERF GRRSFGNRVE NDRERYGNRN
     DDRDNSNRDR REWGRRSPDR DRHRDLEERN RRSSGHRDRE RDSRDRESRR EKEEARGKEK
     PEVTDRAGGN KTVEPPISQV GNVDTASELE KGVSEAAVLK PSEELPAEAT SSVEPEKDSG
     SAAEAPR
//