NHRF1_MOUSE - dbPTM
NHRF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHRF1_MOUSE
UniProt AC P70441
Protein Name Na(+)/H(+) exchange regulatory cofactor NHE-RF1
Gene Name Slc9a3r1
Organism Mus musculus (Mouse).
Sequence Length 355
Subcellular Localization Cytoplasm. Apical cell membrane. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Endomembrane system
Peripheral membrane protein. Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast
Protein Description Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling (By similarity). May participate in HTR4 targeting to microvilli. Involved in the regulation of phosphate reabsorption in the renal proximal tubules (By similarity). Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa..
Protein Sequence MSADAAAGEPLPRLCCLEKGPNGYGFHLHGEKGKVGQFIRLVEPGSPAEKSGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDERLKKLGVSIREELLRPQEKSEQAEPPAAADTHEAGDQNEAEKSHLRELRPRLCTMKKGPNGYGFNLHSDKSKPGQFIRAVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIKGGGDEAKLLVVDKETDEFFKKCKVIPSQEHLDGPLPEPFSNGEIQKESSREALVEPASESPRPALARSASSDTSEELNSQDSPKRQVSTEPSSTSSSSSDPILDLNISLAVAKERAHQKRSSKRAPQMDWSKKNELFSNL
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
2Phosphorylation------MSADAAAGE
------CCCCCCCCC		34.5526824392
2Acetylation------MSADAAAGE
------CCCCCCCCC		34.55-
34UbiquitinationHLHGEKGKVGQFIRL
EEECCCCCCEEEEEE		55.02-
34MalonylationHLHGEKGKVGQFIRL
EEECCCCCCEEEEEE		55.0226320211
46PhosphorylationIRLVEPGSPAEKSGL
EEEECCCCHHHHCCC		31.4929176673
50UbiquitinationEPGSPAEKSGLLAGD
CCCCHHHHCCCCCCC		52.5122790023
69UbiquitinationVNGENVEKETHQQVV
ECCCCCCHHHHHHHH		64.7322790023
77PhosphorylationETHQQVVSRIRAALN
HHHHHHHHHHHHHHH		24.1220200151
101UbiquitinationETDERLKKLGVSIRE
CCHHHHHHHCCCHHH		55.8822790023
105PhosphorylationRLKKLGVSIREELLR
HHHHHCCCHHHHHHC		17.7128285833
116UbiquitinationELLRPQEKSEQAEPP
HHHCHHHHHHCCCCC		54.7922790023
117PhosphorylationLLRPQEKSEQAEPPA
HHCHHHHHHCCCCCC		33.9025521595
128PhosphorylationEPPAAADTHEAGDQN
CCCCCCCCCCCCCCC		19.5220415495
139UbiquitinationGDQNEAEKSHLRELR
CCCCHHHHHHHHHHH		50.6622790023
169UbiquitinationNLHSDKSKPGQFIRA
CCCCCCCCCCCEEEE		59.9322790023
181PhosphorylationIRAVDPDSPAEASGL
EEEECCCCHHHHCCC		31.2529176673
201S-palmitoylationIVEVNGVCMEGKQHG
EEEECCEEECCCCCC		1.8628526873
215UbiquitinationGDVVSAIKGGGDEAK
CCCEEEEECCCCCEE		51.74-
215MalonylationGDVVSAIKGGGDEAK
CCCEEEEECCCCCEE		51.7426320211
228AcetylationAKLLVVDKETDEFFK
EEEEEEECCHHHHHH		51.4021728379
228UbiquitinationAKLLVVDKETDEFFK
EEEEEEECCHHHHHH		51.4022790023
235AcetylationKETDEFFKKCKVIPS
CCHHHHHHHCCCCCC		63.6821728379
255PhosphorylationGPLPEPFSNGEIQKE
CCCCCCCCCCCCCCC		55.4225195567
261UbiquitinationFSNGEIQKESSREAL
CCCCCCCCCHHCHHH		66.2922790023
263PhosphorylationNGEIQKESSREALVE
CCCCCCCHHCHHHCC		41.5525521595
264PhosphorylationGEIQKESSREALVEP
CCCCCCHHCHHHCCC		34.9227087446
273PhosphorylationEALVEPASESPRPAL
HHHCCCCCCCCCHHH		49.6925521595
275PhosphorylationLVEPASESPRPALAR
HCCCCCCCCCHHHHH		24.5827087446
283PhosphorylationPRPALARSASSDTSE
CCHHHHHCCCCCCHH		27.2227087446
285PhosphorylationPALARSASSDTSEEL
HHHHHCCCCCCHHHH		29.9627087446
286PhosphorylationALARSASSDTSEELN
HHHHCCCCCCHHHHH		44.6224925903
288PhosphorylationARSASSDTSEELNSQ
HHCCCCCCHHHHHCC		39.7325521595
289PhosphorylationRSASSDTSEELNSQD
HCCCCCCHHHHHCCC		33.7825521595
294PhosphorylationDTSEELNSQDSPKRQ
CCHHHHHCCCCCCCC		48.2525521595
297PhosphorylationEELNSQDSPKRQVST
HHHHCCCCCCCCCCC		25.3724925903
303PhosphorylationDSPKRQVSTEPSSTS
CCCCCCCCCCCCCCC		20.7926239621
304PhosphorylationSPKRQVSTEPSSTSS
CCCCCCCCCCCCCCC		53.7323984901
307PhosphorylationRQVSTEPSSTSSSSS
CCCCCCCCCCCCCCC		39.7623984901
308PhosphorylationQVSTEPSSTSSSSSD
CCCCCCCCCCCCCCC		42.9223984901
309PhosphorylationVSTEPSSTSSSSSDP
CCCCCCCCCCCCCCC		36.6423984901
310PhosphorylationSTEPSSTSSSSSDPI
CCCCCCCCCCCCCCE		30.1223984901
311PhosphorylationTEPSSTSSSSSDPIL
CCCCCCCCCCCCCEE		34.0423984901
312PhosphorylationEPSSTSSSSSDPILD
CCCCCCCCCCCCEEH		33.3623984901
313PhosphorylationPSSTSSSSSDPILDL
CCCCCCCCCCCEEHH		40.4823984901
314PhosphorylationSSTSSSSSDPILDLN
CCCCCCCCCCEEHHH		49.7223984901
347MalonylationAPQMDWSKKNELFSN
CCCCCHHHHHHHHHC		56.2026320211
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
77SPhosphorylationKinasePRKACAP05132
GPS
77SPhosphorylationKinasePKCAP17252
PSP
77SPhosphorylationKinasePRKCAP20444
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHRF1_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 NHRF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SL9A3_HUMANSLC9A3physical
14580213
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NHRF1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.
"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 SER-283; SER-285; SER-286;SER-289 AND SER-297, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-285, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-297, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of mouse liver using immobilized metalaffinity purification and linear ion trap mass spectrometry.";
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
Cited for: PHOSPHORYLATION AT SER-286.

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