SL9A1_HUMAN - dbPTM
SL9A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SL9A1_HUMAN
UniProt AC P19634
Protein Name Sodium/hydrogen exchanger 1
Gene Name SLC9A1
Organism Homo sapiens (Human).
Sequence Length 815
Subcellular Localization Membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein. Colocalizes with CHP1 at the reticulum endoplasmic (By similarity). Colocalizes with CHP1 and CHP2 at the
Protein Description 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..
Protein Sequence MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFVVALGGVLVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLFCLIARVLGVLGLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKSLPSERILPALSKDKEEEIRKILRNNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITIDPASPQSPESVDLVNEELKGKVLGLSRDPAKVAEEDEDDDGGIMMRSKETSSPGTDDVFTPAPSDSPSSQRIQRCLSDPGPHPEPGEGEPFFPKGQ
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
5Phosphorylation---MVLRSGICGLSP
---CCCCCCCCCCCH		28.4824719451
11PhosphorylationRSGICGLSPHRIFPS
CCCCCCCCHHHHHHH		12.1624719451
18PhosphorylationSPHRIFPSLLVVVAL
CHHHHHHHHHHHHHH		24.4824719451
42O-linked_GlycosylationHGLQLSPTASTIRSS
CCCCCCCCCHHHCCC		29.84-
42PhosphorylationHGLQLSPTASTIRSS
CCCCCCCCCHHHCCC		29.84-
56O-linked_GlycosylationSEPPRERSIGDVTTA
CCCCCCCCCCCCCCC		26.60-
61O-linked_GlycosylationERSIGDVTTAPPEVT
CCCCCCCCCCCCCCC		23.21-
62O-linked_GlycosylationRSIGDVTTAPPEVTP
CCCCCCCCCCCCCCC		36.69-
68PhosphorylationTTAPPEVTPESRPVN
CCCCCCCCCCCCCCC		21.4822210691
68O-linked_GlycosylationTTAPPEVTPESRPVN
CCCCCCCCCCCCCCC		21.48-
75N-linked_GlycosylationTPESRPVNHSVTDHG
CCCCCCCCCCCCCCC		25.138068684
79O-linked_GlycosylationRPVNHSVTDHGMKPR
CCCCCCCCCCCCCCC		25.87OGP
79PhosphorylationRPVNHSVTDHGMKPR
CCCCCCCCCCCCCCC		25.8722210691
96PhosphorylationFPVLGIDYTHVRTPF
CCEECCCCCCCCCHH		9.23-
158PhosphorylationETPPFLQSDVFFLFL
CCCCCCCCCCHHHHC		37.58-
342PhosphorylationFLYSYMAYLSAELFH
HHHHHHHHHHHHHHH		5.6725693802
344PhosphorylationYSYMAYLSAELFHLS
HHHHHHHHHHHHHHH		13.6625693802
351PhosphorylationSAELFHLSGIMALIA
HHHHHHHHHHHHHHH		20.0825693802
359PhosphorylationGIMALIASGVVMRPY
HHHHHHHCCCCCCCE		25.7325693802
372PhosphorylationPYVEANISHKSHTTI
CEEEEECCCCCHHHH		25.3522964224
559UbiquitinationRFNKKYVKKCLIAGE
HHCHHHHHHHHHCCC		34.38-
560UbiquitinationFNKKYVKKCLIAGER
HCHHHHHHHHHCCCC		24.99-
577PhosphorylationEPQLIAFYHKMEMKQ
CCCHHHHHHHHHHHH		7.4825159151
583UbiquitinationFYHKMEMKQAIELVE
HHHHHHHHHHHHHHH		24.2221906983
583 (in isoform 1)Ubiquitination-24.2221890473
599PhosphorylationGGMGKIPSAVSTVSM
CCCCCCCCCCEEEEC		44.7930266825
602PhosphorylationGKIPSAVSTVSMQNI
CCCCCCCEEEECCCC		23.8629255136
603PhosphorylationKIPSAVSTVSMQNIH
CCCCCCEEEECCCCC		15.2530266825
605PhosphorylationPSAVSTVSMQNIHPK
CCCCEEEECCCCCCC		18.1029255136
612 (in isoform 1)Ubiquitination-50.9221890473
612UbiquitinationSMQNIHPKSLPSERI
ECCCCCCCCCCHHHH		50.9221890473
612UbiquitinationSMQNIHPKSLPSERI
ECCCCCCCCCCHHHH		50.9221890473
616PhosphorylationIHPKSLPSERILPAL
CCCCCCCHHHHHHHH		44.8124670416
624PhosphorylationERILPALSKDKEEEI
HHHHHHHCCCHHHHH		40.7023403867
625UbiquitinationRILPALSKDKEEEIR
HHHHHHCCCHHHHHH		73.92-
648PhosphorylationKTRQRLRSYNRHTLV
HHHHHHHHCCCCCCC		31.2018757828
649PhosphorylationTRQRLRSYNRHTLVA
HHHHHHHCCCCCCCC		15.1328122231
653PhosphorylationLRSYNRHTLVADPYE
HHHCCCCCCCCCHHH		21.4924501219
659PhosphorylationHTLVADPYEEAWNQM
CCCCCCHHHHHHHHH		27.2728796482
683PhosphorylationLEQKINNYLTVPAHK
HHHHHHHHCCCCHHH		10.1623927012
685PhosphorylationQKINNYLTVPAHKLD
HHHHHHCCCCHHHCC		17.6823401153
693PhosphorylationVPAHKLDSPTMSRAR
CCHHHCCCCCHHCCC		32.4829255136
695PhosphorylationAHKLDSPTMSRARIG
HHHCCCCCHHCCCCC		31.5623927012
697O-linked_GlycosylationKLDSPTMSRARIGSD
HCCCCCHHCCCCCCC		25.8530379171
697PhosphorylationKLDSPTMSRARIGSD
HCCCCCHHCCCCCCC		25.8523927012
703PhosphorylationMSRARIGSDPLAYEP
HHCCCCCCCCCCCCC		33.4119664994
708PhosphorylationIGSDPLAYEPKEDLP
CCCCCCCCCCCCCCC		40.2123927012
718PhosphorylationKEDLPVITIDPASPQ
CCCCCEEEECCCCCC		21.4028176443
723PhosphorylationVITIDPASPQSPESV
EEEECCCCCCCCHHH		28.9426055452
726PhosphorylationIDPASPQSPESVDLV
ECCCCCCCCHHHHCC		33.7426055452
729PhosphorylationASPQSPESVDLVNEE
CCCCCCHHHHCCCHH		25.0628176443
738 (in isoform 1)Ubiquitination-61.0221890473
738UbiquitinationDLVNEELKGKVLGLS
HCCCHHHCCHHHCCC		61.0221906983
750 (in isoform 1)Ubiquitination-47.5721890473
750UbiquitinationGLSRDPAKVAEEDED
CCCCCHHHHCCCCCC		47.5721906983
766PhosphorylationDGGIMMRSKETSSPG
CCCEEEEEECCCCCC		19.5623927012
769PhosphorylationIMMRSKETSSPGTDD
EEEEEECCCCCCCCC		37.9430278072
770PhosphorylationMMRSKETSSPGTDDV
EEEEECCCCCCCCCC		35.3123927012
771PhosphorylationMRSKETSSPGTDDVF
EEEECCCCCCCCCCC		34.4730278072
774PhosphorylationKETSSPGTDDVFTPA
ECCCCCCCCCCCCCC		32.2023927012
779PhosphorylationPGTDDVFTPAPSDSP
CCCCCCCCCCCCCCC		20.5623927012
783PhosphorylationDVFTPAPSDSPSSQR
CCCCCCCCCCCCHHH		53.4823927012
785PhosphorylationFTPAPSDSPSSQRIQ
CCCCCCCCCCHHHHH		30.9023927012
787PhosphorylationPAPSDSPSSQRIQRC
CCCCCCCCHHHHHHH		42.9523927012
788PhosphorylationAPSDSPSSQRIQRCL
CCCCCCCHHHHHHHH		27.1923927012
796PhosphorylationQRIQRCLSDPGPHPE
HHHHHHHCCCCCCCC		45.4423401153
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
648SPhosphorylationKinaseAKT1P31749
PSP
648SPhosphorylationKinaseAKT-FAMILY-GPS
653TPhosphorylationKinaseBRAFP15056
PSP
653TPhosphorylationKinaseROCK2O75116
PSP
653TPhosphorylationKinaseROCK1Q13464
PSP
693SPhosphorylationKinaseMAPK1P28482
GPS
703SPhosphorylationKinaseRSK_GROUP-PhosphoELM
703SPhosphorylationKinaseAKT1P31749
PSP
703SPhosphorylationKinaseRSK-SUBFAMILY-GPS
703SPhosphorylationKinaseRPS6KA1Q15418
GPS
718TPhosphorylationKinaseMAPK14Q16539
GPS
723SPhosphorylationKinaseMAPK14Q16539
GPS
723SPhosphorylationKinaseMAPK1P28482
GPS
726SPhosphorylationKinaseMAPK1P28482
GPS
726SPhosphorylationKinaseMAPK14Q16539
GPS
729SPhosphorylationKinaseMAPK14Q16539
GPS
770SPhosphorylationKinaseMAPK1P28482
GPS
771SPhosphorylationKinaseMAPK1P28482
GPS
779TPhosphorylationKinaseMAPK1P28482
GPS
785SPhosphorylationKinaseMAPK1P28482
GPS
796SPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:20855896
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SL9A1_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 SL9A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHP3_HUMANTESCphysical
12809501
CHP2_HUMANCHP2physical
12576672
CHP1_HUMANCHP1physical
12576672
CHP1_HUMANCHP1physical
8901634
CHP1_HUMANCHP1physical
11350981
DAXX_HUMANDAXXphysical
18003619
M3K14_HUMANMAP3K14physical
11369779
AKT1_HUMANAKT1physical
27751915
CHP1_HUMANCHP1physical
27751915
HSP74_HUMANHSPA4physical
27751915
HS90A_HUMANHSP90AA1physical
27751915
ENOA_HUMANENO1physical
27751915
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616291Lichtenstein-Knorr syndrome (LIKNS)
Kegg Drug
D03406 Cariporide mesylate (USAN)
D09036 Zoniporide mesylate (INN/USAN)
DrugBank
DB00594Amiloride
Regulatory Network of SL9A1_HUMAN

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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
"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.
"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.
"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.
"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.

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