B3AT_HUMAN - dbPTM
B3AT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B3AT_HUMAN
UniProt AC P02730
Protein Name Band 3 anion transport protein
Gene Name SLC4A1
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Cell membrane
Multi-pass membrane protein . Basolateral cell membrane
Multi-pass membrane protein . Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney.
Protein Description Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine..
Protein Sequence MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV
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
1Acetylation-------MEELQDDY
-------CHHHHHHH		9.012790053
8PhosphorylationMEELQDDYEDMMEEN
CHHHHHHHHHHHHHH		23.321998697
21PhosphorylationENLEQEEYEDPDIPE
HHHHHHHHCCCCCCH		25.531998697
29PhosphorylationEDPDIPESQMEEPAA
CCCCCCHHHCCCCCC		29.491998697
39PhosphorylationEEPAAHDTEATATDY
CCCCCCCCCCCCEEC		20.041998697
42PhosphorylationAAHDTEATATDYHTT
CCCCCCCCCEECCCC		24.691998697
44PhosphorylationHDTEATATDYHTTSH
CCCCCCCEECCCCCC		32.511998697
46PhosphorylationTEATATDYHTTSHPG
CCCCCEECCCCCCCC		9.191998697
48PhosphorylationATATDYHTTSHPGTH
CCCEECCCCCCCCCE		24.621998697
49PhosphorylationTATDYHTTSHPGTHK
CCEECCCCCCCCCEE		16.241998697
50PhosphorylationATDYHTTSHPGTHKV
CEECCCCCCCCCEEE		28.921998697
54PhosphorylationHTTSHPGTHKVYVEL
CCCCCCCCEEEEEEH		23.991998697
162O-linked_GlycosylationRALLLKHSHAGELEA
HHHHHHCCCHHHHHH		17.2812556451
181PhosphorylationKPAVLTRSGDPSQPL
CCEEEECCCCCCCCC		42.1728857561
185PhosphorylationLTRSGDPSQPLLPQH
EECCCCCCCCCCCCC		49.5228857561
193PhosphorylationQPLLPQHSSLETQLF
CCCCCCCCCCEEEEE		31.2228857561
194PhosphorylationPLLPQHSSLETQLFC
CCCCCCCCCEEEEEE		28.2728857561
197PhosphorylationPQHSSLETQLFCEQG
CCCCCCEEEEEEECC		35.5528857561
201S-nitrosylationSLETQLFCEQGDGGT
CCEEEEEEECCCCCC		5.3322178444
201S-nitrosocysteineSLETQLFCEQGDGGT
CCEEEEEEECCCCCC		5.33-
208PhosphorylationCEQGDGGTEGHSPSG
EECCCCCCCCCCCCC		44.3028857561
212PhosphorylationDGGTEGHSPSGILEK
CCCCCCCCCCCCHHC		31.4528857561
214PhosphorylationGTEGHSPSGILEKIP
CCCCCCCCCCHHCCC		41.2928857561
224O-linked_GlycosylationLEKIPPDSEATLVLV
HHCCCCCCCCEEEEE		34.6018984734
303PhosphorylationIDAYMAQSRGELLHS
HHHHHHHCHHHHHHH		32.4922817900
317S-nitrosocysteineSLEGFLDCSLVLPPT
HHHCCCCCEEEECCC		3.54-
317S-nitrosylationSLEGFLDCSLVLPPT
HHHCCCCCEEEECCC		3.5422178444
347PhosphorylationRELLRRRYQSSPAKP
HHHHHHHHHCCCCCC		15.7826657352
349PhosphorylationLLRRRYQSSPAKPDS
HHHHHHHCCCCCCCC		29.3823025827
350PhosphorylationLRRRYQSSPAKPDSS
HHHHHHCCCCCCCCC		17.2224972180
356PhosphorylationSSPAKPDSSFYKGLD
CCCCCCCCCCCCCCC		30.7623911959
357PhosphorylationSPAKPDSSFYKGLDL
CCCCCCCCCCCCCCC		39.7223911959
359PhosphorylationAKPDSSFYKGLDLNG
CCCCCCCCCCCCCCC		13.1912070037
402PhosphorylationSDITDAFSPQVLAAV
HCCCCCCCHHHHHHH		19.0226074081
413PhosphorylationLAAVIFIYFAALSPA
HHHHHHHHHHHHCHH		4.0326074081
418PhosphorylationFIYFAALSPAITFGG
HHHHHHHCHHHHHCH		13.94-
422PhosphorylationAALSPAITFGGLLGE
HHHCHHHHHCHHCCH		20.52-
525PhosphorylationRYTQEIFSFLISLIF
HHHHHHHHHHHHHHH		25.46-
642N-linked_GlycosylationPDGFKVSNSSARGWV
CCCEEECCCCCCCEE		42.8610861210
642N-linked_GlycosylationPDGFKVSNSSARGWV
CCCEEECCCCCCCEE		42.8624121512
745PhosphorylationLTVMGKASTPGAAAQ
EEEEEECCCCCHHHH		38.3223286773
745O-linked_GlycosylationLTVMGKASTPGAAAQ
EEEEEECCCCCHHHH		38.3212556449
746PhosphorylationTVMGKASTPGAAAQI
EEEEECCCCCHHHHH		30.5123025827
757UbiquitinationAAQIQEVKEQRISGL
HHHHHHHHHHHHHHH		47.58-
781PhosphorylationILMEPILSRIPLAVL
HHHHHHHHHHHHHHH		28.96-
818PhosphorylationLLFKPPKYHPDVPYV
HHCCCCCCCCCCCCH		25.1028857561
843S-palmitoylationFTGIQIICLAVLWVV
HHHHHHHHHHHHHHH		1.821885574
894PhosphorylationDADDAKATFDEEEGR
CHHHHCCCCCCCCCC		30.801998697
904PhosphorylationEEEGRDEYDEVAMPV
CCCCCCCCCCCCCCC		22.999207478
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
8YPhosphorylationKinaseZAP70P43403
GPS
8YPhosphorylationKinaseSYKP43405
PSP
8YPhosphorylationKinaseLYNP07948
PSP
8YPhosphorylationKinaseSYKQ15046
PhosphoELM
21YPhosphorylationKinaseSYKP43405
PSP
21YPhosphorylationKinaseSYKQ15046
PhosphoELM
21YPhosphorylationKinaseLYNP07948
PSP
42TPhosphorylationKinaseCSNK1A1P48729
GPS
42TPhosphorylationKinaseCK1-FAMILY-GPS
303SPhosphorylationKinaseCK1-FAMILY-GPS
303SPhosphorylationKinaseCSNK1A1P48729
GPS
359YPhosphorylationKinaseSYKQ15046
PhosphoELM
359YPhosphorylationKinaseLYNP07948
PSP
359YPhosphorylationKinaseSYKP43405
PSP
904YPhosphorylationKinaseLYNP07948
PSP
904YPhosphorylationKinaseSYKQ15046
PhosphoELM
904YPhosphorylationKinaseSYKP43405
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B3AT_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 B3AT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NADAP_HUMANSLC4A1APphysical
9422766
B3AT_HUMANSLC4A1physical
11049968
CAH4_HUMANCA4physical
11994299
CAH2_HUMANCA2physical
9774471
ANK1_HUMANANK1physical
8227202
CALX_HUMANCANXphysical
10364201
CAH2_HUMANCA2physical
11063570
CAH2_HUMANCA2physical
10820026
CLUS_HUMANCLUphysical
22016805
HBA_HUMANHBA1physical
22016805
CDN2A_HUMANCDKN2Aphysical
15811326
ARF_HUMANCDKN2Aphysical
15811326
KAT2B_HUMANKAT2Bphysical
28042499
Drug and Disease Associations
Kegg Disease
H00230 Hereditary spherocytosis (SPH)
H00231 Hereditary elliptocytosis (HE)
H00232 Hereditary stomatocytosis (HSt); Dehydrated hereditary stomatocytosis (DHS); Overhydrated hereditary
H00428 Distal renal tubular acidosis (RTA type 1)
OMIM Disease
109270Elliptocytosis 4 (EL4)
612653Spherocytosis 4 (SPH4)
179800Renal tubular acidosis, distal, autosomal dominant (AD-dRTA)
611590Renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA)
611590Renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of B3AT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Orientation of the band 3 polypeptide from human erythrocytemembranes. Identification of NH2-terminal sequence and site ofcarbohydrate attachment.";
Drickamer L.K.;
J. Biol. Chem. 253:7242-7248(1978).
Cited for: PROTEIN SEQUENCE OF 1-3.
Palmitoylation
ReferencePubMed
"Palmitoylation of cysteine 69 from the COOH-terminal of band 3protein in the human erythrocyte membrane. Acylation occurs in themiddle of the consensus sequence of F--I-IICLAVL found in band 3protein and G2 protein of Rift Valley fever virus.";
Okubo K., Hamasaki N., Hara K., Kageura M.;
J. Biol. Chem. 266:16420-16424(1991).
Cited for: PALMITOYLATION AT CYS-843.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-359 AND TYR-904, ANDMASS SPECTROMETRY.
"Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosinekinases in intact human erythrocytes: identification of primary andsecondary phosphorylation sites.";
Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E.,Pinna L.A., Donella-Deana A.;
Blood 96:1550-1557(2000).
Cited for: PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904.
"Phosphorylation sites in human erythrocyte band 3 protein.";
Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E.;
Biochim. Biophys. Acta 1061:253-266(1991).
Cited for: PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46.

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