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Tumor protein p53-inducible nuclear protein 1 (Stress-induced protein) (Thymus-expressed acidic protein) (TEAP) (p53-dependent damage-inducible nuclear protein 1) (p53DINP1)

 T53I1_MOUSE             Reviewed;         239 AA.
Q9QXE4; Q923I6;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Tumor protein p53-inducible nuclear protein 1;
AltName: Full=Stress-induced protein;
AltName: Full=Thymus-expressed acidic protein;
Short=TEAP;
AltName: Full=p53-dependent damage-inducible nuclear protein 1;
Short=p53DINP1;
Name=Trp53inp1; Synonyms=Sip;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=10630289; DOI=10.1007/s002510050601;
Carrier A., Nguyen C., Victorero G., Granjeaud S., Rocha D.,
Bernard K., Miazek A., Ferrier P., Malissen M., Naquet P.,
Malissen B., Jordan B.R.;
"Differential gene expression in CD3epsilon- and RAG1-deficient
thymuses: definition of a set of genes potentially involved in
thymocyte maturation.";
Immunogenetics 50:255-270(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
PubMed=11557757; DOI=10.1074/jbc.M105647200;
Tomasini R., Samir A.A., Vaccaro M.I., Pebusque M.-J., Dagorn J.-C.,
Iovanna J.L., Dusetti N.J.;
"Molecular and functional characterization of the stress-induced
protein (SIP) gene and its two transcripts generated by alternative
splicing. SIP induced by stress and promotes cell death.";
J. Biol. Chem. 276:44185-44192(2001).
[3]
FUNCTION.
PubMed=16044147; DOI=10.1038/sj.onc.1208951;
Tomasini R., Seux M., Nowak J., Bontemps C., Carrier A., Dagorn J.C.,
Pebusque M.J., Iovanna J.L., Dusetti N.J.;
"TP53INP1 is a novel p73 target gene that induces cell cycle arrest
and cell death by modulating p73 transcriptional activity.";
Oncogene 24:8093-8104(2005).
[4]
FUNCTION.
PubMed=19118006; DOI=10.1158/0008-5472.CAN-08-2320;
Cano C.E., Gommeaux J., Pietri S., Culcasi M., Garcia S., Seux M.,
Barelier S., Vasseur S., Spoto R.P., Pebusque M.J., Dusetti N.J.,
Iovanna J.L., Carrier A.;
"Tumor protein 53-induced nuclear protein 1 is a major mediator of p53
antioxidant function.";
Cancer Res. 69:219-226(2009).
[5]
FUNCTION.
PubMed=21339733; DOI=10.1038/onc.2011.25;
Seux M., Peuget S., Montero M.P., Siret C., Rigot V., Clerc P.,
Gigoux V., Pellegrino E., Pouyet L., N'Guessan P., Garcia S.,
Dufresne M., Iovanna J.L., Carrier A., Andre F., Dusetti N.J.;
"TP53INP1 decreases pancreatic cancer cell migration by regulating
SPARC expression.";
Oncogene 30:3049-3061(2011).
-!- FUNCTION: Antiproliferative and proapoptotic protein involved in
cell stress response which acts as a dual regulator of
transcription and autophagy. Acts as a positive regulator of
autophagy. In response to cellular stress or activation of
autophagy, relocates to autophagosomes where it interacts with
autophagosome-associated proteins GABARAP, GABARAPL1/L2,
MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and
plays a major role in p53/TP53-driven oxidative stress response.
Possesses both a p53/TP53-independent intracellular reactive
oxygen species (ROS) regulatory function and a p53/TP53-dependent
transcription regulatory function. Positively regulates p53/TP53
and p73/TP73 and stimulates their capacity to induce apoptosis and
regulate cell cycle. In response to double-strand DNA breaks,
promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent
apoptosis. Acts as a tumor suppressor by inducing cell death by an
autophagy and caspase-dependent mechanism. Can reduce cell
migration by regulating the expression of SPARC.
{ECO:0000269|PubMed:11557757, ECO:0000269|PubMed:16044147,
ECO:0000269|PubMed:19118006, ECO:0000269|PubMed:21339733}.
-!- SUBUNIT: Interacts with p53/TP53 and HIPK2. Interacts with PRKCG,
GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:11557757}. Nucleus, PML body {ECO:0000250}.
Cytoplasmic vesicle, autophagosome {ECO:0000250}. Note=Shuttles
between the nucleus and the cytoplasm, depending on cellular
stress conditions, and re-localizes to autophagosomes on autophagy
activation. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=SIP27, TEAP;
IsoId=Q9QXE4-1; Sequence=Displayed;
Name=2; Synonyms=SIP18;
IsoId=Q9QXE4-2; Sequence=VSP_013177;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
the thymus. {ECO:0000269|PubMed:10630289,
ECO:0000269|PubMed:11557757}.
-!- INDUCTION: By adriamycin, methymethane sulfonate, ethanol,
H(2)O(2), ultraviolet irradiation and heat shock. Rapidly induced
in acinar cells of the pancreas with acute pancreatitis upon
caerulein treatment. {ECO:0000269|PubMed:11557757}.
-!- DOMAIN: The LC3 interacting region (LIR) motif mediates
interaction with GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B
and MAP1LC3C. {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ131776; CAB66138.1; -; mRNA.
EMBL; AY034611; AAK60419.1; -; mRNA.
EMBL; AY034612; AAK60420.1; -; mRNA.
CCDS; CCDS17964.1; -. [Q9QXE4-1]
RefSeq; NP_001186034.1; NM_001199105.1. [Q9QXE4-2]
RefSeq; NP_068697.1; NM_021897.3. [Q9QXE4-1]
UniGene; Mm.393018; -.
UniGene; Mm.468195; -.
ProteinModelPortal; Q9QXE4; -.
STRING; 10090.ENSMUSP00000029865; -.
PhosphoSitePlus; Q9QXE4; -.
PaxDb; Q9QXE4; -.
PRIDE; Q9QXE4; -.
Ensembl; ENSMUST00000029865; ENSMUSP00000029865; ENSMUSG00000028211. [Q9QXE4-1]
GeneID; 60599; -.
KEGG; mmu:60599; -.
UCSC; uc008ryz.1; mouse. [Q9QXE4-1]
UCSC; uc008rzb.1; mouse. [Q9QXE4-2]
CTD; 60599; -.
MGI; MGI:1926609; Trp53inp1.
eggNOG; ENOG410IJ9V; Eukaryota.
eggNOG; ENOG4111S9D; LUCA.
GeneTree; ENSGT00530000063829; -.
HOGENOM; HOG000010288; -.
HOVERGEN; HBG055647; -.
InParanoid; Q9QXE4; -.
KO; K15310; -.
OMA; WAVHQPC; -.
OrthoDB; EOG091G0FZC; -.
PhylomeDB; Q9QXE4; -.
TreeFam; TF333017; -.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
ChiTaRS; Trp53inp1; mouse.
PRO; PR:Q9QXE4; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028211; -.
ExpressionAtlas; Q9QXE4; baseline and differential.
Genevisible; Q9QXE4; MM.
GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048102; P:autophagic cell death; ISS:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
GO; GO:0071361; P:cellular response to ethanol; IDA:MGI.
GO; GO:0071447; P:cellular response to hydroperoxide; IDA:MGI.
GO; GO:0072703; P:cellular response to methyl methanesulfonate; IDA:MGI.
GO; GO:0034644; P:cellular response to UV; IDA:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IMP:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR029431; TP53INP.
InterPro; IPR029556; TP53INP1.
PANTHER; PTHR31671; PTHR31671; 1.
PANTHER; PTHR31671:SF0; PTHR31671:SF0; 1.
Pfam; PF14839; DOR; 1.
2: Evidence at transcript level;
Activator; Alternative splicing; Antioxidant; Apoptosis; Autophagy;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Nucleus;
Reference proteome; Transcription; Transcription regulation;
Tumor suppressor.
CHAIN 1 239 Tumor protein p53-inducible nuclear
protein 1.
/FTId=PRO_0000072407.
MOTIF 25 37 LIR.
COMPBIAS 46 52 Poly-Glu.
VAR_SEQ 158 239 MEAQSEMGKHIHCCVAALAAQATFLEQPKSFRPSQWIKGHS
ERQSLNRNGLRRQNLTRDCHTRQMKHSGWVVHQPCPRQYNY
-> ARKSCL (in isoform 2).
{ECO:0000303|PubMed:11557757}.
/FTId=VSP_013177.
SEQUENCE 239 AA; 26935 MW; 71F25DB7600D7C7B CRC64;
MFQRLNKMFV GEVTTSSSQE PEFSEKEDDE WILVDFIDTC PGFSAEEEEE DEDIGEESSA
EHTSVFSCLP ASLECLTDTS DSCFLQFESC PMEESWFITP PPCFTAGGLT TIKVETSPME
NLLIEHPSMS VYAVHNSCPG LSEASCGNDE YNSSGPRMEA QSEMGKHIHC CVAALAAQAT
FLEQPKSFRP SQWIKGHSER QSLNRNGLRR QNLTRDCHTR QMKHSGWVVH QPCPRQYNY


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