S12A7_HUMAN - dbPTM
S12A7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S12A7_HUMAN
UniProt AC Q9Y666
Protein Name Solute carrier family 12 member 7
Gene Name SLC12A7
Organism Homo sapiens (Human).
Sequence Length 1083
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification (By similarity)..
Protein Sequence MPTNFTVVPVEAHADGGGDETAERTEAPGTPEGPEPERPSPGDGNPRENSPFLNNVEVEQESFFEGKNMALFEEEMDSNPMVSSLLNKLANYTNLSQGVVEHEEDEESRRREAKAPRMGTFIGVYLPCLQNILGVILFLRLTWIVGVAGVLESFLIVAMCCTCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEIFLTYISPGAAIFQAEAAGGEAAAMLHNMRVYGTCTLVLMALVVFVGVKYVNKLALVFLACVVLSILAIYAGVIKSAFDPPDIPVCLLGNRTLSRRSFDACVKAYGIHNNSATSALWGLFCNGSQPSAACDEYFIQNNVTEIQGIPGAASGVFLENLWSTYAHAGAFVEKKGVPSVPVAEESRASALPYVLTDIAASFTLLVGIYFPSVTGIMAGSNRSGDLKDAQKSIPTGTILAIVTTSFIYLSCIVLFGACIEGVVLRDKFGEALQGNLVIGMLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIARDGIVPFLQVFGHGKANGEPTWALLLTVLICETGILIASLDSVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKFYHWTLSFLGMSLCLALMFICSWYYALSAMLIAGCIYKYIEYRGAEKEWGDGIRGLSLNAARYALLRVEHGPPHTKNWRPQVLVMLNLDAEQAVKHPRLLSFTSQLKAGKGLTIVGSVLEGTYLDKHMEAQRAEENIRSLMSTEKTKGFCQLVVSSSLRDGMSHLIQSAGLGGLKHNTVLMAWPASWKQEDNPFSWKNFVDTVRDTTAAHQALLVAKNVDSFPQNQERFGGGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQVDDNSIQMKKDLQMFLYHLRISAEVEVVEMVENDISAFTYERTLMMEQRSQMLKQMQLSKNEQEREAQLIHDRNTASHTAAAARTQAPPTPDKVQMTWTREKLIAEKYRSRDTSLSGFKDLFSMKPDQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKNRQGDENYMEFLEVLTEGLNRVLLVRGGGREVITIYS
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
3Phosphorylation-----MPTNFTVVPV
-----CCCCEEEEEE
55.6229759185
6Phosphorylation--MPTNFTVVPVEAH
--CCCCEEEEEEEEE
23.7429759185
21PhosphorylationADGGGDETAERTEAP
CCCCCCCCCCCCCCC
38.2625002506
25PhosphorylationGDETAERTEAPGTPE
CCCCCCCCCCCCCCC
28.1830278072
30PhosphorylationERTEAPGTPEGPEPE
CCCCCCCCCCCCCCC
19.6723401153
40PhosphorylationGPEPERPSPGDGNPR
CCCCCCCCCCCCCCC
47.9730266825
50PhosphorylationDGNPRENSPFLNNVE
CCCCCCCCCCCCCCE
16.5730278072
62PhosphorylationNVEVEQESFFEGKNM
CCEECEEHHHCCCCC
34.6221712546
78PhosphorylationLFEEEMDSNPMVSSL
HHHHHHCCCHHHHHH
41.3326657352
83PhosphorylationMDSNPMVSSLLNKLA
HCCCHHHHHHHHHHH
14.7127732954
84PhosphorylationDSNPMVSSLLNKLAN
CCCHHHHHHHHHHHC
26.0124719451
92PhosphorylationLLNKLANYTNLSQGV
HHHHHHCCCCCCCCC
7.4425884760
93PhosphorylationLNKLANYTNLSQGVV
HHHHHCCCCCCCCCC
29.5028152594
96PhosphorylationLANYTNLSQGVVEHE
HHCCCCCCCCCCCCC
27.2720873877
108PhosphorylationEHEEDEESRRREAKA
CCCCCHHHHHHHHHC
29.1030266825
312N-linked_GlycosylationIPVCLLGNRTLSRRS
CCEEEECCCCCCHHH
33.46UniProtKB CARBOHYD
360N-linked_GlycosylationDEYFIQNNVTEIQGI
HHHHHHCCCEEECCC
26.22UniProtKB CARBOHYD
377UbiquitinationAASGVFLENLWSTYA
CCCCHHHHHHHHHHC
38.5227667366
393UbiquitinationAGAFVEKKGVPSVPV
CCCCCCCCCCCCCCC
52.19-
431UbiquitinationVGIYFPSVTGIMAGS
HHHHCCCCCEECCCC
6.0627667366
442UbiquitinationMAGSNRSGDLKDAQK
CCCCCCCCCHHHHHH
40.8227667366
445UbiquitinationSNRSGDLKDAQKSIP
CCCCCCHHHHHHCCC
56.6127667366
468UbiquitinationTTSFIYLSCIVLFGA
CHHHHHHHHHHHHHH
5.7127667366
620UbiquitinationFYHWTLSFLGMSLCL
HHHHHHHHHHHHHHH
8.4322817900
669PhosphorylationGDGIRGLSLNAARYA
CCCHHHHHHHHHHHH
23.5423312004
674UbiquitinationGLSLNAARYALLRVE
HHHHHHHHHHHHHCC
18.1722817900
685UbiquitinationLRVEHGPPHTKNWRP
HHCCCCCCCCCCCCC
52.9922817900
688UbiquitinationEHGPPHTKNWRPQVL
CCCCCCCCCCCCEEE
52.0222817900
711UbiquitinationQAVKHPRLLSFTSQL
HHHCCHHHHHHHCCC
5.7522817900
715PhosphorylationHPRLLSFTSQLKAGK
CHHHHHHHCCCCCCC
16.52-
716PhosphorylationPRLLSFTSQLKAGKG
HHHHHHHCCCCCCCC
31.35-
735PhosphorylationGSVLEGTYLDKHMEA
EEEEECCCHHHHHHH
24.62-
757UbiquitinationRSLMSTEKTKGFCQL
HHHHHCCCCCCCCHH
56.4729967540
759UbiquitinationLMSTEKTKGFCQLVV
HHHCCCCCCCCHHHH
62.14-
780PhosphorylationGMSHLIQSAGLGGLK
HHHHHHHHCCCCCCC
19.8124719451
790PhosphorylationLGGLKHNTVLMAWPA
CCCCCCCEEEEEEEC
18.0924719451
798PhosphorylationVLMAWPASWKQEDNP
EEEEEECCCCCCCCC
30.6324719451
800UbiquitinationMAWPASWKQEDNPFS
EEEECCCCCCCCCCC
41.1232015554
809UbiquitinationEDNPFSWKNFVDTVR
CCCCCCHHHHHHHHH
39.0329967540
824UbiquitinationDTTAAHQALLVAKNV
HCHHHHHHHHHCCCC
7.9423000965
825UbiquitinationTTAAHQALLVAKNVD
CHHHHHHHHHCCCCC
2.9623000965
869UbiquitinationPFLLRQHKVWRKCRM
HHHHHHHHHHHHHCC
34.8421890473
875UbiquitinationHKVWRKCRMRIFTVA
HHHHHHHCCEEEEEE
22.0521890473
878UbiquitinationWRKCRMRIFTVAQVD
HHHHCCEEEEEEEEC
2.1923000965
879UbiquitinationRKCRMRIFTVAQVDD
HHHCCEEEEEEEECC
2.9523000965
889UbiquitinationAQVDDNSIQMKKDLQ
EEECCCCCCCHHHHH
6.1023000965
890UbiquitinationQVDDNSIQMKKDLQM
EECCCCCCCHHHHHH
37.1523000965
892UbiquitinationDDNSIQMKKDLQMFL
CCCCCCCHHHHHHHH
27.1023000965
893UbiquitinationDNSIQMKKDLQMFLY
CCCCCCHHHHHHHHH
59.3323000965
908UbiquitinationHLRISAEVEVVEMVE
HHHHCCEEEEEECCC
7.2721890473
915UbiquitinationVEVVEMVENDISAFT
EEEEECCCCCHHHHH
48.1223000965
916UbiquitinationEVVEMVENDISAFTY
EEEECCCCCHHHHHH
40.2723000965
917UbiquitinationVVEMVENDISAFTYE
EEECCCCCHHHHHHH
23.7822817900
922UbiquitinationENDISAFTYERTLMM
CCCHHHHHHHHHHHH
24.9621890473
923UbiquitinationNDISAFTYERTLMME
CCHHHHHHHHHHHHH
9.2821890473
926PhosphorylationSAFTYERTLMMEQRS
HHHHHHHHHHHHHHH
13.6823401153
929UbiquitinationTYERTLMMEQRSQML
HHHHHHHHHHHHHHH
4.4521890473
933PhosphorylationTLMMEQRSQMLKQMQ
HHHHHHHHHHHHHHH
21.4528857561
934UbiquitinationLMMEQRSQMLKQMQL
HHHHHHHHHHHHHHC
43.3421890473
937UbiquitinationEQRSQMLKQMQLSKN
HHHHHHHHHHHCCCC
38.0823000965
937 (in isoform 1)Ubiquitination-38.0821890473
940UbiquitinationSQMLKQMQLSKNEQE
HHHHHHHHCCCCHHH
39.8421890473
943UbiquitinationLKQMQLSKNEQEREA
HHHHHCCCCHHHHHH
73.4423000965
943 (in isoform 1)Ubiquitination-73.4421890473
958PhosphorylationQLIHDRNTASHTAAA
HHHCCCCHHHHHHHH
30.3620068231
960PhosphorylationIHDRNTASHTAAAAR
HCCCCHHHHHHHHHH
21.2320068231
960UbiquitinationIHDRNTASHTAAAAR
HCCCCHHHHHHHHHH
21.2321890473
962PhosphorylationDRNTASHTAAAARTQ
CCCHHHHHHHHHHCC
18.5920068231
962UbiquitinationDRNTASHTAAAARTQ
CCCHHHHHHHHHHCC
18.5921890473
966UbiquitinationASHTAAAARTQAPPT
HHHHHHHHHCCCCCC
15.4421890473
968PhosphorylationHTAAAARTQAPPTPD
HHHHHHHCCCCCCCC
25.1023403867
971UbiquitinationAAARTQAPPTPDKVQ
HHHHCCCCCCCCCEE
24.3922817900
973PhosphorylationARTQAPPTPDKVQMT
HHCCCCCCCCCEEEE
42.9623401153
973UbiquitinationARTQAPPTPDKVQMT
HHCCCCCCCCCEEEE
42.9621890473
976UbiquitinationQAPPTPDKVQMTWTR
CCCCCCCCEEEEEEH
35.2523000965
976 (in isoform 1)Ubiquitination-35.2521890473
980PhosphorylationTPDKVQMTWTREKLI
CCCCEEEEEEHHHHH
13.4419664994
982PhosphorylationDKVQMTWTREKLIAE
CCEEEEEEHHHHHHH
21.5630266825
982UbiquitinationDKVQMTWTREKLIAE
CCEEEEEEHHHHHHH
21.5622817900
983UbiquitinationKVQMTWTREKLIAEK
CEEEEEEHHHHHHHH
30.5223503661
985UbiquitinationQMTWTREKLIAEKYR
EEEEEHHHHHHHHHH
41.7322817900
987UbiquitinationTWTREKLIAEKYRSR
EEEHHHHHHHHHHCC
7.4321890473
988UbiquitinationWTREKLIAEKYRSRD
EEHHHHHHHHHHCCC
20.0523000965
990UbiquitinationREKLIAEKYRSRDTS
HHHHHHHHHHCCCCC
36.6227667366
990 (in isoform 1)Ubiquitination-36.6221890473
991PhosphorylationEKLIAEKYRSRDTSL
HHHHHHHHHCCCCCC
12.8225839225
993PhosphorylationLIAEKYRSRDTSLSG
HHHHHHHCCCCCCCC
31.2728857561
994UbiquitinationIAEKYRSRDTSLSGF
HHHHHHCCCCCCCCC
42.0823000965
996PhosphorylationEKYRSRDTSLSGFKD
HHHHCCCCCCCCCHH
30.3830266825
997PhosphorylationKYRSRDTSLSGFKDL
HHHCCCCCCCCCHHH
25.4823401153
999PhosphorylationRSRDTSLSGFKDLFS
HCCCCCCCCCHHHHC
41.7830266825
999UbiquitinationRSRDTSLSGFKDLFS
HCCCCCCCCCHHHHC
41.7821890473
1002UbiquitinationDTSLSGFKDLFSMKP
CCCCCCCHHHHCCCC
57.9823000965
1002 (in isoform 1)Ubiquitination-57.9821890473
1005UbiquitinationLSGFKDLFSMKPDQS
CCCCHHHHCCCCCCC
10.8623000965
1006PhosphorylationSGFKDLFSMKPDQSN
CCCHHHHCCCCCCCC
32.9424719451
1008UbiquitinationFKDLFSMKPDQSNVR
CHHHHCCCCCCCCCC
44.2223000965
1008 (in isoform 1)Ubiquitination-44.2221890473
1012PhosphorylationFSMKPDQSNVRRMHT
HCCCCCCCCCCHHHH
44.68-
1013UbiquitinationSMKPDQSNVRRMHTA
CCCCCCCCCCHHHHE
26.1921890473
1025UbiquitinationHTAVKLNGVVLNKSQ
HHEEEECCEEECCCC
22.7323000965
1030UbiquitinationLNGVVLNKSQDAQLV
ECCEEECCCCCCEEE
45.38-
1031UbiquitinationNGVVLNKSQDAQLVL
CCEEECCCCCCEEEE
32.0223000965
1037UbiquitinationKSQDAQLVLLNMPGP
CCCCCEEEEECCCCC
3.6723503661
1046UbiquitinationLNMPGPPKNRQGDEN
ECCCCCCCCCCCCCC
68.8223503661
1048UbiquitinationMPGPPKNRQGDENYM
CCCCCCCCCCCCCHH
48.2423503661
1051UbiquitinationPPKNRQGDENYMEFL
CCCCCCCCCCHHHHH
32.4123503661
1074UbiquitinationRVLLVRGGGREVITI
CEEEEECCCEEEEEE
22.7823503661

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
973TPhosphorylationKinaseSTK39Q9UEW8
GPS
980TPhosphorylationKinaseSTK39Q9UEW8
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S12A7_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 S12A7_HUMAN !!

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

Oops, there are no PPI records of S12A7_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
DB00761Potassium Chloride
Regulatory Network of S12A7_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-50 AND SER-62, 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-50 AND SER-62, AND MASSSPECTROMETRY.

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