NHRF2_HUMAN - dbPTM
NHRF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHRF2_HUMAN
UniProt AC Q15599
Protein Name Na(+)/H(+) exchange regulatory cofactor NHE-RF2
Gene Name SLC9A3R2
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Endomembrane system
Peripheral membrane protein . Nucleus . Apical cell membrane. Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes (By similarity). Nuclear, in a punctate pa
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 cAMP-mediated phosphorylation and inhibition of SLC9A3. [PubMed: 18829453 May also act as scaffold protein in the nucleus.]
Protein Sequence MAAPEPLRPRLCRLVRGEQGYGFHLHGEKGRRGQFIRRVEPGSPAEAAALRAGDRLVEVNGVNVEGETHHQVVQRIKAVEGQTRLLVVDQETDEELRRRQLTCTEEMAQRGLPPAHDPWEPKPDWAHTGSHSSEAGKKDVSGPLRELRPRLCHLRKGPQGYGFNLHSDKSRPGQYIRSVDPGSPAARSGLRAQDRLIEVNGQNVEGLRHAEVVASIKAREDEARLLVVDPETDEHFKRLRVTPTEEHVEGPLPSPVTNGTSPAQLNGGSACSSRSDLPGSDKDTEDGSAWKQDPFQESGLHLSPTAAEAKEKARAMRVNKRAPQMDWNRKREIFSNF
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 3)Phosphorylation-33.9122199227
6 (in isoform 3)Phosphorylation-32.3922199227
8 (in isoform 3)Phosphorylation-25.6322199227
20 (in isoform 3)Phosphorylation-21.8922199227
30 (in isoform 3)Phosphorylation-21.8827251275
43 (in isoform 2)Phosphorylation-31.4924719451
43PhosphorylationIRRVEPGSPAEAAAL
EEECCCCCHHHHHHH		31.4921712546
56UbiquitinationALRAGDRLVEVNGVN
HHHCCCEEEEECCEE		4.6029967540
58UbiquitinationRAGDRLVEVNGVNVE
HCCCEEEEECCEECC		34.5529967540
92PhosphorylationLLVVDQETDEELRRR
EEEEECCCHHHHHHH		42.98-
102PhosphorylationELRRRQLTCTEEMAQ
HHHHHHHHCHHHHHH		14.72-
122UbiquitinationAHDPWEPKPDWAHTG
CCCCCCCCCCCCCCC		44.0629967540
124UbiquitinationDPWEPKPDWAHTGSH
CCCCCCCCCCCCCCC		62.4129967540
126UbiquitinationWEPKPDWAHTGSHSS
CCCCCCCCCCCCCCC		9.5729967540
128PhosphorylationPKPDWAHTGSHSSEA
CCCCCCCCCCCCCHH		32.4127251275
130PhosphorylationPDWAHTGSHSSEAGK
CCCCCCCCCCCHHCC		22.7325159151
132PhosphorylationWAHTGSHSSEAGKKD
CCCCCCCCCHHCCCC		31.4127251275
132 (in isoform 2)Phosphorylation-31.4124719451
133PhosphorylationAHTGSHSSEAGKKDV
CCCCCCCCHHCCCCC		26.4927251275
138UbiquitinationHSSEAGKKDVSGPLR
CCCHHCCCCCCCHHH		63.5529967540
141PhosphorylationEAGKKDVSGPLRELR
HHCCCCCCCHHHHHH		44.8427251275
167PhosphorylationGYGFNLHSDKSRPGQ
CCCCCCCCCCCCCCC		50.3125159151
169UbiquitinationGFNLHSDKSRPGQYI
CCCCCCCCCCCCCEE		51.9129967540
171UbiquitinationNLHSDKSRPGQYIRS
CCCCCCCCCCCEEEE		45.1429967540
178UbiquitinationRPGQYIRSVDPGSPA
CCCCEEEECCCCCHH		22.7029967540
178PhosphorylationRPGQYIRSVDPGSPA
CCCCEEEECCCCCHH		22.7023403867
180UbiquitinationGQYIRSVDPGSPAAR
CCEEEECCCCCHHHH		42.9929967540
183 (in isoform 2)Phosphorylation-19.4324719451
183PhosphorylationIRSVDPGSPAARSGL
EEECCCCCHHHHHHC		19.4325159151
237UbiquitinationPETDEHFKRLRVTPT
CCCHHHHHHCCCCCC		53.0529967540
242PhosphorylationHFKRLRVTPTEEHVE
HHHHCCCCCCHHCCC		20.3328450419
244PhosphorylationKRLRVTPTEEHVEGP
HHCCCCCCHHCCCCC		44.6428450419
254 (in isoform 2)Phosphorylation-39.4224719451
254PhosphorylationHVEGPLPSPVTNGTS
CCCCCCCCCCCCCCC		39.4225159151
257PhosphorylationGPLPSPVTNGTSPAQ
CCCCCCCCCCCCHHH		31.1725159151
257 (in isoform 2)Phosphorylation-31.1724719451
260PhosphorylationPSPVTNGTSPAQLNG
CCCCCCCCCHHHCCC		33.3425159151
261PhosphorylationSPVTNGTSPAQLNGG
CCCCCCCCHHHCCCC		21.4525159151
261 (in isoform 2)Phosphorylation-21.4524719451
269PhosphorylationPAQLNGGSACSSRSD
HHHCCCCCCCCCCCC		27.7426657352
272PhosphorylationLNGGSACSSRSDLPG
CCCCCCCCCCCCCCC		28.6228450419
273PhosphorylationNGGSACSSRSDLPGS
CCCCCCCCCCCCCCC		35.3728450419
275PhosphorylationGSACSSRSDLPGSDK
CCCCCCCCCCCCCCC		45.5123927012
280 (in isoform 2)Phosphorylation-39.2824275569
280PhosphorylationSRSDLPGSDKDTEDG
CCCCCCCCCCCCCCC		39.2823927012
282UbiquitinationSDLPGSDKDTEDGSA
CCCCCCCCCCCCCCC		69.1429967540
284 (in isoform 2)Phosphorylation-41.5428348404
284PhosphorylationLPGSDKDTEDGSAWK
CCCCCCCCCCCCCCC		41.5423663014
287 (in isoform 2)Phosphorylation-17.0327732954
288PhosphorylationDKDTEDGSAWKQDPF
CCCCCCCCCCCCCCC		43.1923403867
291 (in isoform 1)Ubiquitination-44.5321906983
291UbiquitinationTEDGSAWKQDPFQES
CCCCCCCCCCCCCCC		44.532190698
292 (in isoform 2)Phosphorylation-53.5625849741
294 (in isoform 2)Phosphorylation-30.2627732954
298PhosphorylationKQDPFQESGLHLSPT
CCCCCCCCCCCCCCC		35.5521712546
303PhosphorylationQESGLHLSPTAAEAK
CCCCCCCCCCHHHHH		14.9522167270
305PhosphorylationSGLHLSPTAAEAKEK
CCCCCCCCHHHHHHH		34.8122167270
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
303SPhosphorylationKinaseARAFP10398
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHRF2_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 NHRF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN4_HUMANACTN4physical
11948184
SGK1_HUMANSGK1physical
12387817
PDPK1_HUMANPDPK1physical
12387817
AA2BR_HUMANADORA2Bphysical
12080047
PODXL_HUMANPODXLphysical
11997330
PTH1R_HUMANPTH1Rphysical
12075354
PLCB3_HUMANPLCB3physical
10748023
SGK1_HUMANSGK1physical
11751930
LPAR2_HUMANLPAR2physical
19293149
SIN3A_HUMANSIN3Aphysical
22939629
THTR_HUMANTSTphysical
22939629
SMCA2_HUMANSMARCA2physical
22939629
TACO1_HUMANTACO1physical
22939629
UBC12_HUMANUBE2Mphysical
22939629
PPT1_HUMANPPT1physical
22939629
NUSAP_HUMANNUSAP1physical
22939629
NUD19_HUMANNUDT19physical
22939629
RASH_HUMANHRASphysical
22939629
NPC2_HUMANNPC2physical
22939629
SEP11_HUMANSEPT11physical
22939629
RL29_HUMANRPL29physical
22939629
RTN4_HUMANRTN4physical
22939629
TOM40_HUMANTOMM40physical
22939629
MRP4_HUMANABCC4physical
18045536
ANX11_HUMANANXA11physical
26344197
ATX2L_HUMANATXN2Lphysical
26344197
LSM12_HUMANLSM12physical
26344197
SYMM_HUMANMARS2physical
26344197
NDUV1_HUMANNDUFV1physical
26344197
TOM40_HUMANTOMM40physical
26344197
KPCA_HUMANPRKCAphysical
12954600
LPAR2_HUMANLPAR2physical
15143197
YAP1_HUMANYAP1physical
27173435
CTNB1_HUMANCTNNB1physical
27173435
ACTN4_HUMANACTN4physical
27173435
ACTN1_HUMANACTN1physical
27173435
CTNA1_HUMANCTNNA1physical
27173435
AHI1_HUMANAHI1physical
27173435
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
There are no disease associations of PTM sites.
Regulatory Network of NHRF2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-183 AND SER-254, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASSSPECTROMETRY.

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