NHRF3_MOUSE - dbPTM
NHRF3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHRF3_MOUSE
UniProt AC Q9JIL4
Protein Name Na(+)/H(+) exchange regulatory cofactor NHE-RF3
Gene Name Pdzk1
Organism Mus musculus (Mouse).
Sequence Length 519
Subcellular Localization Membrane
Peripheral membrane protein . Cell membrane . Localized in the brush border membrane of renal proximal tubule cells (PubMed:11051556, PubMed:16141316). Associated with peripheral membranes (By similarity). Localizes to the apical compartmen
Protein Description A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with SLC9A3R1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity (By similarity). Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function..
Protein Sequence MASTFNPRECKLSKQEGQNYGFFLRIEKDTDGHLIRVIEEGSPAEKAGLLDGDRVLRINGVFVDKEEHAQVVELVRKSGNSVTLLVLDGDSYEKAVKNQVDLKELDQSQREAALNDKKPGPGMNGAVEPCAQPRLCYLVKEGNSFGFSLKTIQGKKGVYLTDIMPQGVAMKAGVLADDHLIEVNGENVENASHEEVVEKVTKSGSRIMFLLVDKETARCHSEQKTQFKRETASLKLLPHQPRVVVIKKGSNGYGFYLRAGPEQKGQIIKDIEPGSPAEAAGLKNNDLVVAVNGKSVEALDHDGVVEMIRKGGDQTTLLVLDKEAESIYSLARFSPLLYCQSQELPNGSVKEGPAPIPAPLEATGSEPTEDAEGHKPKLCRLLKEDDSYGFHLNAIRGQPGSFVKEVQQGGPADKAGLENEDVIIEVNGENVQEEPYDRVVERIKSSGKHVTLLVCGKMAYSYFQAKKIPIVSSMAEPLVAGPDEKGETSAESEHDAHPAKDRTLSTASHSSSNSEDTEM
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-----MASTFNPREC
-----CCCCCCHHHC		32.0328059163
14UbiquitinationPRECKLSKQEGQNYG
HHHCCCCCCCCCCCE		63.9122790023
28UbiquitinationGFFLRIEKDTDGHLI
EEEEEEEECCCCCEE		64.6522790023
46UbiquitinationEEGSPAEKAGLLDGD
ECCCHHHHCCCCCCC		50.2722790023
65UbiquitinationINGVFVDKEEHAQVV
EECEEECHHHHHHHH		60.7522790023
77UbiquitinationQVVELVRKSGNSVTL
HHHHHHHHCCCEEEE		56.0622790023
78PhosphorylationVVELVRKSGNSVTLL
HHHHHHHCCCEEEEE		32.4225293948
81PhosphorylationLVRKSGNSVTLLVLD
HHHHCCCEEEEEEEC		21.7225293948
83PhosphorylationRKSGNSVTLLVLDGD
HHCCCEEEEEEECCC		17.7525293948
94UbiquitinationLDGDSYEKAVKNQVD
ECCCHHHHHHHCCCC		50.6922790023
97MalonylationDSYEKAVKNQVDLKE
CHHHHHHHCCCCHHH		46.6626320211
97UbiquitinationDSYEKAVKNQVDLKE
CHHHHHHHCCCCHHH		46.66-
103AcetylationVKNQVDLKELDQSQR
HHCCCCHHHHCHHHH		52.3323954790
103UbiquitinationVKNQVDLKELDQSQR
HHCCCCHHHHCHHHH		52.3322790023
108PhosphorylationDLKELDQSQREAALN
CHHHHCHHHHHHHHC		30.76-
117UbiquitinationREAALNDKKPGPGMN
HHHHHCCCCCCCCCC		60.8522790023
118UbiquitinationEAALNDKKPGPGMNG
HHHHCCCCCCCCCCC		59.0622790023
144PhosphorylationYLVKEGNSFGFSLKT
EEEECCCEECEEEEE		37.2922817900
148PhosphorylationEGNSFGFSLKTIQGK
CCCEECEEEEEECCC		29.3622817900
150UbiquitinationNSFGFSLKTIQGKKG
CEECEEEEEECCCCC		42.2422790023
156UbiquitinationLKTIQGKKGVYLTDI
EEEECCCCCEEEEEC		61.5122790023
171UbiquitinationMPQGVAMKAGVLADD
CCCCHHHHHCEECCC		32.0522790023
192PhosphorylationGENVENASHEEVVEK
CCCCCCCCHHHHHHH		42.9122817900
199UbiquitinationSHEEVVEKVTKSGSR
CHHHHHHHHHHCCCE		43.5222790023
214UbiquitinationIMFLLVDKETARCHS
EEEEEEEHHHHCCCH		49.8622790023
224UbiquitinationARCHSEQKTQFKRET
HCCCHHHCHHHHHHH		40.0022790023
235UbiquitinationKRETASLKLLPHQPR
HHHHCCCCCCCCCCE		45.5422790023
248UbiquitinationPRVVVIKKGSNGYGF
CEEEEEECCCCCCEE		57.3522790023
250PhosphorylationVVVIKKGSNGYGFYL
EEEEECCCCCCEEEE		35.6422817900
253PhosphorylationIKKGSNGYGFYLRAG
EECCCCCCEEEEEEC		14.3322817900
264UbiquitinationLRAGPEQKGQIIKDI
EEECHHHCCCEEECC		51.6322790023
269MalonylationEQKGQIIKDIEPGSP
HHCCCEEECCCCCCH		55.0426320211
269UbiquitinationEQKGQIIKDIEPGSP
HHCCCEEECCCCCCH		55.04-
283UbiquitinationPAEAAGLKNNDLVVA
HHHHHCCCCCCEEEE		53.4322790023
294UbiquitinationLVVAVNGKSVEALDH
EEEEECCEEEEEECC		46.2322790023
310UbiquitinationGVVEMIRKGGDQTTL
CCEEEEEECCCCEEE		57.2122790023
322AcetylationTTLLVLDKEAESIYS
EEEEEEECCHHHHHH		55.4523954790
322UbiquitinationTTLLVLDKEAESIYS
EEEEEEECCHHHHHH		55.4522790023
334PhosphorylationIYSLARFSPLLYCQS
HHHHHHHCHHEEEEC		14.7522817900
338PhosphorylationARFSPLLYCQSQELP
HHHCHHEEEECCCCC		8.9823140645
339S-palmitoylationRFSPLLYCQSQELPN
HHCHHEEEECCCCCC		2.9428526873
341PhosphorylationSPLLYCQSQELPNGS
CHHEEEECCCCCCCC		23.2825521595
348PhosphorylationSQELPNGSVKEGPAP
CCCCCCCCCCCCCCC		36.3322324799
350AcetylationELPNGSVKEGPAPIP
CCCCCCCCCCCCCCC		59.6619852221
350UbiquitinationELPNGSVKEGPAPIP
CCCCCCCCCCCCCCC		59.6622790023
363PhosphorylationIPAPLEATGSEPTED
CCCCCCCCCCCCCCC		31.6829472430
365PhosphorylationAPLEATGSEPTEDAE
CCCCCCCCCCCCCCC		35.7325521595
368PhosphorylationEATGSEPTEDAEGHK
CCCCCCCCCCCCCCC		42.3129472430
375UbiquitinationTEDAEGHKPKLCRLL
CCCCCCCCCCHHHHH		55.4922790023
383UbiquitinationPKLCRLLKEDDSYGF
CCHHHHHHCCCCCCE		64.7822790023
387PhosphorylationRLLKEDDSYGFHLNA
HHHHCCCCCCEECHH		39.2025195567
388PhosphorylationLLKEDDSYGFHLNAI
HHHCCCCCCEECHHC		30.7025195567
401PhosphorylationAIRGQPGSFVKEVQQ
HCCCCCCCHHHHHHC		33.2825195567
404UbiquitinationGQPGSFVKEVQQGGP
CCCCCHHHHHHCCCC		50.5922790023
414UbiquitinationQQGGPADKAGLENED
HCCCCCCCCCCCCCC		46.6022790023
448UbiquitinationERIKSSGKHVTLLVC
HHHHHCCCEEEEEEE		36.5322790023
451PhosphorylationKSSGKHVTLLVCGKM
HHCCCEEEEEEECHH		17.6925521595
466UbiquitinationAYSYFQAKKIPIVSS
HHHHHHHCCCCEEEE		40.2222790023
467UbiquitinationYSYFQAKKIPIVSSM
HHHHHHCCCCEEEEC		57.6522790023
472PhosphorylationAKKIPIVSSMAEPLV
HCCCCEEEECCCCCC		18.3423140645
473PhosphorylationKKIPIVSSMAEPLVA
CCCCEEEECCCCCCC		15.8923140645
485UbiquitinationLVAGPDEKGETSAES
CCCCCCCCCCCCCCC		70.2222790023
488PhosphorylationGPDEKGETSAESEHD
CCCCCCCCCCCCCCC		41.7421082442
489PhosphorylationPDEKGETSAESEHDA
CCCCCCCCCCCCCCC		26.2425521595
492PhosphorylationKGETSAESEHDAHPA
CCCCCCCCCCCCCCC		39.6925521595
500UbiquitinationEHDAHPAKDRTLSTA
CCCCCCCCCCCCCCC		52.7922790023
503PhosphorylationAHPAKDRTLSTASHS
CCCCCCCCCCCCCCC		34.8822817900
505PhosphorylationPAKDRTLSTASHSSS
CCCCCCCCCCCCCCC		22.7021743459
506PhosphorylationAKDRTLSTASHSSSN
CCCCCCCCCCCCCCC		34.9821743459
508PhosphorylationDRTLSTASHSSSNSE
CCCCCCCCCCCCCCC		24.8022817900
510PhosphorylationTLSTASHSSSNSEDT
CCCCCCCCCCCCCCC		32.7321743459
511PhosphorylationLSTASHSSSNSEDTE
CCCCCCCCCCCCCCC		28.2822817900
512PhosphorylationSTASHSSSNSEDTEM
CCCCCCCCCCCCCCC		47.6022817900
514PhosphorylationASHSSSNSEDTEM--
CCCCCCCCCCCCC--		38.5021082442
517PhosphorylationSSSNSEDTEM-----
CCCCCCCCCC-----		29.8721743459
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 NHRF3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHRF3_MOUSE !!
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 NHRF3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CFTR_HUMANCFTRphysical
11051556
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NHRF3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488; SER-489; SER-492AND SER-514, AND MASS SPECTROMETRY.

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