S12A4_HUMAN - dbPTM
S12A4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S12A4_HUMAN
UniProt AC Q9UP95
Protein Name Solute carrier family 12 member 4
Gene Name SLC12A4
Organism Homo sapiens (Human).
Sequence Length 1085
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). Isoform 4 has no transport activity..
Protein Sequence MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSDGHGNHRESSPFLSPLEASRGIDYYDRNLALFEEELDIRPKVSSLLGKLVSYTNLTQGAKEHEEAESGEGTRRRAAEAPSMGTLMGVYLPCLQNIFGVILFLRLTWMVGTAGVLQALLIVLICCCCTLLTAISMSAIATNGVVPAGGSYFMISRSLGPEFGGAVGLCFYLGTTFAAAMYILGAIEILLTYIAPPAAIFYPSGAHDTSNATLNNMRVYGTIFLTFMTLVVFVGVKYVNKFASLFLACVIISILSIYAGGIKSIFDPPVFPVCMLGNRTLSRDQFDICAKTAVVDNETVATQLWSFFCHSPNLTTDSCDPYFMLNNVTEIPGIPGAAAGVLQENLWSAYLEKGDIVEKHGLPSADAPSLKESLPLYVVADIATSFTVLVGIFFPSVTGIMAGSNRSGDLRDAQKSIPVGTILAIITTSLVYFSSVVLFGACIEGVVLRDKYGDGVSRNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHGKVNGEPTWALLLTALIAELGILIASLDMVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKYYHWALSFLGMSLCLALMFVSSWYYALVAMLIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKYPRLLTFASQLKAGKGLTIVGSVIQGSFLESYGEAQAAEQTIKNMMEIEKVKGFCQVVVASKVREGLAHLIQSCGLGGMRHNSVVLGWPYGWRQSEDPRAWKTFIDTVRCTTAAHLALLVPKNIAFYPSNHERYLEGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQMDDNSIQMKKDLAVFLYHLRLEAEVEVVEMHNSDISAYTYERTLMMEQRSQMLRQMRLTKTEREREAQLVKDRHSALRLESLYSDEEDESAVGADKIQMTWTRDKYMTETWDPSHAPDNFRELVHIKPDQSNVRRMHTAVKLNEVIVTRSHDARLVLLNMPGPPRNSEGDENYMEFLEVLTEGLERVLLVRGGGREVITIYS
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
4 (in isoform 5)Phosphorylation-8.9724719451
5Phosphorylation---MPHFTVVPVDGP
---CCCEEEEECCCC
19.98-
6 (in isoform 5)Phosphorylation-4.4724719451
17PhosphorylationDGPRRGDYDNLEGLS
CCCCCCCCCCCCCCC
15.0028796482
24PhosphorylationYDNLEGLSWVDYGER
CCCCCCCCCCCCCCC
35.5926657352
28PhosphorylationEGLSWVDYGERAELD
CCCCCCCCCCCEECC
15.9727642862
37PhosphorylationERAELDDSDGHGNHR
CCEECCCCCCCCCCC
45.2029255136
46PhosphorylationGHGNHRESSPFLSPL
CCCCCCCCCCCCCHH
43.1830266825
47PhosphorylationHGNHRESSPFLSPLE
CCCCCCCCCCCCHHH
18.2129255136
51PhosphorylationRESSPFLSPLEASRG
CCCCCCCCHHHHHCC
28.0225159151
56PhosphorylationFLSPLEASRGIDYYD
CCCHHHHHCCCCHHH
22.9730266825
61PhosphorylationEASRGIDYYDRNLAL
HHHCCCCHHHHCHHH
12.8225884760
62PhosphorylationASRGIDYYDRNLALF
HHCCCCHHHHCHHHH
12.5128796482
78UbiquitinationEELDIRPKVSSLLGK
HHHCCHHHHHHHHHH
44.9221906983
78 (in isoform 1)Ubiquitination-44.9221890473
78 (in isoform 2)Ubiquitination-44.9221890473
78 (in isoform 3)Ubiquitination-44.9221890473
78 (in isoform 4)Ubiquitination-44.9221890473
79UbiquitinationELDIRPKVSSLLGKL
HHCCHHHHHHHHHHH
5.3521890473
79UbiquitinationELDIRPKVSSLLGKL
HHCCHHHHHHHHHHH
5.3521890473
79UbiquitinationELDIRPKVSSLLGKL
HHCCHHHHHHHHHHH
5.3521890473
80PhosphorylationLDIRPKVSSLLGKLV
HCCHHHHHHHHHHHH
22.7629514088
81PhosphorylationDIRPKVSSLLGKLVS
CCHHHHHHHHHHHHH
30.5129514088
85AcetylationKVSSLLGKLVSYTNL
HHHHHHHHHHHHCCC
45.7626051181
85UbiquitinationKVSSLLGKLVSYTNL
HHHHHHHHHHHHCCC
45.7621890473
85 (in isoform 1)Ubiquitination-45.7621890473
85 (in isoform 2)Ubiquitination-45.7621890473
85 (in isoform 3)Ubiquitination-45.7621890473
85 (in isoform 4)Ubiquitination-45.7621890473
87UbiquitinationSSLLGKLVSYTNLTQ
HHHHHHHHHHCCCCC
4.7221890473
88PhosphorylationSLLGKLVSYTNLTQG
HHHHHHHHHCCCCCC
36.3521945579
89PhosphorylationLLGKLVSYTNLTQGA
HHHHHHHHCCCCCCH
7.6821945579
90PhosphorylationLGKLVSYTNLTQGAK
HHHHHHHCCCCCCHH
19.0821945579
93PhosphorylationLVSYTNLTQGAKEHE
HHHHCCCCCCHHHHH
27.3321945579
97UbiquitinationTNLTQGAKEHEEAES
CCCCCCHHHHHHHHC
67.4421906983
97 (in isoform 1)Ubiquitination-67.4421890473
97 (in isoform 2)Ubiquitination-67.4421890473
97 (in isoform 3)Ubiquitination-67.4421890473
97 (in isoform 4)Ubiquitination-67.4421890473
104PhosphorylationKEHEEAESGEGTRRR
HHHHHHHCCCCHHHH
49.5526699800
108PhosphorylationEAESGEGTRRRAAEA
HHHCCCCHHHHHHCC
19.3926699800
245N-linked_GlycosylationSGAHDTSNATLNNMR
CCCCCCCCCHHHCCC
38.75UniProtKB CARBOHYD
260PhosphorylationVYGTIFLTFMTLVVF
HHHHHHHHHHHHHHH
10.70-
263PhosphorylationTIFLTFMTLVVFVGV
HHHHHHHHHHHHHCH
16.53-
312N-linked_GlycosylationFPVCMLGNRTLSRDQ
CCEEECCCCCCCHHH
29.78UniProtKB CARBOHYD
331N-linked_GlycosylationAKTAVVDNETVATQL
CEEEEECCHHHHHHH
34.92UniProtKB CARBOHYD
347N-linked_GlycosylationSFFCHSPNLTTDSCD
HHHCCCCCCCCCCCC
53.70UniProtKB CARBOHYD
407PhosphorylationDAPSLKESLPLYVVA
CCCCHHHCCCHHHHH
33.43-
411PhosphorylationLKESLPLYVVADIAT
HHHCCCHHHHHHHHH
7.31-
418PhosphorylationYVVADIATSFTVLVG
HHHHHHHHHHHHHHH
25.38-
439N-linked_GlycosylationTGIMAGSNRSGDLRD
CEECCCCCCCCCHHH
41.02UniProtKB CARBOHYD
441PhosphorylationIMAGSNRSGDLRDAQ
ECCCCCCCCCHHHHH
40.69-
498PhosphorylationSRNLVVGTLAWPSPW
CCCEEEECCCCCCCE
11.16-
529UbiquitinationSLTGAPRLLQAIAKD
HHHCHHHHHHHHHHC
3.9621890473
529UbiquitinationSLTGAPRLLQAIAKD
HHHCHHHHHHHHHHC
3.9621890473
529UbiquitinationSLTGAPRLLQAIAKD
HHHCHHHHHHHHHHC
3.9621890473
535AcetylationRLLQAIAKDNIIPFL
HHHHHHHHCCCCCEE
45.2342369537
535UbiquitinationRLLQAIAKDNIIPFL
HHHHHHHHCCCCCEE
45.23-
535 (in isoform 1)Ubiquitination-45.2321890473
535 (in isoform 2)Ubiquitination-45.2321890473
535 (in isoform 3)Ubiquitination-45.2321890473
535 (in isoform 4)Ubiquitination-45.2321890473
537UbiquitinationLQAIAKDNIIPFLRV
HHHHHHCCCCCEEEH
33.1221890473
659UbiquitinationIEYQGAEKEWGDGIR
HHHCCCCCCCCCCHH
59.23-
659 (in isoform 1)Ubiquitination-59.2321890473
659 (in isoform 2)Ubiquitination-59.2321890473
659 (in isoform 3)Ubiquitination-59.2321890473
659 (in isoform 4)Ubiquitination-59.2321890473
669PhosphorylationGDGIRGLSLSAARYA
CCCHHHHHHHHHHHH
24.0930108239
671PhosphorylationGIRGLSLSAARYALL
CHHHHHHHHHHHHHH
19.2630108239
701UbiquitinationLLVLLKLDEDLHVKY
EEEEEECCCCCCCCC
45.8621890473
701UbiquitinationLLVLLKLDEDLHVKY
EEEEEECCCCCCCCC
45.8621890473
701UbiquitinationLLVLLKLDEDLHVKY
EEEEEECCCCCCCCC
45.8621890473
707UbiquitinationLDEDLHVKYPRLLTF
CCCCCCCCCHHHHHH
38.5021890473
707 (in isoform 1)Ubiquitination-38.5021890473
707 (in isoform 2)Ubiquitination-38.5021890473
707 (in isoform 3)Ubiquitination-38.5021890473
707 (in isoform 4)Ubiquitination-38.5021890473
708PhosphorylationDEDLHVKYPRLLTFA
CCCCCCCCHHHHHHH
7.7822817900
709UbiquitinationEDLHVKYPRLLTFAS
CCCCCCCHHHHHHHH
18.0921890473
716PhosphorylationPRLLTFASQLKAGKG
HHHHHHHHHHHCCCC
31.67-
719UbiquitinationLTFASQLKAGKGLTI
HHHHHHHHCCCCCEE
47.67-
725PhosphorylationLKAGKGLTIVGSVIQ
HHCCCCCEEEEEEEE
23.45-
757MethylationKNMMEIEKVKGFCQV
HHHHHHHHHCCCCCH
55.71-
769MalonylationCQVVVASKVREGLAH
CCHHHHHHHHHHHHH
35.2626320211
836PhosphorylationKNIAFYPSNHERYLE
CCEEECCCCCHHHHC
39.1725159151
926PhosphorylationSAYTYERTLMMEQRS
HHHHHHHHHHHHHHH
13.6823401153
943AcetylationLRQMRLTKTEREREA
HHHHHCCHHHHHHHH
53.647668913
954UbiquitinationEREAQLVKDRHSALR
HHHHHHHHHHHHHHH
58.60-
958PhosphorylationQLVKDRHSALRLESL
HHHHHHHHHHHHHHH
29.8730576142
964PhosphorylationHSALRLESLYSDEED
HHHHHHHHHCCCCCC
36.8822167270
966PhosphorylationALRLESLYSDEEDES
HHHHHHHCCCCCCCC
24.2929255136
967PhosphorylationLRLESLYSDEEDESA
HHHHHHCCCCCCCCC
43.7919664994
969PhosphorylationLESLYSDEEDESAVG
HHHHCCCCCCCCCCC
62.5027251275
973PhosphorylationYSDEEDESAVGADKI
CCCCCCCCCCCCCEE
40.3422167270
982 (in isoform 4)Ubiquitination-3.7321890473
983PhosphorylationGADKIQMTWTRDKYM
CCCEEEEEEECCHHC
13.8130266825
985PhosphorylationDKIQMTWTRDKYMTE
CEEEEEEECCHHCCC
21.5930266825
988UbiquitinationQMTWTRDKYMTETWD
EEEEECCHHCCCCCC
33.3621906983
988 (in isoform 1)Ubiquitination-33.3621890473
988 (in isoform 2)Ubiquitination-33.3621890473
988 (in isoform 3)Ubiquitination-33.3621890473
989PhosphorylationMTWTRDKYMTETWDP
EEEECCHHCCCCCCC
17.3520049867
991PhosphorylationWTRDKYMTETWDPSH
EECCHHCCCCCCCCC
27.46-
993PhosphorylationRDKYMTETWDPSHAP
CCHHCCCCCCCCCCC
26.46-
1004 (in isoform 4)Ubiquitination-42.4621890473
1010UbiquitinationFRELVHIKPDQSNVR
CHHHEECCCCCCCCH
27.882190698
1010 (in isoform 1)Ubiquitination-27.8821890473
1010 (in isoform 2)Ubiquitination-27.8821890473
1014PhosphorylationVHIKPDQSNVRRMHT
EECCCCCCCCHHHHH
44.6820049867
1021PhosphorylationSNVRRMHTAVKLNEV
CCCHHHHHEEECCEE
24.65-
1056PhosphorylationNSEGDENYMEFLEVL
CCCCCCCHHHHHHHH
8.9310942735
1064PhosphorylationMEFLEVLTEGLERVL
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
5TPhosphorylationKinaseSTK39Q9UEW8
GPS
983TPhosphorylationKinaseSTK39Q9UEW8
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S12A4_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 S12A4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMM43_HUMANTMEM43physical
22939629

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
DB00887Bumetanide
DB00761Potassium Chloride
Regulatory Network of S12A4_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-967, 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-51 AND SER-967, AND MASSSPECTROMETRY.

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