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Na( )/H( ) exchange regulatory cofactor NHE-RF1 (NHERF-1) (Ezrin-radixin-moesin-binding phosphoprotein 50) (EBP50) (Regulatory cofactor of Na( )/H( ) exchanger) (Sodium-hydrogen exchanger regulatory factor 1) (Solute carrier family 9 isoform A3 regulatory factor 1)

 NHRF1_MOUSE             Reviewed;         355 AA.
P70441; Q8BYD8;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 167.
RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF1;
Short=NHERF-1;
AltName: Full=Ezrin-radixin-moesin-binding phosphoprotein 50;
Short=EBP50;
AltName: Full=Regulatory cofactor of Na(+)/H(+) exchanger;
AltName: Full=Sodium-hydrogen exchanger regulatory factor 1;
AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 1;
Name=Slc9a3r1; Synonyms=Nherf, Nherf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=10500246; DOI=10.1016/S0167-4781(99)00100-1;
Weinman E.J., Steplock D., Zhang X., Akhter S., Shenolikar S.;
"Molecular cloning of the cDNA and promoter sequences for the mouse
sodium-hydrogen exchanger regulatory factor.";
Biochim. Biophys. Acta 1447:71-76(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND INTERACTION WITH ADRB2.
PubMed=9560162; DOI=10.1038/33458;
Hall R.A., Premont R.T., Chow C.-W., Blitzer J.T., Pitcher J.A.,
Claing A., Stoffel R.H., Barak L.S., Shenolikar S., Weinman E.J.,
Grinstein S., Lefkowitz R.J.;
"The beta2-adrenergic receptor interacts with the Na+/H+-exchanger
regulatory factor to control Na+/H+ exchange.";
Nature 392:626-630(1998).
[5]
INTERACTION WITH PAG1, AND IDENTIFICATION IN A COMPLEX WITH PAG1 AND
MSN.
PubMed=11777944; DOI=10.4049/jimmunol.168.2.541;
Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H.,
Miyazaki M., Nakajima N., Okada M., Saito T.;
"Negative regulation of immune synapse formation by anchoring lipid
raft to cytoskeleton through Cbp-EBP50-ERM assembly.";
J. Immunol. 168:541-544(2002).
[6]
INTERACTION WITH PDZK1.
PubMed=14531806; DOI=10.1046/j.1523-1755.2003.00266.x;
Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A.,
Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.;
"PDZK1: I. a major scaffolder in brush borders of proximal tubular
cells.";
Kidney Int. 64:1733-1745(2003).
[7]
INTERACTION WITH HTR4.
PubMed=15466885; DOI=10.1242/jcs.01379;
Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
Marin P., Dumuis A., Bockaert J.;
"New sorting nexin (SNX27) and NHERF specifically interact with the 5-
HT4a receptor splice variant: roles in receptor targeting.";
J. Cell Sci. 117:5367-5379(2004).
[8]
PHOSPHORYLATION AT SER-286.
PubMed=15378723; DOI=10.1002/rcm.1604;
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
"Phosphoproteome analysis of mouse liver using immobilized metal
affinity purification and linear ion trap mass spectrometry.";
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
[9]
SUBCELLULAR LOCATION.
PubMed=17311105; DOI=10.1371/journal.pone.0000237;
Nielsen J.S., Graves M.L., Chelliah S., Vogl A.W., Roskelley C.D.,
McNagny K.M.;
"The CD34-related molecule podocalyxin is a potent inducer of
microvillus formation.";
PLoS ONE 2:E237-E237(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-297, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; THR-288; SER-289;
SER-294 AND SER-297, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION, INTERACTION WITH CFTR; SLC26A3 AND SLC26A6, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=21976599; DOI=10.1095/biolreprod.111.094037;
Chavez J.C., Hernandez-Gonzalez E.O., Wertheimer E., Visconti P.E.,
Darszon A., Trevino C.L.;
"Participation of the Cl-/HCO(3)- exchangers SLC26A3 and SLC26A6, the
Cl- channel CFTR, and the regulatory factor SLC9A3R1 in mouse sperm
capacitation.";
Biol. Reprod. 86:1-14(2012).
-!- FUNCTION: 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. {ECO:0000250,
ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}.
-!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R2. Binds the N-
termini of EZR, RDX and MSN. Binds the C-termini of PDGFRA,
PDGFRB, ADRB2 and NOS2. Binds ARHGAP17, EPI64, RACK1, OPRK1, GNAQ,
CTNNB1, PLCB3 and CLCN3. Forms a complex with CFTR and SLC4A7.
Forms a complex with SLC4A7 and ATP6V1B1 (By similarity). Binds
PDZK1. Binds the C-terminus of PAG1. In resting T-cells, part of a
PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation.
Directly interacts with HTR4. Interacts with MCC (By similarity).
Interacts with TRPC4 (via the PDZ-binding domain) (By similarity).
Interacts (via the PDZ 1 domain) with PODXL (via the C-terminal
PDZ-binding motif DTHL); interaction is not detected in glomerular
epithelium cells (By similarity). Interacts (via the PDZ 1 domain)
with PODXL (via the C-terminal PDZ-binding motif DTHL); the
interaction take place early in the secretory pathway and is
necessary for its apical membrane sorting (By similarity).
Interacts with SLC34A1 (By similarity). Interacts with CFTR,
SLC26A3 and SLC26A6. {ECO:0000250, ECO:0000269|PubMed:11777944,
ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15466885,
ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:9560162}.
-!- INTERACTION:
P26361:Cftr; NbExp=3; IntAct=EBI-1184085, EBI-6115317;
Q9WVC8:Slc26a3; NbExp=2; IntAct=EBI-1184085, EBI-6895537;
Q8CIW6:Slc26a6; NbExp=2; IntAct=EBI-1184085, EBI-6895517;
Q80ZA5-3:Slc4a10 (xeno); NbExp=3; IntAct=EBI-1184085, EBI-8613086;
-!- SUBCELLULAR LOCATION: Cytoplasm. Apical cell membrane. Cell
projection, filopodium {ECO:0000250}. Cell projection, ruffle
{ECO:0000250}. Cell projection, microvillus {ECO:0000250}.
Endomembrane system {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=Colocalizes with actin in microvilli-rich
apical regions of the syncytiotrophoblast. Present in lipid rafts
of T-cells (By similarity). Translocates from the cytoplasm to the
apical cell membrane in a PODXL-dependent manner. Colocalizes with
CFTR at the midpiece of sperm tail. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70441-1; Sequence=Displayed;
Name=2;
IsoId=P70441-2; Sequence=VSP_027877, VSP_027878;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in spermatogenic cells.
{ECO:0000269|PubMed:21976599}.
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EMBL; U74079; AAB17569.1; -; mRNA.
EMBL; AK040371; BAC30573.2; -; mRNA.
EMBL; BC085141; AAH85141.1; -; mRNA.
CCDS; CCDS36370.1; -. [P70441-1]
RefSeq; NP_036160.1; NM_012030.2. [P70441-1]
UniGene; Mm.27842; -.
ProteinModelPortal; P70441; -.
SMR; P70441; -.
BioGrid; 205077; 4.
CORUM; P70441; -.
IntAct; P70441; 12.
MINT; P70441; -.
STRING; 10090.ENSMUSP00000021077; -.
iPTMnet; P70441; -.
PhosphoSitePlus; P70441; -.
SwissPalm; P70441; -.
EPD; P70441; -.
PaxDb; P70441; -.
PeptideAtlas; P70441; -.
PRIDE; P70441; -.
Ensembl; ENSMUST00000021077; ENSMUSP00000021077; ENSMUSG00000020733. [P70441-1]
GeneID; 26941; -.
KEGG; mmu:26941; -.
UCSC; uc007mgp.1; mouse. [P70441-1]
CTD; 9368; -.
MGI; MGI:1349482; Slc9a3r1.
eggNOG; ENOG410ITAB; Eukaryota.
eggNOG; ENOG4110SZZ; LUCA.
GeneTree; ENSGT00530000062999; -.
HOGENOM; HOG000089940; -.
HOVERGEN; HBG052616; -.
InParanoid; P70441; -.
KO; K13365; -.
OMA; LCAMKKG; -.
OrthoDB; EOG091G086H; -.
PhylomeDB; P70441; -.
TreeFam; TF350449; -.
PMAP-CutDB; P70441; -.
PRO; PR:P70441; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020733; Expressed in 312 organ(s), highest expression level in intestine.
ExpressionAtlas; P70441; baseline and differential.
Genevisible; P70441; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0031526; C:brush border membrane; IDA:MGI.
GO; GO:0071944; C:cell periphery; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005902; C:microvillus; ISS:UniProtKB.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
GO; GO:0032420; C:stereocilium; IDA:MGI.
GO; GO:0032426; C:stereocilium tip; IDA:MGI.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0017081; F:chloride channel regulator activity; ISS:UniProtKB.
GO; GO:0050780; F:dopamine receptor binding; IDA:MGI.
GO; GO:0070851; F:growth factor receptor binding; ISO:MGI.
GO; GO:0045159; F:myosin II binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0032947; F:protein-containing complex scaffold activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IMP:MGI.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
GO; GO:0032782; P:bile acid secretion; IMP:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:MGI.
GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
GO; GO:0034613; P:cellular protein localization; IMP:MGI.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISO:MGI.
GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
GO; GO:0022612; P:gland morphogenesis; ISO:MGI.
GO; GO:0034635; P:glutathione transport; IMP:UniProtKB.
GO; GO:0030033; P:microvillus assembly; ISO:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IGI:MGI.
GO; GO:2000146; P:negative regulation of cell motility; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0010766; P:negative regulation of sodium ion transport; IMP:MGI.
GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IMP:MGI.
GO; GO:0007097; P:nuclear migration; ISO:MGI.
GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IMP:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0034767; P:positive regulation of ion transmembrane transport; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
GO; GO:0008361; P:regulation of cell size; ISO:MGI.
GO; GO:0044062; P:regulation of excretion; IMP:MGI.
GO; GO:0045859; P:regulation of protein kinase activity; IMP:UniProtKB.
GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
GO; GO:0097291; P:renal phosphate ion absorption; ISS:UniProtKB.
GO; GO:0003096; P:renal sodium ion transport; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR015098; EBP50_C-term.
InterPro; IPR031199; NHERF-1.
InterPro; IPR017300; NHERF-1/NHERF-2.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR14191:SF7; PTHR14191:SF7; 1.
Pfam; PF09007; EBP50_C; 1.
Pfam; PF00595; PDZ; 2.
PIRSF; PIRSF037866; EBP50; 1.
ProDom; PD283022; EBP50_C-term; 1.
SMART; SM00228; PDZ; 2.
SUPFAM; SSF50156; SSF50156; 2.
PROSITE; PS50106; PDZ; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Membrane; Phosphoprotein;
Reference proteome; Repeat; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O14745}.
CHAIN 2 355 Na(+)/H(+) exchange regulatory cofactor
NHE-RF1.
/FTId=PRO_0000096800.
DOMAIN 14 94 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 149 229 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O14745}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:O14745}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:O14745}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000250|UniProtKB:O14745}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:O14745}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:Q28619}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15378723}.
MOD_RES 288 288 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 317 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_027877.
VAR_SEQ 318 318 L -> M (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_027878.
SEQUENCE 355 AA; 38600 MW; 331F6BEE31DA0A11 CRC64;
MSADAAAGEP LPRLCCLEKG PNGYGFHLHG EKGKVGQFIR LVEPGSPAEK SGLLAGDRLV
EVNGENVEKE THQQVVSRIR AALNAVRLLV VDPETDERLK KLGVSIREEL LRPQEKSEQA
EPPAAADTHE AGDQNEAEKS HLRELRPRLC TMKKGPNGYG FNLHSDKSKP GQFIRAVDPD
SPAEASGLRA QDRIVEVNGV CMEGKQHGDV VSAIKGGGDE AKLLVVDKET DEFFKKCKVI
PSQEHLDGPL PEPFSNGEIQ KESSREALVE PASESPRPAL ARSASSDTSE ELNSQDSPKR
QVSTEPSSTS SSSSDPILDL NISLAVAKER AHQKRSSKRA PQMDWSKKNE LFSNL


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Catalog number Product name Quantity
15-288-21942B Ezrin-radixin-moesin-binding phosphoprotein 50 - EBP50; Na(+)_H(+) exchange regulatory cofactor NHE-RF; NHERF-1; Regulatory cofactor of Na(+)_H(+) exchanger; Sodium-hydrogen exchanger regulatory facto 0.05 mg
10-288-21942F Ezrin-radixin-moesin-binding phosphoprotein 50 - EBP50; Na(+)_H(+) exchange regulatory cofactor NHE-RF; NHERF-1; Regulatory cofactor of Na(+)_H(+) exchanger; Sodium-hydrogen exchanger regulatory facto 0.05 mg
10-288-21942F Ezrin-radixin-moesin-binding phosphoprotein 50 - EBP50; Na(+)_H(+) exchange regulatory cofactor NHE-RF; NHERF-1; Regulatory cofactor of Na(+)_H(+) exchanger; Sodium-hydrogen exchanger regulatory facto 0.1 mg
15-288-21942B Ezrin-radixin-moesin-binding phosphoprotein 50 - EBP50; Na(+)_H(+) exchange regulatory cofactor NHE-RF; NHERF-1; Regulatory cofactor of Na(+)_H(+) exchanger; Sodium-hydrogen exchanger regulatory facto 0.1 mg
EIAAB27167 Bos taurus,Bovine,EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,NHERF,NHERF1,NHERF-1,Regulatory cofactor of Na(+)_H(+) exchanger,SLC9A3R1,Sodium-
EIAAB27166 EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Mouse,Mus musculus,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,Nherf,Nherf1,NHERF-1,Regulatory cofactor of Na(+)_H(+) exchanger,Slc9a3r1,Sodium
EIAAB27164 EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Homo sapiens,Human,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,NHERF,NHERF1,NHERF-1,Regulatory cofactor of Na(+)_H(+) exchanger,SLC9A3R1,Sodium
EIAAB27165 EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,Nherf,Nherf1,NHERF-1,Rat,Rattus norvegicus,Regulatory cofactor of Na(+)_H(+) exchanger,Slc9a3r1,Sod
EIAAB27163 EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,NHERF,NHERF1,NHERF-1,Oryctolagus cuniculus,Rabbit,Regulatory cofactor of Na(+)_H(+) exchanger,SLC9A
EIAAB27162 Chicken,EBP50,Ezrin-radixin-moesin-binding phosphoprotein 50,Gallus gallus,Na(+)_H(+) exchange regulatory cofactor NHE-RF1,NHERF,NHERF1,NHERF-1,RCJMB04_3g21,Regulatory cofactor of Na(+)_H(+) exchanger
EIAAB27168 Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,Nherf2,NHERF-2,Rat,Rattus norvegicus,SIP-1,Slc9a3r2,Sodium-hydrogen exchanger regulatory factor 2,Solute carrier
EIAAB27169 Homo sapiens,Human,Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,NHERF2,NHERF-2,SIP-1,SLC9A3R2,Sodium-hydrogen exchanger regulatory factor 2,Solute carrier fa
EIAAB27170 Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHERF2,Oryctolagus cuniculus,PDZ domain-containing protein NHERF-2,Rabbit,SLC9A3R2,Sodium-hydrogen exchanger regulatory factor 2,Solute carrier family 9
EIAAB27171 Mouse,Mus musculus,Na(+)_H(+) exchange regulatory cofactor NHE-RF2,NHE3 kinase A regulatory protein E3KARP,Nherf2,NHERF-2,Octs2,SIP-1,Slc9a3r2,Sodium-hydrogen exchanger regulatory factor 2,Solute carr
EIAAB27172 Bos taurus,Bovine,Na(+)_H(+) exchange regulatory cofactor NHE-RF3,Na(+)_H(+) exchanger regulatory factor 3,NHERF3,NHERF-3,PDZ domain-containing protein 1,PDZD1,PDZK1,Sodium-hydrogen exchanger regulato
EIAAB27174 CAP70,CFTR-associated protein of 70 kDa,Na(+)_H(+) exchange regulatory cofactor NHE-RF3,Na(+)_H(+) exchanger regulatory factor 3,NHERF3,NHERF-3,Oryctolagus cuniculus,PDZ domain-containing protein 1,PD
EIAAB27175 Clamp,C-terminal-linking and modulating protein,Dietary Pi-regulated RNA-1,Diphor1,Diphor-1,Na(+)_H(+) exchange regulatory cofactor NHE-RF3,Na(+)_H(+) exchanger regulatory factor 3,Na_Pi cotransporter
EIAAB27176 Cap70,CFTR-associated protein of 70 kDa,Mouse,Mus musculus,Na(+)_H(+) exchange regulatory cofactor NHE-RF3,Na(+)_H(+) exchanger regulatory factor 3,Na_Pi cotransporter C-terminal-associated protein 1,
EIAAB27173 CAP70,CFTR-associated protein of 70 kDa,Homo sapiens,Human,Na(+)_H(+) exchange regulatory cofactor NHE-RF3,Na(+)_H(+) exchanger regulatory factor 3,Na_Pi cotransporter C-terminal-associated protein 1,
EIAAB36190 Mouse,mRS1,Mus musculus,Regulatory solute carrier protein family 1 member 1,Regulatory subunit of SGLT1,Rsc1a1,Transporter regulator RS1
EIAAB47434 HD gene regulatory region-binding protein 2,HDBP2,HDBP-2,HD-regulating factor 2,HDRF-2,Homo sapiens,Human,Huntington disease gene regulatory region-binding protein 2,Papillomavirus regulatory factor 1
31-202 Interferon regulatory factor 8 (IRF8, interferon consensus sequence-binding protein, Ion ChannelSBP) is a transcription factor of the interferon (IFN) regulatory factor (IRF) family. Proteins of this 0.05 mg
25-416 RFX1 is a member of the regulatory factor X protein family, which are transcription factors that contain a highly-conserved winged helix DNA binding domain. RFX1 is structurally related to regulatory 0.05 mg
CSB-EL021734RA Rat Na(+)_H(+) exchange regulatory cofactor NHE-RF2 (SLC9A3R2) ELISA kit 96T
ZN852_HUMAN Rabbit ELISA Kit FOR Na(+) per H(+) exchange regulatory cofactor NHE-RF2 96T


 

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