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Q9Y6R1

- S4A4_HUMAN

UniProt

Q9Y6R1 - S4A4_HUMAN

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Protein

Electrogenic sodium bicarbonate cotransporter 1

Gene

SLC4A4

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

Functioni

Electrogenic sodium/bicarbonate cotransporter with a Na+:HCO3- stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.6 Publications

Enzyme regulationi

Inhibited by stilbene derivatives and regulated by cyclic AMP.

GO - Molecular functioni

  1. inorganic anion exchanger activity Source: InterPro
  2. sodium:bicarbonate symporter activity Source: UniProtKB

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. ion transport Source: Reactome
  3. sodium ion transmembrane transport Source: GOC
  4. transmembrane transport Source: Reactome
  5. transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiREACT_19298. Bicarbonate transporters.

Protein family/group databases

TCDBi2.A.31.2.12. the anion exchanger (ae) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Electrogenic sodium bicarbonate cotransporter 1
Short name:
Sodium bicarbonate cotransporter
Alternative name(s):
Na(+)/HCO3(-) cotransporter
Solute carrier family 4 member 4
kNBC1
Gene namesi
Name:SLC4A4
Synonyms:NBC, NBC1, NBCE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11030. SLC4A4.

Subcellular locationi

Basolateral cell membrane 4 Publications; Multi-pass membrane protein 2 Publications

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Renal tubular acidosis, proximal, with ocular abnormalities and mental retardation (pRTA-OA) [MIM:604278]: An extremely rare autosomal recessive syndrome characterized by short stature, profound proximal renal tubular acidosis, mental retardation, bilateral glaucoma, cataracts and bandkeratopathy. pRTA is due to a failure of the proximal tubular cells to reabsorb filtered bicarbonate from the urine, leading to urinary bicarbonate wasting and subsequent acidemia.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti342 – 3421R → S in pRTA-OA; decreased localization to the basolateral membrane; mistargeting to the apical membrane probably explains the loss of the cotransporter activity. 3 Publications1 Publication
VAR_024751
Natural varianti471 – 4711S → L in pRTA-OA; mistargeting to the apical membrane and altered function. 2 Publications
VAR_024752
Natural varianti529 – 5291T → S in pRTA-OA; decreased cotransporter activity. 1 Publication1 Publication
VAR_024753
Natural varianti530 – 5301G → R in pRTA-OA; decreased cotransporter activity; no effect on localization to the basolateral membrane. 1 Publication
VAR_071661
Natural varianti554 – 5541R → H in pRTA-OA; mistargeting and altered function. 3 Publications
VAR_024754
Natural varianti566 – 5661L → P in pRTA-OA; loss of localization to the plasma membrane; the retention in the cytoplasm probably explains the loss of the cotransporter activity. 1 Publication1 Publication
VAR_071662
Natural varianti843 – 8431A → V in pRTA-OA; altered function. 1 Publication
VAR_024755
Natural varianti925 – 9251R → C in pRTA-OA; altered function. 1 Publication
VAR_024756
Loss of interaction with and stimulation by CA4 is the cause of retinitis pigmentosa type 17 (RP17).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491T → A: Loss of conductance regulation by cAMP; isoform 1. 1 Publication
Mutagenesisi49 – 491T → D: Loss of conductance regulation by cAMP; isoform 1. 1 Publication
Mutagenesisi135 – 1351E → R: Mistargeting and altered function. 1 Publication
Mutagenesisi477 – 4771Y → F: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi493 – 4931D → N: Prevents membrane targeting. 1 Publication
Mutagenesisi494 – 4941A → K: Prevents membrane targeting. 1 Publication
Mutagenesisi503 – 5031E → Q: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi504 – 5041S → L: Prevents membrane targeting. 1 Publication
Mutagenesisi536 – 5361E → Q: Prevents membrane targeting. 1 Publication
Mutagenesisi552 – 5521E → N: Prevents membrane targeting. 1 Publication
Mutagenesisi554 – 5541R → D: Prevents membrane targeting. 1 Publication
Mutagenesisi582 – 5821R → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi582 – 5821R → Q: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi586 – 5861E → Q: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi599 – 5991D → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi600 – 6001A → T: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi602 – 6021K → Q: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi603 – 6031K → Q: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi691 – 6911D → R: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi700 – 7001F → M: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi711 – 7111K → E, N or Q: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi711 – 7111K → R: No effect on the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi712 – 7121K → N: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi714 – 7141K → Q: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi715 – 7151T → N: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi721 – 7211T → G: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi724 – 7241R → E: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi725 – 7251K → N: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi728 – 7281S → G: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi729 – 7291D → N or R: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi743 – 7431D → K or N: Prevents membrane targeting. 1 Publication
Mutagenesisi749 – 7491D → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi752 – 7521K → Q: Prevents membrane targeting. 1 Publication
Mutagenesisi766 – 7661R → Q: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi767 – 7671G → T: Alters interaction with CA4. 1 Publication
Mutagenesisi775 – 7751E → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi798 – 7981D → E, N or R: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi808 – 8092RK → NN: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi814 – 8152KK → NN: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi820 – 8201H → D, N, S or R: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi822 – 8221D → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi851 – 8511H → N: Prevents membrane targeting. 1 Publication
Mutagenesisi853 – 8531D → N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi858 – 8603ETE → MSK: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi875 – 8773EQR → QQQ: Prevents membrane targeting. 1 Publication
Mutagenesisi875 – 8751E → Q: Strong reduction of the sodium-dependent ion transport activity.
Mutagenesisi898 – 8981K → E: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi925 – 9273RLK → NLN: Prevents membrane targeting. 1 Publication
Mutagenesisi948 – 9481R → E: Strong reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi949 – 9491R → E: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi951 – 9511H → D: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi951 – 9511H → N or R: Prevents membrane targeting. 1 Publication
Mutagenesisi968 – 9681K → Q: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi987 – 9871R → E or N: Moderate reduction of the sodium-dependent ion transport activity. 1 Publication
Mutagenesisi1002 – 10021L → N: Partial loss of interaction with CA2. 1 Publication
Mutagenesisi1003 – 10031D → N: Abolishes interaction with CA2. 1 Publication
Mutagenesisi1004 – 10041D → N: Partial loss of interaction with CA2. 1 Publication
Mutagenesisi1026 – 10261S → A: Prevents phosphorylation by PKA. Loss of regulation by cAMP of the transporter stoichiometry. 2 Publications
Mutagenesisi1026 – 10261S → D: Loss of regulation by cAMP of the transporter stoichiometry. Shifts transporter stoichiometry from 3:1 to 2:1. 2 Publications
Mutagenesisi1030 – 10334DNDD → NNNN: Abolishes interaction with CA2. 1 Publication
Mutagenesisi1030 – 10301D → N: Loss of regulation by cAMP of the transporter stoichiometry. Abolishes interaction with CA2. 1 Publication
Mutagenesisi1032 – 10321D → N: Loss of regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. 1 Publication
Mutagenesisi1033 – 10331D → N: No effect on regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. 1 Publication
Mutagenesisi1057 – 10571F → A: Targeting to apical membrane. 1 Publication

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi604278. phenotype.
Orphaneti93607. Autosomal recessive proximal renal tubular acidosis.
PharmGKBiPA35898.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10791079Electrogenic sodium bicarbonate cotransporter 1PRO_0000079227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301PhosphotyrosineBy similarity
Modified residuei49 – 491Phosphothreonine; by PKA1 Publication
Modified residuei254 – 2541PhosphothreonineBy similarity
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei262 – 2621PhosphoserineBy similarity
Glycosylationi641 – 6411N-linked (GlcNAc...)By similarity
Glycosylationi661 – 6611N-linked (GlcNAc...)By similarity
Modified residuei1026 – 10261Phosphoserine; by PKA1 Publication
Modified residuei1029 – 10291PhosphoserineBy similarity
Modified residuei1034 – 10341PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of Ser-1026 by PKA increases the binding of CA2 and changes the Na+:HCO3- stoichiometry of the transporter from 3:1 to 2:1. Phosphorylation of Thr-49 regulates isoform 1 conductance.2 Publications
N-glycosylation is not necessary for the transporter basic functions.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6R1.
PaxDbiQ9Y6R1.
PRIDEiQ9Y6R1.

PTM databases

PhosphoSiteiQ9Y6R1.

Expressioni

Tissue specificityi

Isoform 1 is expressed in pancreas and to a lower extent in heart, skeletal muscle, liver, parotid salivary glands, prostate, colon, stomach, thyroid, brain and spinal chord. Corneal endothelium cells express only isoform 1 (at protein level). Isoform 2 is specifically expressed in kidney at the level of proximal tubules.7 Publications

Gene expression databases

BgeeiQ9Y6R1.
CleanExiHS_SLC4A4.
ExpressionAtlasiQ9Y6R1. baseline and differential.
GenevestigatoriQ9Y6R1.

Organism-specific databases

HPAiCAB022493.
HPA035628.
HPA035629.

Interactioni

Subunit structurei

Interacts with CA2/carbonic anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate transporter activity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CA4P482832EBI-6859278,EBI-6859264From a different organism.

Protein-protein interaction databases

BioGridi114219. 1 interaction.
DIPiDIP-59373N.
IntActiQ9Y6R1. 4 interactions.
STRINGi9606.ENSP00000393557.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6R1.
SMRiQ9Y6R1. Positions 107-382, 453-493.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 468468CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini489 – 50416ExtracellularSequence AnalysisAdd
BLAST
Topological domaini527 – 55428CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini581 – 691111ExtracellularSequence AnalysisAdd
BLAST
Topological domaini711 – 72515CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini749 – 77729ExtracellularSequence AnalysisAdd
BLAST
Topological domaini798 – 82225CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini848 – 88134ExtracellularSequence AnalysisAdd
BLAST
Topological domaini902 – 94948CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini968 – 9703ExtracellularSequence Analysis
Topological domaini987 – 107993CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei469 – 48820HelicalSequence AnalysisAdd
BLAST
Transmembranei505 – 52622HelicalSequence AnalysisAdd
BLAST
Transmembranei555 – 58026HelicalSequence AnalysisAdd
BLAST
Transmembranei692 – 71019HelicalSequence AnalysisAdd
BLAST
Transmembranei726 – 74823HelicalSequence AnalysisAdd
BLAST
Transmembranei778 – 79720HelicalSequence AnalysisAdd
BLAST
Transmembranei823 – 84725HelicalSequence AnalysisAdd
BLAST
Transmembranei882 – 90120HelicalSequence AnalysisAdd
BLAST
Transmembranei950 – 96718HelicalSequence AnalysisAdd
BLAST
Transmembranei971 – 98616HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni748 – 77932Interaction with CA4Add
BLAST
Regioni1002 – 10043CA2-binding
Regioni1030 – 10334CA2-binding
Regioni1057 – 10593Required for basolateral targeting

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1009 – 102416Lys-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG251607.
GeneTreeiENSGT00760000119021.
HOVERGENiHBG004326.
InParanoidiQ9Y6R1.
KOiK13575.
OMAiVCSFMAL.
OrthoDBiEOG7TMZR0.
PhylomeDBiQ9Y6R1.
TreeFamiTF313630.

Family and domain databases

Gene3Di3.40.1100.10. 1 hit.
InterProiIPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR003024. Na/HCO3_transpt.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]
PANTHERiPTHR11453. PTHR11453. 1 hit.
PfamiPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view]
PRINTSiPR01231. HCO3TRNSPORT.
PR01232. NAHCO3TRSPRT.
SUPFAMiSSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00834. ae. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6R1-1) [UniParc]FASTAAdd to Basket

Also known as: hcNBC, hhNBC, hNBC1, pNBC, pNCB1, pNBC-1, NBC1b

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
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG
60 70 80 90 100
HKEKKEKERI SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED
110 120 130 140 150
DSPAPPQLFT ELDELLAVDG QEMEWKETAR WIKFEEKVEQ GGERWSKPHV
160 170 180 190 200
ATLSLHSLFE LRTCMEKGSI MLDREASSLP QLVEMIVDHQ IETGLLKPEL
210 220 230 240 250
KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN PDNGSPAMTH
260 270 280 290 300
RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
310 320 330 340 350
AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD
360 370 380 390 400
EVFHDIAYKA KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS
410 420 430 440 450
DKRKNMYSGG ENVQMNGDTP HDGGHGGGGH GDCEELQRTG RFCGGLIKDI
460 470 480 490 500
KRKAPFFASD FYDALNIQAL SAILFIYLAT VTNAITFGGL LGDATDNMQG
510 520 530 540 550
VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF NFSKDNNFDY
560 570 580 590 600
LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
610 620 630 640 650
FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL
660 670 680 690 700
PTMSSTDMYH NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF
710 720 730 740 750
LGTYTSSMAL KKFKTSPYFP TTARKLISDF AIILSILIFC VIDALVGVDT
760 770 780 790 800
PKLIVPSEFK PTSPNRGWFV PPFGENPWWV CLAAAIPALL VTILIFMDQQ
810 820 830 840 850
ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VICSLMALPW YVAATVISIA
860 870 880 890 900
HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
910 920 930 940 950
PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV
960 970 980 990 1000
HLFTFLQVLC LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS
1010 1020 1030 1040 1050
FLDDVIPEKD KKKKEDEKKK KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD
1060 1070
IMEQQPFLSD SKPSDRERSP TFLERHTSC
Length:1,079
Mass (Da):121,461
Last modified:November 1, 1999 - v1
Checksum:i14B981A94DD64293
GO
Isoform 2 (identifier: Q9Y6R1-2) [UniParc]FASTAAdd to Basket

Also known as: hkNBC, hkNBCe1, kNBC, kNBC1, kNBC-1, NBC1a

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKTGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV

Show »
Length:1,035
Mass (Da):116,040
Checksum:i122096381B33D776
GO
Isoform 3 (identifier: Q9Y6R1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKTGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV
     635-690: ANISISNDTT...LVGNNCNFVP → GEGITLCVYA...EFDVSLPEVF
     691-1079: Missing.

Show »
Length:646
Mass (Da):72,049
Checksum:i285D5E23C540A516
GO
Isoform 4 (identifier: Q9Y6R1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     813-896: Missing.

Show »
Length:995
Mass (Da):112,272
Checksum:i38B4A37EA047E9AC
GO
Isoform 5 (identifier: Q9Y6R1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1034-1079: SDCPYSEKVP...PTFLERHTSC → EKDHQHSLNA...WRSKGTETTL

Show »
Length:1,094
Mass (Da):123,181
Checksum:iB02FF2193A5F95C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61V → A in AAG47773. (PubMed:12907161)Curated
Sequence conflicti49 – 491T → A in BAH58226. 1 PublicationCurated
Sequence conflicti78 – 781S → G in AAF21718. (PubMed:10069984)Curated
Sequence conflicti256 – 2561S → F in AAD42020. (PubMed:10069984)Curated
Sequence conflicti263 – 2631D → E in AAF21718. (PubMed:10069984)Curated
Sequence conflicti298 – 2981P → H in BAH58226. 1 PublicationCurated
Sequence conflicti364 – 3641H → R in AAF21719. (PubMed:10069984)Curated
Sequence conflicti605 – 6051I → V in AAF21718. (PubMed:10069984)Curated
Sequence conflicti654 – 6541S → P in AAF21718. (PubMed:10069984)Curated
Sequence conflicti749 – 7491D → G in AAF21719. (PubMed:10069984)Curated
Sequence conflicti799 – 7991Q → R in AAG47773. (PubMed:12907161)Curated
Sequence conflicti856 – 8561K → R in AAG47773. (PubMed:12907161)Curated
Sequence conflicti912 – 9121M → R in AAF21718. (PubMed:10069984)Curated
Sequence conflicti913 – 9131G → R in AAF21719. (PubMed:10069984)Curated
Sequence conflicti940 – 9401I → V in AAF21718. (PubMed:10069984)Curated
Sequence conflicti1007 – 10071P → S in AAF21719. (PubMed:10069984)Curated
Sequence conflicti1069 – 10691S → P in AAF21719. (PubMed:10069984)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti342 – 3421R → S in pRTA-OA; decreased localization to the basolateral membrane; mistargeting to the apical membrane probably explains the loss of the cotransporter activity. 3 Publications1 Publication
VAR_024751
Natural varianti471 – 4711S → L in pRTA-OA; mistargeting to the apical membrane and altered function. 2 Publications
VAR_024752
Natural varianti529 – 5291T → S in pRTA-OA; decreased cotransporter activity. 1 Publication1 Publication
VAR_024753
Natural varianti530 – 5301G → R in pRTA-OA; decreased cotransporter activity; no effect on localization to the basolateral membrane. 1 Publication
VAR_071661
Natural varianti554 – 5541R → H in pRTA-OA; mistargeting and altered function. 3 Publications
VAR_024754
Natural varianti566 – 5661L → P in pRTA-OA; loss of localization to the plasma membrane; the retention in the cytoplasm probably explains the loss of the cotransporter activity. 1 Publication1 Publication
VAR_071662
Natural varianti843 – 8431A → V in pRTA-OA; altered function. 1 Publication
VAR_024755
Natural varianti925 – 9251R → C in pRTA-OA; altered function. 1 Publication
VAR_024756

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform 2 and isoform 3. 2 PublicationsVSP_016704Add
BLAST
Alternative sequencei45 – 8541HKRKT…LKPLI → MSTENVEGKPSNLGERGRAR SSTFLRVVQPMFNHSIFTSA V in isoform 2 and isoform 3. 2 PublicationsVSP_016705Add
BLAST
Alternative sequencei635 – 69056ANISI…CNFVP → GEGITLCVYARFVFGGRCRL HACKFSTCCHGPQELVLFFS LKNSATEFDVSLPEVF in isoform 3. 1 PublicationVSP_016706Add
BLAST
Alternative sequencei691 – 1079389Missing in isoform 3. 1 PublicationVSP_016707Add
BLAST
Alternative sequencei813 – 89684Missing in isoform 4. 1 PublicationVSP_016708Add
BLAST
Alternative sequencei1034 – 107946SDCPY…RHTSC → EKDHQHSLNATHHADKIPFL QSLGMPSPPRTPVKVVPQIR IELEPEDNDYFWRSKGTETT L in isoform 5. 1 PublicationVSP_041003Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007216 mRNA. Translation: AAC51645.1.
AF011390 mRNA. Translation: AAC39840.1.
AF053753 mRNA. Translation: AAF21718.1.
AF053754 mRNA. Translation: AAF21719.1.
AF069510 mRNA. Translation: AAD42020.1.
AF310248 mRNA. Translation: AAG47773.1.
AF157492 mRNA. Translation: AAF80343.1.
AB470072 mRNA. Translation: BAH58226.1.
AC019089 Genomic DNA. No translation available.
AC079230 Genomic DNA. No translation available.
AC096713 Genomic DNA. No translation available.
AC110783 Genomic DNA. No translation available.
AC112226 Genomic DNA. No translation available.
BC030977 mRNA. Translation: AAH30977.1.
CCDSiCCDS3549.1. [Q9Y6R1-2]
CCDS43236.1. [Q9Y6R1-1]
CCDS47071.1. [Q9Y6R1-5]
RefSeqiNP_001091954.1. NM_001098484.2. [Q9Y6R1-1]
NP_003750.1. NM_003759.3. [Q9Y6R1-2]
UniGeneiHs.5462.

Genome annotation databases

EnsembliENST00000264485; ENSP00000264485; ENSG00000080493. [Q9Y6R1-1]
ENST00000340595; ENSP00000344272; ENSG00000080493. [Q9Y6R1-2]
ENST00000351898; ENSP00000307349; ENSG00000080493. [Q9Y6R1-4]
ENST00000425175; ENSP00000393557; ENSG00000080493. [Q9Y6R1-5]
ENST00000512686; ENSP00000422400; ENSG00000080493. [Q9Y6R1-3]
GeneIDi8671.
KEGGihsa:8671.
UCSCiuc003hfy.3. human. [Q9Y6R1-1]
uc003hga.2. human. [Q9Y6R1-3]
uc003hgc.4. human. [Q9Y6R1-2]
uc010iib.3. human. [Q9Y6R1-4]

Polymorphism databases

DMDMi74721543.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007216 mRNA. Translation: AAC51645.1 .
AF011390 mRNA. Translation: AAC39840.1 .
AF053753 mRNA. Translation: AAF21718.1 .
AF053754 mRNA. Translation: AAF21719.1 .
AF069510 mRNA. Translation: AAD42020.1 .
AF310248 mRNA. Translation: AAG47773.1 .
AF157492 mRNA. Translation: AAF80343.1 .
AB470072 mRNA. Translation: BAH58226.1 .
AC019089 Genomic DNA. No translation available.
AC079230 Genomic DNA. No translation available.
AC096713 Genomic DNA. No translation available.
AC110783 Genomic DNA. No translation available.
AC112226 Genomic DNA. No translation available.
BC030977 mRNA. Translation: AAH30977.1 .
CCDSi CCDS3549.1. [Q9Y6R1-2 ]
CCDS43236.1. [Q9Y6R1-1 ]
CCDS47071.1. [Q9Y6R1-5 ]
RefSeqi NP_001091954.1. NM_001098484.2. [Q9Y6R1-1 ]
NP_003750.1. NM_003759.3. [Q9Y6R1-2 ]
UniGenei Hs.5462.

3D structure databases

ProteinModelPortali Q9Y6R1.
SMRi Q9Y6R1. Positions 107-382, 453-493.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114219. 1 interaction.
DIPi DIP-59373N.
IntActi Q9Y6R1. 4 interactions.
STRINGi 9606.ENSP00000393557.

Chemistry

DrugBanki DB01390. Sodium bicarbonate.

Protein family/group databases

TCDBi 2.A.31.2.12. the anion exchanger (ae) family.

PTM databases

PhosphoSitei Q9Y6R1.

Polymorphism databases

DMDMi 74721543.

Proteomic databases

MaxQBi Q9Y6R1.
PaxDbi Q9Y6R1.
PRIDEi Q9Y6R1.

Protocols and materials databases

DNASUi 8671.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264485 ; ENSP00000264485 ; ENSG00000080493 . [Q9Y6R1-1 ]
ENST00000340595 ; ENSP00000344272 ; ENSG00000080493 . [Q9Y6R1-2 ]
ENST00000351898 ; ENSP00000307349 ; ENSG00000080493 . [Q9Y6R1-4 ]
ENST00000425175 ; ENSP00000393557 ; ENSG00000080493 . [Q9Y6R1-5 ]
ENST00000512686 ; ENSP00000422400 ; ENSG00000080493 . [Q9Y6R1-3 ]
GeneIDi 8671.
KEGGi hsa:8671.
UCSCi uc003hfy.3. human. [Q9Y6R1-1 ]
uc003hga.2. human. [Q9Y6R1-3 ]
uc003hgc.4. human. [Q9Y6R1-2 ]
uc010iib.3. human. [Q9Y6R1-4 ]

Organism-specific databases

CTDi 8671.
GeneCardsi GC04P072017.
HGNCi HGNC:11030. SLC4A4.
HPAi CAB022493.
HPA035628.
HPA035629.
MIMi 603345. gene.
604278. phenotype.
neXtProti NX_Q9Y6R1.
Orphaneti 93607. Autosomal recessive proximal renal tubular acidosis.
PharmGKBi PA35898.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251607.
GeneTreei ENSGT00760000119021.
HOVERGENi HBG004326.
InParanoidi Q9Y6R1.
KOi K13575.
OMAi VCSFMAL.
OrthoDBi EOG7TMZR0.
PhylomeDBi Q9Y6R1.
TreeFami TF313630.

Enzyme and pathway databases

Reactomei REACT_19298. Bicarbonate transporters.

Miscellaneous databases

ChiTaRSi SLC4A4. human.
GeneWikii SLC4A4.
GenomeRNAii 8671.
NextBioi 32523.
PROi Q9Y6R1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6R1.
CleanExi HS_SLC4A4.
ExpressionAtlasi Q9Y6R1. baseline and differential.
Genevestigatori Q9Y6R1.

Family and domain databases

Gene3Di 3.40.1100.10. 1 hit.
InterProi IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR003024. Na/HCO3_transpt.
IPR016152. PTrfase/Anion_transptr.
[Graphical view ]
PANTHERi PTHR11453. PTHR11453. 1 hit.
Pfami PF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view ]
PRINTSi PR01231. HCO3TRNSPORT.
PR01232. NAHCO3TRSPRT.
SUPFAMi SSF55804. SSF55804. 1 hit.
TIGRFAMsi TIGR00834. ae. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression of a human kidney Na+:HCO3-cotransporter."
    Burnham C.E., Amlal H., Wang Z., Shull G.E., Soleimani M.
    J. Biol. Chem. 272:19111-19114(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter."
    Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A., Kurtz I.
    J. Biol. Chem. 273:17689-17695(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Pancreas.
  3. "Cloning and characterization of a human electrogenic Na+-HCO-3 cotransporter isoform (hhNBC)."
    Choi I., Romero M.F., Khandoudi N., Bril A., Boron W.F.
    Am. J. Physiol. 276:C576-C584(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Heart, Kidney and Prostate.
  4. "Identification and cloning of the Na/HCO3- cotransporter (NBC) in human corneal endothelium."
    Sun X.C., Bonanno J.A.
    Exp. Eye Res. 77:287-295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CORNEAL ENDOTHELIAL CELLS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Corneal endothelium.
  5. "Homo sapiens sodium bicarbonate cotransporter NBC1 splice variant."
    Pushkin A., Abuladze N., Kurtz I.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Skeletal muscle.
  6. "cDNA cloning and characterization of human sodium bicarbonate cotransporter, bNBC, a brain type splicing variant of SLC4A4 gene."
    Yamada H., Nagayoshi A., Kuroda Y., Mizutani A., Ando H., Seki G., Mikoshiba K.
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 3).
    Tissue: Kidney.
  9. "Phosphorylation of Ser(982) in the sodium bicarbonate cotransporter kNBC1 shifts the HCO(3)(-):Na(+) stoichiometry from 3:1 to 2:1 in murine proximal tubule cells."
    Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R., Abuladze N., Hopfer U., Kurtz I.
    J. Physiol. (Lond.) 537:659-665(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION, MUTAGENESIS OF SER-1026, PHOSPHORYLATION AT SER-1026.
  10. Erratum
    Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R., Abuladze N., Hopfer U., Kurtz I.
    J. Physiol. (Lond.) 538:1003-1003(2002)
  11. "Expression of a sodium bicarbonate cotransporter in human parotid salivary glands."
    Park K., Hurley P.T., Roussa E., Cooper G.J., Smith C.P., Thevenod F., Steward M.C., Case R.M.
    Arch. Oral Biol. 47:1-9(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Regulation of the sodium bicarbonate cotransporter kNBC1 function: role of Asp(986), Asp(988) and kNBC1-carbonic anhydrase II binding."
    Gross E., Pushkin A., Abuladze N., Fedotoff O., Kurtz I.
    J. Physiol. (Lond.) 544:679-685(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION, MUTAGENESIS OF ASP-1030; ASP-1032 AND ASP-1033, INTERACTION WITH CA2.
  13. "Role of glycosylation in the renal electrogenic Na+-HCO3-cotransporter (NBCe1)."
    Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F.
    Am. J. Physiol. 284:F1199-F1206(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  14. Cited for: TISSUE SPECIFICITY.
  15. "Identification of membrane topography of the electrogenic sodium bicarbonate cotransporter pNBC1 by in vitro transcription/translation."
    Tatishchev S., Abuladze N., Pushkin A., Newman D., Liu W., Weeks D., Sachs G., Kurtz I.
    Biochemistry 42:755-765(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  16. "Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter."
    Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.
    Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION, INTERACTION WITH CA2 AND CA4, MUTAGENESIS OF GLY-767.
  17. "Phosphorylation-induced modulation of pNBC1 function: distinct roles for the amino- and carboxy-termini."
    Gross E., Fedotoff O., Pushkin A., Abuladze N., Newman D., Kurtz I.
    J. Physiol. (Lond.) 549:673-682(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION, MUTAGENESIS OF THR-49 AND SER-1026, PHOSPHORYLATION AT THR-49.
  18. "Expression of Na+/HCO3- co-transporter proteins (NBCs) in rat and human skeletal muscle."
    Kristensen J.M., Kristensen M., Juel C.
    Acta Physiol. Scand. 182:69-76(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  19. "Identification of a carboxyl-terminal motif essential for the targeting of Na+-HCO-3 cotransporter NBC1 to the basolateral membrane."
    Li H.C., Worrell R.T., Matthews J.B., Husseinzadeh H., Neumeier L., Petrovic S., Conforti L., Soleimani M.
    J. Biol. Chem. 279:43190-43197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-1057, SUBCELLULAR LOCATION.
  20. "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells."
    Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.
    J. Physiol. (Lond.) 559:55-65(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CA2, MUTAGENESIS OF 1002-LEU--ASN-1004 AND 1030-ASP--ASP-1033.
  21. Cited for: INTERACTION WITH CA4.
  22. "Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport."
    Abuladze N., Azimov R., Newman D., Sassani P., Liu W., Tatishchev S., Pushkin A., Kurtz I.
    J. Physiol. (Lond.) 565:717-730(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-477; ASP-493; ALA-494; GLU-503; SER-504; GLU-536; GLU-552; ARG-554; ARG-582; GLU-586; ASP-599; ALA-600; LYS-602; LYS-603; ASP-691; PHE-700; LYS-711; LYS-712; LYS-714; THR-715; THR-721; ARG-724; LYS-725; SER-728; ASP-729; ASP-743; ASP-749; LYS-752; ARG-766; GLU-775; ASP-798; 808-ARG--LYS-809; 814-LYS--LYS-815; HIS-820; ASP-822; HIS-851; ASP-853; 858-GLU--GLU-860; 875-GLU--ARG-877; LYS-898; 925-ARG--LYS-927; ARG-948; ARG-949; HIS-951; LYS-968 AND ARG-987.
  23. "Mutations in SLC4A4 cause permanent isolated proximal renal tubular acidosis with ocular abnormalities."
    Igarashi T., Inatomi J., Sekine T., Cha S.H., Kanai Y., Kunimi M., Tsukamoto K., Satoh H., Shimadzu M., Tozawa F., Mori T., Shiobara M., Seki G., Endou H.
    Nat. Genet. 23:264-266(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRTA-OA SER-342 AND HIS-554.
  24. "A novel missense mutation in the sodium bicarbonate cotransporter (NBCe1/SLC4A4) causes proximal tubular acidosis and glaucoma through ion transport defects."
    Dinour D., Chang M.-H., Satoh J., Smith B.L., Angle N., Knecht A., Serban I., Holtzman E.J., Romero M.F.
    J. Biol. Chem. 279:52238-52246(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRTA-OA LEU-471.
  25. "Missense mutations in Na+:HCO3- cotransporter NBC1 show abnormal trafficking in polarized kidney cells: a basis of proximal renal tubular acidosis."
    Li H.C., Szigligeti P., Worrell R.T., Matthews J.B., Conforti L., Soleimani M.
    Am. J. Physiol. 289:F61-F71(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRTA-OA SER-342; LEU-471 AND HIS-554, MUTAGENESIS OF GLU-135.
  26. "Functional analysis of NBC1 mutants associated with proximal renal tubular acidosis and ocular abnormalities."
    Horita S., Yamada H., Inatomi J., Moriyama N., Sekine T., Igarashi T., Endo Y., Dasouki M., Ekim M., Al-Gazali L., Shimadzu M., Seki G., Fujita T.
    J. Am. Soc. Nephrol. 16:2270-2278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRTA-OA SER-342; SER-529; HIS-554; VAL-843 AND CYS-925.
  27. "Proximal renal tubular acidosis and ocular pathology: a novel missense mutation in the gene (SLC4A4) for sodium bicarbonate cotransporter protein (NBCe1)."
    Demirci F.Y., Chang M.H., Mah T.S., Romero M.F., Gorin M.B.
    Mol. Vis. 12:324-330(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRTA-OA PRO-566, CHARACTERIZATION OF VARIANT PRTA-OA PRO-566, FUNCTION, SUBCELLULAR LOCATION.
  28. "Functional analysis of a novel missense NBC1 mutation and of other mutations causing proximal renal tubular acidosis."
    Suzuki M., Vaisbich M.H., Yamada H., Horita S., Li Y., Sekine T., Moriyama N., Igarashi T., Endo Y., Cardoso T.P., de Sa L.C., Koch V.H., Seki G., Fujita T.
    Pflugers Arch. 455:583-593(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRTA-OA ARG-530, CHARACTERIZATION OF VARIANTS PRTA-OA SER-342 SER-529; ARG-530 AND PRO-566, FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiS4A4_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6R1
Secondary accession number(s): C4B714
, O15153, Q8NEJ2, Q9H262, Q9NRZ1, Q9UIC0, Q9UIC1, Q9UP50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 118 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 4
    Human chromosome 4: 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