| |
---|---|
Accession Number: | P19634 |
Protein Name: | Sodium/hydrogen exchanger 1 |
Length: | 815 |
Molecular Weight: | 90763.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 12 |
Location1 / Topology2 / Orientation3: | Membrane1 / Multi-pass membrane protein2 |
Substrate | sodium(1+), hydron, oligosaccharide |
Cross database links:
Entrez Gene ID: | 6548 |
---|---|
Pfam: | PF00999 |
KEGG: | hsa:6548 hsa:6548 |
Gene Ontology
GO:0016021
C:integral to membrane
GO:0015385
F:sodium:hydrogen antiporter activity
GO:0006885
P:regulation of pH
GO:0016323
C:basolateral plasma membrane
GO:0005624
C:membrane fraction
GO:0045121
C:membrane raft
GO:0005886
C:plasma membrane
GO:0015299
F:solute:hydrogen antiporter activity
GO:0030154
P:cell differentiation
GO:0016049
P:cell growth
GO:0007243
P:intracellular protein kinase cascade
GO:0045768
P:positive regulation of anti-apoptosis
GO:0001101
P:response to acid
GO:0010447
P:response to acidity
GO:0042493
P:response to drug
GO:0014070
P:response to organic cyclic compound
| |
References (44)[1] “Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter.” Sardet C.et.al. 2536298 [2] “Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.” Sardet C.et.al. 2154036 [3] “Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger.” Tse C.-M.et.al. 1712287 [4] “Cloning and analysis of the human myocardial Na+/H+ exchanger.” Fliegel L.et.al. 8283968 [5] “Silent polymorphisms within the coding region of human sodium/hydrogen exchanger isoform-1 cDNA in peripheral blood mononuclear cells of leukemia patients: a comparison with healthy controls.” Garden O.A.et.al. 10913675 [6] “The DNA sequence and biological annotation of human chromosome 1.” Gregory S.G.et.al. 16710414 [7] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [8] “The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.” Counillon L.et.al. 8068684 [9] “Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using chymotryptic cleavage.” Shrode L.D.et.al. 9688597 [10] “A novel topology model of the human Na(+)/H(+) exchanger isoform 1.” Wakabayashi S.et.al. 10713111 [11] “Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger type-1.” Mailaender J.et.al. 11696366 [12] “Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.” Pang T.et.al. 11350981 [13] “Expression of calcineurin B homologous protein 2 protects serum deprivation-induced cell death by serum-independent activation of Na+/H+ exchanger.” Pang T.et.al. 12226101 [14] “The Na+/H+ exchanger cytoplasmic tail: structure, function, and interactions with tescalcin.” Li X.et.al. 12809501 [15] “Proline residues in transmembrane segment IV are critical for activity, expression and targeting of the Na+/H+ exchanger isoform 1.” Slepkov E.R.et.al. 14680478 [16] “ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.” Matsuoka S.et.al. 17525332 [17] “Phosphoproteome of resting human platelets.” Zahedi R.P.et.al. 18088087 [18] “A quantitative atlas of mitotic phosphorylation.” Dephoure N.et.al. 18669648 [19] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.” Mayya V.et.al. 19690332 [20] “Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger.” Slepkov E.R.et.al. 15677483 [21] “Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation.” Ammar Y.B.et.al. 16710297 [22] “Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1.” Mishima M.et.al. 17050540 [23] “Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter.” Sardet C.et.al. 2536298 [24] “Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.” Sardet C.et.al. 2154036 [25] “Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger.” Tse C.-M.et.al. 1712287 [26] “Cloning and analysis of the human myocardial Na+/H+ exchanger.” Fliegel L.et.al. 8283968 [27] “Silent polymorphisms within the coding region of human sodium/hydrogen exchanger isoform-1 cDNA in peripheral blood mononuclear cells of leukemia patients: a comparison with healthy controls.” Garden O.A.et.al. 10913675 [28] “The DNA sequence and biological annotation of human chromosome 1.” Gregory S.G.et.al. 16710414 [29] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [30] “The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.” Counillon L.et.al. 8068684 [31] “Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using chymotryptic cleavage.” Shrode L.D.et.al. 9688597 [32] “A novel topology model of the human Na(+)/H(+) exchanger isoform 1.” Wakabayashi S.et.al. 10713111 [33] “Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger type-1.” Mailaender J.et.al. 11696366 [34] “Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers.” Pang T.et.al. 11350981 [35] “Expression of calcineurin B homologous protein 2 protects serum deprivation-induced cell death by serum-independent activation of Na+/H+ exchanger.” Pang T.et.al. 12226101 [36] “The Na+/H+ exchanger cytoplasmic tail: structure, function, and interactions with tescalcin.” Li X.et.al. 12809501 [37] “Proline residues in transmembrane segment IV are critical for activity, expression and targeting of the Na+/H+ exchanger isoform 1.” Slepkov E.R.et.al. 14680478 [38] “ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.” Matsuoka S.et.al. 17525332 [39] “Phosphoproteome of resting human platelets.” Zahedi R.P.et.al. 18088087 [40] “A quantitative atlas of mitotic phosphorylation.” Dephoure N.et.al. 18669648 [41] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.” Mayya V.et.al. 19690332 [42] “Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger.” Slepkov E.R.et.al. 15677483 [43] “Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation.” Ammar Y.B.et.al. 16710297 [44] “Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1.” Mishima M.et.al. 17050540
| |
Structure: | |
[...more] |
External Searches:
|
Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
|
1: MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE PPRERSIGDV 61: TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR TPFEISLWIL LACLMKIGFH 121: VIPTISSIVP ESCLLIVVGL LVGGLIKGVG ETPPFLQSDV FFLFLLPPII LDAGYFLPLR 181: QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV 241: AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV 301: VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG 361: VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF 421: CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF 481: LTAIITVIFF TVFVQGMTIR PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH 541: YGHHHWKDKL NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA 601: VSTVSMQNIH PKSLPSERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN RHTLVADPYE 661: EAWNQMLLRR QKARQLEQKI NNYLTVPAHK LDSPTMSRAR IGSDPLAYEP KEDLPVITID 721: PASPQSPESV DLVNEELKGK VLGLSRDPAK VAEEDEDDDG GIMMRSKETS SPGTDDVFTP 781: APSDSPSSQR IQRCLSDPGP HPEPGEGEPF FPKGQ