ASPP1_HUMAN
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 03-AUG-2022, entry version 166.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 160.
DR CORUM; Q96KQ4; -.
DR ELM; Q96KQ4; -.
DR IntAct; Q96KQ4; 96.
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; Q96KQ4; -.
DR PeptideAtlas; Q96KQ4; -.
DR PRIDE; Q96KQ4; -.
DR ProteomicsDB; 77101; -.
DR Antibodypedia; 87; 240 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 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; EGLICPP; -.
DR OrthoDB; 1041229at2759; -.
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; 11 hits in 1078 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 191 other tissues.
DR ExpressionAtlas; Q96KQ4; baseline and differential.
DR Genevisible; Q96KQ4; HS.
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: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 Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR028319; ASPP_1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR24131:SF5; PTHR24131:SF5; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 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 SUPFAM; SSF54236; SSF54236; 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; 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
