S12A3_HUMAN - dbPTM
S12A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S12A3_HUMAN
UniProt AC P55017
Protein Name Solute carrier family 12 member 3
Gene Name SLC12A3
Organism Homo sapiens (Human).
Sequence Length 1021
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Electroneutral sodium and chloride ion cotransporter. In kidney distal convoluted tubules, key mediator of sodium and chloride reabsorption. [PubMed: 21613606]
Protein Sequence MAELPTTETPGDATLCSGRFTISTLLSSDEPSPPAAYDSSHPSHLTHSSTFCMRTFGYNTIDVVPTYEHYANSTQPGEPRKVRPTLADLHSFLKQEGRHLHALAFDSRPSHEMTDGLVEGEAGTSSEKNPEEPVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWIIILLSVTVTSITGLSISAISTNGKVKSGGTYFLISRSLGPELGGSIGLIFAFANAVGVAMHTVGFAETVRDLLQEYGAPIVDPINDIRIIAVVSVTVLLAISLAGMEWESKAQVLFFLVIMVSFANYLVGTLIPPSEDKASKGFFSYRADIFVQNLVPDWRGPDGTFFGMFSIFFPSATGILAGANISGDLKDPAIAIPKGTLMAIFWTTISYLAISATIGSCVVRDASGVLNDTVTPGWGACEGLACSYGWNFTECTQQHSCHYGLINYYQTMSMVSGFAPLITAGIFGATLSSALACLVSAAKVFQCLCEDQLYPLIGFFGKGYGKNKEPVRGYLLAYAIAVAFIIIAELNTIAPIISNFFLCSYALINFSCFHASITNSPGWRPSFQYYNKWAALFGAIISVVIMFLLTWWAALIAIGVVLFLLLYVIYKKPEVNWGSSVQAGSYNLALSYSVGLNEVEDHIKNYRPQCLVLTGPPNFRPALVDFVGTFTRNLSLMICGHVLIGPHKQRMPELQLIANGHTKWLNKRKIKAFYSDVIAEDLRRGVQILMQAAGLGRMKPNILVVGFKKNWQSAHPATVEDYIGILHDAFDFNYGVCVMRMREGLNVSKMMQAHINPVFDPAEDGKEASARVDPKALVKEEQATTIFQSEQGKKTIDIYWLFDDGGLTLLIPYLLGRKRRWSKCKIRVFVGGQINRMDQERKAIISLLSKFRLGFHEVHILPDINQNPRAEHTKRFEDMIAPFRLNDGFKDEATVNEMRRDCPWKISDEEITKNRVKSLRQVRLNEIVLDYSRDAALIVITLPIGRKGKCPSSLYMAWLETLSQDLRPPVILIRGNQENVLTFYCQ
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
6Phosphorylation--MAELPTTETPGDA
--CCCCCCCCCCCCC		50.3022210691
7Phosphorylation-MAELPTTETPGDAT
-CCCCCCCCCCCCCE		35.6022210691
9PhosphorylationAELPTTETPGDATLC
CCCCCCCCCCCCEEE		30.4029759185
14PhosphorylationTETPGDATLCSGRFT
CCCCCCCEEECCEEE		32.7922210691
17PhosphorylationPGDATLCSGRFTIST
CCCCEEECCEEEEEE		35.7929759185
43PhosphorylationAYDSSHPSHLTHSST
CCCCCCHHHCCCCCC		26.21-
46PhosphorylationSSHPSHLTHSSTFCM
CCCHHHCCCCCCCCC		17.8122817900
49PhosphorylationPSHLTHSSTFCMRTF
HHHCCCCCCCCCHHH		20.21-
50PhosphorylationSHLTHSSTFCMRTFG
HHCCCCCCCCCHHHC		24.70-
55PhosphorylationSSTFCMRTFGYNTID
CCCCCCHHHCCCEEE		8.4321945579
58PhosphorylationFCMRTFGYNTIDVVP
CCCHHHCCCEEEEEC		12.6321945579
60PhosphorylationMRTFGYNTIDVVPTY
CHHHCCCEEEEECCC		15.2921945579
66PhosphorylationNTIDVVPTYEHYANS
CEEEEECCCHHHCCC		29.9021945579
67PhosphorylationTIDVVPTYEHYANST
EEEEECCCHHHCCCC		8.4721945579
70PhosphorylationVVPTYEHYANSTQPG
EECCCHHHCCCCCCC		8.7821945579
73PhosphorylationTYEHYANSTQPGEPR
CCHHHCCCCCCCCCC		21.9021945579
74PhosphorylationYEHYANSTQPGEPRK
CHHHCCCCCCCCCCC		38.2921945579
81UbiquitinationTQPGEPRKVRPTLAD
CCCCCCCCCCCCHHH		54.00-
85PhosphorylationEPRKVRPTLADLHSF
CCCCCCCCHHHHHHH		24.82-
91PhosphorylationPTLADLHSFLKQEGR
CCHHHHHHHHHHCCC		39.3029759185
94UbiquitinationADLHSFLKQEGRHLH
HHHHHHHHHCCCCCE		44.27-
124PhosphorylationLVEGEAGTSSEKNPE
CCCCCCCCCCCCCCC		35.81-
126PhosphorylationEGEAGTSSEKNPEEP
CCCCCCCCCCCCCCC		53.05-
128UbiquitinationEAGTSSEKNPEEPVR
CCCCCCCCCCCCCCC		78.67-
140AcetylationPVRFGWVKGVMIRCM
CCCHHHHHHHHHHHH		39.0020167786
178PhosphorylationTWIIILLSVTVTSIT
HHHHHHHHCHHHHCC		16.5822210691
406N-linked_GlycosylationRDASGVLNDTVTPGW
ECCCCCCCCCCCCCC		40.27UniProtKB CARBOHYD
426N-linked_GlycosylationLACSYGWNFTECTQQ
CCCCCCCCCHHHHHH		29.60UniProtKB CARBOHYD
605PhosphorylationFLLLYVIYKKPEVNW
HHHHHHHHHCCCCCC		11.69-
697PhosphorylationQLIANGHTKWLNKRK
HHHHCCCCHHHCHHH		25.88-
734AcetylationAAGLGRMKPNILVVG
HHCCCCCCCCEEEEE		33.2930592407
743AcetylationNILVVGFKKNWQSAH
CEEEEEECCCHHHCC		38.9930592413
753PhosphorylationWQSAHPATVEDYIGI
HHHCCCCCHHHHHHH		28.9522210691
757PhosphorylationHPATVEDYIGILHDA
CCCCHHHHHHHHHHH		6.3722210691
769PhosphorylationHDAFDFNYGVCVMRM
HHHHCCCCCEEEECC		15.7822210691
783PhosphorylationMREGLNVSKMMQAHI
CCCCCCHHHHHHHHC		17.48-
784UbiquitinationREGLNVSKMMQAHIN
CCCCCHHHHHHHHCC		33.82-
801UbiquitinationFDPAEDGKEASARVD
CCCCCCCCCCCCCCC		63.53-
804PhosphorylationAEDGKEASARVDPKA
CCCCCCCCCCCCHHH		20.0728787133
810UbiquitinationASARVDPKALVKEEQ
CCCCCCHHHHHCHHH		50.30-
810 (in isoform 3)Phosphorylation-50.3029116813
811 (in isoform 2)Phosphorylation-23.9929116813
814UbiquitinationVDPKALVKEEQATTI
CCHHHHHCHHHHHHH		57.28-
820PhosphorylationVKEEQATTIFQSEQG
HCHHHHHHHEECCCC		23.8629759185
828UbiquitinationIFQSEQGKKTIDIYW
HEECCCCCCEEEEEE		46.57-
881PhosphorylationQERKAIISLLSKFRL
HHHHHHHHHHHHHCC		19.6924719451
885AcetylationAIISLLSKFRLGFHE
HHHHHHHHHCCCCCE		34.1830592419
925UbiquitinationFRLNDGFKDEATVNE
CCCCCCCCCCHHHHH		61.25-
940UbiquitinationMRRDCPWKISDEEIT
HHHHCCCCCCHHHHH		19.92-
948UbiquitinationISDEEITKNRVKSLR
CCHHHHHHHHHHHHH		48.71-
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
46TPhosphorylationKinaseOXSR1O95747
GPS
46TPhosphorylationKinaseSTK39Q9UEW8
GPS
46TPhosphorylationKinaseWNK4Q96J92
PSP
50TPhosphorylationKinaseWNK4Q96J92
PSP
55TPhosphorylationKinaseOXSR1O95747
GPS
55TPhosphorylationKinaseSTK39Q9UEW8
GPS
55TPhosphorylationKinaseWNK4Q96J92
PSP
60TPhosphorylationKinaseOXSR1O95747
GPS
60TPhosphorylationKinaseSTK39Q9UEW8
GPS
73SPhosphorylationKinaseOXSR1O95747
GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:23482560
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S12A3_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 S12A3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDIA3_HUMANPDIA3physical
11832422
NEDD4_HUMANNEDD4physical
21852580
KLHL3_HUMANKLHL3physical
22406640
HS90A_HUMANHSP90AA1physical
23482560
DNJB1_HUMANDNAJB1physical
23482560
HSP7C_HUMANHSPA8physical
23482560
ACTB_HUMANACTBphysical
23482560
STIP1_HUMANSTIP1physical
23482560
CHIP_HUMANSTUB1physical
23482560
Drug and Disease Associations
Kegg Disease
H00240 Gitelman syndrome
OMIM Disease
263800Gitelman syndrome (GS)
Kegg Drug
D00272 Chlortalidone (JAN/INN); Chlorthalidone (USP); Hygroton (TN); Thalitone (TN)
D00340 Hydrochlorothiazide (JP16/USP/INN); Esidrix (TN); Microzide (TN)
D00345 Indapamide (JP16/USP); Lozol (TN); Natrix (TN)
D00431 Metolazone (JAN/USP/INN); Zaroxolyn (TN)
D00461 Quinethazone (JAN/INN); Hydromox (TN)
D00519 Chlorothiazide (JAN/USP/INN); Diuril (TN)
D00650 Bendroflumethiazide (JAN/USP/INN); Naturetin (TN)
D00651 Benzthiazide (JAN/INN); Exna (TN)
D00654 Hydroflumethiazide (JAN/USP/INN); Saluron (TN)
D00656 Methyclothiazide (JAN/USP/INN); Enduron (TN)
D00657 Polythiazide (JAN/USAN/INN); Renese (TN)
D00658 Trichlormethiazide (JP16/USP/INN); Naqua (TN)
D01241 Penflutizide (JAN/INN)
D01246 Benzylhydrochlorothiazide (JAN); Behyd (TN)
D01605 Meticrane (JP16/INN); Arresten (TN)
D01877 Mefruside (JP16/USAN/INN); Baycaron (TN)
D03471 Chlorothiazide sodium (USP); Diuril (TN)
D06401 Indapamide hydrate; Tenaxil (TN)
DrugBank
DB00436Bendroflumethiazide
DB00562Benzthiazide
DB00880Chlorothiazide
DB01119Diazoxide
DB00999Hydrochlorothiazide
DB00524Metolazone
DB01324Polythiazide
DB01325Quinethazone
Regulatory Network of S12A3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory