Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0380 Transporter Info
Gene Name	SLC4A1
Transporter Name	Anion exchange protein 1
Gene ID	6521
UniProt ID	P02730

Post-Translational Modification of This DT
Overview ofSLC4A1 Modification Sites with Functional and Structural Information
Sequence	M E E L Q D D Y E D M M E E N L E Q E E Y E D P D I P E S Q M E E P A A H D T E A T A T D Y H T T S H P G T H K V Y V E L Q E L V M D E K N Q E L R W M E A A R W V Q L E E N L G E N G A W G R P H L S H L T F W S L L E L R R V F T K G T V L L D L Q E T S L A G V A N Q L L D R F I F E D Q I R P Q D R E E L L R A L L L K H S H A G E L E A L G G V K P A V L T R S G D P S Q P L L P Q H S S L E T Q L F C E Q G D G G T E G H S P S G I L E K I P P D S E A T L V L V G R A D F L E Q P V L G F V R L Q E A A E L E A V E L P V P I R F L F V L L G P E A P H I D Y T Q L G R A A A T L M S E R V F R I D A Y M A Q S R G E L L H S L E G F L D C S L V L P P T D A P S E Q A L L S L V P V Q R E L L R R R Y Q S S P A K P D S S F Y K G L D L N G G P D D P L Q Q T G Q L F G G L V R D I R R R Y P Y Y L S D I T D A F S P Q V L A A V I F I Y F A A L S P A I T F G G L L G E K T R N Q M G V S E L L I S T A V Q G I L F A L L G A Q P L L V V G F S G P L L V F E E A F F S F C E T N G L E Y I V G R V W I G F W L I L L V V L V V A F E G S F L V R F I S R Y T Q E I F S F L I S L I F I Y E T F S K L I K I F Q D H P L Q K T Y N Y N V L M V P K P Q G P L P N T A L L S L V L M A G T F F F A M M L R K F K N S S Y F P G K L R R V I G D F G V P I S I L I M V L V D F F I Q D T Y T Q K L S V P D G F K V S N S S A R G W V I H P L G L R S E F P I W M M F A S A L P A L L V F I L I F L E S Q I T T L I V S K P E R K M V K G S G F H L D L L L V V G M G G V A A L F G M P W L S A T T V R S V T H A N A L T V M G K A S T P G A A A Q I Q E V K E Q R I S G L L V A V L V G L S I L M E P I L S R I P L A V L F G I F L Y M G V T S L S G I Q L F D R I L L L F K P P K Y H P D V P Y V K R V K T W R M H L F T G I Q I I C L A V L W V V K S T P A S L A L P F V L I L T V P L R R V L L P L I F R N V E L Q C L D A D D A K A T F D E E E G R D E Y D E V A M P V
PTM type	X-Acetylation X-N-glycosylation X-O-glycosylation X-Phosphorylation X-Phosphorylation X-S-nitrosylation X-S-palmitoylation X-Ubiquitination X: Amino Acid

Acetylation
Methionine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[1], [2]
Role of PTM	Potential impacts
Modified Residue	Methionine	Modified Location	1
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC4A1 Methionine 1 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	642
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC4A1 Asparagine 642 has the potential to affect its expression or activity.
O-glycosylation
Serine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	162
Experimental Method	Co-Immunoprecipitation
Detailed Description	O-linked Glycosylation at SLC4A1 Serine 162 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC4A1			[5], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	224
Experimental Method	Co-Immunoprecipitation
Detailed Description	O-linked Glycosylation at SLC4A1 Serine 224 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC4A1			[5], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	745
Experimental Method	Co-Immunoprecipitation
Detailed Description	O-linked Glycosylation at SLC4A1 Serine 745 has the potential to affect its expression or activity.
Phosphorylation
Serine	16 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	29
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 29 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	50
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 50 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	181
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 181 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	185
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 185 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	193
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 193 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	194
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 194 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC4A1			[13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	212
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 212 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC4A1			[13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	214
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 214 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC4A1			[9], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	303
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 303 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC4A1			[13], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	349
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 349 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC4A1			[13], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	350
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 350 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC4A1			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	356
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 356 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLC4A1			[13], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	357
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 357 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLC4A1			[17]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	402
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 402 has the potential to affect its expression or activity.
PTM Phenomenon15	Have the potential to influence SLC4A1			[12], [18]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	745
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 745 has the potential to affect its expression or activity.
PTM Phenomenon16	.			[19]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	781
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Serine 781 has the potential to affect its expression or activity.
Threonine	10 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	39
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 39 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC4A1			[9], [14]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	42
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 42 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC4A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	44
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 44 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	48
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 48 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	49
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 49 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	54
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 54 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	197
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 197 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	208
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 208 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC4A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	746
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 746 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC4A1			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	894
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Threonine 894 has the potential to affect its expression or activity.
Tyrosine	8 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[11], [20]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	8
Related Enzyme	Tyrosine-protein kinase SYK (SYK)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 8 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC4A1			[11], [20]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	21
Related Enzyme	Tyrosine-protein kinase SYK (SYK)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 21 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC4A1			[9], [21]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	46
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 46 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC4A1			[12], [15]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	347
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 347 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC4A1			[11], [20]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	359
Related Enzyme	Tyrosine-protein kinase Lyn (LYN)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 359 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC4A1			[17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	413
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 413 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC4A1			[13]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	818
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 818 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC4A1			[11], [20]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	904
Related Enzyme	Tyrosine-protein kinase Lyn (LYN)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC4A1 Tyrosine 904 has the potential to affect its expression or activity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[22]
Role of PTM	No Significant Effect
Experimental Method	Co-Immunoprecipitation
Detailed Description	Decreased autophosphorylation of Band 3 glycoprotein (SLC4A1) has been observed in myotonic muscular dystrophy, though its functional consequences require further investigation.
S-nitrosylation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	201
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at SLC4A1 Cystine 201 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC4A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	317
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at SLC4A1 Cystine 317 has the potential to affect its expression or activity.
S-palmitoylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC4A1			[25]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	843
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC4A1 Cystine 843 has the potential to affect its expression or activity.
Ubiquitination
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[26]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	757
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC4A1 Lysine 757 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	757
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC4A1 Lysine 757 has the potential to affect its expression or activity.

References
1	Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse. Biochim Biophys Acta. 1989 Sep 14;998(1):43-9.
2	Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment. J Biol Chem. 1978 Oct 25;253(20):7242-8.
3	A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters. J Biol Chem. 2013 Nov 22;288(47):33848-33860.
4	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein. Biochem J. 2000 Jul 1;349(Pt 1):51-7.
5	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes. 2009 Feb;58(2):309-17.
6	The LIM protein FHL3 binds basic Kruppel-like factor/Kruppel-like factor 3 and its co-repressor C-terminal-binding protein 2. J Biol Chem. 2003 Apr 11;278(15):12786-95.
7	Proteolytic processing and oligomerization of bacteriophage-derived endosialidases. J Biol Chem. 2003 Apr 11;278(15):12634-44.
8	Modulation, via protein-protein interactions, of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation. J Biol Chem. 2003 Apr 4;278(14):12078-84.
9	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
10	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
11	Phosphorylation sites in human erythrocyte band 3 protein. Biochim Biophys Acta. 1991 Jan 30;1061(2):253-66.
12	Phosphoproteins in extracellular vesicles as candidate markers for breast cancer. Proc Natl Acad Sci U S A. 2017 Mar 21;114(12):3175-3180.
13	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
14	Identification of the major casein kinase I phosphorylation sites on erythrocyte band 3. Blood. 1997 Apr 15;89(8):3019-24.
15	Phosphoproteome profiling revealed abnormally phosphorylated AMPK and ATF2 involved in glucose metabolism and tumorigenesis of GH-PAs. J Endocrinol Invest. 2019 Feb;42(2):137-148.
16	Residual tissue repositories as a resource for population-based cancer proteomic studies. Clin Proteomics. 2018 Aug 3;15:26.
17	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
18	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
19	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
20	Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites. Blood. 2000 Aug 15;96(4):1550-7.
21	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
22	Isolation of an abnormally phosphorylated erythrocyte membrane band 3 glycoprotein from patients with myotonic muscular dystrophy. J Membr Biol. 1979;45(1-2):147-166.
23	Predict and analyze S-nitrosylation modification sites with the mRMR and IFS approaches. J Proteomics. 2012 Feb 16;75(5):1654-65.
24	Protein thiols and glutathione influence the nitric oxide-dependent regulation of the red blood cell metabolism. Nitric Oxide. 2002 Mar;6(2):186-99.
25	Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus. J Biol Chem. 1991 Sep 5;266(25):16420-4.
26	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.

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Detail Information of Post-Translational Modifications

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