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Q8NBS3

- S4A11_HUMAN

UniProt

Q8NBS3 - S4A11_HUMAN

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Protein

Sodium bicarbonate transporter-like protein 11

Gene

SLC4A11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transporter which plays an important role in sodium-mediated fluid transport in different organs. Prevents severe morphological changes of the cornea caused by increased sodium chloride concentrations in the stroma. In the inner ear, is involved in transport of potassium through the fibrocyte layer to the stria vascularis and is essential for the generation of the endocochlear potential but not for regulation of potassium concentrations in the endolymph. In the kidney, is essential for urinary concentration, mediates a sodium flux into the thin descending limb of Henle loop to allow countercurrent multiplication by osmotic equilibration (By similarity). Involved in borate homeostasis. In the absence of borate, it functions as a Na+ and OH-(H+) channel. In the presence of borate functions as an electrogenic Na+ coupled borate cotransporter.By similarity1 Publication

GO - Molecular functioni

  1. bicarbonate transmembrane transporter activity Source: HGNC
  2. borate transmembrane transporter activity Source: HGNC
  3. hydrogen ion channel activity Source: HGNC
  4. inorganic anion exchanger activity Source: InterPro
  5. protein dimerization activity Source: UniProtKB
  6. sodium channel activity Source: HGNC
  7. symporter activity Source: UniProtKB-KW

GO - Biological processi

  1. bicarbonate transport Source: HGNC
  2. borate transmembrane transport Source: GOC
  3. borate transport Source: HGNC
  4. cellular cation homeostasis Source: HGNC
  5. fluid transport Source: UniProtKB
  6. proton transport Source: HGNC
  7. sodium ion transmembrane transport Source: GOC
  8. sodium ion transport Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Anion exchange, Ion transport, Symport, Transport

Protein family/group databases

TCDBi2.A.31.4.1. the anion exchanger (ae) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium bicarbonate transporter-like protein 11
Alternative name(s):
Bicarbonate transporter-related protein 1
Sodium borate cotransporter 1
Short name:
NaBC1
Solute carrier family 4 member 11
Gene namesi
Name:SLC4A11
Synonyms:BTR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:16438. SLC4A11.

Subcellular locationi

Cell membrane 1 Publication. Membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 375375CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei376 – 39621HelicalSequence AnalysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence AnalysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence AnalysisAdd
BLAST
Transmembranei493 – 51321HelicalSequence AnalysisAdd
BLAST
Topological domaini514 – 57158ExtracellularSequence AnalysisAdd
BLAST
Transmembranei572 – 59221HelicalSequence AnalysisAdd
BLAST
Topological domaini593 – 65361CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei654 – 67421HelicalSequence AnalysisAdd
BLAST
Transmembranei700 – 72021HelicalSequence AnalysisAdd
BLAST
Transmembranei759 – 77921HelicalSequence AnalysisAdd
BLAST
Transmembranei782 – 80221HelicalSequence AnalysisAdd
BLAST
Transmembranei831 – 85121HelicalSequence AnalysisAdd
BLAST
Transmembranei853 – 87321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: HGNC
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy and perceptive deafness (CDPD) [MIM:217400]: An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131S → P in CDPD. 1 Publication
VAR_034946
Natural varianti488 – 4881R → K in CDPD. 1 Publication
VAR_034947
Natural varianti843 – 8431L → P in CDPD. 1 Publication
VAR_034951
Natural varianti856 – 8561M → V in CDPD. 1 Publication
VAR_034953
Corneal dystrophy, endothelial 2, autosomal recessive (CHED2) [MIM:217700]: A congenital corneal dystrophy characterized by thickening and opacification of the cornea, altered morphology of the endothelium, and secretion of an abnormal collagenous layer at the Descemet membrane.9 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251R → H in CHED2. 1 Publication
VAR_063713
Natural varianti143 – 1431E → K in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 1 Publication
VAR_067272
Natural varianti160 – 1601A → T in CHED2. 2 Publications
VAR_034945
Natural varianti209 – 2091R → W in CHED2. 1 Publication
VAR_064978
Natural varianti213 – 2131S → L in CHED2. 1 Publication
VAR_064979
Natural varianti233 – 2331R → C in CHED2. 1 Publication
VAR_064980
Natural varianti269 – 2691A → V in CHED2; affects transport to the cell surface. 1 Publication
VAR_063714
Natural varianti386 – 3861C → R in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 3 Publications
VAR_063715
Natural varianti394 – 3941G → R in CHED2. 2 Publications
VAR_064981
Natural varianti401 – 4011T → K in CHED2. 1 Publication
VAR_064982
Natural varianti418 – 4181G → D in CHED2. 2 Publications
VAR_064983
Natural varianti464 – 4641G → D in CHED2; affects protein processing and transport to the cell surface. 1 Publication
VAR_030662
Natural varianti473 – 4731L → R in CHED2. 1 Publication
VAR_064984
Natural varianti489 – 4891S → L in CHED2; affects protein processing and transport to the cell surface. 2 Publications
VAR_030663
Natural varianti584 – 5841T → K in CHED2. 1 Publication
VAR_064985
Natural varianti755 – 7551R → Q in CHED2; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 4 Publications
VAR_030664
Natural varianti755 – 7551R → W in CHED2. 3 Publications
VAR_063716
Natural varianti773 – 7731P → L in CHED2. 2 Publications
VAR_063717
Natural varianti804 – 8041R → H in CHED2. 1 Publication
VAR_034948
Natural varianti824 – 8241V → M in CHED2; deafness not assessed. 3 Publications
VAR_034949
Natural varianti833 – 8331T → M in CHED2. 1 Publication
VAR_034950
Natural varianti869 – 8691R → C in CHED2; affects protein processing and transport to the cell surface. 3 Publications
VAR_030665
Natural varianti869 – 8691R → H in CHED2. 1 Publication
VAR_034954
Natural varianti873 – 8731L → P in CHED2. 1 Publication
VAR_063718
Corneal dystrophy, Fuchs endothelial, 4 (FECD4) [MIM:613268]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064422
Natural varianti282 – 2821R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064423
Natural varianti399 – 3991E → K in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047809
Natural varianti526 – 5261Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064424
Natural varianti575 – 5751V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064425
Natural varianti583 – 5831G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064426
Natural varianti709 – 7091G → E in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047812
Natural varianti742 – 7421G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
Corresponds to variant rs143965185 [ dbSNP | Ensembl ].
VAR_064427
Natural varianti754 – 7541T → M in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047813
Natural varianti834 – 8341G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064428

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi217400. phenotype.
217700. phenotype.
613268. phenotype.
Orphaneti293603. Congenital hereditary endothelial dystrophy type II.
1490. Corneal dystrophy - perceptive deafness.
98974. Fuchs endothelial corneal dystrophy.
PharmGKBiPA38139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 891891Sodium bicarbonate transporter-like protein 11PRO_0000079236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8NBS3.
PaxDbiQ8NBS3.
PRIDEiQ8NBS3.

PTM databases

PhosphoSiteiQ8NBS3.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in kidney, testis, salivary gland, thyroid, trachea and corneal endothelium. Not detected in retina and lymphocytes.2 Publications

Gene expression databases

BgeeiQ8NBS3.
CleanExiHS_SLC4A11.
ExpressionAtlasiQ8NBS3. baseline and differential.
GenevestigatoriQ8NBS3.

Organism-specific databases

HPAiHPA018120.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi123832. 1 interaction.
STRINGi9606.ENSP00000369396.

Structurei

3D structure databases

ProteinModelPortaliQ8NBS3.
SMRiQ8NBS3. Positions 353-400, 799-831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni376 – 891516Membrane (bicarbonate transporter)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG268067.
GeneTreeiENSGT00760000119021.
HOGENOMiHOG000016966.
HOVERGENiHBG079162.
InParanoidiQ8NBS3.
KOiK13862.
OrthoDBiEOG7M6D7V.
PhylomeDBiQ8NBS3.
TreeFamiTF313630.

Family and domain databases

Gene3Di3.40.930.10. 1 hit.
InterProiIPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
[Graphical view]
PANTHERiPTHR11453. PTHR11453. 1 hit.
PfamiPF00955. HCO3_cotransp. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
PRINTSiPR01231. HCO3TRNSPORT.
SUPFAMiSSF55804. SSF55804. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NBS3-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MSQVGGRGDR CTQEVQGLVH GAGDLSASLA ENSPTMSQNG YFEDSSYYKC
60 70 80 90 100
DTDDTFEARE EILGDEAFDT ANSSIVSGES IRFFVNVNLE MQATNTENEA
110 120 130 140 150
TSGGCVLLHT SRKYLKLKNF KEEIRAHRDL DGFLAQASIV LNETATSLDN
160 170 180 190 200
VLRTMLRRFA RDPDNNEPNC NLDLLMAMLF TDAGAPMRGK VHLLSDTIQG
210 220 230 240 250
VTATVTGVRY QQSWLCIICT MKALQKRHVC ISRLVRPQNW GENSCEVRFV
260 270 280 290 300
ILVLAPPKMK STKTAMEVAR TFATMFSDIA FRQKLLETRT EEEFKEALVH
310 320 330 340 350
QRQLLTMVSH GPVAPRTKER STVSLPAHRH PEPPKCKDFV PFGKGIREDI
360 370 380 390 400
ARRFPLYPLD FTDGIIGKNK AVGKYITTTL FLYFACLLPT IAFGSLNDEN
410 420 430 440 450
TDGAIDVQKT IAGQSIGGLL YALFSGQPLV ILLTTAPLAL YIQVIRVICD
460 470 480 490 500
DYDLDFNSFY AWTGLWNSFF LALYAFFNLS LVMSLFKRST EEIIALFISI
510 520 530 540 550
TFVLDAVKGT VKIFWKYYYG HYLDDYHTKR TSSLVSLSGL GASLNASLHT
560 570 580 590 600
ALNASFLASP TELPSATHSG QATAVLSLLI MLGTLWLGYT LYQFKKSPYL
610 620 630 640 650
HPCVREILSD CALPIAVLAF SLISSHGFRE IEMSKFRYNP SESPFAMAQI
660 670 680 690 700
QSLSLRAVSG AMGLGFLLSM LFFIEQNLVA ALVNAPENRL VKGTAYHWDL
710 720 730 740 750
LLLAIINTGL SLFGLPWIHA AYPHSPLHVR ALALVEERVE NGHIYDTIVN
760 770 780 790 800
VKETRLTSLG ASVLVGLSLL LLPVPLQWIP KPVLYGLFLY IALTSLDGNQ
810 820 830 840 850
LVQRVALLLK EQTAYPPTHY IRRVPQRKIH YFTGLQVLQL LLLCAFGMSS
860 870 880 890
LPYMKMIFPL IMIAMIPIRY ILLPRIIEAK YLDVMDAEHR P
Length:891
Mass (Da):99,581
Last modified:April 4, 2003 - v2
Checksum:i06AC2FED156BF535
GO
Isoform 2 (identifier: Q8NBS3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-482: Missing.

Note: No experimental confirmation available.

Show »
Length:409
Mass (Da):45,762
Checksum:iA3AED736B90209A7
GO
Isoform 3 (identifier: Q8NBS3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MSQVGGRGDRCTQEVQGLVHGAGDLSASLA → MAAATRRVFHLQPC

Note: No experimental confirmation available.

Show »
Length:875
Mass (Da):98,181
Checksum:i6BEDDC9939BADF10
GO
Isoform 4 (identifier: Q8NBS3-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MSQVGGRGDRCTQEVQGLVHGAGDLSASLA → MGVYGPQDRS...FLRKTWISEH

Show »
Length:918
Mass (Da):103,145
Checksum:iBA314E50D8F6CD48
GO

Sequence cautioni

The sequence BAC11536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB90170.4 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAD55942.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti324 – 3241S → P in BAC11536. (PubMed:14702039)Curated
Sequence conflicti576 – 5761L → P in BAG59341. (PubMed:14702039)Curated
Sequence conflicti684 – 6841N → S in BAG59140. (PubMed:14702039)Curated
Sequence conflicti784 – 7841L → R in AAI10541. (PubMed:15489334)Curated
Sequence conflicti834 – 8341G → D in BAG59341. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721N → T.1 Publication
VAR_047806
Natural varianti91 – 911M → V.1 Publication
Corresponds to variant rs200940928 [ dbSNP | Ensembl ].
VAR_047807
Natural varianti125 – 1251R → H in CHED2. 1 Publication
VAR_063713
Natural varianti143 – 1431E → K in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 1 Publication
VAR_067272
Natural varianti150 – 1501N → S.
Corresponds to variant rs34520315 [ dbSNP | Ensembl ].
VAR_034944
Natural varianti160 – 1601A → T in CHED2. 2 Publications
VAR_034945
Natural varianti167 – 1671E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064422
Natural varianti209 – 2091R → W in CHED2. 1 Publication
VAR_064978
Natural varianti213 – 2131S → L in CHED2. 1 Publication
VAR_064979
Natural varianti213 – 2131S → P in CDPD. 1 Publication
VAR_034946
Natural varianti233 – 2331R → C in CHED2. 1 Publication
VAR_064980
Natural varianti269 – 2691A → V in CHED2; affects transport to the cell surface. 1 Publication
VAR_063714
Natural varianti282 – 2821R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064423
Natural varianti327 – 3271A → V.1 Publication
VAR_047808
Natural varianti386 – 3861C → R in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 3 Publications
VAR_063715
Natural varianti394 – 3941G → R in CHED2. 2 Publications
VAR_064981
Natural varianti399 – 3991E → K in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047809
Natural varianti401 – 4011T → K in CHED2. 1 Publication
VAR_064982
Natural varianti408 – 4081Q → H.1 Publication
VAR_015521
Natural varianti409 – 4091K → N.1 Publication
VAR_015522
Natural varianti418 – 4181G → D in CHED2. 2 Publications
VAR_064983
Natural varianti464 – 4641G → D in CHED2; affects protein processing and transport to the cell surface. 1 Publication
VAR_030662
Natural varianti473 – 4731L → R in CHED2. 1 Publication
VAR_064984
Natural varianti483 – 4831M → T.1 Publication
VAR_015523
Natural varianti488 – 4881R → K in CDPD. 1 Publication
VAR_034947
Natural varianti489 – 4891S → L in CHED2; affects protein processing and transport to the cell surface. 2 Publications
VAR_030663
Natural varianti526 – 5261Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064424
Natural varianti561 – 5611T → M.1 Publication
VAR_047810
Natural varianti565 – 5651S → L.1 Publication
VAR_047811
Natural varianti575 – 5751V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064425
Natural varianti583 – 5831G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
VAR_064426
Natural varianti584 – 5841T → K in CHED2. 1 Publication
VAR_064985
Natural varianti708 – 7081T → A.1 Publication
VAR_015524
Natural varianti709 – 7091G → E in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047812
Natural varianti742 – 7421G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
Corresponds to variant rs143965185 [ dbSNP | Ensembl ].
VAR_064427
Natural varianti754 – 7541T → M in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. 1 Publication
VAR_047813
Natural varianti755 – 7551R → Q in CHED2; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 4 Publications
VAR_030664
Natural varianti755 – 7551R → W in CHED2. 3 Publications
VAR_063716
Natural varianti773 – 7731P → L in CHED2. 2 Publications
VAR_063717
Natural varianti804 – 8041R → H in CHED2. 1 Publication
VAR_034948
Natural varianti824 – 8241V → M in CHED2; deafness not assessed. 3 Publications
VAR_034949
Natural varianti833 – 8331T → M in CHED2. 1 Publication
VAR_034950
Natural varianti834 – 8341G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
VAR_064428
Natural varianti843 – 8431L → P in CDPD. 1 Publication
VAR_034951
Natural varianti848 – 8481M → I.
Corresponds to variant rs34224785 [ dbSNP | Ensembl ].
VAR_034952
Natural varianti856 – 8561M → V in CDPD. 1 Publication
VAR_034953
Natural varianti869 – 8691R → C in CHED2; affects protein processing and transport to the cell surface. 3 Publications
VAR_030665
Natural varianti869 – 8691R → H in CHED2. 1 Publication
VAR_034954
Natural varianti873 – 8731L → P in CHED2. 1 Publication
VAR_063718

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 482482Missing in isoform 2. 1 PublicationVSP_035891Add
BLAST
Alternative sequencei1 – 3030MSQVG…SASLA → MAAATRRVFHLQPC in isoform 3. 1 PublicationVSP_044846Add
BLAST
Alternative sequencei1 – 3030MSQVG…SASLA → MGVYGPQDRSESEKRDVQRD PPPWHPRREGERPARARSLP LAAAGQGFLRKTWISEH in isoform 4. 1 PublicationVSP_054049Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336127 mRNA. Translation: AAK16734.1.
AK075303 mRNA. Translation: BAC11536.1. Different initiation.
AK296508 mRNA. Translation: BAG59140.1.
AK296760 mRNA. Translation: BAG59341.1.
AL109976 Genomic DNA. Translation: CAD55941.1.
AL109976 Genomic DNA. Translation: CAD55942.1. Sequence problems.
AL109976 Genomic DNA. Translation: CAB90170.4. Sequence problems.
CH471133 Genomic DNA. Translation: EAX10536.1.
BC110540 mRNA. Translation: AAI10541.1.
BC110541 mRNA. Translation: AAI10542.1.
CCDSiCCDS13052.1. [Q8NBS3-1]
CCDS54445.1. [Q8NBS3-4]
CCDS54446.1. [Q8NBS3-3]
RefSeqiNP_001167560.1. NM_001174089.1. [Q8NBS3-3]
NP_001167561.1. NM_001174090.1. [Q8NBS3-4]
NP_114423.1. NM_032034.3. [Q8NBS3-1]
UniGeneiHs.105607.

Genome annotation databases

EnsembliENST00000380056; ENSP00000369396; ENSG00000088836. [Q8NBS3-1]
ENST00000380059; ENSP00000369399; ENSG00000088836. [Q8NBS3-4]
ENST00000539553; ENSP00000441370; ENSG00000088836. [Q8NBS3-3]
GeneIDi83959.
KEGGihsa:83959.
UCSCiuc002wig.3. human. [Q8NBS3-1]
uc010zqf.2. human.

Polymorphism databases

DMDMi29611858.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336127 mRNA. Translation: AAK16734.1 .
AK075303 mRNA. Translation: BAC11536.1 . Different initiation.
AK296508 mRNA. Translation: BAG59140.1 .
AK296760 mRNA. Translation: BAG59341.1 .
AL109976 Genomic DNA. Translation: CAD55941.1 .
AL109976 Genomic DNA. Translation: CAD55942.1 . Sequence problems.
AL109976 Genomic DNA. Translation: CAB90170.4 . Sequence problems.
CH471133 Genomic DNA. Translation: EAX10536.1 .
BC110540 mRNA. Translation: AAI10541.1 .
BC110541 mRNA. Translation: AAI10542.1 .
CCDSi CCDS13052.1. [Q8NBS3-1 ]
CCDS54445.1. [Q8NBS3-4 ]
CCDS54446.1. [Q8NBS3-3 ]
RefSeqi NP_001167560.1. NM_001174089.1. [Q8NBS3-3 ]
NP_001167561.1. NM_001174090.1. [Q8NBS3-4 ]
NP_114423.1. NM_032034.3. [Q8NBS3-1 ]
UniGenei Hs.105607.

3D structure databases

ProteinModelPortali Q8NBS3.
SMRi Q8NBS3. Positions 353-400, 799-831.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123832. 1 interaction.
STRINGi 9606.ENSP00000369396.

Protein family/group databases

TCDBi 2.A.31.4.1. the anion exchanger (ae) family.

PTM databases

PhosphoSitei Q8NBS3.

Polymorphism databases

DMDMi 29611858.

Proteomic databases

MaxQBi Q8NBS3.
PaxDbi Q8NBS3.
PRIDEi Q8NBS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380056 ; ENSP00000369396 ; ENSG00000088836 . [Q8NBS3-1 ]
ENST00000380059 ; ENSP00000369399 ; ENSG00000088836 . [Q8NBS3-4 ]
ENST00000539553 ; ENSP00000441370 ; ENSG00000088836 . [Q8NBS3-3 ]
GeneIDi 83959.
KEGGi hsa:83959.
UCSCi uc002wig.3. human. [Q8NBS3-1 ]
uc010zqf.2. human.

Organism-specific databases

CTDi 83959.
GeneCardsi GC20M003203.
HGNCi HGNC:16438. SLC4A11.
HPAi HPA018120.
MIMi 217400. phenotype.
217700. phenotype.
610206. gene.
613268. phenotype.
neXtProti NX_Q8NBS3.
Orphaneti 293603. Congenital hereditary endothelial dystrophy type II.
1490. Corneal dystrophy - perceptive deafness.
98974. Fuchs endothelial corneal dystrophy.
PharmGKBi PA38139.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG268067.
GeneTreei ENSGT00760000119021.
HOGENOMi HOG000016966.
HOVERGENi HBG079162.
InParanoidi Q8NBS3.
KOi K13862.
OrthoDBi EOG7M6D7V.
PhylomeDBi Q8NBS3.
TreeFami TF313630.

Miscellaneous databases

GeneWikii SLC4A11.
GenomeRNAii 83959.
NextBioi 73102.
PROi Q8NBS3.
SOURCEi Search...

Gene expression databases

Bgeei Q8NBS3.
CleanExi HS_SLC4A11.
ExpressionAtlasi Q8NBS3. baseline and differential.
Genevestigatori Q8NBS3.

Family and domain databases

Gene3Di 3.40.930.10. 1 hit.
InterProi IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
[Graphical view ]
PANTHERi PTHR11453. PTHR11453. 1 hit.
Pfami PF00955. HCO3_cotransp. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view ]
PRINTSi PR01231. HCO3TRNSPORT.
SUPFAMi SSF55804. SSF55804. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human BTR1, a new bicarbonate transporter superfamily member and human AE4 from kidney."
    Parker M.D., Ourmozdi E.P., Tanner M.J.A.
    Biochem. Biophys. Res. Commun. 282:1103-1109(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS HIS-408; ASN-409; THR-483 AND ALA-708.
    Tissue: Kidney.
  2. "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] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-891 (ISOFORM 1).
    Tissue: Retinoblastoma, Thalamus and Tongue.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
  6. "NaBC1 is a ubiquitous electrogenic Na+-coupled borate transporter essential for cellular boron homeostasis and cell growth and proliferation."
    Park M., Li Q., Shcheynikov N., Zeng W., Muallem S.
    Mol. Cell 16:331-341(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANTS FECD4 LYS-399; GLU-709 AND MET-754, VARIANTS THR-72; VAL-91; VAL-327; MET-561 AND LEU-565, CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND MET-754.
  8. "Oligomerization of SLC4A11 protein and the severity of FECD and CHED2 corneal dystrophies caused by SLC4A11 mutations."
    Vilas G.L., Loganathan S.K., Quon A., Sundaresan P., Vithana E.N., Casey J.
    Hum. Mutat. 33:419-428(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, CHARACTERIZATION OF VARIANTS CHED2 LYS-143; ARG-386 AND TRP-755, CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND MET-754.
  9. Cited for: VARIANTS CHED2 ASP-464; LEU-489; GLN-755 AND CYS-869, CHARACTERIZATION OF VARIANTS CHED2 ASP-464; LEU-489; GLN-755 AND CYS-869, TISSUE SPECIFICITY.
  10. "Novel SLC4A11 mutations in patients with recessive congenital hereditary endothelial dystrophy (CHED2). Mutation in brief #958. Online."
    Ramprasad V.L., Ebenezer N.D., Aung T., Rajagopal R., Yong V.H., Tuft S.J., Viswanathan D., El-Ashry M.F., Liskova P., Tan D.T., Bhattacharya S.S., Kumaramanickavel G., Vithana E.N.
    Hum. Mutat. 28:522-523(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 LYS-143; ARG-386; TRP-755; GLN-755 AND CYS-869.
  11. "Autosomal recessive corneal endothelial dystrophy (CHED2) is associated with mutations in SLC4A11."
    Jiao X., Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., Gangopadhyay N., Hejtmancik J.F., Kannabiran C.
    J. Med. Genet. 44:64-68(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 GLN-755; HIS-804; MET-833 AND HIS-869, VARIANT THR-160.
  12. "Borate transporter SLC4A11 mutations cause both Harboyan syndrome and non-syndromic corneal endothelial dystrophy."
    Desir J., Moya G., Reish O., Van Regemorter N., Deconinck H., David K.L., Meire F.M., Abramowicz M.J.
    J. Med. Genet. 44:322-326(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDPD PRO-213; LYS-488; PRO-843 AND VAL-856, VARIANT CHED2 MET-824.
  13. "Mutational spectrum of the SLC4A11 gene in autosomal recessive congenital hereditary endothelial dystrophy."
    Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., Kannabiran C.
    Mol. Vis. 13:1327-1332(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 TRP-209; LEU-213; CYS-233; LYS-401; ASP-418; ARG-473; LEU-489; LYS-584; TRP-755; GLN-755; LEU-773; MET-824 AND CYS-869.
  14. "Identification of mutations in the SLC4A11 gene in patients with recessive congenital hereditary endothelial dystrophy."
    Hemadevi B., Veitia R.A., Srinivasan M., Arunkumar J., Prajna N.V., Lesaffre C., Sundaresan P.
    Arch. Ophthalmol. 126:700-708(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 HIS-125; THR-160; VAL-269; ARG-386; TRP-755; LEU-773 AND PRO-873.
  15. "Mutational spectrum of SLC4A11 in autosomal recessive CHED in Saudi Arabia."
    Aldahmesh M.A., Khan A.O., Meyer B.F., Alkuraya F.S.
    Invest. Ophthalmol. Vis. Sci. 50:4142-4145(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 ARG-394 AND ASP-418.
  16. "Novel human pathological mutations. Gene symbol: SLC4A11. Disease: Corneal endothelial dystrophy 2."
    Chai S.M., Vithana E.N., Venkataraman D., Saleh H., Chekkalichintavida N.P., al-Sayyed F., Aung T.
    Hum. Genet. 127:110-110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CHED2 ARG-394.
  17. "Missense mutations in the sodium borate cotransporter SLC4A11 cause late-onset Fuchs corneal dystrophya."
    Riazuddin S.A., Vithana E.N., Seet L.F., Liu Y., Al-Saif A., Koh L.W., Heng Y.M., Aung T., Meadows D.N., Eghrari A.O., Gottsch J.D., Katsanis N.
    Hum. Mutat. 31:1261-1268(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FECD4 ASP-167; PRO-282; CYS-526; MET-575; ASP-583; ARG-742 AND SER-834, CHARACTERIZATION OF VARIANTS FECD4 ASP-167; PRO-282; CYS-526; MET-575; ASP-583; ARG-742 AND SER-834.
  18. "SLC4A11 prevents osmotic imbalance leading to corneal endothelial dystrophy, deafness, and polyuria."
    Groger N., Frohlich H., Maier H., Olbrich A., Kostin S., Braun T., Boettger T.
    J. Biol. Chem. 285:14467-14474(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CHED2 VAL-269.
  19. "Congenital hereditary endothelial dystrophy - mutation analysis of SLC4A11 and genotype-phenotype correlation in a North Indian patient cohort."
    Paliwal P., Sharma A., Tandon R., Sharma N., Titiyal J.S., Sen S., Nag T.C., Vajpayee R.B.
    Mol. Vis. 16:2955-2963(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHED2 ARG-386 AND MET-824.

Entry informationi

Entry nameiS4A11_HUMAN
AccessioniPrimary (citable) accession number: Q8NBS3
Secondary accession number(s): B4DKC8
, B4DKX9, G3V1M3, Q2TB62, Q2TB63, Q9BXF4, Q9NTW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: April 4, 2003
Last modified: October 29, 2014
This is version 116 of the entry and version 2 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 20
    Human chromosome 20: 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