MOT2_HUMAN - dbPTM
MOT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOT2_HUMAN
UniProt AC O60669
Protein Name Monocarboxylate transporter 2
Gene Name SLC16A7
Organism Homo sapiens (Human).
Sequence Length 478
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. Functions as high-affinity pyruvate transporter..
Protein Sequence MPPMPSAPPVHPPPDGGWGWIVVGAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFAIMFNGVCHLLCPLAQDYTSLVLYAVFFGLGFGSVSSVLFETLMDLVGAPRFSSAVGLVTIVECGPVLLGPPLAGKLVDLTGEYKYMYMSCGAIVVAASVWLLIGNAINYRLLAKERKEENARQKTRESEPLSKSKHSEDVNVKVSNAQSVTSERETNI
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
33PhosphorylationAFISIGFSYAFPKAV
EEEECCHHHHCCHHH		15.44-
34PhosphorylationFISIGFSYAFPKAVT
EEECCHHHHCCHHHH		15.25-
62PhosphorylationYSEIAWISSIMLAVM
HHHHHHHHHHHHHHH		11.78-
177PhosphorylationNTFGWKGSFLILGSL
HCCCCCCCHHHHHHH		17.1028188228
183PhosphorylationGSFLILGSLLLNACV
CCHHHHHHHHHHHHH		16.6428188228
193PhosphorylationLNACVAGSLMRPLGP
HHHHHHHHHCCCCCC		14.8428188228
213UbiquitinationKSKNKTGKTEDDSSP
CCCCCCCCCCCCCCC		54.71-
218PhosphorylationTGKTEDDSSPKKIKT
CCCCCCCCCCCCCCC		61.9425849741
219PhosphorylationGKTEDDSSPKKIKTK
CCCCCCCCCCCCCCC		47.9729743597
221UbiquitinationTEDDSSPKKIKTKKS
CCCCCCCCCCCCCHH		69.91-
232UbiquitinationTKKSTWEKVNKYLDF
CCHHHHHHHHHHHCH		42.54-
240PhosphorylationVNKYLDFSLFKHRGF
HHHHHCHHHHCCCCE		32.3424719451
281PhosphorylationDQGIDEYSAAFLLSV
HCCCCHHHHHHHHHH		15.8623403867
444UbiquitinationKEENARQKTRESEPL
HHHHHHHHHHCCCCC		43.95-
445PhosphorylationEENARQKTRESEPLS
HHHHHHHHHCCCCCC		31.1926074081
448PhosphorylationARQKTRESEPLSKSK
HHHHHHCCCCCCCCC		41.0228122231
452PhosphorylationTRESEPLSKSKHSED
HHCCCCCCCCCCCCC		45.6726699800
453UbiquitinationRESEPLSKSKHSEDV
HCCCCCCCCCCCCCC		71.81-
454PhosphorylationESEPLSKSKHSEDVN
CCCCCCCCCCCCCCC		32.0226657352
455UbiquitinationSEPLSKSKHSEDVNV
CCCCCCCCCCCCCCE		55.69-
457PhosphorylationPLSKSKHSEDVNVKV
CCCCCCCCCCCCEEE		38.9526657352
463UbiquitinationHSEDVNVKVSNAQSV
CCCCCCEEECCCCCC		34.4421906983
465O-linked_GlycosylationEDVNVKVSNAQSVTS
CCCCEEECCCCCCCC		22.2628657654
465PhosphorylationEDVNVKVSNAQSVTS
CCCCEEECCCCCCCC		22.2622199227
469PhosphorylationVKVSNAQSVTSERET
EEECCCCCCCCCCCC		25.5923927012
471PhosphorylationVSNAQSVTSERETNI
ECCCCCCCCCCCCCC		30.0725159151
472PhosphorylationSNAQSVTSERETNI-
CCCCCCCCCCCCCC-		32.2825159151
476PhosphorylationSVTSERETNI-----
CCCCCCCCCC-----		44.4225627689
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 MOT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOT2_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 MOT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MOT2_HUMAN !!
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
DB01440Gamma Hydroxybutyric Acid
DB04552Niflumic Acid
DB01032Probenecid
DB00119Pyruvic acid
Regulatory Network of MOT2_HUMAN

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Related Literatures of Post-Translational Modification

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