S19A3_HUMAN - dbPTM
S19A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S19A3_HUMAN
UniProt AC Q9BZV2
Protein Name Thiamine transporter 2
Gene Name SLC19A3
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Mediates high affinity thiamine uptake, probably via a proton anti-port mechanism. Has no folate transport activity..
Protein Sequence MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYKPVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQLLVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILSTSGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVEAIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNVERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPDVSHPEEESNIIMSTKL
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
45N-linked_GlycosylationYLSGPDKNLTSAEIT
HCCCCCCCCCHHHHC
56.8019159218
151PhosphorylationRSVTLAAYTAGSVLA
HHHHHHHHHHHHHHH
7.48-
152PhosphorylationSVTLAAYTAGSVLAQ
HHHHHHHHHHHHHHH
21.59-
166N-linked_GlycosylationQLLVSLANMSYFYLN
HHHHHHHCCCHHHHH
25.81UniProtKB CARBOHYD
210PhosphorylationPSREIKKSSSVNPVL
CCCHHHCCCCCCCCH
23.8929978859
211PhosphorylationSREIKKSSSVNPVLE
CCHHHCCCCCCCCHH
47.3829978859
212PhosphorylationREIKKSSSVNPVLEE
CHHHCCCCCCCCHHH
32.7626657352
220PhosphorylationVNPVLEETHEGEAPG
CCCCHHHCCCCCCCC
18.8229978859
234PhosphorylationGCEEQKPTSEILSTS
CCCCCCCCHHHHCCC
46.1323312004
235PhosphorylationCEEQKPTSEILSTSG
CCCCCCCHHHHCCCC
31.0325002506
239PhosphorylationKPTSEILSTSGKLNK
CCCHHHHCCCCCCCC
26.6230242111
240PhosphorylationPTSEILSTSGKLNKG
CCHHHHCCCCCCCCH
37.7427251275
241PhosphorylationTSEILSTSGKLNKGQ
CHHHHCCCCCCCCHH
30.4722798277
472PhosphorylationKSQKDVQSPAPSENP
CCCCCCCCCCCCCCC
23.9128192239
476PhosphorylationDVQSPAPSENPDVSH
CCCCCCCCCCCCCCC
52.7128857561
482PhosphorylationPSENPDVSHPEEESN
CCCCCCCCCCHHHHC
40.4822210691
488PhosphorylationVSHPEEESNIIMSTK
CCCCHHHHCCEEEEC
36.2922210691
493PhosphorylationEESNIIMSTKL----
HHHCCEEEECC----
16.3922210691
494PhosphorylationESNIIMSTKL-----
HHCCEEEECC-----
20.9822210691

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 S19A3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S19A3_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 S19A3_HUMAN !!

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

Oops, there are no PPI records of S19A3_HUMAN !!

Drug and Disease Associations
Kegg Disease
H01231 Biotin-responsive basal ganglia disease (BBGD)
OMIM Disease
607483Thiamine metabolism dysfunction syndrome 2, biotin- or thiamine-responsive type (THMD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00151L-Cysteine
Regulatory Network of S19A3_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45, AND MASS SPECTROMETRY.

TOP