S19A2_HUMAN - dbPTM
S19A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S19A2_HUMAN
UniProt AC O60779
Protein Name Thiamine transporter 1
Gene Name SLC19A2
Organism Homo sapiens (Human).
Sequence Length 497
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description High-affinity transporter for the intake of thiamine..
Protein Sequence MDVPGPVSRRAAAAAATVLLRTARVRRECWFLPTALLCAYGFFASLRPSEPFLTPYLLGPDKNLTEREVFNEIYPVWTYSYLVLLFPVFLATDYLRYKPVVLLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYSVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVAGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYTQGLWEKVMPSRYAAIYNGGVEAVSTLLGAVAVFAVGYIKISWSTWGEMTLSLFSLLIAAAVYIMDTVGNIWVCYASYVVFRIIYMLLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDASGLGLEITTQFLIYASYFALIAVVFLASGAVSVMKKCRKLEDPQSSSQVTTS
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
1Acetylation-------MDVPGPVS
-------CCCCCHHH		12.0622814378
8PhosphorylationMDVPGPVSRRAAAAA
CCCCCHHHHHHHHHH		21.1223186163
17PhosphorylationRAAAAAATVLLRTAR
HHHHHHHHHHHHHHH		13.63-
63N-linked_GlycosylationYLLGPDKNLTEREVF
HHCCCCCCCCHHHHH		60.62UniProtKB CARBOHYD
222PhosphorylationLFFHHIPSTCQRVNG
HHHCCCCCCCCEECC		41.0121712546
223PhosphorylationFFHHIPSTCQRVNGI
HHCCCCCCCCEECCE		13.8030108239
231UbiquitinationCQRVNGIKVQNGGIV
CCEECCEEEECCCEE		38.88-
241PhosphorylationNGGIVTDTPASNHLP
CCCEECCCCCCCCCC		16.0525627689
244PhosphorylationIVTDTPASNHLPGWE
EECCCCCCCCCCCCH		26.4525627689
256UbiquitinationGWEDIESKIPLNMEE
CCHHHHCCCCCCCCC		35.2421906983
256 (in isoform 1)Ubiquitination-35.2421906983
283 (in isoform 2)Ubiquitination-12.8221906983
290PhosphorylationWNDFLMCYSSRPLLC
HHHHHHHHCCCCHHH		8.8424043423
291PhosphorylationNDFLMCYSSRPLLCW
HHHHHHHCCCCHHHH		18.2324043423
292PhosphorylationDFLMCYSSRPLLCWS
HHHHHHCCCCHHHHH		16.0824043423
314N-linked_GlycosylationCGYFQVVNYTQGLWE
CCCHHHEECCCCHHH		34.97UniProtKB CARBOHYD
332PhosphorylationPSRYAAIYNGGVEAV
HHHHHHHHCCHHHHH		11.74-
400PhosphorylationYVVFRIIYMLLITIA
HHHHHHHHHHHHHHH		4.5524043423
405PhosphorylationIIYMLLITIATFQIA
HHHHHHHHHHHHHHH		12.4324043423
408PhosphorylationMLLITIATFQIAANL
HHHHHHHHHHHHHCC		16.5424043423
416PhosphorylationFQIAANLSMERYALV
HHHHHCCCCHHHHHH		20.5724043423
484UbiquitinationSVMKKCRKLEDPQSS
HHHHHHHCCCCCCCC		66.742190698
484 (in isoform 1)Ubiquitination-66.7421906983
490PhosphorylationRKLEDPQSSSQVTTS
HCCCCCCCCCCCCCC		37.0323312004
491PhosphorylationKLEDPQSSSQVTTS-
CCCCCCCCCCCCCC-		21.3923312004
492PhosphorylationLEDPQSSSQVTTS--
CCCCCCCCCCCCC--		33.6421712546
495PhosphorylationPQSSSQVTTS-----
CCCCCCCCCC-----		17.4321712546
496PhosphorylationQSSSQVTTS------
CCCCCCCCC------		33.3227134283
497PhosphorylationSSSQVTTS-------
CCCCCCCC-------		28.9425159151
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 S19A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S19A2_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 S19A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNSL2_HUMANDNASE1L2physical
26186194
PPIE_HUMANPPIEphysical
26186194
PPIE_HUMANPPIEphysical
28514442
DNSL2_HUMANDNASE1L2physical
28514442
ATPB_HUMANATP5Bphysical
28514442
Drug and Disease Associations
Kegg Disease
H01183 Thiamine-responsive megaloblastic anemia (TRMA)
OMIM Disease
249270Thiamine-responsive megaloblastic anemia syndrome (TRMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00152Thiamine
Regulatory Network of S19A2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASSSPECTROMETRY.

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