Full text data of SESN1
SESN1
(PA26, SEST1)
[Confidence: low (only semi-automatic identification from reviews)]
Sestrin-1 (p53-regulated protein PA26)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Sestrin-1 (p53-regulated protein PA26)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y6P5
ID SESN1_HUMAN Reviewed; 492 AA.
AC Q9Y6P5; Q2M2B7; Q5T316; Q9NV00; Q9UPD5; Q9Y6P6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Sestrin-1;
DE AltName: Full=p53-regulated protein PA26;
GN Name=SESN1; Synonyms=PA26, SEST1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS T1; T2 AND T3).
RX PubMed=9926927; DOI=10.1038/sj.onc.1202274;
RA Velasco-Miguel S., Buckbinder L., Jean P., Gelbert L., Talbott R.,
RA Laidlaw J., Seizinger B., Kley N.;
RT "PA26, a novel target of the p53 tumor suppressor and member of the
RT GADD family of DNA damage and growth arrest inducible genes.";
RL Oncogene 18:127-137(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-44, AND TISSUE SPECIFICITY.
RX PubMed=12607115; DOI=10.1007/s00439-003-0917-5;
RA Peeters H., Debeer P., Bairoch A., Wilquet V., Huysmans C.,
RA Parthoens E., Fryns J.-P., Gewillig M., Nakamura Y., Niikawa N.,
RA Van De Ven W., Devriendt K.;
RT "PA26 is a candidate gene for heterotaxia in humans: identification of
RT a novel PA26-related gene family in human and mouse.";
RL Hum. Genet. 112:573-580(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-492.
RC TISSUE=Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP FUNCTION.
RX PubMed=15105503; DOI=10.1126/science.1095569;
RA Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., Chumakov P.M.;
RT "Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of
RT bacterial AhpD.";
RL Science 304:596-600(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Involved in the reduction of peroxiredoxins. May also be
CC regulator of cellular growth.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=T2;
CC IsoId=Q9Y6P5-1; Sequence=Displayed;
CC Name=T1;
CC IsoId=Q9Y6P5-2; Sequence=VSP_006059;
CC Name=T3;
CC IsoId=Q9Y6P5-3; Sequence=VSP_006060;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- INDUCTION: Isoform T2 and isoform T3 are induced by genotoxic
CC stress (UV, gamma-irradiation and cytotoxic drugs) in a p53/TP53-
CC dependent manner. Isoform T1 is not induced by p53/TP53.
CC -!- SIMILARITY: Belongs to the sestrin family.
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DR EMBL; AF033122; AAD04812.1; -; mRNA.
DR EMBL; AF033120; AAD04810.1; -; mRNA.
DR EMBL; AF033121; AAD04811.1; -; mRNA.
DR EMBL; AL390208; CAI16720.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48367.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48368.1; -; Genomic_DNA.
DR EMBL; BC112036; AAI12037.1; -; mRNA.
DR EMBL; BC113569; AAI13570.1; -; mRNA.
DR EMBL; AK001886; BAA91961.1; -; mRNA.
DR RefSeq; NP_001186862.1; NM_001199933.1.
DR RefSeq; NP_001186863.1; NM_001199934.1.
DR RefSeq; NP_055269.1; NM_014454.2.
DR UniGene; Hs.591336; -.
DR ProteinModelPortal; Q9Y6P5; -.
DR STRING; 9606.ENSP00000306734; -.
DR PhosphoSite; Q9Y6P5; -.
DR DMDM; 13633953; -.
DR PaxDb; Q9Y6P5; -.
DR PRIDE; Q9Y6P5; -.
DR DNASU; 27244; -.
DR Ensembl; ENST00000302071; ENSP00000306734; ENSG00000080546.
DR Ensembl; ENST00000356644; ENSP00000349061; ENSG00000080546.
DR Ensembl; ENST00000436639; ENSP00000393762; ENSG00000080546.
DR GeneID; 27244; -.
DR KEGG; hsa:27244; -.
DR UCSC; uc003pst.4; human.
DR CTD; 27244; -.
DR GeneCards; GC06M109353; -.
DR HGNC; HGNC:21595; SESN1.
DR MIM; 606103; gene.
DR neXtProt; NX_Q9Y6P5; -.
DR PharmGKB; PA134927596; -.
DR eggNOG; NOG312456; -.
DR HOGENOM; HOG000232949; -.
DR HOVERGEN; HBG054648; -.
DR KO; K10141; -.
DR OMA; RMYESFW; -.
DR OrthoDB; EOG7SBNNF; -.
DR GeneWiki; SESN1; -.
DR GenomeRNAi; 27244; -.
DR NextBio; 50149; -.
DR PRO; PR:Q9Y6P5; -.
DR Bgee; Q9Y6P5; -.
DR CleanEx; HS_SESN1; -.
DR Genevestigator; Q9Y6P5; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR InterPro; IPR006730; PA26.
DR PANTHER; PTHR12474; PTHR12474; 1.
DR Pfam; PF04636; PA26; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 492 Sestrin-1.
FT /FTId=PRO_0000221178.
FT MOD_RES 293 293 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT VAR_SEQ 1 66 Missing (in isoform T3).
FT /FTId=VSP_006060.
FT VAR_SEQ 1 34 MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDE -> MAE
FT GENEVRWDGLCSRDSTTRETALENIRQTILRKTEYLRSVKE
FT TPHRPSDGLSNTESSDGLNKLLAHLLMLSKRCPFKDVREKS
FT EFILKSIQ (in isoform T1).
FT /FTId=VSP_006059.
FT VARIANT 44 44 L -> I (in dbSNP:rs2273668).
FT /FTId=VAR_014210.
SQ SEQUENCE 492 AA; 56557 MW; 824CF6513634C35E CRC64;
MRLAAAANEA YTAPLAVSGL LGCKQCGGGR DQDEELGIRI PRPLGQGPSR FIPEKEILQV
GSEDAQMHAL FADSFAALGR LDNITLVMVF HPQYLESFLK TQHYLLQMDG PLPLHYRHYI
GIMAAARHQC SYLVNLHVND FLHVGGDPKW LNGLENAPQK LQNLGELNKV LAHRPWLITK
EHIEGLLKAE EHSWSLAELV HAVVLLTHYH SLASFTFGCG ISPEIHCDGG HTFRPPSVSN
YCICDITNGN HSVDEMPVNS AENVSVSDSF FEVEALMEKM RQLQECRDEE EASQEEMASR
FEIEKRESMF VFSSDDEEVT PARAVSRHFE DTSYGYKDFS RHGMHVPTFR VQDYCWEDHG
YSLVNRLYPD VGQLIDEKFH IAYNLTYNTM AMHKDVDTSM LRRAIWNYIH CMFGIRYDDY
DYGEINQLLD RSFKVYIKTV VCTPEKVTKR MYDSFWRQFK HSEKVHVNLL LIEARMQAEL
LYALRAITRY MT
//
ID SESN1_HUMAN Reviewed; 492 AA.
AC Q9Y6P5; Q2M2B7; Q5T316; Q9NV00; Q9UPD5; Q9Y6P6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Sestrin-1;
DE AltName: Full=p53-regulated protein PA26;
GN Name=SESN1; Synonyms=PA26, SEST1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS T1; T2 AND T3).
RX PubMed=9926927; DOI=10.1038/sj.onc.1202274;
RA Velasco-Miguel S., Buckbinder L., Jean P., Gelbert L., Talbott R.,
RA Laidlaw J., Seizinger B., Kley N.;
RT "PA26, a novel target of the p53 tumor suppressor and member of the
RT GADD family of DNA damage and growth arrest inducible genes.";
RL Oncogene 18:127-137(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-44, AND TISSUE SPECIFICITY.
RX PubMed=12607115; DOI=10.1007/s00439-003-0917-5;
RA Peeters H., Debeer P., Bairoch A., Wilquet V., Huysmans C.,
RA Parthoens E., Fryns J.-P., Gewillig M., Nakamura Y., Niikawa N.,
RA Van De Ven W., Devriendt K.;
RT "PA26 is a candidate gene for heterotaxia in humans: identification of
RT a novel PA26-related gene family in human and mouse.";
RL Hum. Genet. 112:573-580(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-492.
RC TISSUE=Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7]
RP FUNCTION.
RX PubMed=15105503; DOI=10.1126/science.1095569;
RA Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., Chumakov P.M.;
RT "Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of
RT bacterial AhpD.";
RL Science 304:596-600(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Involved in the reduction of peroxiredoxins. May also be
CC regulator of cellular growth.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=T2;
CC IsoId=Q9Y6P5-1; Sequence=Displayed;
CC Name=T1;
CC IsoId=Q9Y6P5-2; Sequence=VSP_006059;
CC Name=T3;
CC IsoId=Q9Y6P5-3; Sequence=VSP_006060;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- INDUCTION: Isoform T2 and isoform T3 are induced by genotoxic
CC stress (UV, gamma-irradiation and cytotoxic drugs) in a p53/TP53-
CC dependent manner. Isoform T1 is not induced by p53/TP53.
CC -!- SIMILARITY: Belongs to the sestrin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF033122; AAD04812.1; -; mRNA.
DR EMBL; AF033120; AAD04810.1; -; mRNA.
DR EMBL; AF033121; AAD04811.1; -; mRNA.
DR EMBL; AL390208; CAI16720.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48367.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48368.1; -; Genomic_DNA.
DR EMBL; BC112036; AAI12037.1; -; mRNA.
DR EMBL; BC113569; AAI13570.1; -; mRNA.
DR EMBL; AK001886; BAA91961.1; -; mRNA.
DR RefSeq; NP_001186862.1; NM_001199933.1.
DR RefSeq; NP_001186863.1; NM_001199934.1.
DR RefSeq; NP_055269.1; NM_014454.2.
DR UniGene; Hs.591336; -.
DR ProteinModelPortal; Q9Y6P5; -.
DR STRING; 9606.ENSP00000306734; -.
DR PhosphoSite; Q9Y6P5; -.
DR DMDM; 13633953; -.
DR PaxDb; Q9Y6P5; -.
DR PRIDE; Q9Y6P5; -.
DR DNASU; 27244; -.
DR Ensembl; ENST00000302071; ENSP00000306734; ENSG00000080546.
DR Ensembl; ENST00000356644; ENSP00000349061; ENSG00000080546.
DR Ensembl; ENST00000436639; ENSP00000393762; ENSG00000080546.
DR GeneID; 27244; -.
DR KEGG; hsa:27244; -.
DR UCSC; uc003pst.4; human.
DR CTD; 27244; -.
DR GeneCards; GC06M109353; -.
DR HGNC; HGNC:21595; SESN1.
DR MIM; 606103; gene.
DR neXtProt; NX_Q9Y6P5; -.
DR PharmGKB; PA134927596; -.
DR eggNOG; NOG312456; -.
DR HOGENOM; HOG000232949; -.
DR HOVERGEN; HBG054648; -.
DR KO; K10141; -.
DR OMA; RMYESFW; -.
DR OrthoDB; EOG7SBNNF; -.
DR GeneWiki; SESN1; -.
DR GenomeRNAi; 27244; -.
DR NextBio; 50149; -.
DR PRO; PR:Q9Y6P5; -.
DR Bgee; Q9Y6P5; -.
DR CleanEx; HS_SESN1; -.
DR Genevestigator; Q9Y6P5; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR InterPro; IPR006730; PA26.
DR PANTHER; PTHR12474; PTHR12474; 1.
DR Pfam; PF04636; PA26; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome.
FT CHAIN 1 492 Sestrin-1.
FT /FTId=PRO_0000221178.
FT MOD_RES 293 293 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT VAR_SEQ 1 66 Missing (in isoform T3).
FT /FTId=VSP_006060.
FT VAR_SEQ 1 34 MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDE -> MAE
FT GENEVRWDGLCSRDSTTRETALENIRQTILRKTEYLRSVKE
FT TPHRPSDGLSNTESSDGLNKLLAHLLMLSKRCPFKDVREKS
FT EFILKSIQ (in isoform T1).
FT /FTId=VSP_006059.
FT VARIANT 44 44 L -> I (in dbSNP:rs2273668).
FT /FTId=VAR_014210.
SQ SEQUENCE 492 AA; 56557 MW; 824CF6513634C35E CRC64;
MRLAAAANEA YTAPLAVSGL LGCKQCGGGR DQDEELGIRI PRPLGQGPSR FIPEKEILQV
GSEDAQMHAL FADSFAALGR LDNITLVMVF HPQYLESFLK TQHYLLQMDG PLPLHYRHYI
GIMAAARHQC SYLVNLHVND FLHVGGDPKW LNGLENAPQK LQNLGELNKV LAHRPWLITK
EHIEGLLKAE EHSWSLAELV HAVVLLTHYH SLASFTFGCG ISPEIHCDGG HTFRPPSVSN
YCICDITNGN HSVDEMPVNS AENVSVSDSF FEVEALMEKM RQLQECRDEE EASQEEMASR
FEIEKRESMF VFSSDDEEVT PARAVSRHFE DTSYGYKDFS RHGMHVPTFR VQDYCWEDHG
YSLVNRLYPD VGQLIDEKFH IAYNLTYNTM AMHKDVDTSM LRRAIWNYIH CMFGIRYDDY
DYGEINQLLD RSFKVYIKTV VCTPEKVTKR MYDSFWRQFK HSEKVHVNLL LIEARMQAEL
LYALRAITRY MT
//
MIM
606103
*RECORD*
*FIELD* NO
606103
*FIELD* TI
*606103 SESTRIN 1; SESN1
;;SEST1;;
p53-ACTIVATED GENE 26;;
PA26
*FIELD* TX
CLONING
read more
Transcriptional activation of target genes is a major function of p53
(191170). Using differential cDNA subtraction to identify genes
activated by p53, Buckbinder et al. (1994) identified a cDNA encoding
A26. Northern blot analysis revealed expression of approximately 3.0-
and 4.0-kb A26 transcripts in an osteosarcoma cell line.
Velasco-Miguel et al. (1999) further characterized A26, which they
called PA26. Northern blot analysis detected wide expression of the 2.6-
and 4.0-kb PA26 transcripts in adult tissues. Only the smaller
transcript was transiently induced by p53 or by genotoxic agents in a
p53-dependent manner in a colon carcinoma cell line. By cDNA library
screening and 5-prime RACE, Velasco-Miguel et al. (1999) isolated cDNAs
encoding 3 PA26 variants, T1, T2, and T3, which differ at their N
termini. The deduced proteins, which are 99% identical to the mouse
proteins, contain 551, 491, and 426 amino acids, respectively. RT-PCR
analysis detected induction of T2 in response to p53 or genotoxic
stress; however, T1 was not induced and T3 was only weakly induced.
Western blot analysis showed induction of a predominant 55-kD T2 nuclear
protein rather than the 68-kD T1 protein or the 48-kD T3 protein.
Sequence analysis predicted, and EMSA and reporter analysis confirmed,
that PA26 has a p53-binding site within intron 2. Serum starvation
experiments suggested that PA26 may be a member of the growth arrest-
and DNA damage-inducible, or GADD, gene family (e.g., GADD45G; 604949).
Velasco-Miguel et al. (1999) concluded that PA26, like GADD45, is a p53
target gene and a member of the GADD family.
GENE STRUCTURE
By genomic sequence analysis, Velasco-Miguel et al. (1999) determined
that the PA26 gene contains at least 12 exons and spans more than 20 kb.
GENE FUNCTION
Acting as a signal, hydrogen peroxide circumvents antioxidant defense by
overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize
peroxides. Budanov et al. (2004) showed that sestrins, a family of
proteins whose expression is modulated by p53, are required for
regeneration of Prxs containing cys-SO(2)H, thus reestablishing the
antioxidant firewall. Sestrins contain a predicted redox-active domain
homologous to AhpD, the enzyme catalyzing the reduction of a bacterial
peroxiredoxin, AhpC. Purified Hi95 (sestrin-2; 607767) protein supported
adenosine triphosphate-dependent reduction of overoxidized PrxI in
vitro, indicating that unlike AhpD, which is a disulfide reductase,
sestrins are cysteine sulfinyl reductases.
Sestrins are conserved proteins that accumulate in cells exposed to
stress, potentiate adenosine monophosphate-activated protein kinase
(AMPK; 602739), and inhibit activation of TOR (mTOR; 601231). Lee et al.
(2010) showed that the abundance of Drosophila sestrin is increased upon
chronic TOR activation through accumulation of reactive oxygen species
that cause activation of c-Jun N-terminal kinase (see 601158)and
transcription factor Forkhead box O (FoxO; see 136533). Loss of
Drosophila Sesn resulted in age-associated pathologies including
triglyceride accumulation, mitochondrial dysfunction, muscle
degeneration, and cardiac malfunction, which were prevented by
pharmacologic activation of AMPK or inhibition of TOR. Hence, Lee et al.
(2010) concluded that Drosophila Sesn appears to be a negative feedback
regulator of TOR that integrates metabolic and stress inputs and
prevents pathologies caused by chronic TOR activation that may result
from diminished autophagic clearance of damaged mitochondria, protein
aggregates, or lipids.
MAPPING
Using somatic cell hybrid and FISH analyses, Velasco-Miguel et al.
(1999) mapped the PA26 gene to 6q21, a region associated with deletions
in a number of cancers.
MOLECULAR GENETICS
In a patient with heterotaxia and a de novo reciprocal translocation,
t(6;18)(q21;q21), as reported by Kato et al. (1996) (see 606325),
Peeters et al. (2003) found that the PA26 gene was disrupted by the 6q21
breakpoint. Northern blot analysis showed decreased expression of the
PA26 gene in an Epstein-Barr virus-transformed cell line from this
patient. Mutation analysis of the PA26 gene in 40 unrelated individuals
with unexplained heterotaxia failed to identify mutations, indicating
that PA26 mutations are not a frequent cause of heterotaxia.
*FIELD* RF
1. Buckbinder, L.; Talbott, R.; Seizinger, B. R.; Kley, N.: Gene
regulation by temperature-sensitive p53 mutants: identification of
p53 response genes. Proc. Nat. Acad. Sci. 91: 10640-10644, 1994.
2. Budanov, A. V.; Sablina, A. A.; Feinstein, E.; Koonin, E. V.; Chumakov,
P. M.: Regeneration of peroxiredoxins by p53-regulated sestrins,
homologs of bacterial AhpD. Science 304: 596-600, 2004.
3. Kato, R.; Yamada, Y.; Niikawa, N.: De novo balanced translocation
(6;18)(q21;q21.3) in a patient with heterotaxia. Am. J. Med. Genet. 66:
184-186, 1996. Note: Erratum: Am. J. Med. Genet. 70: 104 only, 1997.
4. Lee, J. H.; Budanov, A. V.; Park, E. J.; Birse, R.; Kim, T. E.;
Perkins, G. A.; Ocorr, K.; Ellisman, M. H.; Bodmer, R.; Bier, E.;
Karin, M.: Sestrin as a feedback inhibitor of TOR that prevents age-related
pathologies. Science 327: 1223-1228, 2010.
5. Peeters, H.; Debeer, P.; Bairoch, A.; Wilquet, V.; Huysmans, C.;
Parthoens, E.; Fryns, J. P.; Gewillig, M.; Nakamura, Y.; Niikawa,
N.; Van de Ven, W.; Devriendt, K.: PA26 is a candidate gene for heterotaxia
in humans: identification of a novel PA26-related gene family in human
and mouse. Hum. Genet. 112: 573-580, 2003.
6. Velasco-Miguel, S.; Buckbinder, L.; Jean, P.; Gelbert, L.; Talbott,
R.; Laidlaw, J.; Seizinger, B.; Kley, N.: PA26, a novel target of
the p53 tumor suppressor and member of the GADD family of DNA damage
and growth arrest inducible genes. Oncogene 18: 127-137, 1999.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
Cassandra L. Kniffin - updated: 9/21/2006
Ada Hamosh - updated: 4/30/2004
Victor A. McKusick - updated: 5/8/2003
*FIELD* CD
Paul J. Converse: 7/12/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
ckniffin: 9/21/2006
alopez: 4/30/2004
terry: 4/30/2004
tkritzer: 5/13/2003
tkritzer: 5/12/2003
terry: 5/8/2003
mgross: 7/12/2001
*RECORD*
*FIELD* NO
606103
*FIELD* TI
*606103 SESTRIN 1; SESN1
;;SEST1;;
p53-ACTIVATED GENE 26;;
PA26
*FIELD* TX
CLONING
read more
Transcriptional activation of target genes is a major function of p53
(191170). Using differential cDNA subtraction to identify genes
activated by p53, Buckbinder et al. (1994) identified a cDNA encoding
A26. Northern blot analysis revealed expression of approximately 3.0-
and 4.0-kb A26 transcripts in an osteosarcoma cell line.
Velasco-Miguel et al. (1999) further characterized A26, which they
called PA26. Northern blot analysis detected wide expression of the 2.6-
and 4.0-kb PA26 transcripts in adult tissues. Only the smaller
transcript was transiently induced by p53 or by genotoxic agents in a
p53-dependent manner in a colon carcinoma cell line. By cDNA library
screening and 5-prime RACE, Velasco-Miguel et al. (1999) isolated cDNAs
encoding 3 PA26 variants, T1, T2, and T3, which differ at their N
termini. The deduced proteins, which are 99% identical to the mouse
proteins, contain 551, 491, and 426 amino acids, respectively. RT-PCR
analysis detected induction of T2 in response to p53 or genotoxic
stress; however, T1 was not induced and T3 was only weakly induced.
Western blot analysis showed induction of a predominant 55-kD T2 nuclear
protein rather than the 68-kD T1 protein or the 48-kD T3 protein.
Sequence analysis predicted, and EMSA and reporter analysis confirmed,
that PA26 has a p53-binding site within intron 2. Serum starvation
experiments suggested that PA26 may be a member of the growth arrest-
and DNA damage-inducible, or GADD, gene family (e.g., GADD45G; 604949).
Velasco-Miguel et al. (1999) concluded that PA26, like GADD45, is a p53
target gene and a member of the GADD family.
GENE STRUCTURE
By genomic sequence analysis, Velasco-Miguel et al. (1999) determined
that the PA26 gene contains at least 12 exons and spans more than 20 kb.
GENE FUNCTION
Acting as a signal, hydrogen peroxide circumvents antioxidant defense by
overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize
peroxides. Budanov et al. (2004) showed that sestrins, a family of
proteins whose expression is modulated by p53, are required for
regeneration of Prxs containing cys-SO(2)H, thus reestablishing the
antioxidant firewall. Sestrins contain a predicted redox-active domain
homologous to AhpD, the enzyme catalyzing the reduction of a bacterial
peroxiredoxin, AhpC. Purified Hi95 (sestrin-2; 607767) protein supported
adenosine triphosphate-dependent reduction of overoxidized PrxI in
vitro, indicating that unlike AhpD, which is a disulfide reductase,
sestrins are cysteine sulfinyl reductases.
Sestrins are conserved proteins that accumulate in cells exposed to
stress, potentiate adenosine monophosphate-activated protein kinase
(AMPK; 602739), and inhibit activation of TOR (mTOR; 601231). Lee et al.
(2010) showed that the abundance of Drosophila sestrin is increased upon
chronic TOR activation through accumulation of reactive oxygen species
that cause activation of c-Jun N-terminal kinase (see 601158)and
transcription factor Forkhead box O (FoxO; see 136533). Loss of
Drosophila Sesn resulted in age-associated pathologies including
triglyceride accumulation, mitochondrial dysfunction, muscle
degeneration, and cardiac malfunction, which were prevented by
pharmacologic activation of AMPK or inhibition of TOR. Hence, Lee et al.
(2010) concluded that Drosophila Sesn appears to be a negative feedback
regulator of TOR that integrates metabolic and stress inputs and
prevents pathologies caused by chronic TOR activation that may result
from diminished autophagic clearance of damaged mitochondria, protein
aggregates, or lipids.
MAPPING
Using somatic cell hybrid and FISH analyses, Velasco-Miguel et al.
(1999) mapped the PA26 gene to 6q21, a region associated with deletions
in a number of cancers.
MOLECULAR GENETICS
In a patient with heterotaxia and a de novo reciprocal translocation,
t(6;18)(q21;q21), as reported by Kato et al. (1996) (see 606325),
Peeters et al. (2003) found that the PA26 gene was disrupted by the 6q21
breakpoint. Northern blot analysis showed decreased expression of the
PA26 gene in an Epstein-Barr virus-transformed cell line from this
patient. Mutation analysis of the PA26 gene in 40 unrelated individuals
with unexplained heterotaxia failed to identify mutations, indicating
that PA26 mutations are not a frequent cause of heterotaxia.
*FIELD* RF
1. Buckbinder, L.; Talbott, R.; Seizinger, B. R.; Kley, N.: Gene
regulation by temperature-sensitive p53 mutants: identification of
p53 response genes. Proc. Nat. Acad. Sci. 91: 10640-10644, 1994.
2. Budanov, A. V.; Sablina, A. A.; Feinstein, E.; Koonin, E. V.; Chumakov,
P. M.: Regeneration of peroxiredoxins by p53-regulated sestrins,
homologs of bacterial AhpD. Science 304: 596-600, 2004.
3. Kato, R.; Yamada, Y.; Niikawa, N.: De novo balanced translocation
(6;18)(q21;q21.3) in a patient with heterotaxia. Am. J. Med. Genet. 66:
184-186, 1996. Note: Erratum: Am. J. Med. Genet. 70: 104 only, 1997.
4. Lee, J. H.; Budanov, A. V.; Park, E. J.; Birse, R.; Kim, T. E.;
Perkins, G. A.; Ocorr, K.; Ellisman, M. H.; Bodmer, R.; Bier, E.;
Karin, M.: Sestrin as a feedback inhibitor of TOR that prevents age-related
pathologies. Science 327: 1223-1228, 2010.
5. Peeters, H.; Debeer, P.; Bairoch, A.; Wilquet, V.; Huysmans, C.;
Parthoens, E.; Fryns, J. P.; Gewillig, M.; Nakamura, Y.; Niikawa,
N.; Van de Ven, W.; Devriendt, K.: PA26 is a candidate gene for heterotaxia
in humans: identification of a novel PA26-related gene family in human
and mouse. Hum. Genet. 112: 573-580, 2003.
6. Velasco-Miguel, S.; Buckbinder, L.; Jean, P.; Gelbert, L.; Talbott,
R.; Laidlaw, J.; Seizinger, B.; Kley, N.: PA26, a novel target of
the p53 tumor suppressor and member of the GADD family of DNA damage
and growth arrest inducible genes. Oncogene 18: 127-137, 1999.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
Cassandra L. Kniffin - updated: 9/21/2006
Ada Hamosh - updated: 4/30/2004
Victor A. McKusick - updated: 5/8/2003
*FIELD* CD
Paul J. Converse: 7/12/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
ckniffin: 9/21/2006
alopez: 4/30/2004
terry: 4/30/2004
tkritzer: 5/13/2003
tkritzer: 5/12/2003
terry: 5/8/2003
mgross: 7/12/2001