MOT7_HUMAN - dbPTM
MOT7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOT7_HUMAN
UniProt AC O15403
Protein Name Monocarboxylate transporter 7
Gene Name SLC16A6
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Proton-linked 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 (By similarity)..
Protein Sequence MTQNKLKLCSKANVYTEVPDGGWGWAVAVSFFFVEVFTYGIIKTFGVFFNDLMDSFNESNSRISWIISICVFVLTFSAPLATVLSNRFGHRLVVMLGGLLVSTGMVAASFSQEVSHMYVAIGIISGLGYCFSFLPTVTILSQYFGKRRSIVTAVASTGECFAVFAFAPAIMALKERIGWRYSLLFVGLLQLNIVIFGALLRPIFIRGPASPKIVIQENRKEAQYMLENEKTRTSIDSIDSGVELTTSPKNVPTHTNLELEPKADMQQVLVKTSPRPSEKKAPLLDFSILKEKSFICYALFGLFATLGFFAPSLYIIPLGISLGIDQDRAAFLLSTMAIAEVFGRIGAGFVLNREPIRKIYIELICVILLTVSLFAFTFATEFWGLMSCSIFFGFMVGTIGGTHIPLLAEDDVVGIEKMSSAAGVYIFIQSIAGLAGPPLAGLLVDQSKIYSRAFYSCAAGMALAAVCLALVRPCKMGLCQHHHSGETKVVSHRGKTLQDIPEDFLEMDLAKNEHRVHVQMEPV
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
212UbiquitinationIRGPASPKIVIQENR
CCCCCCCCEEEECCH		47.30-
220UbiquitinationIVIQENRKEAQYMLE
EEEECCHHHHHHHHH		69.82-
220AcetylationIVIQENRKEAQYMLE
EEEECCHHHHHHHHH		69.8221466224
224PhosphorylationENRKEAQYMLENEKT
CCHHHHHHHHHCCCC		15.6625159151
230UbiquitinationQYMLENEKTRTSIDS
HHHHHCCCCCCCHHH		55.69-
231PhosphorylationYMLENEKTRTSIDSI
HHHHCCCCCCCHHHC		32.7623663014
233PhosphorylationLENEKTRTSIDSIDS
HHCCCCCCCHHHCCC		34.9525159151
234PhosphorylationENEKTRTSIDSIDSG
HCCCCCCCHHHCCCC		22.5525159151
237PhosphorylationKTRTSIDSIDSGVEL
CCCCCHHHCCCCCEE		26.9925159151
240PhosphorylationTSIDSIDSGVELTTS
CCHHHCCCCCEECCC		42.9725159151
245PhosphorylationIDSGVELTTSPKNVP
CCCCCEECCCCCCCC		16.2425159151
246PhosphorylationDSGVELTTSPKNVPT
CCCCEECCCCCCCCC		56.5118669648
247PhosphorylationSGVELTTSPKNVPTH
CCCEECCCCCCCCCC		28.7425159151
249UbiquitinationVELTTSPKNVPTHTN
CEECCCCCCCCCCCC		71.05-
253PhosphorylationTSPKNVPTHTNLELE
CCCCCCCCCCCCEEC		36.7327251275
255PhosphorylationPKNVPTHTNLELEPK
CCCCCCCCCCEECCC		43.9327251275
262UbiquitinationTNLELEPKADMQQVL
CCCEECCCCCHHHEE		47.87-
271UbiquitinationDMQQVLVKTSPRPSE
CHHHEEEECCCCCCC		38.84-
272PhosphorylationMQQVLVKTSPRPSEK
HHHEEEECCCCCCCC		36.1629214152
273PhosphorylationQQVLVKTSPRPSEKK
HHEEEECCCCCCCCC		17.1329214152
277PhosphorylationVKTSPRPSEKKAPLL
EECCCCCCCCCCCCC		64.4321712546
287PhosphorylationKAPLLDFSILKEKSF
CCCCCCHHHHHCHHH		27.0324719451
312PhosphorylationTLGFFAPSLYIIPLG
HHCCCCCCEEEECCC		30.3026074081
314PhosphorylationGFFAPSLYIIPLGIS
CCCCCCEEEECCCCC		10.9226074081
450PhosphorylationLVDQSKIYSRAFYSC
EECHHHHHHHHHHHH		8.8826074081
451PhosphorylationVDQSKIYSRAFYSCA
ECHHHHHHHHHHHHH		22.1724719451
455PhosphorylationKIYSRAFYSCAAGMA
HHHHHHHHHHHHHHH		11.2326074081
456PhosphorylationIYSRAFYSCAAGMAL
HHHHHHHHHHHHHHH		7.2826074081
488UbiquitinationHHHSGETKVVSHRGK
CCCCCCCEEEEECCC		36.02-
495UbiquitinationKVVSHRGKTLQDIPE
EEEEECCCCHHHCCH		46.12-
511UbiquitinationFLEMDLAKNEHRVHV
HHHHHHHCCCCEEEE		70.89-
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 MOT7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOT7_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 MOT7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFF1_HUMANAFF1physical
26496610
CSKP_HUMANCASKphysical
26496610
RB6I2_HUMANERC1physical
26496610
ZN768_HUMANZNF768physical
26496610
CEP78_HUMANCEP78physical
26496610
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
DB00119Pyruvic acid
Regulatory Network of MOT7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-237; SER-240AND SER-247, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-240, ANDMASS SPECTROMETRY.

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