IASPP_HUMAN
ID IASPP_HUMAN Reviewed; 828 AA.
AC Q8WUF5; Q2PNZ9; Q5DU71; Q5I1X4; Q6P1R7; Q6PKF8; Q9Y290;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=RelA-associated inhibitor;
DE AltName: Full=Inhibitor of ASPP protein;
DE Short=Protein iASPP;
DE AltName: Full=NFkB-interacting protein 1;
DE AltName: Full=PPP1R13B-like protein;
GN Name=PPP1R13L; Synonyms=IASPP, NKIP1, PPP1R13BL, RAI;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH TP53, AND CAUTION.
RX PubMed=15489900; DOI=10.1038/sj.onc.1208088;
RA Slee E.A., Gillotin S., Bergamaschi D., Royer C., Llanos S., Ali S.,
RA Jin B., Trigiante G., Lu X.;
RT "The N-terminus of a novel isoform of human iASPP is required for its
RT cytoplasmic localization.";
RL Oncogene 23:9007-9016(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Herron B.J., Rao C., Beier D.R.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, Placenta, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 317-828, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH RELA, AND CAUTION.
RC TISSUE=Placenta;
RX PubMed=10336463; DOI=10.1074/jbc.274.22.15662;
RA Yang J.-P., Hori M., Sanda T., Okamoto T.;
RT "Identification of a novel inhibitor of nuclear factor-kappaB, RelA-
RT associated inhibitor.";
RL J. Biol. Chem. 274:15662-15670(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH SP1.
RX PubMed=12134007; DOI=10.1128/jvi.76.16.8019-8030.2002;
RA Takada N., Sanda T., Okamoto H., Yang J.-P., Asamitsu K., Sarol L.,
RA Kimura G., Uranishi H., Tetsuka T., Okamoto T.;
RT "RelA-associated inhibitor blocks transcription of human immunodeficiency
RT virus type 1 by inhibiting NF-kappaB and Sp1 actions.";
RL J. Virol. 76:8019-8030(2002).
RN [7]
RP FUNCTION, INTERACTION WITH TP53, AND DOMAIN.
RX PubMed=12524540; DOI=10.1038/ng1070;
RA Bergamaschi D., Samuels Y., O'Neil N.J., Trigiante G., Crook T.,
RA Hsieh J.-K., O'Connor D.J., Zhong S., Campargue I., Tomlinson M.L.,
RA Kuwabara P.E., Lu X.;
RT "iASPP oncoprotein is a key inhibitor of p53 conserved from worm to
RT human.";
RL Nat. Genet. 33:162-167(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-113; SER-183 AND
RP SER-187, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-110; SER-113;
RP SER-119; SER-120; THR-123; SER-134; SER-203; SER-316; SER-332; SER-526;
RP SER-567 AND SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-113; SER-183;
RP SER-187; SER-280 AND SER-567, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-100; SER-102;
RP SER-113; SER-134; SER-187; THR-308; SER-332; SER-339; THR-341 AND SER-567,
RP 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 [17]
RP IDENTIFICATION BY 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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-167 AND ARG-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 607-828, AND INTERACTION WITH
RP TP53/P53; TP63 AND TP73.
RX PubMed=18275817; DOI=10.1016/j.str.2007.11.012;
RA Robinson R.A., Lu X., Jones E.Y., Siebold C.;
RT "Biochemical and structural studies of ASPP proteins reveal differential
RT binding to p53, p63, and p73.";
RL Structure 16:259-268(2008).
CC -!- FUNCTION: Regulator that plays a central role in regulation of
CC apoptosis and transcription via its interaction with NF-kappa-B and
CC p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting
CC the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function,
CC possibly by preventing the association between p53/TP53 and ASPP1 or
CC ASPP2, and therefore suppressing the subsequent activation of apoptosis
CC (PubMed:12524540). {ECO:0000269|PubMed:10336463,
CC ECO:0000269|PubMed:12134007, ECO:0000269|PubMed:12524540,
CC ECO:0000269|PubMed:15489900}.
CC -!- SUBUNIT: Interacts with RELA NF-kappa-B subunit and with SP1 via its C-
CC terminus part. Interacts (via SH3 domain and ANK repeats) with
CC p53/TP53; the interaction inhibits pro-apoptotic activity of p53/TP53
CC (PubMed:12524540). Interacts with TP63 and TP73.
CC {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:12134007,
CC ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:15489900,
CC ECO:0000269|PubMed:18275817}.
CC -!- INTERACTION:
CC Q8WUF5; Q09472: EP300; NbExp=2; IntAct=EBI-5550163, EBI-447295;
CC Q8WUF5; P62136: PPP1CA; NbExp=8; IntAct=EBI-5550163, EBI-357253;
CC Q8WUF5; P62140: PPP1CB; NbExp=6; IntAct=EBI-5550163, EBI-352350;
CC Q8WUF5; Q8WUF5: PPP1R13L; NbExp=5; IntAct=EBI-5550163, EBI-5550163;
CC Q8WUF5; P62826: RAN; NbExp=9; IntAct=EBI-5550163, EBI-286642;
CC Q8WUF5; P04637: TP53; NbExp=12; IntAct=EBI-5550163, EBI-366083;
CC Q8WUF5; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-5550163, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15489900}. Nucleus
CC {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:15489900}.
CC Note=Predominantly cytoplasmic but also nuclear.
CC {ECO:0000269|PubMed:15489900}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta and prostate.
CC Weakly expressed in brain, liver, skeletal muscle, testis and
CC peripheral blood leukocyte. {ECO:0000269|PubMed:10336463}.
CC -!- DOMAIN: The N-terminal region is required for cytoplasmic localization.
CC {ECO:0000269|PubMed:15489900}.
CC -!- DOMAIN: The ANK repeats and the SH3 domain are required for specific
CC interactions with p53/TP53. {ECO:0000269|PubMed:12524540}.
CC -!- SIMILARITY: Belongs to the iASPP family. {ECO:0000305}.
CC -!- CAUTION: An alternative product iASPP(RAI) has been described
CC (PubMed:15489900, PubMed:10336463). However, it is not detected in vivo
CC and is most probably a cloning artifact (PubMed:15489900).
CC {ECO:0000269|PubMed:10336463, ECO:0000269|PubMed:15489900}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27004.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD27005.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD27005.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PPP1R13LID42997ch19q13.html";
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DR EMBL; AJ888472; CAI60219.1; -; mRNA.
DR EMBL; AY869712; AAW51146.1; -; mRNA.
DR EMBL; DQ314886; ABC40745.1; -; Genomic_DNA.
DR EMBL; BC001475; AAH01475.1; -; mRNA.
DR EMBL; BC020589; AAH20589.1; -; mRNA.
DR EMBL; BC032298; AAH32298.1; -; mRNA.
DR EMBL; BC064913; AAH64913.1; -; mRNA.
DR EMBL; AF078036; AAD27004.1; ALT_FRAME; mRNA.
DR EMBL; AF078037; AAD27005.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33050.1; -.
DR RefSeq; NP_001135974.1; NM_001142502.1.
DR RefSeq; NP_006654.2; NM_006663.3.
DR RefSeq; XP_016881666.1; XM_017026177.1.
DR RefSeq; XP_016881667.1; XM_017026178.1.
DR PDB; 2VGE; X-ray; 2.10 A; A=607-828.
DR PDB; 6DCX; X-ray; 3.41 A; C/D=608-828.
DR PDB; 6HL6; X-ray; 1.97 A; S=670-693.
DR PDB; 6RZ3; X-ray; 4.23 A; B=625-828.
DR PDBsum; 2VGE; -.
DR PDBsum; 6DCX; -.
DR PDBsum; 6HL6; -.
DR PDBsum; 6RZ3; -.
DR AlphaFoldDB; Q8WUF5; -.
DR SASBDB; Q8WUF5; -.
DR SMR; Q8WUF5; -.
DR BioGRID; 116059; 99.
DR CORUM; Q8WUF5; -.
DR DIP; DIP-29586N; -.
DR IntAct; Q8WUF5; 35.
DR MINT; Q8WUF5; -.
DR STRING; 9606.ENSP00000403902; -.
DR iPTMnet; Q8WUF5; -.
DR PhosphoSitePlus; Q8WUF5; -.
DR BioMuta; PPP1R13L; -.
DR DMDM; 92090607; -.
DR EPD; Q8WUF5; -.
DR jPOST; Q8WUF5; -.
DR MassIVE; Q8WUF5; -.
DR MaxQB; Q8WUF5; -.
DR PaxDb; Q8WUF5; -.
DR PeptideAtlas; Q8WUF5; -.
DR PRIDE; Q8WUF5; -.
DR ProteomicsDB; 74665; -.
DR Antibodypedia; 31307; 271 antibodies from 31 providers.
DR DNASU; 10848; -.
DR Ensembl; ENST00000360957.10; ENSP00000354218.4; ENSG00000104881.16.
DR Ensembl; ENST00000418234.6; ENSP00000403902.1; ENSG00000104881.16.
DR GeneID; 10848; -.
DR KEGG; hsa:10848; -.
DR MANE-Select; ENST00000360957.10; ENSP00000354218.4; NM_006663.4; NP_006654.2.
DR UCSC; uc002pbn.4; human.
DR CTD; 10848; -.
DR DisGeNET; 10848; -.
DR GeneCards; PPP1R13L; -.
DR HGNC; HGNC:18838; PPP1R13L.
DR HPA; ENSG00000104881; Group enriched (esophagus, heart muscle, salivary gland, skin, vagina).
DR MalaCards; PPP1R13L; -.
DR MIM; 607463; gene.
DR neXtProt; NX_Q8WUF5; -.
DR OpenTargets; ENSG00000104881; -.
DR PharmGKB; PA34195; -.
DR VEuPathDB; HostDB:ENSG00000104881; -.
DR eggNOG; KOG0515; Eukaryota.
DR GeneTree; ENSGT00940000160551; -.
DR HOGENOM; CLU_019814_0_0_1; -.
DR InParanoid; Q8WUF5; -.
DR OMA; FQTMNDD; -.
DR OrthoDB; 1041229at2759; -.
DR PhylomeDB; Q8WUF5; -.
DR TreeFam; TF105545; -.
DR PathwayCommons; Q8WUF5; -.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR SignaLink; Q8WUF5; -.
DR BioGRID-ORCS; 10848; 29 hits in 1085 CRISPR screens.
DR ChiTaRS; PPP1R13L; human.
DR EvolutionaryTrace; Q8WUF5; -.
DR GeneWiki; PPP1R13L; -.
DR GenomeRNAi; 10848; -.
DR Pharos; Q8WUF5; Tbio.
DR PRO; PR:Q8WUF5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8WUF5; protein.
DR Bgee; ENSG00000104881; Expressed in lower esophagus mucosa and 139 other tissues.
DR ExpressionAtlas; Q8WUF5; baseline and differential.
DR Genevisible; Q8WUF5; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IEA:Ensembl.
DR GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:0042633; P:hair cycle; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0048871; P:multicellular organismal homeostasis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IEA:Ensembl.
DR CDD; cd11952; SH3_iASPP; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR028320; iASPP.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR042722; SH3_iASPP.
DR PANTHER; PTHR24164; PTHR24164; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Apoptosis; Cytoplasm; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; SH3 domain;
KW Transcription; Transcription regulation.
FT CHAIN 1..828
FT /note="RelA-associated inhibitor"
FT /id="PRO_0000066966"
FT REPEAT 659..691
FT /note="ANK 1"
FT REPEAT 692..724
FT /note="ANK 2"
FT DOMAIN 758..820
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 45..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5I1X5"
FT MOD_RES 142
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5I1X5"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5I1X5"
FT MOD_RES 160
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5I1X5"
FT MOD_RES 167
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 180
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 205
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5I1X5"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT 198
FT /note="P -> S (in Ref. 4; AAH64913)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="L -> I (in Ref. 2; AAW51146)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="PL -> AA (in Ref. 5; AAD27004)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> T (in Ref. 5; AAD27004)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="P -> S (in Ref. 2; AAW51146)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Missing (in Ref. 2; AAW51146)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="P -> Q (in Ref. 5; AAD27004)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="PQ -> HP (in Ref. 5; AAD27004)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="Y -> S (in Ref. 2; AAW51146)"
FT /evidence="ECO:0000305"
FT HELIX 627..637
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 640..649
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 663..669
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 675..679
FT /evidence="ECO:0007829|PDB:6HL6"
FT HELIX 696..702
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 706..713
FT /evidence="ECO:0007829|PDB:2VGE"
FT TURN 714..716
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 741..754
FT /evidence="ECO:0007829|PDB:2VGE"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 759..761
FT /evidence="ECO:0007829|PDB:2VGE"
FT STRAND 762..767
FT /evidence="ECO:0007829|PDB:2VGE"
FT STRAND 784..791
FT /evidence="ECO:0007829|PDB:2VGE"
FT STRAND 796..803
FT /evidence="ECO:0007829|PDB:2VGE"
FT STRAND 806..811
FT /evidence="ECO:0007829|PDB:2VGE"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:2VGE"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:2VGE"
SQ SEQUENCE 828 AA; 89091 MW; 7BEEF239B7CA9C70 CRC64;
MDSEAFQSAR DFLDMNFQSL AMKHMDLKQM ELDTAAAKVD ELTKQLESLW SDSPAPPGPQ
AGPPSRPPRY SSSSIPEPFG SRGSPRKAAT DGADTPFGRS ESAPTLHPYS PLSPKGRPSS
PRTPLYLQPD AYGSLDRATS PRPRAFDGAG SSLGRAPSPR PGPGPLRQQG PPTPFDFLGR
AGSPRGSPLA EGPQAFFPER GPSPRPPATA YDAPASAFGS SLLGSGGSAF APPLRAQDDL
TLRRRPPKAW NESDLDVAYE KKPSQTASYE RLDVFARPAS PSLQLLPWRE SSLDGLGGTG
KDNLTSATLP RNYKVSPLAS DRRSDAGSYR RSLGSAGPSG TLPRSWQPVS RIPMPPSSPQ
PRGAPRQRPI PLSMIFKLQN AFWEHGASRA MLPGSPLFTR APPPKLQPQP QPQPQPQSQP
QPQLPPQPQT QPQTPTPAPQ HPQQTWPPVN EGPPKPPTEL EPEPEIEGLL TPVLEAGDVD
EGPVARPLSP TRLQPALPPE AQSVPELEEV ARVLAEIPRP LKRRGSMEQA PAVALPPTHK
KQYQQIISRL FHRHGGPGPG GPEPELSPIT EGSEARAGPP APAPPAPIPP PAPSQSSPPE
QPQSMEMRSV LRKAGSPRKA RRARLNPLVL LLDAALTGEL EVVQQAVKEM NDPSQPNEEG
ITALHNAICG ANYSIVDFLI TAGANVNSPD SHGWTPLHCA ASCNDTVICM ALVQHGAAIF
ATTLSDGATA FEKCDPYREG YADCATYLAD VEQSMGLMNS GAVYALWDYS AEFGDELSFR
EGESVTVLRR DGPEETDWWW AALHGQEGYV PRNYFGLFPR VKPQRSKV
