S6A20_HUMAN - dbPTM
S6A20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S6A20_HUMAN
UniProt AC Q9NP91
Protein Name Sodium- and chloride-dependent transporter XTRP3
Gene Name SLC6A20
Organism Homo sapiens (Human).
Sequence Length 592
Subcellular Localization Apical cell membrane
Multi-pass membrane protein. Located in the apical brush border membrane of kidney proximal tubule cells..
Protein Description Mediates the calcium-dependent uptake of imino acids such as L-proline, N-methyl-L-proline and pipecolate as well as N-methylated amino acids. Involved in the transport of glycine..
Protein Sequence MEKARPLWANSLQFVFACISYAVGLGNVWRFPYLCQMYGGGSFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGVASVVVSFFLSMYYNVINAWAFWYLFHSFQDPLPWSVCPLNGNHTGYDEECEKASSTQYFWYRKTLNISPSLQENGGVQWEPALCLLLAWLVVYLCILRGTESTGKVVYFTASLPYCVLIIYLIRGLTLHGATNGLMYMFTPKIEQLANPKAWINAATQIFFSLGLGFGSLIAFASYNEPSNNCQKHAIIVSLINSFTSIFASIVTFSIYGFKATFNYENCLKKVSLLLTNTFDLEDGFLTASNLEQVKGYLASAYPSKYSEMFPQIKNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLMLGIGSMLGNTAAILTPLTDSKIISSHLPKEAISGLVCLVNCAIGMVFTMEAGNYWFDIFNDYAATLSLLLIVLVETIAVCYVYGLRRFESDLKAMTGRAVSWYWKVMWAGVSPLLIVSLFVFYLSDYILTGTLKYQAWDASQGQLVTKDYPAYALAVIGLLVASSTMCIPLAALGTFVQRRLKRGDADPVA
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
73PhosphorylationGQRMRQGSIGAWRTI
HHHHHCCCCCCHHHC
14.9829970186
131N-linked_GlycosylationSVCPLNGNHTGYDEE
CCCCCCCCCCCCCHH
28.59UniProtKB CARBOHYD
189PhosphorylationYLCILRGTESTGKVV
HHHHHHCCCCCCCEE
21.9623663014
191PhosphorylationCILRGTESTGKVVYF
HHHHCCCCCCCEEEE
42.1523663014
192PhosphorylationILRGTESTGKVVYFT
HHHCCCCCCCEEEEE
34.4923663014
197PhosphorylationESTGKVVYFTASLPY
CCCCCEEEEECCHHH
9.7423663014
199PhosphorylationTGKVVYFTASLPYCV
CCCEEEEECCHHHHH
9.5423663014
201PhosphorylationKVVYFTASLPYCVLI
CEEEEECCHHHHHHH
27.1523663014
204PhosphorylationYFTASLPYCVLIIYL
EEECCHHHHHHHHHH
10.6523663014
210PhosphorylationPYCVLIIYLIRGLTL
HHHHHHHHHHHCHHH
6.7823663014
221PhosphorylationGLTLHGATNGLMYMF
CHHHHCCCCCCHHCC
34.1227251275
229PhosphorylationNGLMYMFTPKIEQLA
CCCHHCCCHHHHHHC
13.7227251275
303PhosphorylationSIYGFKATFNYENCL
HHHCHHEEECHHHHH
17.01-
306PhosphorylationGFKATFNYENCLKKV
CHHEEECHHHHHHHH
12.34-
339PhosphorylationNLEQVKGYLASAYPS
CHHHHHHHHHHHCCH
8.06-
342PhosphorylationQVKGYLASAYPSKYS
HHHHHHHHHCCHHHH
26.24-
357N-linked_GlycosylationEMFPQIKNCSLESEL
HHCHHHCCCCCHHHH
23.41UniProtKB CARBOHYD
379PhosphorylationGLAFIVYTEAIKNME
CEEEEEEHHHHHCCC
14.1926074081
388PhosphorylationAIKNMEVSQLWSVLY
HHHCCCHHHHHHHHH
13.2726074081
392PhosphorylationMEVSQLWSVLYFFML
CCHHHHHHHHHHHHH
15.7326074081
497PhosphorylationESDLKAMTGRAVSWY
HHHHHHHHCCHHHHH
28.51-

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 S6A20_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S6A20_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 S6A20_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S6A20_HUMAN

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Related Literatures of Post-Translational Modification

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