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TAPR1_MOUSE
ID   TAPR1_MOUSE             Reviewed;         275 AA.
AC   Q14AM7; Q9D905;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Telomere attrition and p53 response 1 protein {ECO:0000250|UniProtKB:Q14CZ0};
GN   Name=Tapr1 {ECO:0000250|UniProtKB:Q14CZ0};
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=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
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).
CC   -!- FUNCTION: Functions as a negative regulator of TP53/P53 in the cellular
CC       response to telomere erosion and probably also DNA damage (By
CC       similarity). May attenuate p53/TP53 activation through the E3 ubiquitin
CC       ligase HUWE1 (By similarity). {ECO:0000250|UniProtKB:Q14CZ0}.
CC   -!- SIMILARITY: Belongs to the TAPR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB25061.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK007485; BAB25061.1; ALT_FRAME; mRNA.
DR   EMBL; BC116778; AAI16779.1; -; mRNA.
DR   EMBL; BC116780; AAI16781.1; -; mRNA.
DR   CCDS; CCDS49756.1; -.
DR   RefSeq; NP_001074869.1; NM_001081400.3.
DR   AlphaFoldDB; Q14AM7; -.
DR   STRING; 10090.ENSMUSP00000023150; -.
DR   iPTMnet; Q14AM7; -.
DR   PhosphoSitePlus; Q14AM7; -.
DR   EPD; Q14AM7; -.
DR   PaxDb; Q14AM7; -.
DR   PeptideAtlas; Q14AM7; -.
DR   PRIDE; Q14AM7; -.
DR   Antibodypedia; 52099; 139 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000023150; ENSMUSP00000023150; ENSMUSG00000022507.
DR   GeneID; 69053; -.
DR   KEGG; mmu:69053; -.
DR   UCSC; uc007yda.2; mouse.
DR   MGI; MGI:1916303; 1810013L24Rik.
DR   VEuPathDB; HostDB:ENSMUSG00000022507; -.
DR   eggNOG; ENOG502QPPE; Eukaryota.
DR   GeneTree; ENSGT00390000002886; -.
DR   HOGENOM; CLU_081329_0_0_1; -.
DR   InParanoid; Q14AM7; -.
DR   OMA; GIQCGYQ; -.
DR   OrthoDB; 1126238at2759; -.
DR   PhylomeDB; Q14AM7; -.
DR   TreeFam; TF323292; -.
DR   BioGRID-ORCS; 69053; 21 hits in 72 CRISPR screens.
DR   PRO; PR:Q14AM7; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q14AM7; protein.
DR   Bgee; ENSMUSG00000022507; Expressed in otolith organ and 228 other tissues.
DR   ExpressionAtlas; Q14AM7; baseline and differential.
DR   Genevisible; Q14AM7; MM.
DR   GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR   InterPro; IPR040308; TAPR1.
DR   InterPro; IPR029196; TAPR1-like.
DR   PANTHER; PTHR31624; PTHR31624; 1.
DR   Pfam; PF15251; DUF4588; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Telomere attrition and p53 response 1 protein"
FT                   /id="PRO_0000297628"
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..228
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..224
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:0000250|UniProtKB:Q14CZ0"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14CZ0"
FT   CONFLICT        224
FT                   /note="R -> Q (in Ref. 1; BAB25061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   275 AA;  30940 MW;  E51C0C7BADB51340 CRC64;
     MEERKEEGEA EIQEHGPEHW FSKWERQCLA EAEQDEQLSP ELQEEAAAAA QPEHKQQKLW
     HLFQNSATAV AQLYKDRVCQ QPGLSLWVPF QNAATAVTNL YKESVDTHQR SFDIGIQIGY
     QRRNKDVLAW VKKRRRTIRR EDLISFLCGK VPPPRNSRAP PRLTVVSPNR ATSTETSSSV
     ETDLQPFREA IALHGLSGAM ASISVRSSTP GSPTHVSSGP NASRRRNGLH DVDLNTFITE
     EMALHLDNGG TRKRTSAQCG DVITDSPTHK RNRML
 
 
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