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   24-JAN-2024, entry version 189.
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="https://atlasgeneticsoncology.org/gene/42997/PPP1R13L";
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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; 112.
DR   CORUM; Q8WUF5; -.
DR   DIP; DIP-29586N; -.
DR   IntAct; Q8WUF5; 35.
DR   MINT; Q8WUF5; -.
DR   STRING; 9606.ENSP00000354218; -.
DR   GlyGen; Q8WUF5; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000403902; -.
DR   PeptideAtlas; Q8WUF5; -.
DR   ProteomicsDB; 74665; -.
DR   Pumba; Q8WUF5; -.
DR   Antibodypedia; 31307; 318 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   AGR; HGNC:18838; -.
DR   CTD; 10848; -.
DR   DisGeNET; 10848; -.
DR   GeneCards; PPP1R13L; -.
DR   HGNC; HGNC:18838; PPP1R13L.
DR   HPA; ENSG00000104881; Tissue enhanced (esophagus, heart muscle, skin).
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; QPNQYKH; -.
DR   OrthoDB; 5476196at2759; -.
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   SIGNOR; Q8WUF5; -.
DR   BioGRID-ORCS; 10848; 29 hits in 1161 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 141 other cell types or tissues.
DR   ExpressionAtlas; Q8WUF5; baseline and differential.
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-level 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; Ankyrin repeat-containing domain; 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; RELA-ASSOCIATED INHIBITOR; 1.
DR   PANTHER; PTHR24164:SF4; RELA-ASSOCIATED INHIBITOR; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q8WUF5; HS.
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
//