B3AT_MOUSE - dbPTM
B3AT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B3AT_MOUSE
UniProt AC P04919
Protein Name Band 3 anion transport protein
Gene Name Slc4a1
Organism Mus musculus (Mouse).
Sequence Length 929
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 MGDMRDHEEVLEIPDRDSEEELENIIGQIAYRDLTIPVTEMQDPEALPTEQTATDYVPSSTSTPHPSSGQVYVELQELMMDQRNQELQWVEAAHWIGLEENLREDGVWGRPHLSYLTFWSLLELQKVFSKGTFLLGLAETSLAGVANHLLDCFIYEDQIRPQDREELLRALLLKRSHAEDLGNLEGVKPAVLTRSGGASEPLLPHQPSLETQLYCGQAEGGSEGPSTSGTLKIPPDSETTLVLVGRANFLEKPVLGFVRLKEAVPLEDLVLPEPVGFLLVLLGPEAPHVDYTQLGRAAATLMTERVFRITASMAHNREELLRSLESFLDCSLVLPPTDAPSEKALLNLVPVQKELLRRRYLPSPAKPDPNLYNTLDLNGGKGGPGDEDDPLRRTGRIFGGLIRDIRRRYPYYLSDITDALSPQVLAAVIFIYFAALSPAVTFGGLLGEKTRNLMGVSELLISTAVQGILFALLGAQPLLVLGFSGPLLVFEEAFFSFCESNNLEYIVGRAWIGFWLILLVMLVVAFEGSFLVQYISRYTQEIFSFLISLIFIYETFSKLIKIFQDYPLQQTYAPVVMKPKPQGPVPNTALFSLVLMAGTFLLAMTLRKFKNSTYFPGKLRRVIGDFGVPISILIMVLVDSFIKGTYTQKLSVPDGLKVSNSSARGWVIHPLGLYRLFPTWMMFASVLPALLVFILIFLESQITTLIVSKPERKMIKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPFVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRLILPLIFRELELQCLDGDDAKVTFDEENGLDEYDEVPMPV
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-------MGDMRDHE
-------CCCCCCHH		10.42-
18PhosphorylationLEIPDRDSEEELENI
HCCCCCCCHHHHHHH		48.0421082442
31PhosphorylationNIIGQIAYRDLTIPV
HHHHHHHHCCCCCEE		13.29-
39PhosphorylationRDLTIPVTEMQDPEA
CCCCCEEECCCCCCC		22.0123737553
49PhosphorylationQDPEALPTEQTATDY
CCCCCCCCCCCCCCC		41.3923737553
52PhosphorylationEALPTEQTATDYVPS
CCCCCCCCCCCCCCC		25.8723737553
54PhosphorylationLPTEQTATDYVPSST
CCCCCCCCCCCCCCC		31.1123737553
56PhosphorylationTEQTATDYVPSSTST
CCCCCCCCCCCCCCC		15.2023737553
59PhosphorylationTATDYVPSSTSTPHP
CCCCCCCCCCCCCCC		35.8823737553
60PhosphorylationATDYVPSSTSTPHPS
CCCCCCCCCCCCCCC		21.9523737553
61PhosphorylationTDYVPSSTSTPHPSS
CCCCCCCCCCCCCCC		40.7423737553
62PhosphorylationDYVPSSTSTPHPSSG
CCCCCCCCCCCCCCC		41.7223737553
63PhosphorylationYVPSSTSTPHPSSGQ
CCCCCCCCCCCCCCC		26.2123737553
67PhosphorylationSTSTPHPSSGQVYVE
CCCCCCCCCCCEEEE		44.0323737553
68PhosphorylationTSTPHPSSGQVYVEL
CCCCCCCCCCEEEEH		37.3823737553
72PhosphorylationHPSSGQVYVELQELM
CCCCCCEEEEHHHHH		4.7423737553
188UbiquitinationLGNLEGVKPAVLTRS
HCCCCCCCCEEEECC		37.8122790023
199PhosphorylationLTRSGGASEPLLPHQ
EECCCCCCCCCCCCC		42.92-
208PhosphorylationPLLPHQPSLETQLYC
CCCCCCCCCCEEEEE		32.0623140645
211PhosphorylationPHQPSLETQLYCGQA
CCCCCCCEEEEEEEC		29.2123140645
214PhosphorylationPSLETQLYCGQAEGG
CCCCEEEEEEECCCC		5.6823984901
222PhosphorylationCGQAEGGSEGPSTSG
EEECCCCCCCCCCCC		50.6825521595
226PhosphorylationEGGSEGPSTSGTLKI
CCCCCCCCCCCCEEC		46.1723984901
227PhosphorylationGGSEGPSTSGTLKIP
CCCCCCCCCCCEECC		34.0223984901
228PhosphorylationGSEGPSTSGTLKIPP
CCCCCCCCCCEECCC		33.8323984901
230PhosphorylationEGPSTSGTLKIPPDS
CCCCCCCCEECCCCC		25.3323984901
252UbiquitinationGRANFLEKPVLGFVR
ECCCCCCCCEEEEEE		42.4422790023
343UbiquitinationPTDAPSEKALLNLVP
CCCCCCHHHHHHCHH		48.98-
353UbiquitinationLNLVPVQKELLRRRY
HHCHHHHHHHHHHCC		51.0322790023
360PhosphorylationKELLRRRYLPSPAKP
HHHHHHCCCCCCCCC		22.5825195567
363PhosphorylationLRRRYLPSPAKPDPN
HHHCCCCCCCCCCCC		34.5923737553
366UbiquitinationRYLPSPAKPDPNLYN
CCCCCCCCCCCCCCC		54.0322790023
372PhosphorylationAKPDPNLYNTLDLNG
CCCCCCCCCCCCCCC		16.85-
374PhosphorylationPDPNLYNTLDLNGGK
CCCCCCCCCCCCCCC		14.2122817900
381UbiquitinationTLDLNGGKGGPGDED
CCCCCCCCCCCCCCC		63.1922790023
660N-linked_GlycosylationPDGLKVSNSSARGWV
CCCEEECCCCCCCEE		42.86-
761UbiquitinationNALTVMGKASGPGAA
CEEEEEEECCCCCHH		22.6822790023
836PhosphorylationLLFKPPKYHPDVPFV
HHCCCCCCCCCCCHH		25.1025195567
861S-palmitoylationFTGIQIICLAVLWVV
HHHHHHHHHHHHHHH		1.82-
922PhosphorylationEENGLDEYDEVPMPV
CCCCCCCCCCCCCCC		19.64-
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 B3AT_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B3AT_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 B3AT_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of B3AT_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of B3AT_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"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-363, AND MASSSPECTROMETRY.

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