dbPTM

NHRF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NHRF1_HUMAN
UniProt AC	O14745
Protein Name	Na(+)/H(+) exchange regulatory cofactor NHE-RF1
Gene Name	SLC9A3R1
Organism	Homo sapiens (Human).
Sequence Length	358
Subcellular Localization	Cytoplasm. Apical cell membrane. Endomembrane system Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent ma
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. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa..
Protein Sequence	MSADAAAGAPLPRLCCLEKGPNGYGFHLHGEKGKLGQYIRLVEPGSPAEKAGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLQKLGVQVREELLRAQEAPGQAEPPAAAEVQGAGNENEPREADKSHPEQRELRPRLCTMKKGPSGYGFNLHSDKSKPGQFIRSVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFKKCRVIPSQEHLNGPLPVPFTNGEIQKENSREALAEAALESPRPALVRSASSDTSEELNSQDSPPKQDSTAPSSTSSSDPILDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSADAAAGA ------CCHHHHCCC	34.55	19413330
2	Phosphorylation	------MSADAAAGA ------CCHHHHCCC	34.55	23401153
15	S-nitrosylation	GAPLPRLCCLEKGPN CCCCCEEEEECCCCC	2.35	24105792
16	S-nitrosylation	APLPRLCCLEKGPNG CCCCEEEEECCCCCC	6.96	24105792
19	Acetylation	PRLCCLEKGPNGYGF CEEEEECCCCCCCEE	67.72	23749302
32	Acetylation	GFHLHGEKGKLGQYI EEEEECCCCCCCEEE	66.97	19608861
34	Acetylation	HLHGEKGKLGQYIRL EEECCCCCCCEEEEE	61.59	25953088
38	Phosphorylation	EKGKLGQYIRLVEPG CCCCCCEEEEEECCC	6.04	22817900
46	Phosphorylation	IRLVEPGSPAEKAGL EEEECCCCHHHHHCC	31.49	25159151
50	Ubiquitination	EPGSPAEKAGLLAGD CCCCHHHHHCCCCCC	50.27	21906983
50	2-Hydroxyisobutyrylation	EPGSPAEKAGLLAGD CCCCHHHHHCCCCCC	50.27	-
58	Methylation	AGLLAGDRLVEVNGE HCCCCCCEEEEECCC	39.45	115484969
69	Ubiquitination	VNGENVEKETHQQVV ECCCCCCHHHHHHHH	64.73	24816145
69	Acetylation	VNGENVEKETHQQVV ECCCCCCHHHHHHHH	64.73	25953088
77	Phosphorylation	ETHQQVVSRIRAALN HHHHHHHHHHHHHHH	24.12	22817900
95	Phosphorylation	LLVVDPETDEQLQKL EEEECCCCHHHHHHH	50.66	22817900
101	Ubiquitination	ETDEQLQKLGVQVRE CCHHHHHHHCHHHHH	56.66	21963094
156	Phosphorylation	ELRPRLCTMKKGPSG HHHHCEECCCCCCCC	36.30	-
158	Ubiquitination	RPRLCTMKKGPSGYG HHCEECCCCCCCCCC	36.10	23503661
159	Ubiquitination	PRLCTMKKGPSGYGF HCEECCCCCCCCCCC	66.29	23503661
162	Phosphorylation	CTMKKGPSGYGFNLH ECCCCCCCCCCCCCC	54.00	25159151
164	Phosphorylation	MKKGPSGYGFNLHSD CCCCCCCCCCCCCCC	23.92	25307156
170	Phosphorylation	GYGFNLHSDKSKPGQ CCCCCCCCCCCCCCC	50.31	20873877
172	Ubiquitination	GFNLHSDKSKPGQFI CCCCCCCCCCCCCEE	64.49	29967540
173	Phosphorylation	FNLHSDKSKPGQFIR CCCCCCCCCCCCEEE	49.42	-
181	Phosphorylation	KPGQFIRSVDPDSPA CCCCEEEECCCCCHH	26.51	28258704
186	Phosphorylation	IRSVDPDSPAEASGL EEECCCCCHHHHCCC	31.25	21815630
191	Phosphorylation	PDSPAEASGLRAQDR CCCHHHHCCCCHHCC	29.84	-
195	Ubiquitination	AEASGLRAQDRIVEV HHHCCCCHHCCEEEE	22.22	-
206	S-nitrosylation	IVEVNGVCMEGKQHG EEEECCEEECCCCCC	1.86	24105792
210	Acetylation	NGVCMEGKQHGDVVS CCEEECCCCCCCCEE	26.30	26051181
217	Phosphorylation	KQHGDVVSAIRAGGD CCCCCCEEEEEECCC	20.16	21406692
226	Phosphorylation	IRAGGDETKLLVVDR EEECCCCCEEEEEEC	31.56	21406692
227	Ubiquitination	RAGGDETKLLVVDRE EECCCCCEEEEEECC	37.46	24816145
240	Acetylation	RETDEFFKKCRVIPS CCHHHHHHHCCCCCC	57.17	25953088
240	2-Hydroxyisobutyrylation	RETDEFFKKCRVIPS CCHHHHHHHCCCCCC	57.17	-
241	Ubiquitination	ETDEFFKKCRVIPSQ CHHHHHHHCCCCCCC	23.32	24816145
247	Phosphorylation	KKCRVIPSQEHLNGP HHCCCCCCCHHCCCC	36.76	24719451
260	Phosphorylation	GPLPVPFTNGEIQKE CCCCCCCCCCCCCCC	35.92	26657352
269	Phosphorylation	GEIQKENSREALAEA CCCCCCCHHHHHHHH	32.37	25159151
280	O-linked_Glycosylation	LAEAALESPRPALVR HHHHHHHCCCCHHHH	27.36	OGP
280	Phosphorylation	LAEAALESPRPALVR HHHHHHHCCCCHHHH	27.36	19664994
288	Phosphorylation	PRPALVRSASSDTSE CCCHHHHCCCCCCHH	25.64	29255136
290	Phosphorylation	PALVRSASSDTSEEL CHHHHCCCCCCHHHH	29.96	29255136
291	Phosphorylation	ALVRSASSDTSEELN HHHHCCCCCCHHHHH	44.62	29255136
293	Phosphorylation	VRSASSDTSEELNSQ HHCCCCCCHHHHHCC	39.73	22167270
294	Phosphorylation	RSASSDTSEELNSQD HCCCCCCHHHHHCCC	33.78	19664994
299	Phosphorylation	DTSEELNSQDSPPKQ CCHHHHHCCCCCCCC	48.25	19664994
302	Phosphorylation	EELNSQDSPPKQDST HHHHCCCCCCCCCCC	35.15	19664994
308	Phosphorylation	DSPPKQDSTAPSSTS CCCCCCCCCCCCCCC	24.79	23663014
309	Phosphorylation	SPPKQDSTAPSSTSS CCCCCCCCCCCCCCC	51.37	23663014
312	Phosphorylation	KQDSTAPSSTSSSDP CCCCCCCCCCCCCCC	43.73	23663014
313	Phosphorylation	QDSTAPSSTSSSDPI CCCCCCCCCCCCCCC	31.11	23663014
314	Phosphorylation	DSTAPSSTSSSDPIL CCCCCCCCCCCCCCC	36.64	26657352
315	Phosphorylation	STAPSSTSSSDPILD CCCCCCCCCCCCCCC	29.77	23663014
316	Phosphorylation	TAPSSTSSSDPILDF CCCCCCCCCCCCCCH	38.56	23663014
317	Phosphorylation	APSSTSSSDPILDFN CCCCCCCCCCCCCHH	47.36	30278072
326	Phosphorylation	PILDFNISLAMAKER CCCCHHHHHHHHHHH	15.92	20068231
339	Phosphorylation	ERAHQKRSSKRAPQM HHHHHHHHCCCCCCC	47.44	17613530
340	Phosphorylation	RAHQKRSSKRAPQMD HHHHHHHCCCCCCCC	30.14	17613530
349	Phosphorylation	RAPQMDWSKKNELFS CCCCCCHHHHHHHHH	29.50	26074081
350	Ubiquitination	APQMDWSKKNELFSN CCCCCHHHHHHHHHC	56.20	29967540
351	Ubiquitination	PQMDWSKKNELFSNL CCCCHHHHHHHHHCC	50.57	-
356	Phosphorylation	SKKNELFSNL----- HHHHHHHHCC-----	50.26	28555341

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
77	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
156	T	Phosphorylation	Kinase	AKT1	P31749	PSP
156	T	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
162	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
280	S	Phosphorylation	Kinase	CDK1	P06493	PSP
290	S	Phosphorylation	Kinase	GRK6	P43250	PhosphoELM
302	S	Phosphorylation	Kinase	CDK1	P06493	PSP
339	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
340	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NHRF1_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 NHRF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OPRK_HUMAN	OPRK1	physical	15070904
NHRF1_HUMAN	SLC9A3R1	physical	15070904
SL9A3_HUMAN	SLC9A3	physical	14580213
CFTR_HUMAN	CFTR	physical	9613608
TRPC5_MOUSE	Trpc5	physical	10980202
TRPC4_MOUSE	Trpc4	physical	10980202
PLCB1_HUMAN	PLCB1	physical	10980202
PLCB1_BOVIN	PLCB1	physical	10980202
YAP1_HUMAN	YAP1	physical	10562288
YES_HUMAN	YES1	physical	10562288
ADRB2_HUMAN	ADRB2	physical	11882663
S4A8_HUMAN	SLC4A8	physical	12444018
TB10A_HUMAN	TBC1D10A	physical	11285285
CFTR_HUMAN	CFTR	physical	10852925
CLCN3_HUMAN	CLCN3	physical	12471024
CFTR_HUMAN	CFTR	physical	12471024
PGFRA_HUMAN	PDGFRA	physical	11046132
PGFRB_HUMAN	PDGFRB	physical	11046132
NHRF1_HUMAN	SLC9A3R1	physical	11046132
PHAG1_HUMAN	PAG1	physical	11684085
EZRI_HUMAN	EZR	physical	9314537
CFTR_HUMAN	CFTR	physical	9677412
CFTR_HUMAN	CFTR	physical	12403779
ADRB2_HUMAN	ADRB2	physical	11526121
RNT2_HUMAN	RNASET2	physical	22939629
TACC1_HUMAN	TACC1	physical	22939629
UCRI_HUMAN	UQCRFS1	physical	22939629
PCYOX_HUMAN	PCYOX1	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
PPME1_HUMAN	PPME1	physical	22939629
PALM2_HUMAN	PALM2	physical	22939629
PTEN_HUMAN	PTEN	physical	23118026
EPHB1_HUMAN	EPHB1	physical	23118026
MRP4_HUMAN	ABCC4	physical	18045536
ZN468_HUMAN	ZNF468	physical	21988832
GNA11_HUMAN	GNA11	physical	12193606
CAN1_HUMAN	CAPN1	physical	22863883
KCRB_HUMAN	CKB	physical	22863883
G6PD_HUMAN	G6PD	physical	22863883
LDHB_HUMAN	LDHB	physical	22863883
SIAS_HUMAN	NANS	physical	22863883
RL23_HUMAN	RPL23	physical	22863883
TGM2_HUMAN	TGM2	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
MRP4_HUMAN	ABCC4	physical	18559527
SKP2_HUMAN	SKP2	physical	25492869
AKT1_HUMAN	AKT1	physical	25492869
IREB2_HUMAN	IREB2	physical	26344197
S4A7_HUMAN	SLC4A7	physical	12403779
KPCA_HUMAN	PRKCA	physical	12954600
PHLP1_HUMAN	PHLPP1	physical	21804599
PHLP2_HUMAN	PHLPP2	physical	21804599
MRP2_HUMAN	ABCC2	physical	25163515
MK01_HUMAN	MAPK1	physical	20736378
CADH2_HUMAN	CDH2	physical	20736378

Drug and Disease Associations

Kegg Disease
H00888	Nephrolithiasis/osteoporosis, hypophosphatemic
OMIM Disease
612287	Nephrolithiasis/osteoporosis, hypophosphatemic, 2 (NPHLOP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NHRF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-46 AND SER-280, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-290; SER-291AND THR-293, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.	17081983 [Abstract]