SL9A1_MOUSE - dbPTM
SL9A1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SL9A1_MOUSE
UniProt AC Q61165
Protein Name Sodium/hydrogen exchanger 1
Gene Name Slc9a1
Organism Mus musculus (Mouse).
Sequence Length 820
Subcellular Localization Membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein. Colocalizes with CHP1 and CHP2 at the reticulum endoplasmic and plasma membrane..
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 MMLRWSGVWGFHPPRIFPSLLVVVALVGLLPVLRSHGLQHSPTASTIRGSEPPRERSIGDVTTAPSEPLHRPDDHNLTNLIIEHGGKPSRKAFPVLDIDYPHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLLYAVCLVGGEQINNIGLLDTLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFASYDSVGISDIFLGFLSFFVVALGGVFVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHQWNWTFVISTLLFCLIARVLGVLVLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKAVTSDRILPALSKDKEEEIRKILRSNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKITNYLTVPAHKLDSPTLSRARIGSDPLAYEPKADLPVITIDPASPQSPESVDLVNEELKGKVLGLNRGPRVTPEEEEEDEDGIIMIRSKEPSSPGTDDVFTPGSSDSPSSQRIQRCLSDPGPHPEPGEGEPFIPKGQ
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
41PhosphorylationRSHGLQHSPTASTIR
HHCCCCCCCCCHHCC		15.8130165576
43PhosphorylationHGLQHSPTASTIRGS
CCCCCCCCCHHCCCC		35.9330165576
45PhosphorylationLQHSPTASTIRGSEP
CCCCCCCHHCCCCCC		27.1830165576
46PhosphorylationQHSPTASTIRGSEPP
CCCCCCHHCCCCCCC		16.5430165576
374N-linked_GlycosylationMRPYVEANISHKSHT
CCCEEEEECCCCCHH		23.84-
573UbiquitinationLIAGERSKEPQLIAF
HHCCCCCCCCCHHHH		78.58-
581PhosphorylationEPQLIAFYHKMEMKQ
CCCHHHHHHHHHHHH		7.4829514104
595PhosphorylationQAIELVESGGMGKIP
HHHHHHHCCCCCCCC		32.9225338131
603PhosphorylationGGMGKIPSAVSTVSM
CCCCCCCCCCEEEEC		44.7925521595
606PhosphorylationGKIPSAVSTVSMQNI
CCCCCCCEEEECCCC		23.8625521595
607PhosphorylationKIPSAVSTVSMQNIH
CCCCCCEEEECCCCC		15.2527087446
609PhosphorylationPSAVSTVSMQNIHPK
CCCCEEEECCCCCCC		18.1025521595
610OxidationSAVSTVSMQNIHPKA
CCCEEEECCCCCCCC		2.8417242355
616UbiquitinationSMQNIHPKAVTSDRI
ECCCCCCCCCCCCCC		41.13-
628PhosphorylationDRILPALSKDKEEEI
CCCHHHCCCCHHHHH		40.7029472430
641PhosphorylationEIRKILRSNLQKTRQ
HHHHHHHHHHHHHHH		38.15-
657PhosphorylationLRSYNRHTLVADPYE
HHHCCCCCCCCCHHH		21.4927600695
685PhosphorylationRQLEQKITNYLTVPA
HHHHHHHHHHCCCCH		25.5024068923
687PhosphorylationLEQKITNYLTVPAHK
HHHHHHHHCCCCHHH		8.6325159016
689PhosphorylationQKITNYLTVPAHKLD
HHHHHHCCCCHHHCC		17.6822942356
697PhosphorylationVPAHKLDSPTLSRAR
CCHHHCCCCCHHCCC		30.1627087446
699PhosphorylationAHKLDSPTLSRARIG
HHHCCCCCHHCCCCC		41.1225521595
701PhosphorylationKLDSPTLSRARIGSD
HCCCCCHHCCCCCCC		26.7727742792
707PhosphorylationLSRARIGSDPLAYEP
HHCCCCCCCCCCCCC		33.4124925903
712PhosphorylationIGSDPLAYEPKADLP
CCCCCCCCCCCCCCC		40.2128833060
722PhosphorylationKADLPVITIDPASPQ
CCCCCEEEECCCCCC		21.4024925903
727PhosphorylationVITIDPASPQSPESV
EEEECCCCCCCCHHH		28.9424925903
730PhosphorylationIDPASPQSPESVDLV
ECCCCCCCCHHHHCC		33.7424925903
733PhosphorylationASPQSPESVDLVNEE
CCCCCCHHHHCCCHH		25.0624925903
755PhosphorylationLNRGPRVTPEEEEED
CCCCCCCCCHHHCCC		26.6822942356
771PhosphorylationDGIIMIRSKEPSSPG
CCEEEEEECCCCCCC		30.3725619855
775PhosphorylationMIRSKEPSSPGTDDV
EEEECCCCCCCCCCC		50.7025619855
776PhosphorylationIRSKEPSSPGTDDVF
EEECCCCCCCCCCCC		37.7627742792
779PhosphorylationKEPSSPGTDDVFTPG
CCCCCCCCCCCCCCC		32.2027087446
784PhosphorylationPGTDDVFTPGSSDSP
CCCCCCCCCCCCCCC		26.9627087446
787PhosphorylationDDVFTPGSSDSPSSQ
CCCCCCCCCCCCCHH		31.9825521595
788PhosphorylationDVFTPGSSDSPSSQR
CCCCCCCCCCCCHHH		48.2825521595
790PhosphorylationFTPGSSDSPSSQRIQ
CCCCCCCCCCHHHHH		28.7327087446
792PhosphorylationPGSSDSPSSQRIQRC
CCCCCCCCHHHHHHH		42.9527087446
793PhosphorylationGSSDSPSSQRIQRCL
CCCCCCCHHHHHHHH		27.1927087446
801PhosphorylationQRIQRCLSDPGPHPE
HHHHHHHCCCCCCCC		45.4425521595
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

Oops, there are no upstream regulatory protein records of SL9A1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SL9A1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SL9A1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SL9A1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707 AND THR-755, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-606 ANDSER-609, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND MASSSPECTROMETRY.

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