NHRF1_RAT - dbPTM
NHRF1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHRF1_RAT
UniProt AC Q9JJ19
Protein Name Na(+)/H(+) exchange regulatory cofactor NHE-RF1
Gene Name Slc9a3r1
Organism Rattus norvegicus (Rat).
Sequence Length 356
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. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules (By similarity)..
Protein Sequence MSADAAAGEPLPRLCCLEKGPNGYGFHLHGEKGKVGQFIRLVEPGSPAEKSGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLKKLGVPIREELLRAQEKSEHTEPPAAADTKKAGDQNEAEKSHLERCELRPRLCTMKKGPNGYGFNLHSDKSKPGQFIRAVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIKAGGDEAKLLVVDKETDEFFKKCRVTPSQEHLDGPLPEPFSNGEIQKENSREALVEPASESPRPALARSASSDTSEELNAQDSPKRHDSTEPSSTSSSSDPILDFNISLAVAKERAHQKRSSKRAPQMDWSKKNELFSNL
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
------CCCCHHCCC		34.5527097102
2Acetylation------MSADAAAGE
------CCCCHHCCC		34.55-
46PhosphorylationIRLVEPGSPAEKSGL
EEEECCCCHHHHCCC		31.4928432305
50AcetylationEPGSPAEKSGLLAGD
CCCCHHHHCCCCCCC		52.5122902405
50UbiquitinationEPGSPAEKSGLLAGD
CCCCHHHHCCCCCCC		52.51-
51PhosphorylationPGSPAEKSGLLAGDR
CCCHHHHCCCCCCCE		26.6122673903
69AcetylationVNGENVEKETHQQVV
ECCCCCCHHHHHHHH		64.7322902405
100AcetylationPETDEQLKKLGVPIR
CCCHHHHHHHCCCHH		45.7222902405
116UbiquitinationELLRAQEKSEHTEPP
HHHHHHHHCCCCCCC		49.41-
117PhosphorylationLLRAQEKSEHTEPPA
HHHHHHHCCCCCCCH		33.5825575281
120PhosphorylationAQEKSEHTEPPAAAD
HHHHCCCCCCCHHHC		46.2525575281
139AcetylationGDQNEAEKSHLERCE
CCCCHHHHHHHHHHC		50.6622902405
167PhosphorylationGYGFNLHSDKSKPGQ
CCCCCCCCCCCCCCC		50.3125575281
183PhosphorylationIRAVDPDSPAEASGL
EEEECCCCHHHHCCC		31.2528689409
188PhosphorylationPDSPAEASGLRAQDR
CCCHHHHCCCCHHCC		29.8425575281
217AcetylationGDVVSAIKAGGDEAK
CCHHEEEEECCCCCE		40.4722902405
230UbiquitinationAKLLVVDKETDEFFK
CEEEEEECCHHHHHH		51.40-
230AcetylationAKLLVVDKETDEFFK
CEEEEEECCHHHHHH		51.4022902405
237AcetylationKETDEFFKKCRVTPS
CCHHHHHHHCCCCCC		57.1722902405
242PhosphorylationFFKKCRVTPSQEHLD
HHHHCCCCCCHHHCC		9.6228689409
257PhosphorylationGPLPEPFSNGEIQKE
CCCCCCCCCCCCCCC		55.4228689409
266PhosphorylationGEIQKENSREALVEP
CCCCCCCCCHHHCCC		32.3729779826
275PhosphorylationEALVEPASESPRPAL
HHHCCCCCCCCCHHH		49.6923712012
277PhosphorylationLVEPASESPRPALAR
HCCCCCCCCCHHHHH		24.5823712012
285PhosphorylationPRPALARSASSDTSE
CCHHHHHCCCCCCHH		27.2223712012
287PhosphorylationPALARSASSDTSEEL
HHHHHCCCCCCHHHH		29.9615878350
288PhosphorylationALARSASSDTSEELN
HHHHCCCCCCHHHHH		44.6223712012
290PhosphorylationARSASSDTSEELNAQ
HHCCCCCCHHHHHCC		39.7319700791
291PhosphorylationRSASSDTSEELNAQD
HCCCCCCHHHHHCCC		33.7819700791
299PhosphorylationEELNAQDSPKRHDST
HHHHCCCCCCCCCCC		21.9023712012
305PhosphorylationDSPKRHDSTEPSSTS
CCCCCCCCCCCCCCC		28.6623984901
306PhosphorylationSPKRHDSTEPSSTSS
CCCCCCCCCCCCCCC		58.9523984901
309PhosphorylationRHDSTEPSSTSSSSD
CCCCCCCCCCCCCCC		39.7623984901
310PhosphorylationHDSTEPSSTSSSSDP
CCCCCCCCCCCCCCC		42.9223984901
311PhosphorylationDSTEPSSTSSSSDPI
CCCCCCCCCCCCCCC		36.6423984901
312PhosphorylationSTEPSSTSSSSDPIL
CCCCCCCCCCCCCCC		30.1223984901
313PhosphorylationTEPSSTSSSSDPILD
CCCCCCCCCCCCCCC		33.6723984901
314PhosphorylationEPSSTSSSSDPILDF
CCCCCCCCCCCCCCE		38.2323984901
315PhosphorylationPSSTSSSSDPILDFN
CCCCCCCCCCCCCEE		49.7223984901
337PhosphorylationERAHQKRSSKRAPQM
HHHHHHHHCCCCCCC		47.4422817900
338PhosphorylationRAHQKRSSKRAPQMD
HHHHHHHCCCCCCCC		30.1422817900
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 NHRF1_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHRF1_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP2_RATAbcc2physical
20404332
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NHRF1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; THR-290 ANDSER-291, AND MASS SPECTROMETRY.

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