ASPP1_MOUSE
ID ASPP1_MOUSE Reviewed; 1087 AA.
AC Q62415;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
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;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 944-1087.
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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-552, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 via its interaction with p53/TP53 (By similarity). Regulates
CC TP53 by enhancing the DNA binding and transactivation function of TP53
CC on the promoters of proapoptotic genes in vivo (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q96KQ4}.
CC -!- SUBUNIT: Interacts with P53/TP53; the interaction promotes pro-
CC apoptotic activity. {ECO:0000250|UniProtKB:Q96KQ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic (By similarity). Some fraction is
CC nuclear. {ECO:0000250}.
CC -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
CC specific interactions with TP53. {ECO:0000250}.
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; BC054788; AAH54788.1; -; mRNA.
DR EMBL; BC053092; AAH53092.1; -; mRNA.
DR EMBL; U58881; AAC52638.1; -; mRNA.
DR CCDS; CCDS56866.1; -.
DR RefSeq; NP_035755.1; NM_011625.1.
DR AlphaFoldDB; Q62415; -.
DR SMR; Q62415; -.
DR BioGRID; 204283; 11.
DR IntAct; Q62415; 1.
DR STRING; 10090.ENSMUSP00000062464; -.
DR iPTMnet; Q62415; -.
DR PhosphoSitePlus; Q62415; -.
DR EPD; Q62415; -.
DR MaxQB; Q62415; -.
DR PaxDb; Q62415; -.
DR PeptideAtlas; Q62415; -.
DR PRIDE; Q62415; -.
DR ProteomicsDB; 277047; -.
DR Antibodypedia; 87; 240 antibodies from 30 providers.
DR DNASU; 21981; -.
DR Ensembl; ENSMUST00000054815; ENSMUSP00000062464; ENSMUSG00000021285.
DR GeneID; 21981; -.
DR KEGG; mmu:21981; -.
DR UCSC; uc007ped.1; mouse.
DR CTD; 23368; -.
DR MGI; MGI:1336199; Ppp1r13b.
DR VEuPathDB; HostDB:ENSMUSG00000021285; -.
DR eggNOG; KOG0515; Eukaryota.
DR GeneTree; ENSGT00940000153463; -.
DR HOGENOM; CLU_008234_0_0_1; -.
DR InParanoid; Q62415; -.
DR OMA; EGLICPP; -.
DR OrthoDB; 1041229at2759; -.
DR PhylomeDB; Q62415; -.
DR TreeFam; TF105545; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR BioGRID-ORCS; 21981; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r13b; mouse.
DR PRO; PR:Q62415; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q62415; protein.
DR Bgee; ENSMUSG00000021285; Expressed in dorsal pancreas and 225 other tissues.
DR ExpressionAtlas; Q62415; baseline and differential.
DR Genevisible; Q62415; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; IBA:GO_Central.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:InterPro.
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 ANK repeat; Apoptosis; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1087
FT /note="Apoptosis-stimulating of p53 protein 1"
FT /id="PRO_0000066963"
FT REPEAT 917..949
FT /note="ANK 1"
FT REPEAT 950..982
FT /note="ANK 2"
FT DOMAIN 1016..1078
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 82..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ4"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ4"
FT MOD_RES 552
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ4"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1087 AA; 119170 MW; 8B3E9CC4B2390F13 CRC64;
MMPMILTVFL SNNEQILTEV PITPETTCRD VVEFCKEPGE GGCHLAEVWR GSERPIPYDH
MMYEHLQKWG PRREEVKFFL RHEDSPTESS EQGARQTQEQ RTQRSVVNVP GEKRTENGVG
NPRVELTLSE LQDMAARQQQ QIENQQQMLV AKEQRLHFLK QQERRQQQSV SENEKLQKLK
ERVEAQENKL KKIRAMRGQV DYSKIMNGNL SAEIERFSAM FQEKKQEVQT AILRVDQLSQ
QLEDLKKGKL NGFQSYNGRL TGPAAVELKR LYQELQIRNQ LNQEQNSKLQ QQKELLNKRN
MEVAMMDKRI SELRERLYGK KIQLNRVNGT SSPQSPLSTS GRVAAVGPYI QVPSTGGFPL
PGDPVKPQSL TIASSAAHGR SKSANDGNWP PLKQNSASVK STQMTGDWKD SGMEGTLKQG
AISSQPLPLS ALGATEKLGI EIGKGPPPIP GVGKPLPPSY GTYPSSGPLG PGSTSSLERR
KEGSLPRPGA GPPSRQKPAP LPPASNAPQP GSSQQIQQRI SVPPSPTYPP AGPPAFPTGD
GKPELPLTVA IRPFLADKGS RPQSPRKGPQ TVNSSSIYSM YLQQATPPKN YQPPAHGTLN
KSVKAVYGKP VLPSGSASPS PLPFLHGSLG TGTAQPQPPS DSAEKEPEQE GPSVPGEGST
VESLPRPLSP TKLTPIVHSP LRYQSDADLE ALRRKLANAP RPLKKRSSIT EPEGPGGPNI
QKLLYQRFNT LAGGMEGTPF YQPSPSQDFV GTLADMDNGN TNANGNLDEP FPPRPTAPLP
EELAPSSDAN DNELPSPEPE ELICPQTTHQ TAEPTEDNNN NVAPVPSTEQ IPSPVAEAPS
EEDQVPPAPL SPVIHPPAAS ASKRTNLKKP NSERTGHGLR VRFNPLALLL DASLEGEFDL
VQRIIYEVED PSKPNDEGIT PLHNAVCAGH HHIVKFLLDF GVNVNAADSD GWTPLHCAAS
CNSVHLCKQL VESGAAIFAS TISDIETAAD KCEEMEEGYI QCSQFLYGVQ EKLGVMNKGT
VYALWDYEAQ NSDELSFHEG DAITILRRKD ENETEWWWAR LGDREGYVPK NLLGLYPRIK
PRQRTLA
