SC5A1_HUMAN - dbPTM
SC5A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC5A1_HUMAN
UniProt AC P13866
Protein Name Sodium/glucose cotransporter 1
Gene Name SLC5A1
Organism Homo sapiens (Human).
Sequence Length 664
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Actively transports glucose into cells by Na(+) cotransport with a Na(+) to glucose coupling ratio of 2:1. Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na(+)/glucose cotransporter arranged in series along kidney proximal tubules..
Protein Sequence MDSSTWSPKTTAVTRPVETHELIRNAADISIIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAASGIAIGGFEWNALVLVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGQRIQVYLSLLSLLLYIFTKISADIFSGAIFINLALGLNLYLAIFLLLAITALYTITGGLAAVIYTDTLQTVIMLVGSLILTGFAFHEVGGYDAFMEKYMKAIPTIVSDGNTTFQEKCYTPRADSFHIFRDPLTGDLPWPGFIFGMSILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMPMFIMVMPGMISRILYTEKIACVVPSECEKYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSASTLFTMDIYAKVRKRASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFWKRVNEPGAFWGLILGLLIGISRMITEFAYGTGSCMEPSNCPTIICGVHYLYFAIILFAISFITIVVISLLTKPIPDVHLYRLCWSLRNSKEERIDLDAEEENIQEGPKETIEIETQVPEKKKGIFRRAYDLFCGLEQHGAPKMTEEEEKAMKMKMTDTSEKPLWRTVLNVNGIILVTVAVFCHAYFA
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
7Phosphorylation-MDSSTWSPKTTAVT
-CCCCCCCCCCCCCC
19.3324719451
10O-linked_GlycosylationSSTWSPKTTAVTRPV
CCCCCCCCCCCCCCC
24.30OGP
14O-linked_GlycosylationSPKTTAVTRPVETHE
CCCCCCCCCCCCHHH
27.13OGP
19PhosphorylationAVTRPVETHELIRNA
CCCCCCCHHHHHHHH
22.3822210691
35PhosphorylationDISIIVIYFVVVMAV
HHHHHHHHHHHHHHH
4.5722210691
50PhosphorylationGLWAMFSTNRGTVGG
HHHHHHCCCCCCCCE
20.0522210691
229PhosphorylationAFHEVGGYDAFMEKY
HHHHCCCHHHHHHHH
9.7322468782
236PhosphorylationYDAFMEKYMKAIPTI
HHHHHHHHHHHCCEE
7.19-
242PhosphorylationKYMKAIPTIVSDGNT
HHHHHCCEECCCCCC
28.09-
245PhosphorylationKAIPTIVSDGNTTFQ
HHCCEECCCCCCEEC
35.6322468782
248N-linked_GlycosylationPTIVSDGNTTFQEKC
CEECCCCCCEECCCC
40.728567640
271PhosphorylationHIFRDPLTGDLPWPG
EEECCCCCCCCCCCH
33.75-
335PhosphorylationMVMPGMISRILYTEK
HHCCCHHHHHHHHCC
12.36-
437PhosphorylationILVLIGISIAWVPIV
HHHHHCHHHHHHHHH
10.88-
545PhosphorylationFITIVVISLLTKPIP
HHHHHHHHHHCCCCC
13.0124719451
562PhosphorylationHLYRLCWSLRNSKEE
HHHHHHHHHHCCCCC
19.2224719451
587PhosphorylationIQEGPKETIEIETQV
CCCCCCCCEEEEECC
30.00-
606PhosphorylationKGIFRRAYDLFCGLE
CCHHHHHHHHHHCHH
16.03-
636PhosphorylationKMKMTDTSEKPLWRT
HCCCCCCCCCCHHHH
46.5729759185

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 SC5A1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC5A1_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 SC5A1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAWR_HUMANPAWRphysical
15090548

Drug and Disease Associations
Kegg Disease
H01261 Congenital glucose-galactose malabsorption (GGM)
OMIM Disease
606824Congenital glucose/galactose malabsorption (GGM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC5A1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Membrane topology of the human Na+/glucose cotransporter SGLT1.";
Turk E., Kerner C.J., Lostao M.P., Wright E.M.;
J. Biol. Chem. 271:1925-1934(1996).
Cited for: TOPOLOGY, MUTAGENESIS OF ASN-248, AND GLYCOSYLATION AT ASN-248.

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