SEC13_MOUSE - dbPTM
SEC13_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC13_MOUSE
UniProt AC Q9D1M0
Protein Name Protein SEC13 homolog {ECO:0000305}
Gene Name Sec13
Organism Mus musculus (Mouse).
Sequence Length 322
Subcellular Localization Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Nucleus, nuclear pore complex . Lysosome membrane . In interphase,
Protein Description Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles.; As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1..
Protein Sequence MVSVMNTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWKEENGTWEKTHEHSGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWREEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASGNMWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASITEGQQNEQ
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
2Acetylation------MVSVMNTVD
------CCCCCCCCC
6.25-
3Phosphorylation-----MVSVMNTVDT
-----CCCCCCCCCC
17.85-
10PhosphorylationSVMNTVDTSHEDMIH
CCCCCCCCCHHHHHC
27.87-
11PhosphorylationVMNTVDTSHEDMIHD
CCCCCCCCHHHHHCH
22.03-
38AcetylationCSSDRSVKIFDVRNG
CCCCCCEEEEEECCC
38.6122826441
87AcetylationDRKVIIWKEENGTWE
CCEEEEEECCCCCEE
44.7523954790
87UbiquitinationDRKVIIWKEENGTWE
CCEEEEEECCCCCEE
44.75-
87SuccinylationDRKVIIWKEENGTWE
CCEEEEEECCCCCEE
44.7523954790
166PhosphorylationAPAVVPGSLIDQPSG
CCEECCCCCCCCCCC
18.97-
175UbiquitinationIDQPSGQKPNYIKKF
CCCCCCCCCCHHHHH
38.4622790023
181AcetylationQKPNYIKKFASGGCD
CCCCHHHHHHCCCCH
36.2822826441
181UbiquitinationQKPNYIKKFASGGCD
CCCCHHHHHHCCCCH
36.2822790023
184PhosphorylationNYIKKFASGGCDNLI
CHHHHHHCCCCHHHH
38.5628066266
192AcetylationGGCDNLIKLWREEED
CCCHHHHHHHHHCCC
45.2022826441
203AcetylationEEEDGQWKEEQKLEA
HCCCCCCCHHHHHHH
43.4123954790
234GlutathionylationPTSTIASCSQDGRVF
CCHHEEEECCCCCEE
2.9024333276
234S-palmitoylationPTSTIASCSQDGRVF
CCHHEEEECCCCCEE
2.9028526873
292PhosphorylationKVTLWKESVDGQWVC
EEEEEEECCCCEEEE
23.0623140645
301PhosphorylationDGQWVCISDVNKGQG
CCEEEEEEEECCCCC
30.3123140645
309PhosphorylationDVNKGQGSVSASITE
EECCCCCEEEEEECC
12.6626824392
311PhosphorylationNKGQGSVSASITEGQ
CCCCCEEEEEECCCC
20.2823684622
313PhosphorylationGQGSVSASITEGQQN
CCCEEEEEECCCCCC
23.6520415495
315PhosphorylationGSVSASITEGQQNEQ
CEEEEEECCCCCCCC
31.4129550500

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 SEC13_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC13_MOUSE !!

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 SEC13_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SEC13_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEC13_MOUSE

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Related Literatures of Post-Translational Modification

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