ID   MBB1A_MOUSE             Reviewed;        1344 AA.
AC   Q7TPV4; O35851; Q80Y66; Q8R4X2; Q99KP0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Myb-binding protein 1A;
DE   AltName: Full=Myb-binding protein of 160 kDa;
GN   Name=Mybbp1a; Synonyms=P160;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-53; 205-211; 286-290;
RP   458-465 AND 488-496, FUNCTION, INTERACTION WITH JUN AND MYB, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9447996; DOI=10.1128/mcb.18.2.989;
RA   Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J.,
RA   Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S.,
RA   Gonda T.J.;
RT   "Molecular cloning reveals that the p160 Myb-binding protein is a novel,
RT   predominantly nucleolar protein which may play a role in transactivation by
RT   Myb.";
RL   Mol. Cell. Biol. 18:989-1002(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Keough R.A., Gonda T.J.;
RT   "Structural organization of the murine myb-binding protein p160 (Mybbp1a)
RT   gene.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Eye, Mammary gland, and Osteoblast;
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   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND INTERACTION WITH AHR.
RX   PubMed=11956195; DOI=10.1074/jbc.m200740200;
RA   Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.;
RT   "Myb-binding protein 1a augments AhR-dependent gene expression.";
RL   J. Biol. Chem. 277:22515-22519(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, INTERACTION WITH KPNA2, MUTAGENESIS OF LEU-249;
RP   VAL-251; LEU-272 AND LEU-274, AND DOMAINS NES AND NLS.
RX   PubMed=12941609; DOI=10.1016/s0014-4827(03)00262-3;
RA   Keough R.A., Macmillan E.M., Lutwyche J.K., Gardner J.M., Tavner F.J.,
RA   Jans D.A., Henderson B.R., Gonda T.J.;
RT   "Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that
RT   utilizes CRM1-dependent and independent nuclear export pathways.";
RL   Exp. Cell Res. 289:108-123(2003).
RN   [7]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP   PPARGC1A.
RX   PubMed=14744933; DOI=10.1101/gad.1152204;
RA   Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J.,
RA   Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
RT   "Suppression of mitochondrial respiration through recruitment of p160 myb
RT   binding protein to PGC-1alpha: modulation by p38 MAPK.";
RL   Genes Dev. 18:278-289(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1277 AND SER-1280, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253 AND SER-1280, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-1253, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK AND CRY1.
RX   PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA   Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT   "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT   promoter.";
RL   Nucleic Acids Res. 37:1115-1126(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164; SER-1244; SER-1253;
RP   THR-1256; THR-1277; SER-1280; SER-1323 AND SER-1325, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [15]
RP   CITRULLINATION AT ARG-1322.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
CC   -!- FUNCTION: May activate or repress transcription via interactions with
CC       sequence specific DNA-binding proteins (PubMed:9447996,
CC       PubMed:11956195, PubMed:14744933). Repression may be mediated at least
CC       in part by histone deacetylase activity (HDAC activity)
CC       (PubMed:14744933). Acts as a corepressor and in concert with CRY1,
CC       represses the transcription of the core circadian clock component PER2
CC       (PubMed:19129230). Preferentially binds to dimethylated histone H3
CC       'Lys-9' (H3K9me2) on the PER2 promoter (PubMed:19129230). Has a role in
CC       rRNA biogenesis together with PWP1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BQG0, ECO:0000269|PubMed:11956195,
CC       ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230,
CC       ECO:0000269|PubMed:9447996}.
CC   -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC       SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21
CC       (By similarity). Binds to and represses JUN and MYB via the leucine
CC       zipper regions present in these proteins. Also binds to and represses
CC       PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated
CC       by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to
CC       KPNA2. Interacts with CLOCK and CRY1. {ECO:0000250|UniProtKB:Q9BQG0,
CC       ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:12941609,
CC       ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230,
CC       ECO:0000269|PubMed:9447996}.
CC   -!- INTERACTION:
CC       Q7TPV4; P12813: Nr4a1; NbExp=3; IntAct=EBI-1373622, EBI-10896863;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12941609}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:12941609, ECO:0000269|PubMed:19129230}.
CC       Cytoplasm {ECO:0000269|PubMed:12941609}. Note=Predominantly nucleolar.
CC       Also shuttles between the nucleus and cytoplasm. Nuclear import may be
CC       mediated by KPNA2, while export appears to depend partially on
CC       XPO1/CRM1. {ECO:0000269|PubMed:12941609}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:9447996}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC   -!- SIMILARITY: Belongs to the MYBBP1A family. {ECO:0000305}.
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DR   EMBL; U63648; AAC39954.1; -; mRNA.
DR   EMBL; AF345640; AAL83748.1; -; Genomic_DNA.
DR   EMBL; AL662812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004078; AAH04078.1; -; mRNA.
DR   EMBL; BC048858; AAH48858.1; -; mRNA.
DR   EMBL; BC052889; AAH52889.1; -; mRNA.
DR   CCDS; CCDS24986.1; -.
DR   PIR; T34188; T34188.
DR   RefSeq; NP_058056.2; NM_016776.2.
DR   AlphaFoldDB; Q7TPV4; -.
DR   BioGRID; 201999; 45.
DR   ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR   CORUM; Q7TPV4; -.
DR   DIP; DIP-39831N; -.
DR   IntAct; Q7TPV4; 18.
DR   MINT; Q7TPV4; -.
DR   STRING; 10090.ENSMUSP00000044827; -.
DR   GlyGen; Q7TPV4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7TPV4; -.
DR   PhosphoSitePlus; Q7TPV4; -.
DR   SwissPalm; Q7TPV4; -.
DR   EPD; Q7TPV4; -.
DR   jPOST; Q7TPV4; -.
DR   MaxQB; Q7TPV4; -.
DR   PaxDb; 10090-ENSMUSP00000044827; -.
DR   ProteomicsDB; 287318; -.
DR   Pumba; Q7TPV4; -.
DR   Antibodypedia; 23280; 326 antibodies from 31 providers.
DR   DNASU; 18432; -.
DR   Ensembl; ENSMUST00000045633.6; ENSMUSP00000044827.6; ENSMUSG00000040463.17.
DR   GeneID; 18432; -.
DR   KEGG; mmu:18432; -.
DR   UCSC; uc007jyy.1; mouse.
DR   AGR; MGI:106181; -.
DR   CTD; 10514; -.
DR   MGI; MGI:106181; Mybbp1a.
DR   VEuPathDB; HostDB:ENSMUSG00000040463; -.
DR   eggNOG; KOG1926; Eukaryota.
DR   GeneTree; ENSGT00390000017457; -.
DR   HOGENOM; CLU_005997_1_0_1; -.
DR   InParanoid; Q7TPV4; -.
DR   OMA; VWKHDDP; -.
DR   OrthoDB; 2911826at2759; -.
DR   PhylomeDB; Q7TPV4; -.
DR   TreeFam; TF317401; -.
DR   Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR   BioGRID-ORCS; 18432; 30 hits in 83 CRISPR screens.
DR   ChiTaRS; Mybbp1a; mouse.
DR   PRO; PR:Q7TPV4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q7TPV4; Protein.
DR   Bgee; ENSMUSG00000040463; Expressed in embryonic post-anal tail and 276 other cell types or tissues.
DR   ExpressionAtlas; Q7TPV4; baseline and differential.
DR   GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; NAS:ComplexPortal.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR   GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:MGI.
DR   GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR007015; DNA_pol_V/MYBBP1A.
DR   PANTHER; PTHR13213:SF2; MYB-BINDING PROTEIN 1A; 1.
DR   PANTHER; PTHR13213; MYB-BINDING PROTEIN 1A FAMILY MEMBER; 1.
DR   Pfam; PF04931; DNA_pol_phi; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; Q7TPV4; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Biological rhythms; Citrullination; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Ribosome biogenesis; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   CHAIN           2..1344
FT                   /note="Myb-binding protein 1A"
FT                   /id="PRO_0000096256"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..580
FT                   /note="Interaction with MYB"
FT                   /evidence="ECO:0000269|PubMed:9447996"
FT   REGION          710..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1152..1344
FT                   /note="Required for nuclear and nucleolar localization"
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   MOTIF           238..256
FT                   /note="Nuclear export signal 1"
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   MOTIF           261..279
FT                   /note="Nuclear export signal 2"
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   COMPBIAS        724..748
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1231..1260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1283..1299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         156
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1191
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1251
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1256
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1277
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MOD_RES         1322
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         1323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   CROSSLNK        1149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT   MUTAGEN         249
FT                   /note="L->A: Reduced nuclear export; when associated with
FT                   A-251."
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   MUTAGEN         251
FT                   /note="V->A: Reduced nuclear export; when associated with
FT                   A-249."
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   MUTAGEN         272
FT                   /note="L->A: Reduced nuclear export; when associated with
FT                   A-274."
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   MUTAGEN         274
FT                   /note="L->A: Reduced nuclear export; when associated with
FT                   A-272."
FT                   /evidence="ECO:0000269|PubMed:12941609"
FT   CONFLICT        87
FT                   /note="R -> T (in Ref. 1; AAC39954 and 2; AAL83748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="P -> A (in Ref. 1; AAC39954)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        505..508
FT                   /note="DRNR -> HASG (in Ref. 4; AAH04078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1282
FT                   /note="I -> V (in Ref. 4; AAH52889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1344 AA;  152037 MW;  64D3420981CD0767 CRC64;
     MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR
     TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIPLCDIL DQIQEKYSLQ
     AMNKAMMRPS LFANLFGVLA LFQSGRLVKD KEALMKSVQL LKILSQHPNH LQGQPIKALV
     DILSEVPESM FQEILPKVLK GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED
     NIPSLVNILK VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS
     YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI STYVGTFLEG
     CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA LQSYVAWLRD MFLQPDLNSL
     VDFSTANQKR AQDASLNVPE RAVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH
     AFFKTKKATP QIPETKQHFS FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT
     YRLVQLADML LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV
     GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV EILLSLLAQP
     SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED DNVVVTDDAD EKQLQHGEDE
     DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD VDPGFRQQLM EVLKAGNALG GVDNEEEEEL
     GDEAMMALDQ NLASLFKEQK MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE
     HPLILELLEP LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL
     HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG ADTEDSEDQA
     ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY PVICKNLLPV LAQHVAGPSR
     PRHQAQACLM LQKTLSAREL RVCFEDPEWE QLITQLLGKA TQTLQTLGEA QSKGEHQKEL
     SILELLNTLL RTVNHEKLSV DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM
     RMLGVQRPKS EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ
     DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP TLSPSTPAKT
     PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI RKSPHPQSAL PKKRARLSLV
     SRSPSLLQSG VKKRRVASRR VQTP
//