Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y6R1

- S4A4_HUMAN

UniProt

Q9Y6R1 - S4A4_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.4 Publications

    Enzyme regulationi

    Inhibited by stilbene derivatives and regulated by cyclic AMP.

    GO - Molecular functioni

    1. inorganic anion exchanger activity Source: InterPro
    2. protein binding Source: DFLAT
    3. sodium:bicarbonate symporter activity Source: ProtInc

    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

    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 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

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

    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.4 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; mistargeting and altered function. 3 Publications
    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; mistargeting and altered function. 1 Publication
    VAR_024753
    Natural varianti554 – 5541R → H in pRTA-OA; mistargeting and altered function. 3 Publications
    VAR_024754
    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. 2 Publications
    Mutagenesisi49 – 491T → D: Loss of conductance regulation by cAMP; isoform 1. 2 Publications
    Mutagenesisi135 – 1351E → R: Mistargeting and altered function. 2 Publications
    Mutagenesisi477 – 4771Y → F: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi493 – 4931D → N: Prevents membrane targeting. 2 Publications
    Mutagenesisi494 – 4941A → K: Prevents membrane targeting. 2 Publications
    Mutagenesisi503 – 5031E → Q: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi504 – 5041S → L: Prevents membrane targeting. 2 Publications
    Mutagenesisi536 – 5361E → Q: Prevents membrane targeting. 2 Publications
    Mutagenesisi552 – 5521E → N: Prevents membrane targeting. 2 Publications
    Mutagenesisi554 – 5541R → D: Prevents membrane targeting. 2 Publications
    Mutagenesisi582 – 5821R → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi582 – 5821R → Q: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi586 – 5861E → Q: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi599 – 5991D → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi600 – 6001A → T: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi602 – 6021K → Q: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi603 – 6031K → Q: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi691 – 6911D → R: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi700 – 7001F → M: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi711 – 7111K → E, N or Q: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi711 – 7111K → R: No effect on the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi712 – 7121K → N: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi714 – 7141K → Q: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi715 – 7151T → N: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi721 – 7211T → G: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi724 – 7241R → E: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi725 – 7251K → N: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi728 – 7281S → G: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi729 – 7291D → N or R: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi743 – 7431D → K or N: Prevents membrane targeting. 2 Publications
    Mutagenesisi749 – 7491D → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi752 – 7521K → Q: Prevents membrane targeting. 2 Publications
    Mutagenesisi766 – 7661R → Q: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi767 – 7671G → T: Alters interaction with CA4. 2 Publications
    Mutagenesisi775 – 7751E → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi798 – 7981D → E, N or R: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    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. 2 Publications
    Mutagenesisi822 – 8221D → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi851 – 8511H → N: Prevents membrane targeting. 2 Publications
    Mutagenesisi853 – 8531D → N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    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. 1 Publication
    Mutagenesisi898 – 8981K → E: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi925 – 9273RLK → NLN: Prevents membrane targeting. 1 Publication
    Mutagenesisi948 – 9481R → E: Strong reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi949 – 9491R → E: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi951 – 9511H → D: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi951 – 9511H → N or R: Prevents membrane targeting. 2 Publications
    Mutagenesisi968 – 9681K → Q: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    Mutagenesisi987 – 9871R → E or N: Moderate reduction of the sodium-dependent ion transport activity. 2 Publications
    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. 3 Publications
    Mutagenesisi1026 – 10261S → D: Loss of regulation by cAMP of the transporter stoichiometry. Shifts transporter stoichiometry from 3:1 to 2:1. 3 Publications
    Mutagenesisi1030 – 10334DNDD → NNNN: Abolishes interaction with CA2. 2 Publications
    Mutagenesisi1030 – 10301D → N: Loss of regulation by cAMP of the transporter stoichiometry. Abolishes interaction with CA2. 2 Publications
    Mutagenesisi1032 – 10321D → N: Loss of regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. 2 Publications
    Mutagenesisi1033 – 10331D → N: No effect on regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. 2 Publications
    Mutagenesisi1057 – 10571F → A: Targeting to apical membrane. 2 Publications

    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

    ArrayExpressiQ9Y6R1.
    BgeeiQ9Y6R1.
    CleanExiHS_SLC4A4.
    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.
    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

    MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG     50
    HKEKKEKERI SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED 100
    DSPAPPQLFT ELDELLAVDG QEMEWKETAR WIKFEEKVEQ GGERWSKPHV 150
    ATLSLHSLFE LRTCMEKGSI MLDREASSLP QLVEMIVDHQ IETGLLKPEL 200
    KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN PDNGSPAMTH 250
    RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI 300
    AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD 350
    EVFHDIAYKA KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS 400
    DKRKNMYSGG ENVQMNGDTP HDGGHGGGGH GDCEELQRTG RFCGGLIKDI 450
    KRKAPFFASD FYDALNIQAL SAILFIYLAT VTNAITFGGL LGDATDNMQG 500
    VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF NFSKDNNFDY 550
    LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA 600
    FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL 650
    PTMSSTDMYH NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF 700
    LGTYTSSMAL KKFKTSPYFP TTARKLISDF AIILSILIFC VIDALVGVDT 750
    PKLIVPSEFK PTSPNRGWFV PPFGENPWWV CLAAAIPALL VTILIFMDQQ 800
    ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VICSLMALPW YVAATVISIA 850
    HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI 900
    PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV 950
    HLFTFLQVLC LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS 1000
    FLDDVIPEKD KKKKEDEKKK KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD 1050
    IMEQQPFLSD SKPSDRERSP TFLERHTSC 1079
    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; mistargeting and altered function. 3 Publications
    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; mistargeting and altered function. 1 Publication
    VAR_024753
    Natural varianti554 – 5541R → H in pRTA-OA; mistargeting and altered function. 3 Publications
    VAR_024754
    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.
    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

    ArrayExpressi Q9Y6R1.
    Bgeei Q9Y6R1.
    CleanExi HS_SLC4A4.
    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

    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.

    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 1, 2014
    This is version 117 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