SC6A6_HUMAN - dbPTM
SC6A6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC6A6_HUMAN
UniProt AC P31641
Protein Name Sodium- and chloride-dependent taurine transporter
Gene Name SLC6A6
Organism Homo sapiens (Human).
Sequence Length 620
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake..
Protein Sequence MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLFSGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNKSVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPNWAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNSRTVMNGALVKPTHIIVETMM
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
4Ubiquitination----MATKEKLQCLK
----CCHHHHHHHHH
43.23-
6Ubiquitination--MATKEKLQCLKDF
--CCHHHHHHHHHHH
45.47-
11UbiquitinationKEKLQCLKDFHKDIL
HHHHHHHHHHHHHHH
67.01-
11SumoylationKEKLQCLKDFHKDIL
HHHHHHHHHHHHHHH
67.01-
15UbiquitinationQCLKDFHKDILKPSP
HHHHHHHHHHHCCCC
46.5921890473
19UbiquitinationDFHKDILKPSPGKSP
HHHHHHHCCCCCCCC
43.7321890473
19SumoylationDFHKDILKPSPGKSP
HHHHHHHCCCCCCCC
43.73-
21PhosphorylationHKDILKPSPGKSPGT
HHHHHCCCCCCCCCC
44.7025159151
24UbiquitinationILKPSPGKSPGTRPE
HHCCCCCCCCCCCCH
57.7821890473
25PhosphorylationLKPSPGKSPGTRPED
HCCCCCCCCCCCCHH
34.1829255136
28PhosphorylationSPGKSPGTRPEDEAE
CCCCCCCCCCHHHCC
46.5723663014
37UbiquitinationPEDEAEGKPPQREKW
CHHHCCCCCCCHHHH
45.0621890473
163N-linked_GlycosylationELPWAHCNHSWNTPH
HCCCCCCCCCCCCCC
23.51UniProtKB CARBOHYD
179N-linked_GlycosylationMEDTMRKNKSVWITI
HHHHHHHCCCEEEEE
31.31UniProtKB CARBOHYD
190N-linked_GlycosylationWITISSTNFTSPVIE
EEEEECCCCCCCCHH
39.9019349973
275UbiquitinationPGAGAGIKFYLYPDI
CCCCCCCEEEECCCC
27.34-
322PhosphorylationYNKYKYNSYRDCMLL
CCCCCCCCHHHHCHH
20.60-
577UbiquitinationGPFLVRVKYLLTPRE
CCEEEEEEEEECCCC
21.4421890473
577UbiquitinationGPFLVRVKYLLTPRE
CCEEEEEEEEECCCC
21.4421890473
596PhosphorylationAVEREGATPYNSRTV
EEECCCCCCCCCCEE
36.8428555341
610UbiquitinationVMNGALVKPTHIIVE
EECCCCCCCEEEEEE
45.0821890473

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 SC6A6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
322SPhosphorylation

-

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 SC6A6_HUMAN !!

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

Oops, there are no PPI records of SC6A6_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
There are no disease associations of PTM sites.
Regulatory Network of SC6A6_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190, AND MASSSPECTROMETRY.

TOP