ID   ASPP1_HUMAN             Reviewed;        1090 AA.
AC   Q96KQ4; B2RMX5; O94870;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Apoptosis-stimulating of p53 protein 1;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 13B;
GN   Name=PPP1R13B; Synonyms=ASPP1, KIAA0771;
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, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH TP53.
RX   PubMed=11684014; DOI=10.1016/s1097-2765(01)00367-7;
RA   Samuels-Lev Y., O'Connor D.J., Bergamaschi D., Trigiante G., Hsieh J.-K.,
RA   Zhong S., Campargue I., Naumovski L., Crook T., Lu X.;
RT   "ASPP proteins specifically stimulate the apoptotic function of p53.";
RL   Mol. Cell 8:781-794(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [LARGE SCALE MRNA] OF 143-1090.
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH TP53.
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-335, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [10]
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).
CC   -!- FUNCTION: Regulator that plays a central role in regulation of
CC       apoptosis via its interaction with p53/TP53 (PubMed:11684014,
CC       PubMed:12524540). Regulates TP53 by enhancing the DNA binding and
CC       transactivation function of TP53 on the promoters of proapoptotic genes
CC       in vivo. {ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540}.
CC   -!- SUBUNIT: Interacts with P53/TP53; the interaction promotes pro-
CC       apoptotic activity. {ECO:0000269|PubMed:11684014,
CC       ECO:0000269|PubMed:12524540}.
CC   -!- INTERACTION:
CC       Q96KQ4; Q4G176: ACSF3; NbExp=3; IntAct=EBI-1105153, EBI-10714818;
CC       Q96KQ4; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-1105153, EBI-2825900;
CC       Q96KQ4; Q13515: BFSP2; NbExp=3; IntAct=EBI-1105153, EBI-10229433;
CC       Q96KQ4; Q9NWW7: C2orf42; NbExp=3; IntAct=EBI-1105153, EBI-2812028;
CC       Q96KQ4; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-1105153, EBI-1765641;
CC       Q96KQ4; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1105153, EBI-11524851;
CC       Q96KQ4; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-1105153, EBI-10171570;
CC       Q96KQ4; Q52MB2: CCDC184; NbExp=3; IntAct=EBI-1105153, EBI-10179526;
CC       Q96KQ4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1105153, EBI-10175300;
CC       Q96KQ4; Q99459: CDC5L; NbExp=5; IntAct=EBI-1105153, EBI-374880;
CC       Q96KQ4; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-1105153, EBI-11752486;
CC       Q96KQ4; B9EK46: CGN; NbExp=3; IntAct=EBI-1105153, EBI-14314072;
CC       Q96KQ4; P61024: CKS1B; NbExp=3; IntAct=EBI-1105153, EBI-456371;
CC       Q96KQ4; Q05D60: DEUP1; NbExp=3; IntAct=EBI-1105153, EBI-748597;
CC       Q96KQ4; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-1105153, EBI-742953;
CC       Q96KQ4; O95057: DIRAS1; NbExp=3; IntAct=EBI-1105153, EBI-11993172;
CC       Q96KQ4; O60941-5: DTNB; NbExp=3; IntAct=EBI-1105153, EBI-11984733;
CC       Q96KQ4; Q09472: EP300; NbExp=2; IntAct=EBI-1105153, EBI-447295;
CC       Q96KQ4; Q8NB25: FAM184A; NbExp=3; IntAct=EBI-1105153, EBI-9917523;
CC       Q96KQ4; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1105153, EBI-6658203;
CC       Q96KQ4; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-1105153, EBI-7960826;
CC       Q96KQ4; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-1105153, EBI-747500;
CC       Q96KQ4; Q92805: GOLGA1; NbExp=3; IntAct=EBI-1105153, EBI-6164177;
CC       Q96KQ4; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-1105153, EBI-713401;
CC       Q96KQ4; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-1105153, EBI-1018153;
CC       Q96KQ4; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-1105153, EBI-8472129;
CC       Q96KQ4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1105153, EBI-14069005;
CC       Q96KQ4; P35900: KRT20; NbExp=3; IntAct=EBI-1105153, EBI-742094;
CC       Q96KQ4; P19013: KRT4; NbExp=3; IntAct=EBI-1105153, EBI-2371606;
CC       Q96KQ4; P20700: LMNB1; NbExp=3; IntAct=EBI-1105153, EBI-968218;
CC       Q96KQ4; Q03252: LMNB2; NbExp=3; IntAct=EBI-1105153, EBI-2830427;
CC       Q96KQ4; P25800: LMO1; NbExp=3; IntAct=EBI-1105153, EBI-8639312;
CC       Q96KQ4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1105153, EBI-11742507;
CC       Q96KQ4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1105153, EBI-739832;
CC       Q96KQ4; O95460-2: MATN4; NbExp=3; IntAct=EBI-1105153, EBI-12072296;
CC       Q96KQ4; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1105153, EBI-348259;
CC       Q96KQ4; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-1105153, EBI-2548751;
CC       Q96KQ4; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-1105153, EBI-1104552;
CC       Q96KQ4; P40692: MLH1; NbExp=3; IntAct=EBI-1105153, EBI-744248;
CC       Q96KQ4; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-1105153, EBI-3911716;
CC       Q96KQ4; O14777: NDC80; NbExp=3; IntAct=EBI-1105153, EBI-715849;
CC       Q96KQ4; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-1105153, EBI-2859639;
CC       Q96KQ4; O75145: PPFIA3; NbExp=3; IntAct=EBI-1105153, EBI-1763225;
CC       Q96KQ4; P62136: PPP1CA; NbExp=11; IntAct=EBI-1105153, EBI-357253;
CC       Q96KQ4; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-1105153, EBI-2557469;
CC       Q96KQ4; O43741: PRKAB2; NbExp=3; IntAct=EBI-1105153, EBI-1053424;
CC       Q96KQ4; P41219: PRPH; NbExp=3; IntAct=EBI-1105153, EBI-752074;
CC       Q96KQ4; P0CG20: PRR35; NbExp=3; IntAct=EBI-1105153, EBI-11986293;
CC       Q96KQ4; Q15311: RALBP1; NbExp=3; IntAct=EBI-1105153, EBI-749285;
CC       Q96KQ4; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-1105153, EBI-3437896;
CC       Q96KQ4; Q8NHQ8-2: RASSF8; NbExp=6; IntAct=EBI-1105153, EBI-10976415;
CC       Q96KQ4; Q9NSC2: SALL1; NbExp=3; IntAct=EBI-1105153, EBI-11317266;
CC       Q96KQ4; O94964-4: SOGA1; NbExp=3; IntAct=EBI-1105153, EBI-14083835;
CC       Q96KQ4; P56279: TCL1A; NbExp=3; IntAct=EBI-1105153, EBI-749995;
CC       Q96KQ4; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-1105153, EBI-750487;
CC       Q96KQ4; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-1105153, EBI-12090309;
CC       Q96KQ4; Q8N6V9: TEX9; NbExp=3; IntAct=EBI-1105153, EBI-746341;
CC       Q96KQ4; Q13077: TRAF1; NbExp=3; IntAct=EBI-1105153, EBI-359224;
CC       Q96KQ4; Q99816: TSG101; NbExp=3; IntAct=EBI-1105153, EBI-346882;
CC       Q96KQ4; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-1105153, EBI-744794;
CC       Q96KQ4; P40222: TXLNA; NbExp=3; IntAct=EBI-1105153, EBI-359793;
CC       Q96KQ4; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-1105153, EBI-10183064;
CC       Q96KQ4; Q8IYH5: ZZZ3; NbExp=3; IntAct=EBI-1105153, EBI-2795524;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11684014}. Nucleus
CC       {ECO:0000269|PubMed:11684014}. Note=Predominantly cytoplasmic. Some
CC       fraction is nuclear.
CC   -!- TISSUE SPECIFICITY: Reduced expression in breast carcinomas expressing
CC       a wild-type TP53 protein. {ECO:0000269|PubMed:11684014}.
CC   -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for
CC       specific interactions with TP53.
CC   -!- MISCELLANEOUS: In contrast to its official gene name, it is not a
CC       regulatory subunit of protein phosphatase 1. This name was given due to
CC       its similarity with a protein that binds to protein phosphatase 1.
CC   -!- SIMILARITY: Belongs to the ASPP family. {ECO:0000305}.
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DR   EMBL; AJ318887; CAC83011.2; -; mRNA.
DR   EMBL; AL049840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81847.1; -; Genomic_DNA.
DR   EMBL; BC136527; AAI36528.1; -; mRNA.
DR   EMBL; AB018314; BAA34491.1; -; mRNA.
DR   CCDS; CCDS41997.1; -.
DR   RefSeq; NP_056131.2; NM_015316.2.
DR   PDB; 6HL5; X-ray; 1.98 A; S=932-954.
DR   PDBsum; 6HL5; -.
DR   AlphaFoldDB; Q96KQ4; -.
DR   SMR; Q96KQ4; -.
DR   BioGRID; 116948; 163.
DR   CORUM; Q96KQ4; -.
DR   ELM; Q96KQ4; -.
DR   IntAct; Q96KQ4; 100.
DR   MINT; Q96KQ4; -.
DR   STRING; 9606.ENSP00000202556; -.
DR   CarbonylDB; Q96KQ4; -.
DR   iPTMnet; Q96KQ4; -.
DR   PhosphoSitePlus; Q96KQ4; -.
DR   BioMuta; PPP1R13B; -.
DR   DMDM; 296439434; -.
DR   EPD; Q96KQ4; -.
DR   jPOST; Q96KQ4; -.
DR   MassIVE; Q96KQ4; -.
DR   MaxQB; Q96KQ4; -.
DR   PaxDb; 9606-ENSP00000202556; -.
DR   PeptideAtlas; Q96KQ4; -.
DR   ProteomicsDB; 77101; -.
DR   Pumba; Q96KQ4; -.
DR   Antibodypedia; 87; 274 antibodies from 30 providers.
DR   DNASU; 23368; -.
DR   Ensembl; ENST00000202556.14; ENSP00000202556.9; ENSG00000088808.18.
DR   GeneID; 23368; -.
DR   KEGG; hsa:23368; -.
DR   MANE-Select; ENST00000202556.14; ENSP00000202556.9; NM_015316.3; NP_056131.2.
DR   UCSC; uc001yof.2; human.
DR   AGR; HGNC:14950; -.
DR   CTD; 23368; -.
DR   DisGeNET; 23368; -.
DR   GeneCards; PPP1R13B; -.
DR   HGNC; HGNC:14950; PPP1R13B.
DR   HPA; ENSG00000088808; Low tissue specificity.
DR   MIM; 606455; gene.
DR   neXtProt; NX_Q96KQ4; -.
DR   OpenTargets; ENSG00000088808; -.
DR   PharmGKB; PA33622; -.
DR   VEuPathDB; HostDB:ENSG00000088808; -.
DR   eggNOG; KOG0515; Eukaryota.
DR   GeneTree; ENSGT00940000153463; -.
DR   HOGENOM; CLU_008234_0_0_1; -.
DR   InParanoid; Q96KQ4; -.
DR   OMA; GFQSHNG; -.
DR   OrthoDB; 5476196at2759; -.
DR   PhylomeDB; Q96KQ4; -.
DR   TreeFam; TF105545; -.
DR   PathwayCommons; Q96KQ4; -.
DR   Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
DR   Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR   Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR   Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
DR   Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR   SignaLink; Q96KQ4; -.
DR   BioGRID-ORCS; 23368; 13 hits in 1156 CRISPR screens.
DR   ChiTaRS; PPP1R13B; human.
DR   GeneWiki; PPP1R13B; -.
DR   GenomeRNAi; 23368; -.
DR   Pharos; Q96KQ4; Tbio.
DR   PRO; PR:Q96KQ4; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q96KQ4; Protein.
DR   Bgee; ENSG00000088808; Expressed in right lobe of thyroid gland and 193 other cell types or tissues.
DR   ExpressionAtlas; Q96KQ4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0002039; F:p53 binding; IBA:GO_Central.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
DR   GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd17224; RA_ASPP1; 1.
DR   CDD; cd11954; SH3_ASPP1; 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; IPR047163; ASPP1/2.
DR   InterPro; IPR028319; ASPP1_RA.
DR   InterPro; IPR048942; ASPP2-like_RA.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR24131; APOPTOSIS-STIMULATING OF P53 PROTEIN; 1.
DR   PANTHER; PTHR24131:SF5; APOPTOSIS-STIMULATING OF P53 PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF21801; ASPP2-like_RA; 1.
DR   Pfam; PF00018; SH3_1; 1.
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   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q96KQ4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Apoptosis; Cytoplasm; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT   CHAIN           1..1090
FT                   /note="Apoptosis-stimulating of p53 protein 1"
FT                   /id="PRO_0000066962"
FT   REPEAT          920..952
FT                   /note="ANK 1"
FT   REPEAT          953..985
FT                   /note="ANK 2"
FT   DOMAIN          1019..1081
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          82..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..542
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..859
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         554
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62415"
FT   MOD_RES         681
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CONFLICT        68
FT                   /note="K -> I (in Ref. 1; CAC83011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="E -> D (in Ref. 1; CAC83011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="N -> Y (in Ref. 1; CAC83011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1090 AA;  119565 MW;  0026F07D7AB33295 CRC64;
     MMPMILTVFL SNNEQILTEV PITPETTCRD VVEFCKEPGE GSCHLAEVWR GNERPIPFDH
     MMYEHLQKWG PRREEVKFFL RHEDSPTENS EQGGRQTQEQ RTQRNVINVP GEKRTENGVG
     NPRVELTLSE LQDMAARQQQ QIENQQQMLV AKEQRLHFLK QQERRQQQSI SENEKLQKLK
     ERVEAQENKL KKIRAMRGQV DYSKIMNGNL SAEIERFSAM FQEKKQEVQT AILRVDQLSQ
     QLEDLKKGKL NGFQSYNGKL TGPAAVELKR LYQELQIRNQ LNQEQNSKLQ QQKELLNKRN
     MEVAMMDKRI SELRERLYGK KIQLNRVNGT SSPQSPLSTS GRVAAVGPYI QVPSAGSFPV
     LGDPIKPQSL SIASNAAHGR SKSANDGNWP TLKQNSSSSV KPVQVAGADW KDPSVEGSVK
     QGTVSSQPVP FSALGPTEKP GIEIGKVPPP IPGVGKQLPP SYGTYPSPTP LGPGSTSSLE
     RRKEGSLPRP SAGLPSRQRP TLLPATGSTP QPGSSQQIQQ RISVPPSPTY PPAGPPAFPA
     GDSKPELPLT VAIRPFLADK GSRPQSPRKG PQTVNSSSIY SMYLQQATPP KNYQPAAHSA
     LNKSVKAVYG KPVLPSGSTS PSPLPFLHGS LSTGTPQPQP PSESTEKEPE QDGPAAPADG
     STVESLPRPL SPTKLTPIVH SPLRYQSDAD LEALRRKLAN APRPLKKRSS ITEPEGPGGP
     NIQKLLYQRF NTLAGGMEGT PFYQPSPSQD FMGTLADVDN GNTNANGNLE ELPPAQPTAP
     LPAEPAPSSD ANDNELPSPE PEELICPQTT HQTAEPAEDN NNNVATVPTT EQIPSPVAEA
     PSPGEEQVPP APLPPASHPP ATSTNKRTNL KKPNSERTGH GLRVRFNPLA LLLDASLEGE
     FDLVQRIIYE VEDPSKPNDE GITPLHNAVC AGHHHIVKFL LDFGVNVNAA DSDGWTPLHC
     AASCNSVHLC KQLVESGAAI FASTISDIET AADKCEEMEE GYIQCSQFLY GVQEKLGVMN
     KGVAYALWDY EAQNSDELSF HEGDALTILR RKDESETEWW WARLGDREGY VPKNLLGLYP
     RIKPRQRTLA
//