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Sestrin-2 (EC 1.11.1.15) (Hypoxia-induced gene)

 SESN2_HUMAN             Reviewed;         480 AA.
P58004; Q5T7D0; Q96SI5;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Sestrin-2 {ECO:0000305};
EC=1.11.1.15 {ECO:0000305|PubMed:26612684};
AltName: Full=Hypoxia-induced gene {ECO:0000303|PubMed:12203114};
Name=SESN2 {ECO:0000312|HGNC:HGNC:20746};
Synonyms=Hi95 {ECO:0000303|PubMed:12203114},
SEST2 {ECO:0000303|PubMed:12607115};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=12203114; DOI=10.1038/sj.onc.1205877;
Budanov A.V., Shoshani T., Faerman A., Zelin E., Kamer I.,
Kalinski H., Gorodin S., Fishman A., Chajut A., Einat P., Skaliter R.,
Gudkov A.V., Chumakov P.M., Feinstein E.;
"Identification of a novel stress-responsive gene Hi95 involved in
regulation of cell viability.";
Oncogene 21:6017-6031(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hepatoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=12607115; DOI=10.1007/s00439-003-0917-5;
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).
[8]
FUNCTION, INTERACTION WITH PRDX1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-125; CYS-314; CYS-399 AND CYS-430.
PubMed=15105503; DOI=10.1126/science.1095569;
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).
[9]
FUNCTION, INTERACTION WITH TSC1; TSC2 AND AMPK, AND MUTAGENESIS OF
CYS-125.
PubMed=18692468; DOI=10.1016/j.cell.2008.06.028;
Budanov A.V., Karin M.;
"p53 target genes sestrin1 and sestrin2 connect genotoxic stress and
mTOR signaling.";
Cell 134:451-460(2008).
[10]
FUNCTION.
PubMed=19113821; DOI=10.1089/ARS.2008.2360;
Woo H.A., Bae S.H., Park S., Rhee S.G.;
"Sestrin 2 is not a reductase for cysteine sulfinic acid of
peroxiredoxins.";
Antioxid. Redox Signal. 11:739-745(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
FUNCTION, AND INTERACTION WITH KEAP1; RBX1 AND SQSTM1.
PubMed=23274085; DOI=10.1016/j.cmet.2012.12.002;
Bae S.H., Sung S.H., Oh S.Y., Lim J.M., Lee S.K., Park Y.N., Lee H.E.,
Kang D., Rhee S.G.;
"Sestrins activate Nrf2 by promoting p62-dependent autophagic
degradation of Keap1 and prevent oxidative liver damage.";
Cell Metab. 17:73-84(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
INTERACTION WITH RRAGA; RRAGB; RRAGC AND RRAGD.
PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
Peng M., Yin N., Li M.O.;
"Sestrins function as guanine nucleotide dissociation inhibitors for
Rag GTPases to control mTORC1 signaling.";
Cell 159:122-133(2014).
[16]
FUNCTION, AND INTERACTION WITH GATOR2 COMPLEX.
PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
"The Sestrins interact with GATOR2 to negatively regulate the amino-
acid-sensing pathway upstream of mTORC1.";
Cell Rep. 9:1-8(2014).
[17]
FUNCTION, AND INTERACTION WITH GATOR2 COMPLEX.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[18]
INTERACTION WITH SQSTM1 AND ULK1, AND PHOSPHORYLATION BY ULK1.
PubMed=25040165; DOI=10.1111/febs.12905;
Ro S.H., Semple I.A., Park H., Park H., Park H.W., Kim M., Kim J.S.,
Lee J.H.;
"Sestrin2 promotes Unc-51-like kinase 1 mediated phosphorylation of
p62/sequestosome-1.";
FEBS J. 281:3816-3827(2014).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
FUNCTION, AND INDUCTION.
PubMed=24947615; DOI=10.1038/ncomms5233;
Park H.W., Park H., Ro S.H., Jang I., Semple I.A., Kim D.N., Kim M.,
Nam M., Zhang D., Yin L., Lee J.H.;
"Hepatoprotective role of Sestrin2 against chronic ER stress.";
Nat. Commun. 5:4233-4233(2014).
[21]
FUNCTION, INTERACTION WITH GATOR2 COMPLEX, LEUCINE-BINDING, AND
MUTAGENESIS OF SER-190; LEU-261 AND GLU-451.
PubMed=26449471; DOI=10.1126/science.aab2674;
Wolfson R.L., Chantranupong L., Saxton R.A., Shen K., Scaria S.M.,
Cantor J.R., Sabatini D.M.;
"Sestrin2 is a leucine sensor for the mTORC1 pathway.";
Science 351:43-48(2016).
[22]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
DOMAIN, ACTIVE SITE, AND MUTAGENESIS OF PRO-87; HIS-113; CYS-125;
TYR-127; LEU-128; HIS-132; CYS-204; CYS-214; VAL-258; GLU-259;
LEU-261; 262-MET--ARG-264; ARG-264; 336-THR-PHE-337; 340-GLN-ASP-341;
LEU-373; ASN-376; ASP-385; SER-387; CYS-399; ASP-406; ASP-407;
ASP-409; GLY-411; GLN-415; ARG-419; LYS-422; LYS-426 AND CYS-430.
PubMed=26612684; DOI=10.1038/ncomms10025;
Kim H., An S., Ro S.H., Teixeira F., Jin Park G., Kim C., Cho C.S.,
Kim J.S., Jakob U., Lee J.H., Cho U.S.;
"Janus-faced Sestrin2 controls ROS and mTOR signalling through two
separate functional domains.";
Nat. Commun. 6:10025-10025(2015).
[23]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH LEUCINE,
FUNCTION, INTERACTION WITH GATOR2 COMPLEX, REGION, AND MUTAGENESIS OF
HIS-86; THR-374; TYR-375; THR-386; ARG-390; 406-ASP-ASP-407; TRP-444
AND GLU-451.
PubMed=26586190; DOI=10.1126/science.aad2087;
Saxton R.A., Knockenhauer K.E., Wolfson R.L., Chantranupong L.,
Pacold M.E., Wang T., Schwartz T.U., Sabatini D.M.;
"Structural basis for leucine sensing by the Sestrin2-mTORC1
pathway.";
Science 351:53-58(2016).
-!- FUNCTION: Functions as an intracellular leucine sensor that
negatively regulates the TORC1 signaling pathway through the GATOR
complex. In absence of leucine, binds the GATOR subcomplex GATOR2
and prevents TORC1 signaling (PubMed:18692468, PubMed:25263562,
PubMed:25457612, PubMed:26449471, PubMed:26612684,
PubMed:26586190). Binding of leucine to SESN2 disrupts its
interaction with GATOR2 thereby activating the TORC1 signaling
pathway (PubMed:26449471, PubMed:26586190). This stress-inducible
metabolic regulator also plays a role in protection against
oxidative and genotoxic stresses. May negatively regulate protein
translation in response to endoplasmic reticulum stress, via TORC1
(PubMed:24947615). May positively regulate the transcription by
NFE2L2 of genes involved in the response to oxidative stress by
facilitating the SQSTM1-mediated autophagic degradation of KEAP1
(PubMed:23274085). May also mediate TP53 inhibition of TORC1
signaling upon genotoxic stress (PubMed:18692468). Has an
alkylhydroperoxide reductase activity born by the N-terminal
domain of the protein (PubMed:26612684). Was originally reported
to contribute to oxidative stress resistance by reducing PRDX1
(PubMed:15105503). However, this could not be confirmed
(PubMed:19113821). {ECO:0000269|PubMed:15105503,
ECO:0000269|PubMed:18692468, ECO:0000269|PubMed:19113821,
ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:24947615,
ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
ECO:0000269|PubMed:26449471, ECO:0000269|PubMed:26586190,
ECO:0000269|PubMed:26612684}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000305|PubMed:26612684}.
-!- SUBUNIT: Interacts with the GATOR2 complex which is composed of
MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is negatively
regulated by leucine (PubMed:25263562, PubMed:25457612,
PubMed:26449471). Interacts with RRAGA, RRAGB, RRAGC and RRAGD;
may function as a guanine nucleotide dissociation inhibitor for
RRAGs and regulate them (PubMed:25259925). May interact with the
TORC2 complex (By similarity). Interacts with KEAP1, RBX1, SQSTM
and ULK1; to regulate the degradation of KEAP1 (PubMed:23274085,
PubMed:25040165). May also associate with the complex composed of
TSC1, TSC2 and the AMP-responsive protein kinase/AMPK to regulate
TORC1 signaling (PubMed:18692468). May interact with PRDX1
(PubMed:15105503). {ECO:0000250|UniProtKB:P58043,
ECO:0000269|PubMed:15105503, ECO:0000269|PubMed:18692468,
ECO:0000269|PubMed:23274085, ECO:0000269|PubMed:25040165,
ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25263562,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26449471}.
-!- INTERACTION:
Q13501:SQSTM1; NbExp=5; IntAct=EBI-3939642, EBI-307104;
O70405:Ulk1 (xeno); NbExp=5; IntAct=EBI-3939642, EBI-8390771;
Q96S15:WDR24; NbExp=11; IntAct=EBI-3939642, EBI-746424;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15105503}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12607115}.
-!- INDUCTION: Up-regulated by hypoxia and DNA damage
(PubMed:12203114). Up-regulated by treatments inducing endoplasmic
reticulum stress (PubMed:24947615). {ECO:0000269|PubMed:12203114,
ECO:0000269|PubMed:24947615}.
-!- DOMAIN: Composed of an N-terminal domain that has an
alkylhydroperoxide reductase activity and a C-terminal domain that
mediates interaction with GATOR2 through which it regulates TORC1
signaling. {ECO:0000269|PubMed:26612684}.
-!- PTM: Phosphorylated by ULK1 at multiple sites.
{ECO:0000269|PubMed:25040165}.
-!- SIMILARITY: Belongs to the sestrin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB55438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY123223; AAM92261.1; -; mRNA.
EMBL; AL136551; CAB66486.1; -; mRNA.
EMBL; AK027896; BAB55438.1; ALT_INIT; mRNA.
EMBL; AK025640; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK315710; BAG38070.1; -; mRNA.
EMBL; AL353622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07703.1; -; Genomic_DNA.
EMBL; BC013304; AAH13304.1; -; mRNA.
EMBL; BC033719; AAH33719.1; -; mRNA.
CCDS; CCDS321.1; -.
RefSeq; NP_113647.1; NM_031459.4.
UniGene; Hs.469543; -.
PDB; 5CUF; X-ray; 3.50 A; A/B/C/D/E=1-480.
PDB; 5DJ4; X-ray; 2.70 A; A/B/C/D/E=1-480.
PDB; 5T0N; X-ray; 3.00 A; A/B/C/D/E=1-480.
PDBsum; 5CUF; -.
PDBsum; 5DJ4; -.
PDBsum; 5T0N; -.
ProteinModelPortal; P58004; -.
SMR; P58004; -.
BioGrid; 123724; 14.
DIP; DIP-62044N; -.
IntAct; P58004; 10.
MINT; MINT-4715291; -.
STRING; 9606.ENSP00000253063; -.
iPTMnet; P58004; -.
PhosphoSitePlus; P58004; -.
BioMuta; SESN2; -.
DMDM; 13633882; -.
EPD; P58004; -.
MaxQB; P58004; -.
PaxDb; P58004; -.
PeptideAtlas; P58004; -.
PRIDE; P58004; -.
DNASU; 83667; -.
Ensembl; ENST00000253063; ENSP00000253063; ENSG00000130766.
GeneID; 83667; -.
KEGG; hsa:83667; -.
UCSC; uc001bps.4; human.
CTD; 83667; -.
DisGeNET; 83667; -.
EuPathDB; HostDB:ENSG00000130766.4; -.
GeneCards; SESN2; -.
HGNC; HGNC:20746; SESN2.
HPA; HPA018191; -.
MIM; 607767; gene.
neXtProt; NX_P58004; -.
OpenTargets; ENSG00000130766; -.
PharmGKB; PA134882791; -.
eggNOG; KOG3746; Eukaryota.
eggNOG; ENOG410XP7Z; LUCA.
GeneTree; ENSGT00440000040103; -.
HOGENOM; HOG000232949; -.
HOVERGEN; HBG054648; -.
InParanoid; P58004; -.
KO; K20394; -.
OMA; ASSWRHY; -.
OrthoDB; EOG091G0IVA; -.
PhylomeDB; P58004; -.
TreeFam; TF314230; -.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
SIGNOR; P58004; -.
ChiTaRS; SESN2; human.
GeneWiki; SESN2; -.
GenomeRNAi; 83667; -.
PRO; PR:P58004; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000130766; -.
CleanEx; HS_SESN2; -.
Genevisible; P58004; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:InterPro.
GO; GO:0031932; C:TORC2 complex; IEA:Ensembl.
GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:Ensembl.
GO; GO:0070728; F:leucine binding; IDA:UniProtKB.
GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:UniProtKB.
GO; GO:0032542; F:sulfiredoxin activity; IDA:UniProtKB.
GO; GO:0098869; P:cellular oxidant detoxification; IDA:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:UniProtKB.
GO; GO:0071233; P:cellular response to leucine; IMP:UniProtKB.
GO; GO:1990253; P:cellular response to leucine starvation; IMP:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:0046323; P:glucose import; IEA:Ensembl.
GO; GO:0032042; P:mitochondrial DNA metabolic process; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
GO; GO:1902010; P:negative regulation of translation in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:1904504; P:positive regulation of lipophagy; IEA:Ensembl.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IEA:Ensembl.
GO; GO:0090526; P:regulation of gluconeogenesis involved in cellular glucose homeostasis; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:1901031; P:regulation of response to reactive oxygen species; IEA:InterPro.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
Gene3D; 1.20.1290.10; -; 1.
InterPro; IPR029032; AhpD-like.
InterPro; IPR006730; Sestrin.
Pfam; PF04636; PA26; 1.
SUPFAM; SSF69118; SSF69118; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 480 Sestrin-2.
/FTId=PRO_0000221181.
REGION 66 239 N-terminal domain; mediates the
alkylhydroperoxide reductase activity.
{ECO:0000269|PubMed:26612684}.
REGION 308 480 C-terminal domain; mediates TORC1
regulation.
{ECO:0000269|PubMed:26612684}.
REGION 374 377 Leucine-binding. {ECO:0000244|PDB:5DJ4,
ECO:0000269|PubMed:26586190}.
ACT_SITE 125 125 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:26612684}.
BINDING 386 386 Leucine; via carbonyl oxygen.
{ECO:0000244|PDB:5DJ4,
ECO:0000269|PubMed:26586190}.
BINDING 451 451 Leucine. {ECO:0000244|PDB:5DJ4,
ECO:0000269|PubMed:26586190}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 320 320 T -> A (in dbSNP:rs2274848).
/FTId=VAR_022101.
MUTAGEN 86 86 H->A: Loss of leucine-binding.
{ECO:0000269|PubMed:26586190}.
MUTAGEN 87 87 P->S: No effect on the ability to inhibit
the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 113 113 H->E: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with C-128.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 125 125 C->S: Decreased alkylhydroperoxide
reductase activity and loss of the
ability to decrease intracellular
reactive oxygen species. No effect on
interaction with the GATOR2 complex. No
effect on inhibition of TOR signaling.
{ECO:0000269|PubMed:15105503,
ECO:0000269|PubMed:18692468,
ECO:0000269|PubMed:26612684}.
MUTAGEN 127 127 Y->F: Decreased alkylhydroperoxide
reductase activity. No effect on the
ability to inhibit the TORC1 signaling
pathway. {ECO:0000269|PubMed:26612684}.
MUTAGEN 128 128 L->C: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with E-113.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 132 132 H->A: Decreased alkylhydroperoxide
reductase activity. No effect on the
ability to inhibit the TORC1 signaling
pathway. {ECO:0000269|PubMed:26612684}.
MUTAGEN 190 190 S->W: Loss of interaction with GATOR2. No
effect on leucine-binding. Unable to
mediate leucine-induced inhibition of the
TORC1 signaling pathway.
{ECO:0000269|PubMed:26449471}.
MUTAGEN 204 204 C->S: No effect on alkylhydroperoxide
reductase activity. No effect on the
ability to inhibit the TORC1 signaling
pathway. {ECO:0000269|PubMed:26612684}.
MUTAGEN 214 214 C->S: No effect on alkylhydroperoxide
reductase activity.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 258 258 V->R: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with L-259 and R-261.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 259 259 E->L: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with R-258 and R-261.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 261 261 L->A: Decreased leucine-binding.
{ECO:0000269|PubMed:26449471}.
MUTAGEN 261 261 L->R: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with R-258 and L-259.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 262 264 MER->LMM: No effect on the ability to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 264 264 R->P: No effect on the ability to inhibit
the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 314 314 C->S: No effect on ability to decrease
intracellular reactive oxygen species.
{ECO:0000269|PubMed:15105503}.
MUTAGEN 336 337 TF->AA: No effect on the ability to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 340 341 QD->AA: No effect on the ability to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 373 373 L->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-376.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 374 374 T->A: Loss of leucine-binding.
Constitutively interacts with the GATOR2
complex. {ECO:0000269|PubMed:26586190}.
MUTAGEN 375 375 Y->A: Loss of leucine-binding.
{ECO:0000269|PubMed:26586190}.
MUTAGEN 376 376 N->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-373.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 385 385 D->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-387.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 386 386 T->A: Loss of leucine-binding.
Constitutively interacts with the GATOR2
complex. {ECO:0000269|PubMed:26586190}.
MUTAGEN 387 387 S->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-385.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 390 390 R->A: Loss of leucine-binding.
Constitutively interacts with the GATOR2
complex. {ECO:0000269|PubMed:26586190}.
MUTAGEN 399 399 C->S: No effect on alkylhydroperoxide
reductase activity. Altered ability to
decrease intracellular reactive oxygen
species. No effect on the ability to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:15105503,
ECO:0000269|PubMed:26612684}.
MUTAGEN 406 407 DD->AA: Loss of interaction with the
GATOR2 complex. No effect on leucine-
binding. {ECO:0000269|PubMed:26586190}.
MUTAGEN 406 406 D->A: No effect on alkylhydroperoxide
reductase activity. Loss of interaction
with the GATOR2 complex. Unable to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 407 407 D->A: No effect on alkylhydroperoxide
reductase activity. Loss of interaction
with the GATOR2 complex. Unable to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 409 409 D->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-411 and A-415.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 411 411 G->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-409 and A-415.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 415 415 Q->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-409 and A-411.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 419 419 R->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-422 and A-426.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 422 422 K->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-419 and A-426.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 426 426 K->A: No effect on the ability to inhibit
the TORC1 signaling pathway; when
associated with A-419 and A-422.
{ECO:0000269|PubMed:26612684}.
MUTAGEN 430 430 C->S: No effect on alkylhydroperoxide
reductase activity. Altered ability to
decrease intracellular reactive oxygen
species. No effect on the ability to
inhibit the TORC1 signaling pathway.
{ECO:0000269|PubMed:15105503,
ECO:0000269|PubMed:26612684}.
MUTAGEN 444 444 W->E: Loss of leucine-binding.
{ECO:0000269|PubMed:26586190}.
MUTAGEN 444 444 W->L: Decreased affinity for leucine.
Requires increased leucine concentration
to dissociate from GATOR2 and activate
TORC1 signaling.
{ECO:0000269|PubMed:26586190}.
MUTAGEN 451 451 E->A: Decreased leucine-binding.
{ECO:0000269|PubMed:26449471}.
MUTAGEN 451 451 E->Q: Loss of leucine-binding.
Constitutively interacts with the GATOR2
complex. {ECO:0000269|PubMed:26586190}.
HELIX 68 71 {ECO:0000244|PDB:5DJ4}.
TURN 72 74 {ECO:0000244|PDB:5DJ4}.
HELIX 78 83 {ECO:0000244|PDB:5DJ4}.
HELIX 87 102 {ECO:0000244|PDB:5DJ4}.
HELIX 109 121 {ECO:0000244|PDB:5DJ4}.
TURN 122 124 {ECO:0000244|PDB:5DJ4}.
HELIX 126 138 {ECO:0000244|PDB:5DJ4}.
HELIX 143 147 {ECO:0000244|PDB:5DJ4}.
HELIX 149 151 {ECO:0000244|PDB:5DJ4}.
HELIX 154 157 {ECO:0000244|PDB:5DJ4}.
HELIX 160 168 {ECO:0000244|PDB:5DJ4}.
HELIX 170 172 {ECO:0000244|PDB:5DJ4}.
HELIX 175 182 {ECO:0000244|PDB:5DJ4}.
STRAND 185 187 {ECO:0000244|PDB:5DJ4}.
HELIX 191 213 {ECO:0000244|PDB:5DJ4}.
STRAND 228 230 {ECO:0000244|PDB:5CUF}.
STRAND 235 237 {ECO:0000244|PDB:5DJ4}.
HELIX 257 270 {ECO:0000244|PDB:5DJ4}.
HELIX 283 292 {ECO:0000244|PDB:5DJ4}.
HELIX 313 315 {ECO:0000244|PDB:5DJ4}.
STRAND 328 330 {ECO:0000244|PDB:5DJ4}.
HELIX 339 341 {ECO:0000244|PDB:5DJ4}.
TURN 344 347 {ECO:0000244|PDB:5DJ4}.
HELIX 348 355 {ECO:0000244|PDB:5DJ4}.
HELIX 357 371 {ECO:0000244|PDB:5DJ4}.
STRAND 376 378 {ECO:0000244|PDB:5T0N}.
STRAND 381 383 {ECO:0000244|PDB:5T0N}.
HELIX 387 400 {ECO:0000244|PDB:5DJ4}.
HELIX 411 416 {ECO:0000244|PDB:5DJ4}.
HELIX 419 430 {ECO:0000244|PDB:5DJ4}.
HELIX 432 434 {ECO:0000244|PDB:5DJ4}.
HELIX 437 442 {ECO:0000244|PDB:5DJ4}.
HELIX 449 479 {ECO:0000244|PDB:5DJ4}.
SEQUENCE 480 AA; 54494 MW; 9C13371316D84060 CRC64;
MIVADSECRA ELKDYLRFAP GGVGDSGPGE EQRESRARRG PRGPSAFIPV EEVLREGAES
LEQHLGLEAL MSSGRVDNLA VVMGLHPDYF TSFWRLHYLL LHTDGPLASS WRHYIAIMAA
ARHQCSYLVG SHMAEFLQTG GDPEWLLGLH RAPEKLRKLS EINKLLAHRP WLITKEHIQA
LLKTGEHTWS LAELIQALVL LTHCHSLSSF VFGCGILPEG DADGSPAPQA PTPPSEQSSP
PSRDPLNNSG GFESARDVEA LMERMQQLQE SLLRDEGTSQ EEMESRFELE KSESLLVTPS
ADILEPSPHP DMLCFVEDPT FGYEDFTRRG AQAPPTFRAQ DYTWEDHGYS LIQRLYPEGG
QLLDEKFQAA YSLTYNTIAM HSGVDTSVLR RAIWNYIHCV FGIRYDDYDY GEVNQLLERN
LKVYIKTVAC YPEKTTRRMY NLFWRHFRHS EKVHVNLLLL EARMQAALLY ALRAITRYMT


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