IASPP_MOUSE
ID IASPP_MOUSE Reviewed; 824 AA.
AC Q5I1X5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 {ECO:0000312|MGI:MGI:3525053};
GN Synonyms=Nkip1 {ECO:0000303|PubMed:15661756};
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] {ECO:0000305, ECO:0000312|EMBL:AAW51145.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISEASE, AND INTERACTION
RP WITH RELA.
RC STRAIN=DBA/2J {ECO:0000312|EMBL:AAW51145.1};
RX PubMed=15661756; DOI=10.1093/hmg/ddi063;
RA Herron B.J., Rao C., Liu S., Laprade L., Richardson J.A., Olivieri E.,
RA Semsarian C., Millar S.E., Stubbs L., Beier D.R.;
RT "A mutation in NFkB interacting protein 1 results in cardiomyopathy and
RT abnormal skin development in wa3 mice.";
RL Hum. Mol. Genet. 14:667-677(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-123; SER-183 AND
RP THR-275, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Testis;
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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-137; ARG-142; ARG-144; ARG-160;
RP ARG-167 AND ARG-205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
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. Inhibits p53/TP53 function, possibly by preventing
CC the association between p53/TP53 and ASPP1 or ASPP2, and therefore
CC suppressing the subsequent activation of apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUF5}.
CC -!- SUBUNIT: Interacts with TP63 and TP73 (By similarity). Interacts with
CC RELA NF-kappa-B subunit and with SP1 via its C-terminal part. Interacts
CC (via SH3 domain and ANK repeats) with p53/TP53; the interaction
CC inhibits pro-apoptotic activity of p53/TP53 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q8WUF5,
CC ECO:0000269|PubMed:15661756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUF5}. Nucleus
CC {ECO:0000250|UniProtKB:Q8WUF5}. Note=Predominantly cytoplasmic but also
CC nuclear. {ECO:0000250|UniProtKB:Q8WUF5}.
CC -!- TISSUE SPECIFICITY: Most abundant in skin with high levels also found
CC in heart, testis and stomach. In 15.5 dpc embryonic heart, expressed at
CC higher levels in atria than ventricles. {ECO:0000269|PubMed:15661756}.
CC -!- DOMAIN: The N-terminal region is required for cytoplasmic localization.
CC {ECO:0000250|UniProtKB:Q8WUF5}.
CC -!- DOMAIN: The ANK repeats and the SH3 domain are required for specific
CC interactions with p53/TP53. {ECO:0000250|UniProtKB:Q8WUF5}.
CC -!- DISEASE: Note=Defects in Ppp1r13l are the cause of the waved 3
CC phenotype, a recessive mutation characterized by abnormalities of the
CC heart and skin. Affected animals have open eyes at birth and hair
CC abnormalities. They develop focal cardiac necrosis at an early age
CC which progresses to fatal dilated cardiomyopathy. This is due to a 14-
CC bp deletion which gives rise to a truncated protein.
CC {ECO:0000269|PubMed:15661756}.
CC -!- SIMILARITY: Belongs to the iASPP family. {ECO:0000255}.
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DR EMBL; AY869711; AAW51145.1; -; mRNA.
DR CCDS; CCDS20899.1; -.
DR RefSeq; NP_001010836.1; NM_001010836.3.
DR RefSeq; XP_006540189.1; XM_006540126.1.
DR RefSeq; XP_006540190.1; XM_006540127.3.
DR RefSeq; XP_006540191.1; XM_006540128.2.
DR RefSeq; XP_006540192.1; XM_006540129.1.
DR AlphaFoldDB; Q5I1X5; -.
DR SMR; Q5I1X5; -.
DR BioGRID; 237177; 3.
DR IntAct; Q5I1X5; 1.
DR STRING; 10090.ENSMUSP00000047839; -.
DR iPTMnet; Q5I1X5; -.
DR PhosphoSitePlus; Q5I1X5; -.
DR EPD; Q5I1X5; -.
DR MaxQB; Q5I1X5; -.
DR PaxDb; Q5I1X5; -.
DR PRIDE; Q5I1X5; -.
DR ProteomicsDB; 267079; -.
DR Antibodypedia; 31307; 271 antibodies from 31 providers.
DR DNASU; 333654; -.
DR Ensembl; ENSMUST00000047621; ENSMUSP00000047839; ENSMUSG00000040734.
DR GeneID; 333654; -.
DR KEGG; mmu:333654; -.
DR UCSC; uc009flo.1; mouse.
DR CTD; 10848; -.
DR MGI; MGI:3525053; Ppp1r13l.
DR VEuPathDB; HostDB:ENSMUSG00000040734; -.
DR eggNOG; KOG0515; Eukaryota.
DR GeneTree; ENSGT00940000160551; -.
DR HOGENOM; CLU_019814_0_0_1; -.
DR InParanoid; Q5I1X5; -.
DR OMA; FQTMNDD; -.
DR OrthoDB; 1041229at2759; -.
DR PhylomeDB; Q5I1X5; -.
DR TreeFam; TF105545; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR BioGRID-ORCS; 333654; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q5I1X5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q5I1X5; protein.
DR Bgee; ENSMUSG00000040734; Expressed in interventricular septum and 182 other tissues.
DR ExpressionAtlas; Q5I1X5; baseline and differential.
DR Genevisible; Q5I1X5; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:MGI.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0042633; P:hair cycle; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0048871; P:multicellular organismal homeostasis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
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; IMP:MGI.
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 Acetylation; ANK repeat; Apoptosis; Cytoplasm; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; SH3 domain;
KW Transcription; Transcription regulation.
FT CHAIN 1..824
FT /note="RelA-associated inhibitor"
FT /id="PRO_0000066967"
FT REPEAT 655..684
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 688..717
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT DOMAIN 754..816
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 48..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 137
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 142
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 160
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
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:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 205
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUF5"
SQ SEQUENCE 824 AA; 88976 MW; 57AC88589BC8AA8B CRC64;
MDSEAFQHAR DLLDLNFQSL AMKHMDLKQM ELDTAAAKVD ELTKQLESLW SDSPAPPGAQ
AGVPSRMARY STSPVPEHFG SRGSPQKIAT DGIEARFGRS ESAPSLHPYS PLSPKGRPSS
PRTPIYLQPD TYSSLDRAPS PRPRAFDGAG SPHGRAPSPR PGIGPVRQPG PSTPFDYLGR
AGSPRGSPLA EGPQAFFPER GPSPRPPAAA YDTAGTFGSP LLGAGGSAFT PPLRAQDDST
LRRRPPKAWN ESDLDVAYEK KSSQTASYER LDVFTRPASP GLQLLPWRES SLDGLGASGK
DHLTSATLPR NYKVSPLASD RRSDVGSYRR SLGSAGPSGT LPRSWQPVSR IPMPPSSPQP
RSTPRQRPIP LSMIFKLQNA FWEHGAGRAV LPGSPIFSRA PPPKLPPQPP PQPQMQPQPQ
PQPQMQPQSQ AQPQTPAPQQ TWSPMNEGLL KSPAELEPEP ELEVLLAPVE EAGDADEGTV
TRPLSPTRLQ PALPPEAQTV PELEEVARVL AEIPRPLKRR GSMEQSPAVA LPPTHKKQYQ
QIINRLFHRH GGPGPGGPEP ELSTITEGSE ARAGPPAPAP PAPIPPPAPP QSSPPEQPQS
MEMRSVLRKV GSPRKARRAR LNPLVLLLDA ALTGELDVVQ QAVKEMNDPS QPNEEGITAL
HNAICGANYP IVDFLIAAGA NVNSPDSHGW TPLHCAASCN DTAICTALVQ HGAAIFATTL
SDGATAIEKC DPYREGYADC ATYLADVEQS MGLMHNGVVY ALWDYSAEFG DELSFREGES
VTVLRRDGPE ETDWWWASLH GQEGYVPRNY FGLFPRVKSQ RSKI
