S26A6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: S26A6_HUMAN
• UniProt AC: Q9BXS9
• Protein Name: Solute carrier family 26 member 6
• Gene Name: SLC26A6
• Organism: Homo sapiens (Human).
• Sequence Length: 759
• Subcellular Localization: Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Microsome. Localized in sperm membranes. Colocalizes with
• Protein Description: Apical membrane anion-exchanger with wide epithelial distribution that plays a role as a component of the pH buffering system for maintaining acid-base homeostasis. Acts as a versatile DIDS-sensitive inorganic and organic anion transporter that mediates the uptake of monovalent anions like chloride, bicarbonate, formate and hydroxyl ion and divalent anions like sulfate and oxalate. Function in multiple exchange modes involving pairs of these anions, which include chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate-sulfate and chloride-formate exchange. Apical membrane chloride-bicarbonate exchanger that mediates luminal chloride absorption and bicarbonate secretion by the small intestinal brush border membrane and contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption, possibly by providing a bicarbonate import pathway. Mediates also intestinal chloride absorption and oxalate secretion, thereby preventing hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate secretion, chloride-formate, chloride-oxalate and chloride-bicarbonate transport activities in the duodenum are inhibited by PKC activation in a calcium-independent manner. The apical membrane chloride-bicarbonate exchanger provides also a major route for fluid and bicarbonate secretion into the proximal tubules of the kidney as well as into the proximal part of the interlobular pancreatic ductal tree, where it mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize protein-rich acinar secretion. Mediates also the transcellular sulfate absorption and oxalate secretion across the apical membrane in the duodenum and the formate ion efflux at the apical brush border of cells in the proximal tubules of kidney. Plays a role in sperm capacitation by increasing intracellular pH.; Isoform 4: Apical membrane chloride-bicarbonate exchanger. Its association with carbonic anhydrase CA2 forms a bicarbonate transport metabolon; hence maximizes the local concentration of bicarbonate at the transporter site..
• Protein Sequence: MGLADASGPRDTQALLSATQAMDLRRRDYHMERPLLNQEHLEELGRWGSAPRTHQWRTWLQCSRARAYALLLQHLPVLVWLPRYPVRDWLLGDLLSGLSVAIMQLPQGLAYALLAGLPPVFGLYSSFYPVFIYFLFGTSRHISVGTFAVMSVMVGSVTESLAPQALNDSMINETARDAARVQVASTLSVLVGLFQVGLGLIHFGFVVTYLSEPLVRGYTTAAAVQVFVSQLKYVFGLHLSSHSGPLSLIYTVLEVCWKLPQSKVGTVVTAAVAGVVLVVVKLLNDKLQQQLPMPIPGELLTLIGATGISYGMGLKHRFEVDVVGNIPAGLVPPVAPNTQLFSKLVGSAFTIAVVGFAIAISLGKIFALRHGYRVDSNQELVALGLSNLIGGIFQCFPVSCSMSRSLVQESTGGNSQVAGAISSLFILLIIVKLGELFHDLPKAVLAAIIIVNLKGMLRQLSDMRSLWKANRADLLIWLVTFTATILLNLDLGLVVAVIFSLLLVVVRTQMPHYSVLGQVPDTDIYRDVAEYSEAKEVRGVKVFRSSATVYFANAEFYSDALKQRCGVDVDFLISQKKKLLKKQEQLKLKQLQKEEKLRKQAASPKGASVSINVNTSLEDMRSNNVEDCKMMQVSSGDKMEDATANGQEDSKAPDGSTLKALGLPQPDFHSLILDLGALSFVDTVCLKSLKNIFHDFREIEVEVYMAACHSPVVSQLEAGHFFDASITKKHLFASVHDAVTFALQHPRPVPDSPVSVTRL

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
7	Phosphorylation	-MGLADASGPRDTQA -CCCCCCCCCHHHHH	50.29	29978859
12	Phosphorylation	DASGPRDTQALLSAT CCCCCHHHHHHHHHH	19.61	29759185
17	Phosphorylation	RDTQALLSATQAMDL HHHHHHHHHHHHHHH	30.07	29978859
19	Phosphorylation	TQALLSATQAMDLRR HHHHHHHHHHHHHHH	17.31	29978859
62	S-palmitoylation	QWRTWLQCSRARAYA HHHHHHHHHHHHHHH	2.52	29575903
342	Phosphorylation	APNTQLFSKLVGSAF CCCHHHHHHHHHHHH	33.40	24719451
364	Ubiquitination	AIAISLGKIFALRHG HHHHHHHHHHHHHCC	39.69	-
405	Phosphorylation	VSCSMSRSLVQESTG CCCHHCHHHHHHHCC	26.11	-
423	Phosphorylation	QVAGAISSLFILLII HHHHHHHHHHHHHHH	22.61	-
499	Ubiquitination	GLVVAVIFSLLLVVV HHHHHHHHHHHHHHH	3.19	21906983
535 (in isoform 3)	Ubiquitination	-	53.33	-
535 (in isoform 2)	Ubiquitination	-	53.33	21906983
535 (in isoform 1)	Ubiquitination	-	53.33	21906983
535	Ubiquitination	VAEYSEAKEVRGVKV HHHHHHHHHHCCEEE	53.33	21906983
535	Ubiquitination	VAEYSEAKEVRGVKV HHHHHHHHHHCCEEE	53.33	21906983
574	Phosphorylation	VDVDFLISQKKKLLK CCHHHHHHHHHHHHH	37.79	15990874
587	Ubiquitination	LKKQEQLKLKQLQKE HHHHHHHHHHHHHHH	54.02	-
593	Ubiquitination	LKLKQLQKEEKLRKQ HHHHHHHHHHHHHHH	76.16	-
602	Ubiquitination	EKLRKQAASPKGASV HHHHHHCCCCCCCEE	24.71	-
603	Phosphorylation	KLRKQAASPKGASVS HHHHHCCCCCCCEEE	30.11	15990874
608	Phosphorylation	AASPKGASVSINVNT CCCCCCCEEEEECCC	25.68	27251275
610	Phosphorylation	SPKGASVSINVNTSL CCCCCEEEEECCCCH	13.12	25219547
615	Ubiquitination	SVSINVNTSLEDMRS EEEEECCCCHHHHHC	30.33	21906983
615	Phosphorylation	SVSINVNTSLEDMRS EEEEECCCCHHHHHC	30.33	23663014
616	Phosphorylation	VSINVNTSLEDMRSN EEEECCCCHHHHHCC	25.26	30266825
622	Phosphorylation	TSLEDMRSNNVEDCK CCHHHHHCCCHHHCE	26.56	-
629	Ubiquitination	SNNVEDCKMMQVSSG CCCHHHCEEEECCCC	50.13	-
629 (in isoform 3)	Ubiquitination	-	50.13	-
632 (in isoform 2)	Ubiquitination	-	28.57	21906983
634	Phosphorylation	DCKMMQVSSGDKMED HCEEEECCCCCCHHH	16.23	23312004
635	Phosphorylation	CKMMQVSSGDKMEDA CEEEECCCCCCHHHC	52.75	23312004
637 (in isoform 3)	Ubiquitination	-	49.42	-
638 (in isoform 1)	Ubiquitination	-	47.95	21906983
638	Ubiquitination	MQVSSGDKMEDATAN EECCCCCCHHHCCCC	47.95	21906983
643	Phosphorylation	GDKMEDATANGQEDS CCCHHHCCCCCCCCC	32.74	23312004
650 (in isoform 3)	Ubiquitination	-	29.93	-
650	Phosphorylation	TANGQEDSKAPDGST CCCCCCCCCCCCCCC	29.93	23312004
650	Ubiquitination	TANGQEDSKAPDGST CCCCCCCCCCCCCCC	29.93	21906983
651 (in isoform 1)	Ubiquitination	-	76.02	21906983
651	Ubiquitination	ANGQEDSKAPDGSTL CCCCCCCCCCCCCCC	76.02	2190698
729	Ubiquitination	FDASITKKHLFASVH CCEECCHHHHHHHHH	36.57	-
734	Phosphorylation	TKKHLFASVHDAVTF CHHHHHHHHHHHHHH	16.79	20068231
740	Phosphorylation	ASVHDAVTFALQHPR HHHHHHHHHHHCCCC	12.62	20068231
752	Phosphorylation	HPRPVPDSPVSVTRL CCCCCCCCCCCCCCC	22.56	19664994
755	Phosphorylation	PVPDSPVSVTRL--- CCCCCCCCCCCC---	22.58	29255136
757	Phosphorylation	PDSPVSVTRL----- CCCCCCCCCC-----	20.81	30266825

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
574	S	Phosphorylation	Kinase	PKC	-	Uniprot
603	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of S26A6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of S26A6_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of S26A6_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752 AND SER-755, ANDMASS SPECTROMETRY.
PubMed: 17081983