MOT1_MOUSE - dbPTM
MOT1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOT1_MOUSE
UniProt AC P53986
Protein Name Monocarboxylate transporter 1
Gene Name Slc16a1
Organism Mus musculus (Mouse).
Sequence Length 493
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis..
Protein Sequence MPPAIGGPVGYTPPDGGWGWAVLVGAFISIGFSYAFPKSITVFFKEIEVIFSATTSEVSWISSIMLAVMYAGGPISSILVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYLCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFDIFDWRGSFLILGGLLLNCCVAGSLMRPIGPEQVKLEKLKSKESLQEAGKSDANTDLIGGSPKGEKLSVFQTINKFLDLSLFTHRGFLLYLSGNVVMFFGLFTPLVFLSSYGKSKDFSSEKSAFLLSILAFVDMVARPSMGLAANTKWIRPRIQYFFAASVVANGVCHLLAPLSTTYVGFCVYAGVFGFAFGWLSSVLFETLMDLIGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGIYLFIGMGINYRLLAKEQKAEEKQKREGKEDEASTDVDEKPKETMKAAQSPQQHSSGDPTEEESPV
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
204UbiquitinationPIGPEQVKLEKLKSK
CCCHHHHHHHHHCCH		51.10-
210PhosphorylationVKLEKLKSKESLQEA
HHHHHHCCHHHHHHH		52.6827087446
211UbiquitinationKLEKLKSKESLQEAG
HHHHHCCHHHHHHHC		50.1322790023
213PhosphorylationEKLKSKESLQEAGKS
HHHCCHHHHHHHCCC		38.8027087446
219UbiquitinationESLQEAGKSDANTDL
HHHHHHCCCCCCCCC		52.8122790023
220PhosphorylationSLQEAGKSDANTDLI
HHHHHCCCCCCCCCC		40.8324925903
224PhosphorylationAGKSDANTDLIGGSP
HCCCCCCCCCCCCCC		33.6225521595
230PhosphorylationNTDLIGGSPKGEKLS
CCCCCCCCCCCCCCC		20.4425521595
232UbiquitinationDLIGGSPKGEKLSVF
CCCCCCCCCCCCCHH		79.8422790023
456UbiquitinationEKQKREGKEDEASTD
HHHHHCCCCCHHCCC		58.1822790023
461PhosphorylationEGKEDEASTDVDEKP
CCCCCHHCCCCCCCH		24.0827087446
462PhosphorylationGKEDEASTDVDEKPK
CCCCHHCCCCCCCHH		47.2727087446
467AcetylationASTDVDEKPKETMKA
HCCCCCCCHHHHHHH		57.8523954790
467UbiquitinationASTDVDEKPKETMKA
HCCCCCCCHHHHHHH		57.8522790023
469UbiquitinationTDVDEKPKETMKAAQ
CCCCCCHHHHHHHHH		76.5122790023
471PhosphorylationVDEKPKETMKAAQSP
CCCCHHHHHHHHHCC		30.0525619855
473UbiquitinationEKPKETMKAAQSPQQ
CCHHHHHHHHHCCCC		48.2522790023
477PhosphorylationETMKAAQSPQQHSSG
HHHHHHHCCCCCCCC		21.6824925903
482PhosphorylationAQSPQQHSSGDPTEE
HHCCCCCCCCCCCCC		31.5124925903
483PhosphorylationQSPQQHSSGDPTEEE
HCCCCCCCCCCCCCC		45.1224925903
487PhosphorylationQHSSGDPTEEESPV-
CCCCCCCCCCCCCC-		61.8524925903
491PhosphorylationGDPTEEESPV-----
CCCCCCCCCC-----		33.9524925903
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 MOT1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOT1_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 MOT1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MOT1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOT1_MOUSE

loading...

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-213, 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-213; SER-230; SER-461;THR-462 AND SER-491, AND MASS SPECTROMETRY.
"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-210; SER-213 ANDSER-461, AND MASS SPECTROMETRY.
"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-213, 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-213 AND SER-491, ANDMASS SPECTROMETRY.
"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-213, 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-477 AND SER-491, ANDMASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-213, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory