ITM2C_MOUSE - dbPTM
ITM2C_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITM2C_MOUSE
UniProt AC Q91VK4
Protein Name Integral membrane protein 2C
Gene Name Itm2c
Organism Mus musculus (Mouse).
Sequence Length 269
Subcellular Localization Lysosome membrane
Single-pass type II membrane protein . Cell membrane
Single-pass type II membrane protein.
Protein Description Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation..
Protein Sequence MVKISFQPAVAGIKADKADKAAASGPASASAPAAEILLTPAREERPPRHRSRKGGSVGGVCYLSMGMVVLLMGLVFASVYIYRYFFLAQLARDNFFHCGVLYEDSLSSQIRTRLELEEDVKIYLEENYERINVPVPQFGGGDPADIIHDFQRGLTAYHDISLDKCYVIELNTTIVLPPRNFWELLMNVKRGTYLPQTYIIQEEMVVTEHVRDKEALGSFIYHLCNGKDTYRLRRRSTRRRINKRGGKNCNAIRHFENTFVVETLICGVV
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
3Ubiquitination-----MVKISFQPAV
-----CCEEEECCCC
31.19-
14UbiquitinationQPAVAGIKADKADKA
CCCCCCCCCCHHHHH
50.0027667366
17UbiquitinationVAGIKADKADKAAAS
CCCCCCCHHHHHHHC
64.4427667366
20UbiquitinationIKADKADKAAASGPA
CCCCHHHHHHHCCCC
44.8027667366
39PhosphorylationPAAEILLTPAREERP
CHHHHHCCCCCCCCC
16.0821082442
96UbiquitinationQLARDNFFHCGVLYE
HHHHHCCEEEEEEEC
6.1327667366
99UbiquitinationRDNFFHCGVLYEDSL
HHCCEEEEEEECHHH
12.1427667366
102UbiquitinationFFHCGVLYEDSLSSQ
CEEEEEEECHHHHHH
18.4527667366
107PhosphorylationVLYEDSLSSQIRTRL
EEECHHHHHHHHHHC
24.9328285833
108PhosphorylationLYEDSLSSQIRTRLE
EECHHHHHHHHHHCC
34.6128285833
112PhosphorylationSLSSQIRTRLELEED
HHHHHHHHHCCHHHH
41.0328285833
166PhosphorylationDISLDKCYVIELNTT
ECCCCCEEEEEECCE
15.3724719451
171N-linked_GlycosylationKCYVIELNTTIVLPP
CEEEEEECCEEEECC
23.53-
173PhosphorylationYVIELNTTIVLPPRN
EEEEECCEEEECCCC
14.1724719451
198PhosphorylationGTYLPQTYIIQEEMV
CCCCCCEEEEEEEEE
7.2628059163

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 ITM2C_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITM2C_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 ITM2C_MOUSE !!

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

Oops, there are no PPI records of ITM2C_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITM2C_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39, AND MASSSPECTROMETRY.

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