SESN2_HUMAN - dbPTM
SESN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SESN2_HUMAN
UniProt AC P58004
Protein Name Sestrin-2 {ECO:0000305}
Gene Name SESN2 {ECO:0000312|HGNC:HGNC:20746}
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization 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. [PubMed: 18692468]
Protein Sequence MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT
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
1Acetylation-------MIVADSEC
-------CCCCCHHH
5.1222814378
13UbiquitinationSECRAELKDYLRFAP
HHHHHHHHHHHHHCC
35.5127667366
26PhosphorylationAPGGVGDSGPGEEQR
CCCCCCCCCCCHHHH
40.7421815630
45PhosphorylationRRGPRGPSAFIPVEE
HHCCCCCCCCCCHHH
38.34-
89PhosphorylationVMGLHPDYFTSFWRL
HHCCCHHHHHHHHHH
17.1324248375
91PhosphorylationGLHPDYFTSFWRLHY
CCCHHHHHHHHHHHH
19.4524248375
158UbiquitinationRAPEKLRKLSEINKL
CCHHHHHHHHHHHHH
67.7929967540
160PhosphorylationPEKLRKLSEINKLLA
HHHHHHHHHHHHHHH
39.1924702127
164UbiquitinationRKLSEINKLLAHRPW
HHHHHHHHHHHCCCC
51.0029967540
249PhosphorylationSRDPLNNSGGFESAR
CCCCCCCCCCCHHHH
38.9430278072
254PhosphorylationNNSGGFESARDVEAL
CCCCCCHHHHHHHHH
26.7530278072
271PhosphorylationRMQQLQESLLRDEGT
HHHHHHHHHHHCCCC
21.5330108239
274MethylationQLQESLLRDEGTSQE
HHHHHHHHCCCCCHH
45.27115916497
278PhosphorylationSLLRDEGTSQEEMES
HHHHCCCCCHHHHHH
25.7830108239
279PhosphorylationLLRDEGTSQEEMESR
HHHCCCCCHHHHHHH
46.5930108239
285PhosphorylationTSQEEMESRFELEKS
CCHHHHHHHHHHHHC
40.7430108239
323PhosphorylationVEDPTFGYEDFTRRG
EECCCCCCCCCHHCC
14.24-
374PhosphorylationFQAAYSLTYNTIAMH
HHHHHHCCHHHHHHH
14.5822210691
377PhosphorylationAYSLTYNTIAMHSGV
HHHCCHHHHHHHCCC
10.3322210691
426UbiquitinationRNLKVYIKTVACYPE
HCCEEEEEEEEECCH
21.1829967540
434UbiquitinationTVACYPEKTTRRMYN
EEEECCHHHHHHHHH
51.1727667366
470PhosphorylationRMQAALLYALRAITR
HHHHHHHHHHHHHHH
12.3918491316

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 SESN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SESN2_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 SESN2_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
ULK1_HUMANULK1physical
25040165
RBCC1_HUMANRB1CC1physical
25040165
ATG13_HUMANATG13physical
25040165
SQSTM_HUMANSQSTM1physical
27337507

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 SESN2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP