NFAC2_MOUSE
ID NFAC2_MOUSE Reviewed; 927 AA.
AC Q60591; A2APK2; A2APK3; A2AQC5; A2AQC6; A2AQC7; B5B2Q3; Q60984; Q60985;
AC Q91Y65;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 2;
DE Short=NF-ATc2;
DE Short=NFATc2;
DE AltName: Full=NFAT pre-existing subunit;
DE Short=NF-ATp;
DE AltName: Full=T-cell transcription factor NFAT1;
GN Name=Nfatc2; Synonyms=Nfat1, Nfatp;
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], AND PARTIAL PROTEIN SEQUENCE (ISOFORM A).
RX PubMed=8235597; DOI=10.1126/science.8235597;
RA McCaffrey P.G., Luo C., Kerpolla T.K., Jain J., Badalian T.M., Ho A.M.,
RA Burgeon E., Lane W.S., Lambert J.N., Curran T., Verdine G.L., Rao A.,
RA Hogan P.G.;
RT "Isolation of the cyclosporin-sensitive T cell transcription factor
RT NFATp.";
RL Science 262:750-754(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RX PubMed=8668213; DOI=10.1128/mcb.16.7.3955;
RA Luo C., Burgeon E., Carew J.A., McCaffrey P.G., Badalian T.M., Lane W.S.,
RA Hogan P.G., Rao A.;
RT "Recombinant NFAT1 (NFATp) is regulated by calcineurin in T cells and
RT mediates transcription of several cytokine genes.";
RL Mol. Cell. Biol. 16:3955-3966(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11278367; DOI=10.1074/jbc.m007854200;
RA Plyte S., Boncristiano M., Fattori E., Galvagni F., Paccani S.R.,
RA Majolini M.B., Oliviero S., Ciliberto G., Telford J.L., Baldari C.T.;
RT "Identification and characterization of a novel nuclear factor of activated
RT T-cells-1 isoform expressed in mouse brain.";
RL J. Biol. Chem. 276:14350-14358(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=18675896; DOI=10.1016/j.ygeno.2008.06.011;
RA Vihma H., Pruunsild P., Timmusk T.;
RT "Alternative splicing and expression of human and mouse NFAT genes.";
RL Genomics 92:279-291(2008).
RN [5]
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 [6]
RP MUTAGENESIS OF ARG-423; HIS-425; TYR-426; THR-428 AND GLU-429.
RX PubMed=7876165; DOI=10.1074/jbc.270.28.16854;
RA Jain J., Burgeon E., Badalian T.M., Hogan P.G., Rao A.;
RT "A similar DNA-binding motif in NFAT family proteins and the Rel homology
RT region.";
RL J. Biol. Chem. 270:4138-4145(1995).
RN [7]
RP INTERACTION WITH NFATC2IP.
RX PubMed=8943202; DOI=10.1126/science.274.5294.1903;
RA Hodge M.R., Chun H.J., Rengarajan J., Alt A., Lieberson R., Glimcher L.H.;
RT "NF-AT-driven interleukin-4 transcription potentiated by NIP45.";
RL Science 274:1903-1905(1996).
RN [8]
RP MUTAGENESIS OF ARG-112; GLU-114 AND THR-116.
RX PubMed=9660947; DOI=10.1016/s1097-2765(00)80063-5;
RA Aramburu J., Garcia-Cozar F., Raghavan A., Okamura H., Rao A., Hogan P.G.;
RT "Selective inhibition of NFAT activation by a peptide spanning the
RT calcineurin targeting site of NFAT.";
RL Mol. Cell 1:627-637(1998).
RN [9]
RP REVIEW.
RX PubMed=10089876; DOI=10.1016/s0092-8674(00)80571-1;
RA Crabtree G.R.;
RT "Generic signals and specific outcomes: signaling through Ca2+,
RT calcineurin, and NF-AT.";
RL Cell 96:611-614(1999).
RN [10]
RP PHOSPHORYLATION AT SER-99; SER-136; SER-170; SER-173; SER-174; SER-176;
RP SER-177; SER-179; SER-182; SER-215; SER-219; SER-223; SER-238; SER-245;
RP SER-270; SER-276; SER-278; SER-282; SER-328 AND SER-365, SUBCELLULAR
RP LOCATION, INTERACTION WITH XPO1, MUTAGENESIS OF ARG-164, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=11030334; DOI=10.1016/s1097-2765(00)00053-8;
RA Okamura H., Aramburu J., Garcia-Rodriguez C., Viola J.P.B., Raghavan A.,
RA Tahiliani M., Zhang X., Qin J., Hogan P.G., Rao A.;
RT "Concerted dephosphorylation of the transcription factor NFAT1 induces a
RT conformational switch that regulates transcriptional activity.";
RL Mol. Cell 6:539-550(2000).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=17198697; DOI=10.1016/j.ydbio.2006.11.036;
RA Yang X.Y., Yang T.T.C., Schubert W., Factor S.M., Chow C.-W.;
RT "Dosage-dependent transcriptional regulation by the calcineurin/NFAT
RT signaling in developing myocardium transition.";
RL Dev. Biol. 303:825-837(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-257 AND SER-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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 [13]
RP INTERACTION WITH TBX21.
RX PubMed=23616576; DOI=10.4049/jimmunol.1203403;
RA Jang E.J., Park H.R., Hong J.H., Hwang E.S.;
RT "Lysine 313 of T-box is crucial for modulation of protein stability, DNA
RT binding, and threonine phosphorylation of T-bet.";
RL J. Immunol. 190:5764-5770(2013).
RN [14]
RP INTERACTION WITH KAT2A.
RX PubMed=28424240; DOI=10.4049/jimmunol.1600312;
RA Gao B., Kong Q., Zhang Y., Yun C., Dent S.Y.R., Song J., Zhang D.D.,
RA Wang Y., Li X., Fang D.;
RT "The histone acetyltransferase Gcn5 positively regulates T cell
RT activation.";
RL J. Immunol. 198:3927-3938(2017).
CC -!- FUNCTION: Plays a role in the inducible expression of cytokine genes in
CC T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha
CC or GM-CSF. Promotes invasive migration through the activation of GPC6
CC expression and WNT5A signaling pathway. {ECO:0000250|UniProtKB:Q13469}.
CC -!- SUBUNIT: Member of the multicomponent NFATC transcription complex that
CC consists of at least two components, a pre-existing cytoplasmic
CC component NFATC2 and an inducible nuclear component NFATC1. Other
CC members such as NFATC4, NFATC3 or members of the activating protein-1
CC family, MAF, GATA4 and Cbp/p300 can also bind the complex. The
CC phosphorylated form specifically interacts with XPO1; which mediates
CC nuclear export. NFATC proteins bind to DNA as monomers. Interacts with
CC NFATC2IP. Interacts with FOXP3 (By similarity). Interacts with TBX21
CC ('Thr-302' phosphorylated form) (PubMed:23616576). Interacts with KAT2A
CC (PubMed:28424240). Interacts with HOMER2 and HOMER3; this interaction
CC competes with calcineurin/PPP3CA-binding and hence prevents NFATC2
CC dephosphorylation and activation (By similarity). Interacts with
CC protein phosphatase PPP3CA/calcineurin A (By similarity).
CC {ECO:0000250|UniProtKB:Q13469, ECO:0000269|PubMed:11030334,
CC ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:28424240,
CC ECO:0000269|PubMed:8943202}.
CC -!- INTERACTION:
CC Q60591; Q86Y07-1: VRK2; Xeno; NbExp=2; IntAct=EBI-643104, EBI-1207633;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11030334}. Nucleus
CC {ECO:0000269|PubMed:11030334}. Note=Cytoplasmic for the phosphorylated
CC form and nuclear after activation that is controlled by calcineurin-
CC mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to
CC be one mechanism by which cells distinguish between sustained and
CC transient calcium signals. The subcellular localization of NFATC plays
CC a key role in the regulation of gene transcription.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C;
CC IsoId=Q60591-3; Sequence=Displayed;
CC Name=B;
CC IsoId=Q60591-2; Sequence=VSP_005596;
CC Name=D;
CC IsoId=Q60591-4; Sequence=VSP_005597;
CC Name=A;
CC IsoId=Q60591-1; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, testis, brain,
CC placenta, muscle and pancreas. {ECO:0000269|PubMed:18675896}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing heart at 13.5 and 16.5
CC dpc, during the transition from spongy to compact myocardium.
CC {ECO:0000269|PubMed:17198697}.
CC -!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and cooperative
CC interactions with AP1 factors. {ECO:0000250}.
CC -!- PTM: In resting cells, phosphorylated by NFATC-kinase on at least 18
CC sites in the 99-365 region. Upon cell stimulation, all these sites
CC except Ser-245 are dephosphorylated by calcineurin. Dephosphorylation
CC induces a conformational change that simultaneously exposes an NLS and
CC masks an NES, which results in nuclear localization. Simultaneously,
CC one site among Ser-53; Ser-54 and Ser-56 is phosphorylated; which is
CC required for full transcriptional activity.
CC {ECO:0000269|PubMed:11030334}.
CC -!- PTM: Ubiquitinated in endothelial cells by RNF213 downstream of the
CC non-canonical Wnt signaling pathway, leading to its degradation by the
CC proteasome. {ECO:0000250|UniProtKB:Q13469}.
CC -!- MISCELLANEOUS: [Isoform A]: PubMed:8668213 (AAC52929) sequence is a
CC chimeric cDNA. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52929.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA fused with Phyhd1 (Lrrc8a).; Evidence={ECO:0000305};
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DR EMBL; U02079; AAC52929.1; ALT_SEQ; mRNA.
DR EMBL; U36575; AAC52930.1; -; mRNA.
DR EMBL; U36576; AAC52931.1; -; mRNA.
DR EMBL; AF289078; AAK49895.1; -; mRNA.
DR EMBL; EU887588; ACG55608.1; -; mRNA.
DR EMBL; AL840639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17112.1; -. [Q60591-3]
DR CCDS; CCDS50803.1; -. [Q60591-2]
DR PIR; A48753; A48753.
DR RefSeq; NP_035029.2; NM_010899.3. [Q60591-3]
DR AlphaFoldDB; Q60591; -.
DR SMR; Q60591; -.
DR BioGRID; 201739; 2.
DR ComplexPortal; CPX-610; AP-1 transcription factor complex FOS-JUN-NFATC2.
DR CORUM; Q60591; -.
DR DIP; DIP-49476N; -.
DR ELM; Q60591; -.
DR IntAct; Q60591; 11.
DR STRING; 10090.ENSMUSP00000074198; -.
DR MoonDB; Q60591; Predicted.
DR iPTMnet; Q60591; -.
DR PhosphoSitePlus; Q60591; -.
DR EPD; Q60591; -.
DR jPOST; Q60591; -.
DR MaxQB; Q60591; -.
DR PaxDb; Q60591; -.
DR PeptideAtlas; Q60591; -.
DR PRIDE; Q60591; -.
DR ProteomicsDB; 287400; -. [Q60591-3]
DR ProteomicsDB; 287401; -. [Q60591-2]
DR ProteomicsDB; 287402; -. [Q60591-4]
DR Antibodypedia; 1758; 544 antibodies from 46 providers.
DR DNASU; 18019; -.
DR Ensembl; ENSMUST00000074618; ENSMUSP00000074198; ENSMUSG00000027544. [Q60591-3]
DR Ensembl; ENSMUST00000109184; ENSMUSP00000104812; ENSMUSG00000027544. [Q60591-2]
DR GeneID; 18019; -.
DR KEGG; mmu:18019; -.
DR UCSC; uc008oau.2; mouse. [Q60591-3]
DR CTD; 4773; -.
DR MGI; MGI:102463; Nfatc2.
DR VEuPathDB; HostDB:ENSMUSG00000027544; -.
DR eggNOG; ENOG502QTJI; Eukaryota.
DR GeneTree; ENSGT00940000156230; -.
DR HOGENOM; CLU_010185_1_0_1; -.
DR InParanoid; Q60591; -.
DR OMA; PAYSEHT; -.
DR PhylomeDB; Q60591; -.
DR TreeFam; TF326480; -.
DR Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR BioGRID-ORCS; 18019; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Nfatc2; mouse.
DR PRO; PR:Q60591; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60591; protein.
DR Bgee; ENSMUSG00000027544; Expressed in lumbar subsegment of spinal cord and 208 other tissues.
DR ExpressionAtlas; Q60591; baseline and differential.
DR Genevisible; Q60591; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0035976; C:transcription factor AP-1 complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IGI:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0014904; P:myotube cell development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..927
FT /note="Nuclear factor of activated T-cells, cytoplasmic 2"
FT /id="PRO_0000205179"
FT REPEAT 186..202
FT /note="1"
FT REPEAT 215..231
FT /note="2"
FT REPEAT 274..290
FT /note="3; approximate"
FT DOMAIN 394..576
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DNA_BIND 423..430
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..116
FT /note="Calcineurin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT REGION 119..201
FT /note="Trans-activation domain A (TAD-A)"
FT REGION 163..177
FT /note="Required for cytoplasmic retention of the
FT phosphorylated form"
FT REGION 186..292
FT /note="3 X approximate SP repeats"
FT REGION 203..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 253..255
FT /note="Nuclear localization signal"
FT COMPBIAS 211..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11030334"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11030334,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13469"
FT VAR_SEQ 619..806
FT /note="DGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRS
FT QPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAP
FT CQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLV
FT HAGSQGQGQGSTLPHTSS -> GPAGTCETRPLPISLISADRLSPWLSRLQRNPPGSVF
FT RCSVLLPAPGSSLVLLAL (in isoform D)"
FT /evidence="ECO:0000303|PubMed:11278367"
FT /id="VSP_005597"
FT VAR_SEQ 910..927
FT /note="VNEIIRKEFSGPPSRNQT -> ELIDTHLSWIQNIL (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8668213"
FT /id="VSP_005596"
FT MUTAGEN 112
FT /note="R->A: Lowers dephosphorylation."
FT /evidence="ECO:0000269|PubMed:9660947"
FT MUTAGEN 114
FT /note="E->A: Lowers dephosphorylation."
FT /evidence="ECO:0000269|PubMed:9660947"
FT MUTAGEN 116
FT /note="T->A: No dephosphorylation."
FT /evidence="ECO:0000269|PubMed:9660947"
FT MUTAGEN 164
FT /note="R->A: Induces aberrant nuclear localization of the
FT phosphorylated form."
FT /evidence="ECO:0000269|PubMed:11030334"
FT MUTAGEN 423
FT /note="R->A: Decrease in binding to DNA."
FT /evidence="ECO:0000269|PubMed:7876165"
FT MUTAGEN 425
FT /note="H->A: No change in binding to DNA."
FT /evidence="ECO:0000269|PubMed:7876165"
FT MUTAGEN 426
FT /note="Y->A: Decrease in binding to DNA."
FT /evidence="ECO:0000269|PubMed:7876165"
FT MUTAGEN 428
FT /note="T->A: No change in binding to DNA."
FT /evidence="ECO:0000269|PubMed:7876165"
FT MUTAGEN 428
FT /note="T->C: No change in binding to DNA and confers DNA-
FT binding sensitivity to sulfhydryl modifications."
FT /evidence="ECO:0000269|PubMed:7876165"
FT MUTAGEN 429
FT /note="E->A: Decrease in binding to DNA."
FT /evidence="ECO:0000269|PubMed:7876165"
FT CONFLICT 78
FT /note="L -> P (in Ref. 3; AAK49895)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> P (in Ref. 2; AAC52929/AAC52930/AAC52931)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="P -> R (in Ref. 2; AAC52929/AAC52930/AAC52931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 927 AA; 100020 MW; F21E7BABE7DBB40F CRC64;
MDVPEPQPDP DGGDGPGHEP GGSPQDELDF SILFDYDYLN PIEEEPIAHK AISSPSGLAY
PDDVLDYGLK PCNPLASLSG EPPGRFGEPD SIGFQNFLSP VKPAGASGPS PRIEITPSHE
LMQAGGALRG RDAGLSPEQP ALALAGVAAS PRFTLPVPGY EGYREPLCLS PASSGSSASF
ISDTFSPYTS PCVSPNNAGP DDLCPQFQNI PAHYSPRTSP IMSPRTSLAE DSCLGRHSPV
PRPASRSSSP GAKRRHSCAE ALVAPLPAAS PQRSRSPSPQ PSPHVALQDD SIPAGYPPTA
GSAVLMDALN TLATDSPCGI PSKIWKTSPD PTPVSTAPSK AGLARHIYPT VEFLGPCEQE
ERRNSAPESI LLVPPTWPKQ LVPAIPICSI PVTASLPPLE WPLSNQSGSY ELRIEVQPKP
HHRAHYETEG SRGAVKAPTG GHPVVQLHGY MENKPLGLQI FIGTADERIL KPHAFYQVHR
ITGKTVTTTS YEKIVGNTKV LEIPLEPKNN MRATIDCAGI LKLRNADIEL RKGETDIGRK
NTRVRLVFRV HVPEPSGRIV SLQAASNPIE CSQRSAHELP MVERQDMDSC LVYGGQQMIL
TGQNFTAESK VVFMEKTTDG QQIWEMEATV DKDKSQPNML FVEIPEYRNK HIRVPVKVNF
YVINGKRKRS QPQHFTYHPV PAIKTEPSDE YEPSLICSPA HGGLGSQPYY PQHPMLAESP
SCLVATMAPC QQFRSGLSSP DARYQQQSPA AALYQRSKSL SPGLLGYQQP SLLAAPLGLA
DAHRSVLVHA GSQGQGQGST LPHTSSASQQ ASPVIHYSPT NQQLRGGGHQ EFQHIMYCEN
FGPSSARPGP PPINQGQRLS PGAYPTVIQQ QTAPSQRAAK NGPSDQKEAL PTGVTVKQEQ
NLDQTYLDDV NEIIRKEFSG PPSRNQT
