SESN1_HUMAN - dbPTM
SESN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SESN1_HUMAN
UniProt AC Q9Y6P5
Protein Name Sestrin-1 {ECO:0000305}
Gene Name SESN1 {ECO:0000312|HGNC:HGNC:21595}
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Nucleus . Cytoplasm .
Protein Description 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]
Protein Sequence MRLAAAANEAYTAPLAVSGLLGCKQCGGGRDQDEELGIRIPRPLGQGPSRFIPEKEILQVGSEDAQMHALFADSFAALGRLDNITLVMVFHPQYLESFLKTQHYLLQMDGPLPLHYRHYIGIMAAARHQCSYLVNLHVNDFLHVGGDPKWLNGLENAPQKLQNLGELNKVLAHRPWLITKEHIEGLLKAEEHSWSLAELVHAVVLLTHYHSLASFTFGCGISPEIHCDGGHTFRPPSVSNYCICDITNGNHSVDEMPVNSAENVSVSDSFFEVEALMEKMRQLQECRDEEEASQEEMASRFEIEKRESMFVFSSDDEEVTPARAVSRHFEDTSYGYKDFSRHGMHVPTFRVQDYCWEDHGYSLVNRLYPDVGQLIDEKFHIAYNLTYNTMAMHKDVDTSMLRRAIWNYIHCMFGIRYDDYDYGEINQLLDRSFKVYIKTVVCTPEKVTKRMYDSFWRQFKHSEKVHVNLLLIEARMQAELLYALRAITRYMT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
73 (in isoform 2)Phosphorylation-36.63-
97PhosphorylationFHPQYLESFLKTQHY
ECHHHHHHHHHHHHH
33.0324719451
101PhosphorylationYLESFLKTQHYLLQM
HHHHHHHHHHHHHHC
23.7924043423
104PhosphorylationSFLKTQHYLLQMDGP
HHHHHHHHHHHCCCC
10.1724043423
116PhosphorylationDGPLPLHYRHYIGIM
CCCCCCCHHHHHHHH
13.5324043423
119PhosphorylationLPLHYRHYIGIMAAA
CCCCHHHHHHHHHHH
7.58-
271 (in isoform 3)Ubiquitination-13.7221890473
271UbiquitinationVSVSDSFFEVEALME
EECCCCHHHHHHHHH
13.7221890473
293PhosphorylationCRDEEEASQEEMASR
CCCHHHHCHHHHHHH
41.2117525332
313PhosphorylationRESMFVFSSDDEEVT
CCCCEEECCCCCCCC
27.7930576142
314PhosphorylationESMFVFSSDDEEVTP
CCCEEECCCCCCCCH
37.3023898821
320PhosphorylationSSDDEEVTPARAVSR
CCCCCCCCHHHHHHH
17.9527251275
326PhosphorylationVTPARAVSRHFEDTS
CCHHHHHHHHCCCCC
21.03-
332PhosphorylationVSRHFEDTSYGYKDF
HHHHCCCCCCCCCCH
19.3629978859
333PhosphorylationSRHFEDTSYGYKDFS
HHHCCCCCCCCCCHH
28.9629978859
334PhosphorylationRHFEDTSYGYKDFSR
HHCCCCCCCCCCHHH
26.9429978859
336PhosphorylationFEDTSYGYKDFSRHG
CCCCCCCCCCHHHCC
10.1129978859
337UbiquitinationEDTSYGYKDFSRHGM
CCCCCCCCCHHHCCC
48.1923000965
337 (in isoform 1)Ubiquitination-48.1921890473
340PhosphorylationSYGYKDFSRHGMHVP
CCCCCCHHHCCCCCC
33.2429978859
396UbiquitinationTMAMHKDVDTSMLRR
CCCCCCCCCHHHHHH
11.7421890473
396 (in isoform 2)Ubiquitination-11.7421890473
398PhosphorylationAMHKDVDTSMLRRAI
CCCCCCCHHHHHHHH
18.8429759185
399PhosphorylationMHKDVDTSMLRRAIW
CCCCCCHHHHHHHHH
16.0329759185
482PhosphorylationRMQAELLYALRAITR
HHHHHHHHHHHHHHH
19.0622210691
488PhosphorylationLYALRAITRYMT---
HHHHHHHHHHCC---
18.1122210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SESN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SESN1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SESN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRDX1_HUMANPRDX1physical
15105503
SQSTM_HUMANSQSTM1physical
23274085
RBX1_HUMANRBX1physical
23274085
KEAP1_HUMANKEAP1physical
23274085

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SESN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASSSPECTROMETRY.

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