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Protein

Sestrin-1

Gene

SESN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway (PubMed:25263562, PubMed:26449471). This stress-inducible metabolic regulator may also play a role in protection against oxidative and genotoxic stresses (By similarity). 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 have an alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 (PubMed:15105503). However, this could not be confirmed (By similarity).By similarity4 Publications

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei130 – 1301Cysteine sulfenic acid (-SOH) intermediateBy similarity
Binding sitei398 – 3981Leucine; via carbonyl oxygenBy similarity
Binding sitei463 – 4631LeucineBy similarity

GO - Molecular functioni

  • leucine binding Source: UniProtKB

GO - Biological processi

  • cellular oxidant detoxification Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • negative regulation of TORC1 signaling Source: UniProtKB
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of response to reactive oxygen species Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Sestrin-1Curated (EC:1.11.1.15By similarity)
Alternative name(s):
p53-regulated protein PA261 Publication
Gene namesi
Name:SESN1Imported
Synonyms:PA261 Publication, SEST11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21595. SESN1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301C → S: Loss of the ability to decrease intracellular reactive oxygen species. 1 Publication

Organism-specific databases

PharmGKBiPA134927596.

Polymorphism and mutation databases

BioMutaiSESN1.
DMDMi13633953.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Sestrin-1PRO_0000221178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei293 – 2931PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y6P5.
MaxQBiQ9Y6P5.
PaxDbiQ9Y6P5.
PeptideAtlasiQ9Y6P5.
PRIDEiQ9Y6P5.

PTM databases

iPTMnetiQ9Y6P5.
PhosphoSiteiQ9Y6P5.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Isoform T2 and isoform T3 are induced by genotoxic stress (UV, gamma-irradiation and cytotoxic drugs) in a p53/TP53-dependent manner. Isoform T1 is not induced by p53/TP53.1 Publication

Gene expression databases

BgeeiQ9Y6P5.
CleanExiHS_SESN1.
GenevisibleiQ9Y6P5. HS.

Interactioni

Subunit structurei

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:26449471). Interacts with RRAGA, RRAGB, RRAGC and RRAGD; may function as a guanine nucleotide dissociation inhibitor for RRAGs and regulate them (PubMed:25259925). Interacts with KEAP1, RBX1 and SQSTM1; in the SQSTM1-dependent autophagic degradation of KEAP1 (PubMed:23274085). May interact with PRDX1 (PubMed:15105503).5 Publications

Protein-protein interaction databases

BioGridi118092. 5 interactions.
STRINGi9606.ENSP00000393762.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6P5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 252182N-terminal domain; mediates the alkylhydroperoxide reductase activityBy similarityAdd
BLAST
Regioni321 – 492172C-terminal domain; mediates TORC1 regulationBy similarityAdd
BLAST
Regioni386 – 3894Leucine-bindingBy similarity

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the sestrin family.Curated

Phylogenomic databases

eggNOGiKOG3746. Eukaryota.
ENOG410XP7Z. LUCA.
GeneTreeiENSGT00440000040103.
HOGENOMiHOG000232949.
HOVERGENiHBG054648.
InParanoidiQ9Y6P5.
KOiK10141.
OMAiRMYESFW.
OrthoDBiEOG7SBNNF.
PhylomeDBiQ9Y6P5.
TreeFamiTF314230.

Family and domain databases

Gene3Di1.20.1290.10. 1 hit.
InterProiIPR029032. AhpD-like.
IPR006730. Sestrin.
[Graphical view]
PfamiPF04636. PA26. 1 hit.
[Graphical view]
SUPFAMiSSF69118. SSF69118. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform T2 (identifier: Q9Y6P5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLAAAANEA YTAPLAVSGL LGCKQCGGGR DQDEELGIRI PRPLGQGPSR
60 70 80 90 100
FIPEKEILQV GSEDAQMHAL FADSFAALGR LDNITLVMVF HPQYLESFLK
110 120 130 140 150
TQHYLLQMDG PLPLHYRHYI GIMAAARHQC SYLVNLHVND FLHVGGDPKW
160 170 180 190 200
LNGLENAPQK LQNLGELNKV LAHRPWLITK EHIEGLLKAE EHSWSLAELV
210 220 230 240 250
HAVVLLTHYH SLASFTFGCG ISPEIHCDGG HTFRPPSVSN YCICDITNGN
260 270 280 290 300
HSVDEMPVNS AENVSVSDSF FEVEALMEKM RQLQECRDEE EASQEEMASR
310 320 330 340 350
FEIEKRESMF VFSSDDEEVT PARAVSRHFE DTSYGYKDFS RHGMHVPTFR
360 370 380 390 400
VQDYCWEDHG YSLVNRLYPD VGQLIDEKFH IAYNLTYNTM AMHKDVDTSM
410 420 430 440 450
LRRAIWNYIH CMFGIRYDDY DYGEINQLLD RSFKVYIKTV VCTPEKVTKR
460 470 480 490
MYDSFWRQFK HSEKVHVNLL LIEARMQAEL LYALRAITRY MT
Length:492
Mass (Da):56,557
Last modified:April 27, 2001 - v2
Checksum:i824CF6513634C35E
GO
Isoform T1 (identifier: Q9Y6P5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDE → MAEGENEVRW...KSEFILKSIQ

Show »
Length:551
Mass (Da):63,826
Checksum:iABFE480007D623BE
GO
Isoform T3 (identifier: Q9Y6P5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:426
Mass (Da):49,624
Checksum:i7B076B9C7783E125
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441L → I.1 Publication
Corresponds to variant rs2273668 [ dbSNP | Ensembl ].
VAR_014210

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform T3. 1 PublicationVSP_006060Add
BLAST
Alternative sequencei1 – 3434MRLAA…RDQDE → MAEGENEVRWDGLCSRDSTT RETALENIRQTILRKTEYLR SVKETPHRPSDGLSNTESSD GLNKLLAHLLMLSKRCPFKD VREKSEFILKSIQ in isoform T1. 2 PublicationsVSP_006059Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033122 mRNA. Translation: AAD04812.1.
AF033120 mRNA. Translation: AAD04810.1.
AF033121 mRNA. Translation: AAD04811.1.
AL390208 Genomic DNA. Translation: CAI16720.1.
CH471051 Genomic DNA. Translation: EAW48367.1.
CH471051 Genomic DNA. Translation: EAW48368.1.
BC112036 mRNA. Translation: AAI12037.1.
BC113569 mRNA. Translation: AAI13570.1.
AK001886 mRNA. Translation: BAA91961.1.
CCDSiCCDS5070.1. [Q9Y6P5-2]
CCDS56444.1. [Q9Y6P5-3]
CCDS56445.1. [Q9Y6P5-1]
RefSeqiNP_001186862.1. NM_001199933.1. [Q9Y6P5-1]
NP_001186863.1. NM_001199934.1. [Q9Y6P5-3]
NP_055269.1. NM_014454.2. [Q9Y6P5-2]
UniGeneiHs.591336.

Genome annotation databases

EnsembliENST00000302071; ENSP00000306734; ENSG00000080546. [Q9Y6P5-3]
ENST00000356644; ENSP00000349061; ENSG00000080546. [Q9Y6P5-1]
ENST00000436639; ENSP00000393762; ENSG00000080546. [Q9Y6P5-2]
GeneIDi27244.
KEGGihsa:27244.
UCSCiuc003pst.5. human. [Q9Y6P5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033122 mRNA. Translation: AAD04812.1.
AF033120 mRNA. Translation: AAD04810.1.
AF033121 mRNA. Translation: AAD04811.1.
AL390208 Genomic DNA. Translation: CAI16720.1.
CH471051 Genomic DNA. Translation: EAW48367.1.
CH471051 Genomic DNA. Translation: EAW48368.1.
BC112036 mRNA. Translation: AAI12037.1.
BC113569 mRNA. Translation: AAI13570.1.
AK001886 mRNA. Translation: BAA91961.1.
CCDSiCCDS5070.1. [Q9Y6P5-2]
CCDS56444.1. [Q9Y6P5-3]
CCDS56445.1. [Q9Y6P5-1]
RefSeqiNP_001186862.1. NM_001199933.1. [Q9Y6P5-1]
NP_001186863.1. NM_001199934.1. [Q9Y6P5-3]
NP_055269.1. NM_014454.2. [Q9Y6P5-2]
UniGeneiHs.591336.

3D structure databases

ProteinModelPortaliQ9Y6P5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118092. 5 interactions.
STRINGi9606.ENSP00000393762.

PTM databases

iPTMnetiQ9Y6P5.
PhosphoSiteiQ9Y6P5.

Polymorphism and mutation databases

BioMutaiSESN1.
DMDMi13633953.

Proteomic databases

EPDiQ9Y6P5.
MaxQBiQ9Y6P5.
PaxDbiQ9Y6P5.
PeptideAtlasiQ9Y6P5.
PRIDEiQ9Y6P5.

Protocols and materials databases

DNASUi27244.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302071; ENSP00000306734; ENSG00000080546. [Q9Y6P5-3]
ENST00000356644; ENSP00000349061; ENSG00000080546. [Q9Y6P5-1]
ENST00000436639; ENSP00000393762; ENSG00000080546. [Q9Y6P5-2]
GeneIDi27244.
KEGGihsa:27244.
UCSCiuc003pst.5. human. [Q9Y6P5-1]

Organism-specific databases

CTDi27244.
GeneCardsiSESN1.
HGNCiHGNC:21595. SESN1.
MIMi606103. gene.
neXtProtiNX_Q9Y6P5.
PharmGKBiPA134927596.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3746. Eukaryota.
ENOG410XP7Z. LUCA.
GeneTreeiENSGT00440000040103.
HOGENOMiHOG000232949.
HOVERGENiHBG054648.
InParanoidiQ9Y6P5.
KOiK10141.
OMAiRMYESFW.
OrthoDBiEOG7SBNNF.
PhylomeDBiQ9Y6P5.
TreeFamiTF314230.

Enzyme and pathway databases

ReactomeiR-HSA-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiSESN1. human.
GeneWikiiSESN1.
GenomeRNAii27244.
PROiQ9Y6P5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6P5.
CleanExiHS_SESN1.
GenevisibleiQ9Y6P5. HS.

Family and domain databases

Gene3Di1.20.1290.10. 1 hit.
InterProiIPR029032. AhpD-like.
IPR006730. Sestrin.
[Graphical view]
PfamiPF04636. PA26. 1 hit.
[Graphical view]
SUPFAMiSSF69118. SSF69118. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes."
    Velasco-Miguel S., Buckbinder L., Jean P., Gelbert L., Talbott R., Laidlaw J., Seizinger B., Kley N.
    Oncogene 18:127-137(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS T1; T2 AND T3), INDUCTION.
  2. "PA26 is a candidate gene for heterotaxia in humans: identification of a novel PA26-related gene family in human and mouse."
    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.
    Hum. Genet. 112:573-580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-44, TISSUE SPECIFICITY.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T1).
    Tissue: Lung.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-492.
    Tissue: Placenta.
  7. "Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD."
    Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., Chumakov P.M.
    Science 304:596-600(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRDX1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-130.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage."
    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.
    Cell Metab. 17:73-84(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KEAP1; RBX1 AND SQSTM1.
  11. "Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling."
    Peng M., Yin N., Li M.O.
    Cell 159:122-133(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RRAGA; RRAGB; RRAGC AND RRAGD.
  12. "The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1."
    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.
    Cell Rep. 9:1-8(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GATOR2 COMPLEX.
  13. Cited for: FUNCTION, INTERACTION WITH GATOR2 COMPLEX, LEUCINE-BINDING.

Entry informationi

Entry nameiSESN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6P5
Secondary accession number(s): Q2M2B7
, Q5T316, Q9NV00, Q9UPD5, Q9Y6P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.