S4A8_HUMAN - dbPTM
S4A8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S4A8_HUMAN
UniProt AC Q2Y0W8
Protein Name Electroneutral sodium bicarbonate exchanger 1
Gene Name SLC4A8 {ECO:0000312|EMBL:AAY79176.1, ECO:0000312|HGNC:HGNC:11034}
Organism Homo sapiens (Human).
Sequence Length 1093
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1. Plays a major role in pH regulation in neurons. May be involved in cell pH regulation by transporting HCO3(-) from blood to cell. Enhanced expression in severe acid stress could be important for cell survival by mediating the influx of HCO3(-) into the cells. Also mediates lithium-dependent HCO3(-) cotransport. May be regulated by osmolarity..
Protein Sequence MPAAGSNEPDGVLSYQRPDEEAVVDQGGTSTILNIHYEKEELEGHRTLYVGVRMPLGRQSHRHHRTHGQKHRRRGRGKGASQGEEGLEALAHDTPSQRVQFILGTEEDEEHVPHELFTELDEICMKEGEDAEWKETARWLKFEEDVEDGGERWSKPYVATLSLHSLFELRSCLINGTVLLDMHANSIEEISDLILDQQELSSDLNDSMRVKVREALLKKHHHQNEKKRNNLIPIVRSFAEVGKKQSDPHLMDKHGQTVSPQSVPTTNLEVKNGVNCEHSPVDLSKVDLHFMKKIPTGAEASNVLVGEVDILDRPIVAFVRLSPAVLLSGLTEVPIPTRFLFILLGPVGKGQQYHEIGRSMATIMTDEIFHDVAYKAKERDDLLAGIDEFLDQVTVLPPGEWDPSIRIEPPKNVPSQEKRKMPGVPNGNVCHIEQEPHGGHSGPELQRTGRLFGGLVLDIKRKAPWYWSDYRDALSLQCLASFLFLYCACMSPVITFGGLLGEATEGRISAIESLFGASMTGIAYSLFAGQALTILGSTGPVLVFEKILFKFCKDYALSYLSLRACIGLWTAFLCIVLVATDASSLVCYITRFTEEAFASLICIIFIYEAIEKLIHLAETYPIHMHSQLDHLSLYYCRCTLPENPNNHTLQYWKDHNIVTAEVHWANLTVSECQEMHGEFMGSACGHHGPYTPDVLFWSCILFFTTFILSSTLKTFKTSRYFPTRVRSMVSDFAVFLTIFTMVIIDFLIGVPSPKLQVPSVFKPTRDDRGWIINPIGPNPWWTVIAAIIPALLCTILIFMDQQITAVIINRKEHKLKKGCGYHLDLLMVAIMLGVCSIMGLPWFVAATVLSITHVNSLKLESECSAPGEQPKFLGIREQRVTGLMIFVLMGCSVFMTAILKFIPMPVLYGVFLYMGVSSLQGIQFFDRLKLFGMPAKHQPDFIYLRHVPLRKVHLFTLIQLTCLVLLWVIKASPAAIVFPMMVLALVFVRKVMDLCFSKRELSWLDDLMPESKKKKLDDAKKKAKEEEEAEKMLEIGGDKFPLESRKLLSSPGKNISCRCDPSEINISDEMPKTTVWKALSMNSGNAKEKSLFN
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
6Phosphorylation--MPAAGSNEPDGVL
--CCCCCCCCCCCCE		33.0424043423
14PhosphorylationNEPDGVLSYQRPDEE
CCCCCCEEECCCCCC		19.4724043423
15PhosphorylationEPDGVLSYQRPDEEA
CCCCCEEECCCCCCC		12.3624043423
25UbiquitinationPDEEAVVDQGGTSTI
CCCCCEECCCCCEEE		34.5032142685
49PhosphorylationLEGHRTLYVGVRMPL
HCCCCEEEEEEECCC		8.4425884760
78UbiquitinationHRRRGRGKGASQGEE
HCCCCCCCCCCCCHH		50.3632142685
81PhosphorylationRGRGKGASQGEEGLE
CCCCCCCCCCHHHHH		47.5924173317
157PhosphorylationGERWSKPYVATLSLH
CCCCCCCEEEEEEHH		13.37-
160PhosphorylationWSKPYVATLSLHSLF
CCCCEEEEEEHHHHH		13.56-
184PhosphorylationTVLLDMHANSIEEIS
EEEEECCCCCHHHHH		12.5832142685
237PhosphorylationNLIPIVRSFAEVGKK
CHHHHHHHHHHHCCC		20.2230266825
246PhosphorylationAEVGKKQSDPHLMDK
HHHCCCCCCCCCCCC		63.0930266825
259PhosphorylationDKHGQTVSPQSVPTT
CCCCCCCCCCCCCCC		22.1725307156
279PhosphorylationNGVNCEHSPVDLSKV
CCCCCCCCCCCHHHC		12.3430266825
284PhosphorylationEHSPVDLSKVDLHFM
CCCCCCHHHCCHHHH		26.6030266825
301PhosphorylationIPTGAEASNVLVGEV
CCCCCHHHCCEEEEE		20.9822817900
404PhosphorylationPPGEWDPSIRIEPPK
CCCCCCCCCCCCCCC		23.2526074081
407UbiquitinationEWDPSIRIEPPKNVP
CCCCCCCCCCCCCCC		9.93-
460UbiquitinationGGLVLDIKRKAPWYW
CCEEEEEHHHCCCCC		47.73-
475PhosphorylationSDYRDALSLQCLASF
CCHHHHHHHHHHHHH		20.3627461979
481PhosphorylationLSLQCLASFLFLYCA
HHHHHHHHHHHHHHH		14.9927461979
486PhosphorylationLASFLFLYCACMSPV
HHHHHHHHHHHHCCC		3.1727461979
491PhosphorylationFLYCACMSPVITFGG
HHHHHHHCCCCCCCH		18.8527461979
495PhosphorylationACMSPVITFGGLLGE
HHHCCCCCCCHHHCC		19.2327461979
504PhosphorylationGGLLGEATEGRISAI
CHHHCCCCHHHHHHH		34.3727461979
619PhosphorylationKLIHLAETYPIHMHS
HHHHHHHHCCCCCCC		29.0524043423
620PhosphorylationLIHLAETYPIHMHSQ
HHHHHHHCCCCCCCC		7.5324043423
626PhosphorylationTYPIHMHSQLDHLSL
HCCCCCCCCCCCEEE		25.5124043423
632PhosphorylationHSQLDHLSLYYCRCT
CCCCCCEEEEEEEEC		15.7724043423
634PhosphorylationQLDHLSLYYCRCTLP
CCCCEEEEEEEECCC		9.3524043423
635PhosphorylationLDHLSLYYCRCTLPE
CCCEEEEEEEECCCC		4.4424043423
639PhosphorylationSLYYCRCTLPENPNN
EEEEEEECCCCCCCC		26.4629978859
648PhosphorylationPENPNNHTLQYWKDH
CCCCCCCCEEEECCC		20.0629978859
651PhosphorylationPNNHTLQYWKDHNIV
CCCCCEEEECCCCEE		19.9629978859
717PhosphorylationSTLKTFKTSRYFPTR
HHHHHHCCCCCCCHH		17.78-
718PhosphorylationTLKTFKTSRYFPTRV
HHHHHCCCCCCCHHH		26.10-
727PhosphorylationYFPTRVRSMVSDFAV
CCCHHHHHHHHHHHH		22.2224275569
730PhosphorylationTRVRSMVSDFAVFLT
HHHHHHHHHHHHHHH		20.5424275569
752PhosphorylationDFLIGVPSPKLQVPS
HHHHCCCCCCCCCCC		32.0624719451
764PhosphorylationVPSVFKPTRDDRGWI
CCCCCCCCCCCCCEE		47.5228555341
943PhosphorylationKHQPDFIYLRHVPLR
CCCCCEEEEECCCCC		9.55-
959 (in isoform 5)Ubiquitination-33.5621906983
959 (in isoform 4)Ubiquitination-33.5621906983
971AcetylationVLLWVIKASPAAIVF
HHHHHHHHCHHHHHH		15.0419608861
981 (in isoform 4)Phosphorylation-1.9724043423
983 (in isoform 4)Phosphorylation-1.3324043423
987 (in isoform 4)Phosphorylation-4.5924043423
989 (in isoform 4)Phosphorylation-17.8724043423
1002PhosphorylationCFSKRELSWLDDLMP
HCCHHHHHHHHHHCC		22.3529083192
1011PhosphorylationLDDLMPESKKKKLDD
HHHHCCHHHHHCHHH		43.8529083192
1012 (in isoform 3)Ubiquitination-67.9321906983
1012 (in isoform 1)Ubiquitination-67.9321906983
1012UbiquitinationDDLMPESKKKKLDDA
HHHCCHHHHHCHHHH		67.93-
1024AcetylationDDAKKKAKEEEEAEK
HHHHHHHHHHHHHHH		74.6419608861
1034 (in isoform 3)Phosphorylation-35.7724043423
1036 (in isoform 3)Phosphorylation-28.9524043423
1039AcetylationMLEIGGDKFPLESRK
HHHHCCCCCCHHHHH		52.7511925327
1039 (in isoform 2)Ubiquitination-52.7521906983
1040 (in isoform 3)Phosphorylation-11.2624043423
1042 (in isoform 3)Phosphorylation-11.9824043423
1049PhosphorylationLESRKLLSSPGKNIS
HHHHHHHCCCCCCCE		44.9430266825
1050PhosphorylationESRKLLSSPGKNISC
HHHHHHCCCCCCCEE		37.3329514088
1056PhosphorylationSSPGKNISCRCDPSE
CCCCCCCEEECCHHH		12.61-
1061 (in isoform 2)Phosphorylation-37.1724043423
1063 (in isoform 2)Phosphorylation-45.5024043423
1067 (in isoform 2)Phosphorylation-24.0324043423
1067PhosphorylationDPSEINISDEMPKTT
CHHHCCCCCCCCCCH		24.03-
1069 (in isoform 2)Phosphorylation-51.0624043423
1080PhosphorylationTTVWKALSMNSGNAK
CHHHHHHHCCCCCCC		22.3024173317
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 S4A8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S4A8_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 S4A8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADCK2_HUMANADCK2physical
28514442
ADCY3_HUMANADCY3physical
28514442
AT2A3_HUMANATP2A3physical
28514442
SNX14_HUMANSNX14physical
28514442
CSCL2_HUMANTMEM63Bphysical
28514442
MRP4_HUMANABCC4physical
28514442
CA043_HUMANC1orf43physical
28514442
PCX3_HUMANPCNXL3physical
28514442
S12A6_HUMANSLC12A6physical
28514442
ULBP2_HUMANULBP2physical
28514442
GHDC_HUMANGHDCphysical
28514442
ST7L_HUMANST7Lphysical
28514442
S4A7_HUMANSLC4A7physical
28514442
GBB2_HUMANGNB2physical
28514442
AT132_HUMANATP13A2physical
28514442
EMC7_HUMANEMC7physical
28514442
TMX2_HUMANTMX2physical
28514442
EMC3_HUMANEMC3physical
28514442
RASN_HUMANNRASphysical
28514442
ATG9A_HUMANATG9Aphysical
28514442
CSCL1_HUMANTMEM63Aphysical
28514442
B3A2_HUMANSLC4A2physical
28514442
LCLT1_HUMANLCLAT1physical
28514442
SRBP2_HUMANSREBF2physical
28514442
OMA1_HUMANOMA1physical
28514442
FYN_HUMANFYNphysical
28514442
REN3B_HUMANUPF3Bphysical
28514442
GPHRA_HUMANGPR89Bphysical
28514442
GPHRB_HUMANGPR89Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S4A8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-237, AND MASSSPECTROMETRY.

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