TMX1_MOUSE - dbPTM
TMX1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMX1_MOUSE
UniProt AC Q8VBT0
Protein Name Thioredoxin-related transmembrane protein 1
Gene Name Tmx1
Organism Mus musculus (Mouse).
Sequence Length 278
Subcellular Localization Membrane
Single-pass type I membrane protein . Endoplasmic reticulum membrane
Single-pass type I membrane protein . Predominantly found in the endoplasmic reticulum..
Protein Description May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions..
Protein Sequence MAHLGRLMVPLAALVLLLWAVPGAHGRRNNVRVLTDENWTSLLEGEWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVKVAKVDVTEQTGLSGRFIITALPSIYHCKDGEFRRYVGPRTKKDFINFVSDKEWKNIEPISSWFGPSSVLMTMMSALFQLSVYIRTSHSYFVHDLGIPAWGSYLVFAFATVLSGLLLGLCMIFVADCLCPSKRRKPQQQYAKKTSPEFSQPLKKVEEEQEADEEDVSEEEAEDREGASKATSQSSIRQRCVGLPSATDTS
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
82UbiquitinationDLEVKVAKVDVTEQT
CCEEEEEEEECCCCC
41.7922790023
106S-palmitoylationALPSIYHCKDGEFRR
ECCEEEECCCCCCHH
2.1128526873
222PhosphorylationQQQYAKKTSPEFSQP
HHHHHHHCCHHHCHH
49.1325521595
223PhosphorylationQQYAKKTSPEFSQPL
HHHHHHCCHHHCHHH
31.1726824392
227PhosphorylationKKTSPEFSQPLKKVE
HHCCHHHCHHHHHHH
29.2629514104
231UbiquitinationPEFSQPLKKVEEEQE
HHHCHHHHHHHHHHH
62.5527667366
245PhosphorylationEADEEDVSEEEAEDR
HCCCCCCCHHHHHHH
52.1727087446
256PhosphorylationAEDREGASKATSQSS
HHHHHHHCHHCCHHH
33.4127742792
259PhosphorylationREGASKATSQSSIRQ
HHHHCHHCCHHHHHH
30.9128066266
260PhosphorylationEGASKATSQSSIRQR
HHHCHHCCHHHHHHH
32.6928066266
262PhosphorylationASKATSQSSIRQRCV
HCHHCCHHHHHHHHC
27.7425266776
263PhosphorylationSKATSQSSIRQRCVG
CHHCCHHHHHHHHCC
17.7230352176
273PhosphorylationQRCVGLPSATDTS--
HHHCCCCCCCCCC--
49.1725619855
275PhosphorylationCVGLPSATDTS----
HCCCCCCCCCC----
44.1125619855
277PhosphorylationGLPSATDTS------
CCCCCCCCC------
31.7925521595
278PhosphorylationLPSATDTS-------
CCCCCCCC-------
40.8227087446

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 TMX1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMX1_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 TMX1_MOUSE !!

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

Oops, there are no PPI records of TMX1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TMX1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.
"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 SER-245, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY.

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