TAPR1_HUMAN
ID TAPR1_HUMAN Reviewed; 275 AA.
AC Q14CZ0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Telomere attrition and p53 response 1 protein {ECO:0000303|PubMed:33660365};
GN Name=TAPR1 {ECO:0000303|PubMed:33660365}; Synonyms=C16orf72;
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 [LARGE SCALE MRNA].
RC 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [4]
RP FUNCTION, AND INTERACTION WITH HUWE1.
RX PubMed=33660365; DOI=10.1111/acel.13331;
RA Benslimane Y., Sanchez-Osuna M., Coulombe-Huntington J., Bertomeu T.,
RA Henry D., Huard C., Bonneil E., Thibault P., Tyers M., Harrington L.;
RT "A novel p53 regulator, C16ORF72/TAPR1, buffers against telomerase
RT inhibition.";
RL Aging Cell 20:e13331-e13331(2021).
CC -!- FUNCTION: Functions as a negative regulator of TP53/P53 in the cellular
CC response to telomere erosion and probably also DNA damage
CC (PubMed:33660365). May attenuate p53/TP53 activation through the E3
CC ubiquitin ligase HUWE1 (PubMed:33660365).
CC {ECO:0000269|PubMed:33660365}.
CC -!- INTERACTION:
CC Q14CZ0; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-10234807, EBI-10175124;
CC Q14CZ0; Q96CB8: INTS12; NbExp=5; IntAct=EBI-10234807, EBI-1049156;
CC -!- SIMILARITY: Belongs to the TAPR1 family. {ECO:0000305}.
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DR EMBL; BC113570; AAI13571.1; -; mRNA.
DR CCDS; CCDS10538.1; -.
DR RefSeq; NP_054836.2; NM_014117.2.
DR AlphaFoldDB; Q14CZ0; -.
DR BioGRID; 118829; 8.
DR IntAct; Q14CZ0; 3.
DR STRING; 9606.ENSP00000331720; -.
DR iPTMnet; Q14CZ0; -.
DR PhosphoSitePlus; Q14CZ0; -.
DR BioMuta; C16orf72; -.
DR DMDM; 121940554; -.
DR EPD; Q14CZ0; -.
DR jPOST; Q14CZ0; -.
DR MassIVE; Q14CZ0; -.
DR MaxQB; Q14CZ0; -.
DR PaxDb; Q14CZ0; -.
DR PeptideAtlas; Q14CZ0; -.
DR PRIDE; Q14CZ0; -.
DR ProteomicsDB; 60337; -.
DR Antibodypedia; 52099; 139 antibodies from 16 providers.
DR DNASU; 29035; -.
DR Ensembl; ENST00000327827.12; ENSP00000331720.7; ENSG00000182831.12.
DR GeneID; 29035; -.
DR KEGG; hsa:29035; -.
DR MANE-Select; ENST00000327827.12; ENSP00000331720.7; NM_014117.3; NP_054836.2.
DR UCSC; uc002czm.4; human.
DR CTD; 29035; -.
DR DisGeNET; 29035; -.
DR GeneCards; C16orf72; -.
DR HGNC; HGNC:30103; C16orf72.
DR HPA; ENSG00000182831; Tissue enhanced (bone).
DR neXtProt; NX_Q14CZ0; -.
DR OpenTargets; ENSG00000182831; -.
DR PharmGKB; PA145149589; -.
DR VEuPathDB; HostDB:ENSG00000182831; -.
DR eggNOG; ENOG502QPPE; Eukaryota.
DR GeneTree; ENSGT00390000002886; -.
DR HOGENOM; CLU_081329_0_0_1; -.
DR InParanoid; Q14CZ0; -.
DR OMA; GIQCGYQ; -.
DR OrthoDB; 1126238at2759; -.
DR PhylomeDB; Q14CZ0; -.
DR TreeFam; TF323292; -.
DR PathwayCommons; Q14CZ0; -.
DR SignaLink; Q14CZ0; -.
DR BioGRID-ORCS; 29035; 275 hits in 1059 CRISPR screens.
DR ChiTaRS; C16orf72; human.
DR GenomeRNAi; 29035; -.
DR Pharos; Q14CZ0; Tdark.
DR PRO; PR:Q14CZ0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14CZ0; protein.
DR Bgee; ENSG00000182831; Expressed in secondary oocyte and 188 other tissues.
DR ExpressionAtlas; Q14CZ0; baseline and differential.
DR Genevisible; Q14CZ0; HS.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR InterPro; IPR040308; TAPR1.
DR InterPro; IPR029196; TAPR1-like.
DR PANTHER; PTHR31624; PTHR31624; 1.
DR Pfam; PF15251; DUF4588; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..275
FT /note="Telomere attrition and p53 response 1 protein"
FT /id="PRO_0000297627"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 221
FT /note="N -> S (in dbSNP:rs34869458)"
FT /id="VAR_034657"
SQ SEQUENCE 275 AA; 30926 MW; E901B9A3C4A2B23C CRC64;
MEERKEEGEA EIQEHGPEHW FSKWERQCLA EAEQDEQLPP ELQEEAAAAA QPEHKQQKLW
HLFQNSATAV AQLYKDRVCQ QPGLSLWVPF QNAATAVTNL YKESVDTHQR SFDIGIQIGY
QRRNKDVLAW VKKRRRTIRR EDLISFLCGK VPPPRNSRAP PRLTVVSPNR ATSTETSSSV
ETDLQPFREA IALHGLSGAM ASISVRSSTP GSPTHVSSGS NASRRRNGLH DVDLNTFISE
EMALHLDNGG TRKRTSAQCG DVITDSPTHK RNRMI
