MOT8_HUMAN - dbPTM
MOT8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOT8_HUMAN
UniProt AC P36021
Protein Name Monocarboxylate transporter 8
Gene Name SLC16A2
Organism Homo sapiens (Human).
Sequence Length 539
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr..
Protein Sequence MALQSQASEEAKGPWQEADQEQQEPVGSPEPESEPEPEPEPEPVPVPPPEPQPEPQPLPDPAPLPELEFESERVHEPEPTPTVETRGTARGFQPPEGGFGWVVVFAATWCNGSIFGIHNSVGILYSMLLEEEKEKNRQVEFQAAWVGALAMGMIFFCSPIVSIFTDRLGCRITATAGAAVAFIGLHTSSFTSSLSLRYFTYGILFGCGCSFAFQPSLVILGHYFQRRLGLANGVVSAGSSIFSMSFPFLIRMLGDKIKLAQTFQVLSTFMFVLMLLSLTYRPLLPSSQDTPSKRGVRTLHQRFLAQLRKYFNMRVFRQRTYRIWAFGIAAAALGYFVPYVHLMKYVEEEFSEIKETWVLLVCIGATSGLGRLVSGHISDSIPGLKKIYLQVLSFLLLGLMSMMIPLCRDFGGLIVVCLFLGLCDGFFITIMAPIAFELVGPMQASQAIGYLLGMMALPMIAGPPIAGLLRNCFGDYHVAFYFAGVPPIIGAVILFFVPLMHQRMFKKEQRDSSKDKMLAPDPDPNGELLPGSPNPEEPI
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
2Acetylation------MALQSQASE
------CCCCCCCCH
17.8222223895
5Phosphorylation---MALQSQASEEAK
---CCCCCCCCHHHC
28.6729514088
8PhosphorylationMALQSQASEEAKGPW
CCCCCCCCHHHCCCH
28.4725849741
71PhosphorylationLPELEFESERVHEPE
CCCCEECCCCCCCCC
35.7024275569
80PhosphorylationRVHEPEPTPTVETRG
CCCCCCCCCCEEECC
29.9030266825
82PhosphorylationHEPEPTPTVETRGTA
CCCCCCCCEEECCCC
33.1930266825
85PhosphorylationEPTPTVETRGTARGF
CCCCCEEECCCCCCC
30.0230266825
193PhosphorylationHTSSFTSSLSLRYFT
ECCCCCCCHHHHHHH
20.9417081983
195PhosphorylationSSFTSSLSLRYFTYG
CCCCCCHHHHHHHHH
16.8517081983
267PhosphorylationAQTFQVLSTFMFVLM
HHHHHHHHHHHHHHH
22.2717081983
290PhosphorylationLLPSSQDTPSKRGVR
CCCCCCCCCCCCHHH
23.0920068230
532PhosphorylationNGELLPGSPNPEEPI
CCCCCCCCCCCCCCC
21.4029514088

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 MOT8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOT8_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 MOT8_HUMAN !!

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

Oops, there are no PPI records of MOT8_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00650 Allan-Herndon-Dudley syndrome; Monocarboxylate transporter 8 deficiency
OMIM Disease
300523Monocarboxylate transporter 8 deficiency (MCT8 deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00149L-Leucine
DB00150L-Tryptophan
DB00135L-Tyrosine
DB00451Levothyroxine
DB01583Liotrix
DB00119Pyruvic acid
Regulatory Network of MOT8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-193 AND SER-195, ANDMASS SPECTROMETRY.

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