T53I2_HUMAN
ID T53I2_HUMAN Reviewed; 220 AA.
AC Q8IXH6; A8K8S8; E1P5P6; Q5JX64; Q8IYL5; Q9NU00;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tumor protein p53-inducible nuclear protein 2;
DE AltName: Full=Diabetes and obesity-regulated gene;
DE AltName: Full=p53-inducible protein U;
DE Short=PIG-U;
GN Name=TP53INP2; Synonyms=C20orf110, DOR, PINH;
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 THRA.
RC TISSUE=Heart;
RX PubMed=18030323; DOI=10.1371/journal.pone.0001183;
RA Baumgartner B.G., Orpinell M., Duran J., Ribas V., Burghardt H.E., Bach D.,
RA Villar A.V., Paz J.C., Gonzalez M., Camps M., Oriola J., Rivera F.,
RA Palacin M., Zorzano A.;
RT "Identification of a novel modulator of thyroid hormone receptor-mediated
RT action.";
RL PLoS ONE 2:E1183-E1183(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guo Z., Wu G., Sidransky D., Trink B.;
RT "PIG-U is a novel oncogene in human bladder cancer.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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 REVIEW ON FUNCTION.
RX PubMed=19145107; DOI=10.4161/auto.5.3.7698;
RA Nowak J., Iovanna J.L.;
RT "TP53INP2 is the new guest at the table of self-eating.";
RL Autophagy 5:383-384(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VMP1; GABARAP;
RP GABARAPL2 AND MAP1LC3A.
RX PubMed=19056683; DOI=10.1091/mbc.e08-07-0671;
RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J.,
RA Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
RT "The TP53INP2 protein is required for autophagy in mammalian cells.";
RL Mol. Biol. Cell 20:870-881(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GABARAP; GABARAPL1;
RP GABARAPL2; MAP1LC3A; MAP1LC3B AND MAP1LC3C.
RX PubMed=22470510; DOI=10.1371/journal.pone.0034034;
RA Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T.,
RA Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M.,
RA Johansen T., Zorzano A.;
RT "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual
RT regulators of autophagy and transcription.";
RL PLoS ONE 7:E34034-E34034(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP 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: Dual regulator of transcription and autophagy. Positively
CC regulates autophagy and is required for autophagosome formation and
CC processing. May act as a scaffold protein that recruits MAP1LC3A,
CC GABARAP and GABARAPL2 and brings them to the autophagosome membrane by
CC interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase
CC class III complex, they trigger autophagosome development. Acts as a
CC transcriptional activator of THRA. {ECO:0000269|PubMed:18030323,
CC ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22470510}.
CC -!- SUBUNIT: Interacts with VMP1, GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A,
CC MAP1LC3B, MAP1LC3C and THRA. {ECO:0000269|PubMed:18030323,
CC ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22470510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Nucleus, PML body.
CC Cytoplasmic vesicle, autophagosome. Note=Shuttles between the nucleus
CC and the cytoplasm, depending on cellular stress conditions, and re-
CC localizes to autophagosomes on autophagy activation.
CC -!- DOMAIN: The LC3 interacting region (LIR) motif mediates interaction
CC with GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C.
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DR EMBL; AJ297792; CAC82592.1; -; mRNA.
DR EMBL; AY422170; AAR23799.1; -; mRNA.
DR EMBL; AK292443; BAF85132.1; -; mRNA.
DR EMBL; AL109824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76256.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76257.1; -; Genomic_DNA.
DR EMBL; BC035639; AAH35639.1; -; mRNA.
DR CCDS; CCDS13240.1; -.
DR RefSeq; NP_001316358.1; NM_001329429.1.
DR RefSeq; NP_001316359.1; NM_001329430.1.
DR RefSeq; NP_001316360.1; NM_001329431.1.
DR RefSeq; NP_067025.1; NM_021202.2.
DR AlphaFoldDB; Q8IXH6; -.
DR SMR; Q8IXH6; -.
DR BioGRID; 121809; 3.
DR IntAct; Q8IXH6; 4.
DR MINT; Q8IXH6; -.
DR STRING; 9606.ENSP00000363943; -.
DR BindingDB; Q8IXH6; -.
DR iPTMnet; Q8IXH6; -.
DR PhosphoSitePlus; Q8IXH6; -.
DR BioMuta; TP53INP2; -.
DR MassIVE; Q8IXH6; -.
DR MaxQB; Q8IXH6; -.
DR PaxDb; Q8IXH6; -.
DR PeptideAtlas; Q8IXH6; -.
DR PRIDE; Q8IXH6; -.
DR ProteomicsDB; 70992; -.
DR Antibodypedia; 43096; 190 antibodies from 20 providers.
DR DNASU; 58476; -.
DR Ensembl; ENST00000374809.6; ENSP00000363942.2; ENSG00000078804.13.
DR Ensembl; ENST00000374810.8; ENSP00000363943.3; ENSG00000078804.13.
DR GeneID; 58476; -.
DR KEGG; hsa:58476; -.
DR MANE-Select; ENST00000374810.8; ENSP00000363943.3; NM_021202.3; NP_067025.1.
DR UCSC; uc002xau.2; human.
DR CTD; 58476; -.
DR DisGeNET; 58476; -.
DR GeneCards; TP53INP2; -.
DR HGNC; HGNC:16104; TP53INP2.
DR HPA; ENSG00000078804; Group enriched (brain, choroid plexus).
DR MIM; 617549; gene.
DR neXtProt; NX_Q8IXH6; -.
DR OpenTargets; ENSG00000078804; -.
DR PharmGKB; PA25650; -.
DR VEuPathDB; HostDB:ENSG00000078804; -.
DR eggNOG; ENOG502RZHB; Eukaryota.
DR GeneTree; ENSGT00530000063829; -.
DR HOGENOM; CLU_091034_0_0_1; -.
DR InParanoid; Q8IXH6; -.
DR OMA; EDPECPR; -.
DR OrthoDB; 1537138at2759; -.
DR PhylomeDB; Q8IXH6; -.
DR TreeFam; TF333017; -.
DR PathwayCommons; Q8IXH6; -.
DR SignaLink; Q8IXH6; -.
DR SIGNOR; Q8IXH6; -.
DR BioGRID-ORCS; 58476; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; TP53INP2; human.
DR GenomeRNAi; 58476; -.
DR Pharos; Q8IXH6; Tbio.
DR PRO; PR:Q8IXH6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8IXH6; protein.
DR Bgee; ENSG00000078804; Expressed in inferior vagus X ganglion and 187 other tissues.
DR ExpressionAtlas; Q8IXH6; baseline and differential.
DR Genevisible; Q8IXH6; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IDA:GO_Central.
DR GO; GO:1903828; P:negative regulation of protein localization; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR InterPro; IPR029431; TP53INP.
DR InterPro; IPR029558; TP53INP2.
DR PANTHER; PTHR31671; PTHR31671; 1.
DR PANTHER; PTHR31671:SF2; PTHR31671:SF2; 1.
DR Pfam; PF14839; DOR; 1.
PE 1: Evidence at protein level;
KW Activator; Autophagy; Cytoplasm; Cytoplasmic vesicle; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..220
FT /note="Tumor protein p53-inducible nuclear protein 2"
FT /id="PRO_0000072409"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 26..41
FT /note="LIR"
FT COMPBIAS 47..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 136
FT /note="S -> N (in Ref. 1; CAC82592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 23980 MW; D64E010B2F68A705 CRC64;
MFQRLSSLFF STPSPPEDPD CPRAFVSEED EVDGWLIIDL PDSYAAPPSP GAAPAPAGRP
PPAPSLMDES WFVTPPACFT AEGPGLGPAR LQSSPLEDLL IEHPSMSVYV TGSTIVLEPG
SPSPLPDAAL PDGDLSEGEL TPARREPRAA RHAAPLPARA ALLEKAGQVR RLQRARQRAE
RHALSAKAVQ RQNRARESRP RRSKNQSSFI YQPCQRQFNY
