S12A6_HUMAN - dbPTM
S12A6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S12A6_HUMAN
UniProt AC Q9UHW9
Protein Name Solute carrier family 12 member 6
Gene Name SLC12A6
Organism Homo sapiens (Human).
Sequence Length 1150
Subcellular Localization Basolateral cell membrane
Multi-pass membrane protein.
Protein Description Mediates electroneutral potassium-chloride cotransport. May be activated by cell swelling. May contribute to cell volume homeostasis in single cells..
Protein Sequence MHPPETTTKMASVRFMVTPTKIDDIPGLSDTSPDLSSRSSSRVRFSSRESVPETSRSEPMSEMSGATTSLATVALDPPSDRTSHPQDVIEDLSQNSITGEHSQLLDDGHKKARNAYLNNSNYEEGDEYFDKNLALFEEEMDTRPKVSSLLNRMANYTNLTQGAKEHEEAENITEGKKKPTKTPQMGTFMGVYLPCLQNIFGVILFLRLTWVVGTAGVLQAFAIVLICCCCTMLTAISMSAIATNGVVPAGGSYFMISRALGPEFGGAVGLCFYLGTTFAAAMYILGAIEIFLVYIVPRAAIFHSDDALKESAAMLNNMRVYGTAFLVLMVLVVFIGVRYVNKFASLFLACVIVSILAIYAGAIKSSFAPPHFPVCMLGNRTLSSRHIDVCSKTKEINNMTVPSKLWGFFCNSSQFFNATCDEYFVHNNVTSIQGIPGLASGIITENLWSNYLPKGEIIEKPSAKSSDVLGSLNHEYVLVDITTSFTLLVGIFFPSVTGIMAGSNRSGDLKDAQKSIPIGTILAILTTSFVYLSNVVLFGACIEGVVLRDKFGDAVKGNLVVGTLSWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHSKANGEPTWALLLTAAIAELGILIASLDLVAPILSMFFLMCYLFVNLACALQTLLRTPNWRPRFRYYHWALSFMGMSICLALMFISSWYYAIVAMVIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARFALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKHPRLLTFASQLKAGKGLTIVGSVIVGNFLENYGEALAAEQTIKHLMEAEKVKGFCQLVVAAKLREGISHLIQSCGLGGMKHNTVVMGWPNGWRQSEDARAWKTFIGTVRVTTAAHLALLVAKNISFFPSNVEQFSEGNIDVWWIVHDGGMLMLLPFLLKQHKVWRKCSIRIFTVAQLEDNSIQMKKDLATFLYHLRIEAEVEVVEMHDSDISAYTYERTLMMEQRSQMLRHMRLSKTERDREAQLVKDRNSMLRLTSIGSDEDEETETYQEKVHMTWTKDKYMASRGQKAKSMEGFQDLLNMRPDQSNVRRMHTAVKLNEVIVNKSHEAKLVLLNMPGPPRNPEGDENYMEFLEVLTEGLERVLLVRGGGSEVITIYS
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
5 (in isoform 2)Phosphorylation-64.34-
5 (in isoform 6)Phosphorylation-64.34-
12PhosphorylationETTTKMASVRFMVTP
CCCCCCEEEEEEECC
15.4426074081
18PhosphorylationASVRFMVTPTKIDDI
EEEEEEECCCCHHCC
17.2922199227
19 (in isoform 2)Phosphorylation-21.9326657352
19 (in isoform 6)Phosphorylation-21.9326657352
20PhosphorylationVRFMVTPTKIDDIPG
EEEEECCCCHHCCCC
31.1326074081
21 (in isoform 2)Phosphorylation-45.3926657352
21 (in isoform 6)Phosphorylation-45.3926657352
25 (in isoform 2)Phosphorylation-2.3026657352
25 (in isoform 6)Phosphorylation-2.3026657352
29PhosphorylationIDDIPGLSDTSPDLS
HHCCCCCCCCCCCCC
44.7730266825
30 (in isoform 2)Ubiquitination-57.1321890473
31PhosphorylationDIPGLSDTSPDLSSR
CCCCCCCCCCCCCCC
38.4930266825
32PhosphorylationIPGLSDTSPDLSSRS
CCCCCCCCCCCCCCC
22.7723401153
36PhosphorylationSDTSPDLSSRSSSRV
CCCCCCCCCCCCCCC
30.9629255136
36 (in isoform 2)Phosphorylation-30.9628450419
37PhosphorylationDTSPDLSSRSSSRVR
CCCCCCCCCCCCCCC
43.4029255136
39PhosphorylationSPDLSSRSSSRVRFS
CCCCCCCCCCCCCCC
34.3129116813
40PhosphorylationPDLSSRSSSRVRFSS
CCCCCCCCCCCCCCC
22.5129116813
41PhosphorylationDLSSRSSSRVRFSSR
CCCCCCCCCCCCCCC
35.7229116813
42 (in isoform 2)Phosphorylation-26.1130108239
45 (in isoform 2)Phosphorylation-7.7125159151
46PhosphorylationSSSRVRFSSRESVPE
CCCCCCCCCCCCCCC
20.2328450419
47PhosphorylationSSRVRFSSRESVPET
CCCCCCCCCCCCCCC
37.0420363803
47 (in isoform 2)Phosphorylation-37.0430108239
50PhosphorylationVRFSSRESVPETSRS
CCCCCCCCCCCCCCC
41.6920363803
51 (in isoform 2)Phosphorylation-4.2128450419
54PhosphorylationSRESVPETSRSEPMS
CCCCCCCCCCCCCHH
24.3027486199
61PhosphorylationTSRSEPMSEMSGATT
CCCCCCHHHCCCCCC
40.6418669648
64PhosphorylationSEPMSEMSGATTSLA
CCCHHHCCCCCCCEE
22.6423532336
67PhosphorylationMSEMSGATTSLATVA
HHHCCCCCCCEEEEE
22.0524043423
68PhosphorylationSEMSGATTSLATVAL
HHCCCCCCCEEEEEC
22.6224043423
69PhosphorylationEMSGATTSLATVALD
HCCCCCCCEEEEECC
16.2018669648
72PhosphorylationGATTSLATVALDPPS
CCCCCEEEEECCCCC
16.1725954137
79PhosphorylationTVALDPPSDRTSHPQ
EEECCCCCCCCCCCH
45.1523322592
80 (in isoform 2)Ubiquitination-64.75-
93PhosphorylationQDVIEDLSQNSITGE
HHHHHHHHHCCCCCC
39.3725921289
96PhosphorylationIEDLSQNSITGEHSQ
HHHHHHCCCCCCHHH
17.5623401153
98PhosphorylationDLSQNSITGEHSQLL
HHHHCCCCCCHHHHC
36.0230108239
102PhosphorylationNSITGEHSQLLDDGH
CCCCCCHHHHCCHHC
20.4430108239
116PhosphorylationHKKARNAYLNNSNYE
CHHHHHHHHCCCCCC
17.3221945579
120PhosphorylationRNAYLNNSNYEEGDE
HHHHHCCCCCCCCHH
39.4521945579
122PhosphorylationAYLNNSNYEEGDEYF
HHHCCCCCCCCHHHH
18.3821945579
125 (in isoform 2)Ubiquitination-22.5521890473
128PhosphorylationNYEEGDEYFDKNLAL
CCCCCHHHHHHHHHH
23.0922199227
131UbiquitinationEGDEYFDKNLALFEE
CCHHHHHHHHHHHHH
43.92-
145UbiquitinationEEMDTRPKVSSLLNR
HHHCCCHHHHHHHHH
52.00-
147PhosphorylationMDTRPKVSSLLNRMA
HCCCHHHHHHHHHHH
22.7629978859
148PhosphorylationDTRPKVSSLLNRMAN
CCCHHHHHHHHHHHH
39.6023401153
156PhosphorylationLLNRMANYTNLTQGA
HHHHHHHHCCCCHHH
6.3521945579
157PhosphorylationLNRMANYTNLTQGAK
HHHHHHHCCCCHHHH
24.4521945579
160PhosphorylationMANYTNLTQGAKEHE
HHHHCCCCHHHHHHH
27.3328851738
164UbiquitinationTNLTQGAKEHEEAEN
CCCCHHHHHHHHHHC
67.44-
176UbiquitinationAENITEGKKKPTKTP
HHCCCCCCCCCCCCC
51.932190698
176 (in isoform 1)Ubiquitination-51.9321890473
182PhosphorylationGKKKPTKTPQMGTFM
CCCCCCCCCCHHHHH
22.6424043423
187PhosphorylationTKTPQMGTFMGVYLP
CCCCCHHHHHHHHHH
12.7124043423
192PhosphorylationMGTFMGVYLPCLQNI
HHHHHHHHHHHHHHH
10.1324043423
321PhosphorylationMLNNMRVYGTAFLVL
HHHCCHHHHHHHHHH
9.82-
323PhosphorylationNNMRVYGTAFLVLMV
HCCHHHHHHHHHHHH
9.13-
379N-linked_GlycosylationFPVCMLGNRTLSSRH
CCEEEECCCCCCCCC
29.78UniProtKB CARBOHYD
398N-linked_GlycosylationSKTKEINNMTVPSKL
CCCCCCCCCCCCHHH
32.91UniProtKB CARBOHYD
411N-linked_GlycosylationKLWGFFCNSSQFFNA
HHHHHHCCHHHHHCC
39.27UniProtKB CARBOHYD
428N-linked_GlycosylationDEYFVHNNVTSIQGI
CCEEEECCCCCCCCC
24.46UniProtKB CARBOHYD
460AcetylationPKGEIIEKPSAKSSD
CCCCCCCCCCCCCCC
33.5911922915
460UbiquitinationPKGEIIEKPSAKSSD
CCCCCCCCCCCCCCC
33.59-
464AcetylationIIEKPSAKSSDVLGS
CCCCCCCCCCCCCCC
55.6311922927
465PhosphorylationIEKPSAKSSDVLGSL
CCCCCCCCCCCCCCC
31.3322468782
541UbiquitinationNVVLFGACIEGVVLR
CCHHHHHHEECCCCH
2.7321890473
549UbiquitinationIEGVVLRDKFGDAVK
EECCCCHHCCCCHHC
46.6121890473
549 (in isoform 2)Ubiquitination-46.6121890473
585UbiquitinationFSTCGAGLQSLTGAP
HHCCCHHHHHHHCHH
2.8721890473
591UbiquitinationGLQSLTGAPRLLQAI
HHHHHHCHHHHHHHH
4.8421890473
600AcetylationRLLQAIAKDNIIPFL
HHHHHHHHCCCHHHH
45.2323954790
600UbiquitinationRLLQAIAKDNIIPFL
HHHHHHHHCCCHHHH
45.23-
600 (in isoform 1)Ubiquitination-45.2321890473
673 (in isoform 2)Ubiquitination-21.1121890473
724UbiquitinationIEYQGAEKEWGDGIR
HHHCCCCCCCCCCHH
59.23-
724 (in isoform 1)Ubiquitination-59.2321890473
734PhosphorylationGDGIRGLSLSAARFA
CCCHHHHHHHHHHHH
24.0930108239
736PhosphorylationGIRGLSLSAARFALL
CHHHHHHHHHHHHHH
19.2630108239
772UbiquitinationLDEDLHVKHPRLLTF
CCCCCCCCCHHHHHH
36.82-
778PhosphorylationVKHPRLLTFASQLKA
CCCHHHHHHHHHHHC
23.03-
781PhosphorylationPRLLTFASQLKAGKG
HHHHHHHHHHHCCCC
31.67-
784UbiquitinationLTFASQLKAGKGLTI
HHHHHHHHCCCCCEE
47.67-
940PhosphorylationHKVWRKCSIRIFTVA
CHHHHHCCEEEEEEE
20.2425278378
945PhosphorylationKCSIRIFTVAQLEDN
HCCEEEEEEEEECCC
16.7425278378
965PhosphorylationKDLATFLYHLRIEAE
HHHHHHHHHHHHCEE
8.4624114839
981PhosphorylationEVVEMHDSDISAYTY
EEEECCCCCCHHHHH
23.3618669648
991PhosphorylationSAYTYERTLMMEQRS
HHHHHHHHHHHHHHH
13.6823401153
1007PhosphorylationMLRHMRLSKTERDRE
HHHHHHCCCCHHHHH
27.45-
1019UbiquitinationDREAQLVKDRNSMLR
HHHHHHHHCCHHCCC
60.61-
1023PhosphorylationQLVKDRNSMLRLTSI
HHHHCCHHCCCEEEC
21.7923401153
1028PhosphorylationRNSMLRLTSIGSDED
CHHCCCEEECCCCCC
16.3222167270
1029PhosphorylationNSMLRLTSIGSDEDE
HHCCCEEECCCCCCC
29.5522167270
1032PhosphorylationLRLTSIGSDEDEETE
CCEEECCCCCCCCCC
35.8410187864
1038PhosphorylationGSDEDEETETYQEKV
CCCCCCCCCHHHHHH
31.4222167270
1040PhosphorylationDEDEETETYQEKVHM
CCCCCCCHHHHHHHC
37.6123403867
1048PhosphorylationYQEKVHMTWTKDKYM
HHHHHHCHHCHHHHH
18.3323401153
1050PhosphorylationEKVHMTWTKDKYMAS
HHHHCHHCHHHHHHH
21.8723403867
1063UbiquitinationASRGQKAKSMEGFQD
HHCCHHCHHCHHHHH
58.32-
1064PhosphorylationSRGQKAKSMEGFQDL
HCCHHCHHCHHHHHH
27.2523898821
1086PhosphorylationSNVRRMHTAVKLNEV
HHHHHHHHHHHHCEE
24.65-
1097UbiquitinationLNEVIVNKSHEAKLV
HCEEEECCCCCEEEE
42.15-
1121PhosphorylationNPEGDENYMEFLEVL
CCCCCCCHHHHHHHH
8.9322817900
1129PhosphorylationMEFLEVLTEGLERVL
HHHHHHHHHCCCEEE
32.93-

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
96SPhosphorylationKinaseSTK39Q9UEW8
GPS
96SPhosphorylationKinaseWNK3Q9BYP7
PSP
160TPhosphorylationKinaseSTK39Q9UEW8
GPS
991TPhosphorylationKinaseWNK1Q9H4A3
PSP
991TPhosphorylationKinaseWNK3Q9BYP7
PSP
1048TPhosphorylationKinaseSTK39Q9UEW8
GPS
1048TPhosphorylationKinaseWNK1Q9H4A3
PSP
1048TPhosphorylationKinaseWNK3Q9BYP7
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S12A6_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 S12A6_HUMAN !!

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

Oops, there are no PPI records of S12A6_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00816 Agenesis of the corpus callosum with peripheral neuropathy (ACCPN)
OMIM Disease
218000Agenesis of the corpus callosum, with peripheral neuropathy (ACCPN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00761Potassium Chloride
Regulatory Network of S12A6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1032, ANDMASS SPECTROMETRY.

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