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Q9BXS9

- S26A6_HUMAN

UniProt

Q9BXS9 - S26A6_HUMAN

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Protein
Solute carrier family 26 member 6
Gene
SLC26A6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications
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.3 Publications

Enzyme regulationi

Apical membrane chloride-formate exchange activity in the proximal tubules of the kidney and oxalate secretion in the duodenum are inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters) By similarity. Apical membrane chloride-bicarbonate exchange activity of the pancreatic duct is inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters). Isoform 4, isoform 5 and isoform 6 chloride, bicarbonate and sulfate transport activities are inhibited by DIDS.3 Publications

GO - Molecular functioni

  1. PDZ domain binding Source: UniProtKB
  2. anion:anion antiporter activity Source: UniProtKB
  3. bicarbonate transmembrane transporter activity Source: UniProtKB
  4. chloride channel activity Source: UniProtKB-KW
  5. chloride transmembrane transporter activity Source: UniProtKB
  6. efflux transmembrane transporter activity Source: UniProtKB
  7. formate efflux transmembrane transporter activity Source: UniProtKB
  8. formate transmembrane transporter activity Source: UniProtKB
  9. formate uptake transmembrane transporter activity Source: UniProtKB
  10. oxalate transmembrane transporter activity Source: UniProtKB
  11. protein binding Source: UniProtKB
  12. secondary active sulfate transmembrane transporter activity Source: InterPro
  13. sulfate transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. angiotensin-activated signaling pathway Source: UniProtKB
  2. anion transport Source: GOC
  3. bicarbonate transport Source: GOC
  4. cellular response to cAMP Source: UniProtKB
  5. cellular response to fructose stimulus Source: UniProtKB
  6. cellular response to interferon-gamma Source: UniProtKB
  7. chloride transmembrane transport Source: GOC
  8. chloride transport Source: GOC
  9. epithelial fluid transport Source: UniProtKB
  10. formate transport Source: UniProtKB
  11. intestinal absorption Source: UniProtKB
  12. intracellular pH elevation Source: UniProtKB
  13. ion transport Source: Reactome
  14. mannitol transport Source: UniProtKB
  15. oxalate transport Source: UniProtKB
  16. oxalic acid secretion Source: UniProtKB
  17. positive regulation of dipeptide transmembrane transport Source: UniProtKB
  18. protein kinase C signaling Source: UniProtKB
  19. regulation of intracellular pH Source: UniProtKB
  20. sperm capacitation Source: UniProtKB
  21. sulfate transmembrane transport Source: GOC
  22. sulfate transport Source: UniProtKB
  23. transepithelial chloride transport Source: UniProtKB
  24. transepithelial transport Source: UniProtKB
  25. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel

Keywords - Biological processi

Anion exchange, Antiport, Ion transport, Transport

Keywords - Ligandi

Chloride

Enzyme and pathway databases

ReactomeiREACT_19357. Multifunctional anion exchangers.

Protein family/group databases

TCDBi2.A.53.2.7. the sulfate permease (sulp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 26 member 6
Alternative name(s):
Anion exchange transporter
Pendrin-like protein 1
Short name:
Pendrin-L1
Gene namesi
Name:SLC26A6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:14472. SLC26A6.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein By similarity. Microsome By similarity
Note: Localized in sperm membranes. Colocalizes with CFTR at the midpiece of sperm tail. Localizes to the apical membrane brush border of epithelial cells in the proximal tubules of kidney, of enterocytes of the small intestine and of gastric parietal cells in the stomach. May be translocated from the cytosolic surface of the cell membrane to the intracellular space by PKC in phorbol myristate acetate (PMA)-induced cells By similarity. Colocalized with CA2 at the surface of the cell membrane in order to form a bicarbonate transport metabolon; colocalization is reduced in phorbol myristate acetate (PMA)-induced cells.4 Publications
Isoform 4 : Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein
Note: Localizes to the apical and basolateral surfaces of tubular wall cells in kidney and in the brush border of pancreatic duct cells.4 Publications
Isoform 5 : Cell membrane; Multi-pass membrane protein 4 Publications
Isoform 6 : Cell membrane; Multi-pass membrane protein 4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 115115Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei116 – 13621Helical; Reviewed prediction
Add
BLAST
Topological domaini137 – 18650Extracellular Reviewed prediction
Add
BLAST
Transmembranei187 – 20721Helical; Reviewed prediction
Add
BLAST
Topological domaini208 – 26356Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei264 – 28421Helical; Reviewed prediction
Add
BLAST
Topological domaini285 – 2939Extracellular Reviewed prediction
Transmembranei294 – 31421Helical; Reviewed prediction
Add
BLAST
Topological domaini315 – 34733Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei348 – 36821Helical; Reviewed prediction
Add
BLAST
Topological domaini369 – 37911Extracellular Reviewed prediction
Add
BLAST
Transmembranei380 – 40021Helical; Reviewed prediction
Add
BLAST
Topological domaini401 – 41616Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei417 – 43721Helical; Reviewed prediction
Add
BLAST
Topological domaini438 – 48447Extracellular Reviewed prediction
Add
BLAST
Transmembranei485 – 50521Helical; Reviewed prediction
Add
BLAST
Topological domaini506 – 759254Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. brush border membrane Source: UniProtKB
  4. chloride channel complex Source: UniProtKB-KW
  5. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  6. endoplasmic reticulum Source: UniProtKB-KW
  7. integral component of membrane Source: UniProtKB-KW
  8. membrane Source: UniProtKB
  9. membrane-bounded vesicle Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. sperm midpiece Source: UniProtKB
  12. vesicle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi568 – 5703DVD → NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport. 1 Publication
Mutagenesisi574 – 5741S → A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells. 1 Publication
Mutagenesisi603 – 6031S → A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells. 1 Publication

Organism-specific databases

PharmGKBiPA37889.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Solute carrier family 26 member 6
PRO_0000080171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei574 – 5741Phosphoserine; by PKC Inferred
Modified residuei603 – 6031Phosphoserine; by PKC Inferred
Modified residuei616 – 6161Phosphoserine1 Publication
Modified residuei752 – 7521Phosphoserine2 Publications
Modified residuei755 – 7551Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues by PKC; the phosphorylation disrupts interaction with carbonic anhydrase CA2 and reduces bicarbonate transport activity in a phorbol myristate acetate (PMA)-induced manner.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BXS9.
PaxDbiQ9BXS9.
PRIDEiQ9BXS9.

PTM databases

PhosphoSiteiQ9BXS9.

Expressioni

Tissue specificityi

Ubiquitous. Highest levels in kidney and pancreas. Lower expression in heart, skeletal muscle, liver and placenta. Also found in lung and brain. Isoform 4 is ubiquitously expressed. Isoform 6 is expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis and ovary. Isoform 5 is expressed weakly in placenta, lung, liver and pancreas.2 Publications

Inductioni

Down-regulated by pro-inflammatory cytokine IFN gamma.4 Publications

Gene expression databases

ArrayExpressiQ9BXS9.
BgeeiQ9BXS9.
CleanExiHS_SLC26A6.
GenevestigatoriQ9BXS9.

Organism-specific databases

HPAiHPA048363.

Interactioni

Subunit structurei

Interacts (via C-terminal domain) with PDZK1 (via C-terminal PDZ domain); the interaction induces chloride and oxalate exchange transport. Interacts with CFTR, SLC26A3 and SLC9A3R1 By similarity. Isoform 4 interacts (via C-terminal cytoplasmic domain) with CA2; the interaction stimulates chloride-bicarbonate exchange activity. Isoform 4 and isoform 5 interact with SLC9A3R1 (via the PDZ domains). Isoform 4 and isoform 5 interact with SLC9A3R2 (via the PDZ domains).2 Publications

Protein-protein interaction databases

BioGridi122373. 1 interaction.
STRINGi9606.ENSP00000378920.

Structurei

3D structure databases

ProteinModelPortaliQ9BXS9.
SMRiQ9BXS9. Positions 511-560, 667-739.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini530 – 742213STAS
Add
BLAST

Sequence similaritiesi

Contains 1 STAS domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0659.
HOGENOMiHOG000006546.
HOVERGENiHBG000639.
KOiK14704.
OMAiNNVEDCK.
OrthoDBiEOG76T9QT.
PhylomeDBiQ9BXS9.
TreeFamiTF313784.

Family and domain databases

Gene3Di3.30.750.24. 2 hits.
InterProiIPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view]
PfamiPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 2 hits.
TIGRFAMsiTIGR00815. sulP. 1 hit.
PROSITEiPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BXS9-1) [UniParc]FASTAAdd to Basket

Also known as: SLC26A6b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGLADASGPR DTQALLSATQ AMDLRRRDYH MERPLLNQEH LEELGRWGSA    50
PRTHQWRTWL QCSRARAYAL LLQHLPVLVW LPRYPVRDWL LGDLLSGLSV 100
AIMQLPQGLA YALLAGLPPV FGLYSSFYPV FIYFLFGTSR HISVGTFAVM 150
SVMVGSVTES LAPQALNDSM INETARDAAR VQVASTLSVL VGLFQVGLGL 200
IHFGFVVTYL SEPLVRGYTT AAAVQVFVSQ LKYVFGLHLS SHSGPLSLIY 250
TVLEVCWKLP QSKVGTVVTA AVAGVVLVVV KLLNDKLQQQ LPMPIPGELL 300
TLIGATGISY GMGLKHRFEV DVVGNIPAGL VPPVAPNTQL FSKLVGSAFT 350
IAVVGFAIAI SLGKIFALRH GYRVDSNQEL VALGLSNLIG GIFQCFPVSC 400
SMSRSLVQES TGGNSQVAGA ISSLFILLII VKLGELFHDL PKAVLAAIII 450
VNLKGMLRQL SDMRSLWKAN RADLLIWLVT FTATILLNLD LGLVVAVIFS 500
LLLVVVRTQM PHYSVLGQVP DTDIYRDVAE YSEAKEVRGV KVFRSSATVY 550
FANAEFYSDA LKQRCGVDVD FLISQKKKLL KKQEQLKLKQ LQKEEKLRKQ 600
AASPKGASVS INVNTSLEDM RSNNVEDCKM MQVSSGDKME DATANGQEDS 650
KAPDGSTLKA LGLPQPDFHS LILDLGALSF VDTVCLKSLK NIFHDFREIE 700
VEVYMAACHS PVVSQLEAGH FFDASITKKH LFASVHDAVT FALQHPRPVP 750
DSPVSVTRL 759
Length:759
Mass (Da):82,967
Last modified:June 1, 2001 - v1
Checksum:i63CB0B756C9675C6
GO
Isoform 2 (identifier: Q9BXS9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     602-631: ASPKGASVSINVNTSLEDMRSNNVEDCKMM → GPLLSACLAPQ

Note: No experimental confirmation available.

Show »
Length:740
Mass (Da):80,807
Checksum:i9BBFAB68E0D8B2C5
GO
Isoform 3 (identifier: Q9BXS9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     632-632: Missing.

Show »
Length:758
Mass (Da):82,839
Checksum:i6CC16170D6F9F01C
GO
Isoform 4 (identifier: Q9BXS9-4) [UniParc]FASTAAdd to Basket

Also known as: SLC26A6a

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     632-632: Missing.

Show »
Length:737
Mass (Da):80,782
Checksum:i1AFAFB8DEDB69E6E
GO
Isoform 5 (identifier: Q9BXS9-5) [UniParc]FASTAAdd to Basket

Also known as: SLC26A6c

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     264-301: Missing.
     632-632: Missing.

Show »
Length:699
Mass (Da):76,876
Checksum:i8E03EA6F5DE56EFC
GO
Isoform 6 (identifier: Q9BXS9-6) [UniParc]FASTAAdd to Basket

Also known as: SLC26A6d

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     632-759: QVSSGDKMED...PDSPVSVTRL → VRLEVGKEVT...SGSVVICHRI

Show »
Length:671
Mass (Da):73,817
Checksum:iB2C9AD808C256713
GO
Isoform 7 (identifier: Q9BXS9-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     145-216: GTFAVMSVMV...VTYLSEPLVR → ATPGPLPLLT...PLWATVPHLL
     217-252: Missing.

Note: No experimental confirmation available.

Show »
Length:723
Mass (Da):79,159
Checksum:iA3D9F408FD3DD9F3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti206 – 2061V → M.1 Publication
Corresponds to variant rs13324142 [ dbSNP | Ensembl ].
VAR_012776

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 4, isoform 5 and isoform 6.
VSP_046807Add
BLAST
Alternative sequencei145 – 21672GTFAV…EPLVR → ATPGPLPLLTAPGRPTGGAG PDPLRLRGHLPVRTSCPRLY HSCSCAGLRLTAQVCVWPPS EQPLWATVPHLL in isoform 7.
VSP_055273Add
BLAST
Alternative sequencei217 – 25236Missing in isoform 7.
VSP_055274Add
BLAST
Alternative sequencei264 – 30138Missing in isoform 5.
VSP_047851Add
BLAST
Alternative sequencei602 – 63130ASPKG…DCKMM → GPLLSACLAPQ in isoform 2.
VSP_006169Add
BLAST
Alternative sequencei632 – 759128QVSSG…SVTRL → VRLEVGKEVTAVSCRDAGST CLMRNAMDPAAVGSRVLRRW QEEWGGWVRYSSGSVVICHR I in isoform 6.
VSP_047852Add
BLAST
Alternative sequencei632 – 6321Missing in isoform 3, isoform 4 and isoform 5.
VSP_040127

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF279265 mRNA. Translation: AAF81911.1.
AF288410 mRNA. Translation: AAK19153.1.
AF416721 mRNA. Translation: AAN07094.1.
AB033288 mRNA. Translation: BAB69041.1.
AK297695 mRNA. Translation: BAG60053.1.
AC121252 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64901.1.
CH471055 Genomic DNA. Translation: EAW64903.1.
BC017697 mRNA. Translation: AAH17697.1.
CCDSiCCDS43087.1. [Q9BXS9-1]
CCDS46824.1. [Q9BXS9-2]
CCDS46825.1. [Q9BXS9-3]
RefSeqiNP_001035544.1. NM_001040454.1.
NP_001268661.1. NM_001281732.1.
NP_001268662.1. NM_001281733.1.
NP_075062.2. NM_022911.2. [Q9BXS9-1]
NP_599025.2. NM_134263.2. [Q9BXS9-3]
NP_602298.2. NM_134426.2. [Q9BXS9-2]
UniGeneiHs.631925.
Hs.663208.

Genome annotation databases

EnsembliENST00000358747; ENSP00000351597; ENSG00000225697.
ENST00000383733; ENSP00000373239; ENSG00000225697. [Q9BXS9-2]
ENST00000395550; ENSP00000378920; ENSG00000225697. [Q9BXS9-1]
ENST00000420764; ENSP00000404684; ENSG00000225697. [Q9BXS9-3]
ENST00000455886; ENSP00000401066; ENSG00000225697.
GeneIDi65010.
KEGGihsa:65010.
UCSCiuc003cug.3. human. [Q9BXS9-1]
uc003cui.3. human.
uc003cuj.3. human. [Q9BXS9-2]

Polymorphism databases

DMDMi20140224.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF279265 mRNA. Translation: AAF81911.1 .
AF288410 mRNA. Translation: AAK19153.1 .
AF416721 mRNA. Translation: AAN07094.1 .
AB033288 mRNA. Translation: BAB69041.1 .
AK297695 mRNA. Translation: BAG60053.1 .
AC121252 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64901.1 .
CH471055 Genomic DNA. Translation: EAW64903.1 .
BC017697 mRNA. Translation: AAH17697.1 .
CCDSi CCDS43087.1. [Q9BXS9-1 ]
CCDS46824.1. [Q9BXS9-2 ]
CCDS46825.1. [Q9BXS9-3 ]
RefSeqi NP_001035544.1. NM_001040454.1.
NP_001268661.1. NM_001281732.1.
NP_001268662.1. NM_001281733.1.
NP_075062.2. NM_022911.2. [Q9BXS9-1 ]
NP_599025.2. NM_134263.2. [Q9BXS9-3 ]
NP_602298.2. NM_134426.2. [Q9BXS9-2 ]
UniGenei Hs.631925.
Hs.663208.

3D structure databases

ProteinModelPortali Q9BXS9.
SMRi Q9BXS9. Positions 511-560, 667-739.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122373. 1 interaction.
STRINGi 9606.ENSP00000378920.

Protein family/group databases

TCDBi 2.A.53.2.7. the sulfate permease (sulp) family.

PTM databases

PhosphoSitei Q9BXS9.

Polymorphism databases

DMDMi 20140224.

Proteomic databases

MaxQBi Q9BXS9.
PaxDbi Q9BXS9.
PRIDEi Q9BXS9.

Protocols and materials databases

DNASUi 65010.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358747 ; ENSP00000351597 ; ENSG00000225697 .
ENST00000383733 ; ENSP00000373239 ; ENSG00000225697 . [Q9BXS9-2 ]
ENST00000395550 ; ENSP00000378920 ; ENSG00000225697 . [Q9BXS9-1 ]
ENST00000420764 ; ENSP00000404684 ; ENSG00000225697 . [Q9BXS9-3 ]
ENST00000455886 ; ENSP00000401066 ; ENSG00000225697 .
GeneIDi 65010.
KEGGi hsa:65010.
UCSCi uc003cug.3. human. [Q9BXS9-1 ]
uc003cui.3. human.
uc003cuj.3. human. [Q9BXS9-2 ]

Organism-specific databases

CTDi 65010.
GeneCardsi GC03M048664.
HGNCi HGNC:14472. SLC26A6.
HPAi HPA048363.
MIMi 610068. gene.
neXtProti NX_Q9BXS9.
PharmGKBi PA37889.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0659.
HOGENOMi HOG000006546.
HOVERGENi HBG000639.
KOi K14704.
OMAi NNVEDCK.
OrthoDBi EOG76T9QT.
PhylomeDBi Q9BXS9.
TreeFami TF313784.

Enzyme and pathway databases

Reactomei REACT_19357. Multifunctional anion exchangers.

Miscellaneous databases

GeneWikii SLC26A6.
GenomeRNAii 65010.
NextBioi 35473466.
PROi Q9BXS9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BXS9.
Bgeei Q9BXS9.
CleanExi HS_SLC26A6.
Genevestigatori Q9BXS9.

Family and domain databases

Gene3Di 3.30.750.24. 2 hits.
InterProi IPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view ]
Pfami PF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view ]
SUPFAMi SSF52091. SSF52091. 2 hits.
TIGRFAMsi TIGR00815. sulP. 1 hit.
PROSITEi PS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger."
    Lohi H., Kujala M., Kerkelae E., Saarialho-Kere U., Kestilae M., Kere J.
    Genomics 70:102-112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Cloning and characterization of SLC26A6, a novel member of the solute carrier 26 gene family."
    Waldegger S., Moschen I., Ramirez A., Smith R.J.H., Ayadi H., Lang F., Kubisch C.
    Genomics 72:43-50(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT MET-206.
  3. "Molecular characterization of the murine Slc26a6 anion exchanger: functional comparison with Slc26a1."
    Xie Q., Welch R., Mercado A., Romero M.F., Mount D.B.
    Am. J. Physiol. 283:F826-F838(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. "Molecular cloning of a new putative sulfate anion transporter."
    Ishibashi K.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Tissue: Lung.
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Duodenum.
  9. "Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains."
    Lohi H., Lamprecht G., Markovich D., Heil A., Kujala M., Seidler U., Kere J.
    Am. J. Physiol. 284:C769-C779(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 4; 5 AND 6), FUNCTION, ENZYME REGULATION, INTERACTION WITH SLC9A3R1 AND SLC9A3R2, SUBCELLULAR LOCATION, TOPOLOGY.
  10. "Metabolon disruption: a mechanism that regulates bicarbonate transport."
    Alvarez B.V., Vilas G.L., Casey J.R.
    EMBO J. 24:2499-2511(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 4), ENZYME REGULATION, INTERACTION WITH CA2, PHOSPHORYLATION AT SER-574 AND SER-603 BY PKC, SUBCELLULAR LOCATION, MUTAGENESIS OF 568-ASP--ASP-570; SER-574 AND SER-603.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Characterization of the 5'-flanking region and regulation of expression of human anion exchanger SLC26A6."
    Saksena S., Dwivedi A., Singla A., Gill R.K., Tyagi S., Borthakur A., Alrefai W.A., Ramaswamy K., Dudeja P.K.
    J. Cell. Biochem. 105:454-466(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. "Parsing apical oxalate exchange in Caco-2BBe1 monolayers: siRNA knockdown of SLC26A6 reveals the role and properties of PAT-1."
    Freel R.W., Morozumi M., Hatch M.
    Am. J. Physiol. 297:G918-G929(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616; SER-752 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiS26A6_HUMAN
AccessioniPrimary (citable) accession number: Q9BXS9
Secondary accession number(s): B4DMZ1
, Q548A7, Q96Q90, Q9NQU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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