Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Sodium/hydrogen exchanger 1  

UniProtKB / Swiss-Prot ID :  SL9A1_HUMAN

Gene Name (Synonyms) : 
SLC9A1, APNH1, NHE1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Membrane; Multi-pass membrane protein. 

Protein Function :  Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. 

Transmembrane Topology (topPTM) : SL9A1_HUMAN 

Protein Sequence MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPE...
Predicted Secondary Structure CCEECCCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
682N -> K (in dbSNP:rs35703140). VAR_050231
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
75N-linked (GlcNAc...).SRPVNHSVT
CCCCCCCCC
25.13UniProtKB
Link-
583Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KMEMKQAIE
HHCHHHHHH
24.22Phosphositeplus
Link-
602PhosphoserinePSAVSTVSM
CCCCCCCCC
23.86Phosphositeplus
Link-
603PhosphothreonineSAVSTVSMQ
CCCCCCCCC
15.25Phosphositeplus
Link-
605PhosphoserineVSTVSMQNI
CCCCCCCCC
18.10Phosphositeplus
Link-
612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NIHPKSLPS
CCCCCCCHH
50.92Phosphositeplus
Link-
648PhosphoserineQRLRSYNRH
HHHHHHHHC
31.20Phosphositeplus
Link-
659PhosphotyrosineVADPYEEAW
CCCHHHHHH
27.27Phosphositeplus
Link-
683PhosphotyrosineKINNYLTVP
HHCCCCCCC
10.16HPRD
Link-
683PhosphotyrosineKINNYLTVP
HHCCCCCCC
10.16Phosphositeplus
Link-
683PhosphotyrosineKINNYLTVP
HHCCCCCCC
10.16SysPTM
Link-
685PhosphothreonineNNYLTVPAH
CCCCCCCCC
17.68Phosphositeplus
Link-
693PhosphoserineHKLDSPTMS
CCCCCHHHH
32.48PhosphoELM
Link-
693PhosphoserineHKLDSPTMS
CCCCCHHHH
32.48Phosphositeplus
Link-
693Phosphoserine (MAPK1)HKLDSPTMS
CCCCCHHHH
32.48HPRD
Link-
695PhosphothreonineLDSPTMSRA
CCCHHHHHH
31.56HPRD
Link-
695PhosphothreonineLDSPTMSRA
CCCHHHHHH
31.56PhosphoELM
Link-
695PhosphothreonineLDSPTMSRA
CCCHHHHHH
31.56Phosphositeplus
Link-
695PhosphothreonineLDSPTMSRA
CCCHHHHHH
31.56SysPTM
Link-
695Phosphothreonine.LDSPTMSRA
CCCHHHHHH
31.56UniProtKB
Link-
697PhosphoserineSPTMSRARI
CHHHHHHHC
25.85HPRD
Link-
697PhosphoserineSPTMSRARI
CHHHHHHHC
25.85PhosphoELM
Link-
697PhosphoserineSPTMSRARI
CHHHHHHHC
25.85Phosphositeplus
Link-
697PhosphoserineSPTMSRARI
CHHHHHHHC
25.85SysPTM
Link-
697Phosphoserine.SPTMSRARI
CHHHHHHHC
25.85UniProtKB
Link-
703PhosphoserineARIGSDPLA
HHCCCCCCC
33.41HPRD
Link-
703PhosphoserineARIGSDPLA
HHCCCCCCC
33.41Phosphositeplus
Link-
703PhosphoserineARIGSDPLA
HHCCCCCCC
33.41SysPTM
Link-
703Phosphoserine (RSK_group)ARIGSDPLA
HHCCCCCCC
33.41PhosphoELM
Link-
703Phosphoserine.ARIGSDPLA
HHCCCCCCC
33.41UniProtKB
Link-
718PhosphothreonineLPVITIDPA
CCEEEECCC
21.40Phosphositeplus
Link-
718Phosphothreonine (MAPK14)LPVITIDPA
CCEEEECCC
21.40HPRD
Link-
718Phosphothreonine (MAPK14)LPVITIDPA
CCEEEECCC
21.40PhosphoELM
Link-
723PhosphoserineIDPASPQSP
ECCCCCCCC
28.94Phosphositeplus
Link-
723PhosphoserineIDPASPQSP
ECCCCCCCC
28.94SysPTM
Link-
723Phosphoserine (MAPK14)IDPASPQSP
ECCCCCCCC
28.94HPRD
Link-
723Phosphoserine (MAPK14)IDPASPQSP
ECCCCCCCC
28.94PhosphoELM
Link-
723Phosphoserine.IDPASPQSP
ECCCCCCCC
28.94UniProtKB
Link-
726PhosphoserineASPQSPESV
CCCCCCCCC
33.74Phosphositeplus
Link-
726PhosphoserineASPQSPESV
CCCCCCCCC
33.74SysPTM
Link-
726Phosphoserine (MAPK14)ASPQSPESV
CCCCCCCCC
33.74HPRD
Link-
726Phosphoserine (MAPK14)ASPQSPESV
CCCCCCCCC
33.74PhosphoELM
Link-
726Phosphoserine.ASPQSPESV
CCCCCCCCC
33.74UniProtKB
Link-
729PhosphoserineQSPESVDLV
CCCCCCCCC
25.06Phosphositeplus
Link-
729PhosphoserineQSPESVDLV
CCCCCCCCC
25.06SysPTM
Link-
729Phosphoserine (MAPK14)QSPESVDLV
CCCCCCCCC
25.06HPRD
Link-
729Phosphoserine (MAPK14)QSPESVDLV
CCCCCCCCC
25.06PhosphoELM
Link-
729Phosphoserine.QSPESVDLV
CCCCCCCCC
25.06UniProtKB
Link-
738Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NEELKGKVL
CCCHHHHHC
61.02Phosphositeplus
Link-
750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RDPAKVAEE
CCCCCCCCC
47.57Phosphositeplus
Link-
766Phosphoserine (MAPK1)IMMRSKETS
CCCCCCCCC
19.56HPRD
Link-
770PhosphoserineSKETSSPGT
CCCCCCCCC
35.31PhosphoELM
Link-
770PhosphoserineSKETSSPGT
CCCCCCCCC
35.31Phosphositeplus
Link-
770Phosphoserine (MAPK1)SKETSSPGT
CCCCCCCCC
35.31HPRD
Link-
771PhosphoserineKETSSPGTD
CCCCCCCCC
34.47HPRD
Link-
771PhosphoserineKETSSPGTD
CCCCCCCCC
34.47PhosphoELM
Link-
771PhosphoserineKETSSPGTD
CCCCCCCCC
34.47Phosphositeplus
Link-
779Phosphothreonine (MAPK1)DDVFTPAPS
CCCCCCCCC
20.56HPRD
Link-
783PhosphoserineTPAPSDSPS
CCCCCCCCC
53.48HPRD
Link-
783PhosphoserineTPAPSDSPS
CCCCCCCCC
53.48PhosphoELM
Link-
783PhosphoserineTPAPSDSPS
CCCCCCCCC
53.48Phosphositeplus
Link-
785PhosphoserineAPSDSPSSQ
CCCCCCCHH
30.90PhosphoELM
Link-
785PhosphoserineAPSDSPSSQ
CCCCCCCHH
30.90Phosphositeplus
Link-
785PhosphoserineAPSDSPSSQ
CCCCCCCHH
30.90SysPTM
Link-
785Phosphoserine (MAPK1)APSDSPSSQ
CCCCCCCHH
30.90HPRD
Link-
785Phosphoserine.APSDSPSSQ
CCCCCCCHH
30.90UniProtKB
Link-
787PhosphoserineSDSPSSQRI
CCCCCHHHH
42.95HPRD
Link-
787PhosphoserineSDSPSSQRI
CCCCCHHHH
42.95PhosphoELM
Link-
787PhosphoserineSDSPSSQRI
CCCCCHHHH
42.95Phosphositeplus
Link-
787Phosphoserine.SDSPSSQRI
CCCCCHHHH
42.95UniProtKB
Link-
788PhosphoserineDSPSSQRIQ
CCCCHHHHH
27.19HPRD
Link-
788PhosphoserineDSPSSQRIQ
CCCCHHHHH
27.19PhosphoELM
Link-
788PhosphoserineDSPSSQRIQ
CCCCHHHHH
27.19Phosphositeplus
Link-
788Phosphoserine.DSPSSQRIQ
CCCCHHHHH
27.19UniProtKB
Link-
796PhosphoserineQRCLSDPGP
HHHHHCCCC
45.44Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MDFI_HUMANphysical interactionMINT-66368MINT16189514
MDFI_HUMANyeast 2-hybridHPRD:00123HPRD16189514
MK03_HUMANENSP00000263980STRING
CALM_HUMANENSP00000263980STRING
CAH2_HUMANENSP00000263980STRING
ETV5_HUMANENSP00000263980STRING
CHP1_HUMANENSP00000263980STRING
CHP1_HUMANENSP00000263980STRING
EZRI_HUMANENSP00000263980STRING
RADI_HUMANENSP00000263980STRING
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Disease Reference
Kegg disease
OMIM disease
616291Lichtenstein-Knorr syndrome (LIKNS)
Drug Reference
Kegg drug
D03406 Cariporide mesylate (USAN)
D09036 Zoniporide mesylate (INN/USAN)
DrugBank
DB00594Amiloride
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylationrestricted to the first N-terminal extracellular domain.";
Counillon L., Pouyssegur J., Reithmeier R.A.;
Biochemistry 33:10463-10469(1994).
Cited for: GLYCOSYLATION AT ASN-75, AND O-LINKED GLYCOSYLATION.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787 AND SER-788, ANDMASS SPECTROMETRY.
"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 THR-695; SER-703 ANDSER-785, AND MASS SPECTROMETRY.
"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-697; SER-703; SER-723;SER-726; SER-729 AND SER-785, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures