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Q9NRA2

- S17A5_HUMAN

UniProt

Q9NRA2 - S17A5_HUMAN

Protein

Sialin

Gene

SLC17A5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Transports glucuronic acid and free sialic acid out of the lysosome after it is cleaved from sialoglycoconjugates undergoing degradation, this is required for normal CNS myelination. Mediates aspartate and glutamate membrane potential-dependent uptake into synaptic vesicles and synaptic-like microvesicles. Also functions as an electrogenic 2NO3-/H+ cotransporter in the plasma membrane of salivary gland acinar cells, mediating the physiological nitrate efflux, 25% of the circulating nitrate ions is typically removed and secreted in saliva.5 Publications

    GO - Molecular functioni

    1. sialic acid transmembrane transporter activity Source: MGI
    2. sugar:proton symporter activity Source: ProtInc

    GO - Biological processi

    1. amino acid transport Source: UniProtKB-KW
    2. anion transport Source: ProtInc
    3. ion transport Source: Reactome
    4. proton transport Source: GOC
    5. sialic acid transport Source: MGI
    6. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Amino-acid transport, Symport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_19372. Organic anion transporters.
    REACT_200874. Sialic acid metabolism.

    Protein family/group databases

    TCDBi2.A.1.14.10. the major facilitator superfamily (mfs).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialin
    Alternative name(s):
    H(+)/nitrate cotransporter
    H(+)/sialic acid cotransporter
    Short name:
    AST
    Membrane glycoprotein HP59
    Solute carrier family 17 member 5
    Vesicular H(+)/Aspartate-glutamate cotransporter
    Gene namesi
    Name:SLC17A5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10933. SLC17A5.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: HPA
    3. integral component of plasma membrane Source: ProtInc
    4. lysosomal membrane Source: UniProtKB
    5. membrane Source: ProtInc
    6. plasma membrane Source: HPA
    7. synaptic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Salla disease (SD) [MIM:604369]: Sialic acid storage disease (SASD). SASDs are autosomal recessive neurodegenerative disorders characterized by hypotonia, cerebellar ataxia and mental retardation. They are caused by a defect in the metabolism of sialic acid which results in increased urinary excretion of unconjugated sialic acid, specifically N-acetylneuraminic acid. Enlarged lysosomes are seen on electron microscopic studies. Clinical symptoms of SD present usually at age less than 1 year and progression is slow.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391R → C in SD; completely devoid of aspartate and glutamate transport activity, but retains appreciable H(+)/sialic acid cotransport activity, frequent mutation in Finland. 4 Publications
    VAR_018684
    Natural varianti136 – 1361K → E in SD. 1 Publication
    VAR_018685
    Natural varianti183 – 1831H → R in ISSD. 2 Publications
    VAR_018686
    Natural varianti268 – 2725Missing in ISSD.
    VAR_018687
    Natural varianti334 – 3341P → R in ISSD. 2 Publications
    VAR_018688
    Natural varianti371 – 3711G → V in ISSD. 1 Publication
    VAR_018689
    Infantile sialic acid storage disorder (ISSD) [MIM:269920]: Severe form of sialic acid storage disease. Affected newborns exhibit visceromegaly, coarse features and failure to thrive immediately after birth. These patients have a shortened life span, usually less than 2 years.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831H → R in ISSD. 2 Publications
    VAR_018686
    Natural varianti268 – 2725Missing in ISSD.
    VAR_018687
    Natural varianti334 – 3341P → R in ISSD. 2 Publications
    VAR_018688
    Natural varianti371 – 3711G → V in ISSD. 1 Publication
    VAR_018689
    Infantile sialic acid storage disorder is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 232LL → GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH. 1 Publication
    Mutagenesisi179 – 1791F → C: 15 fold increase in affinity for glucuronic acid. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi269920. phenotype.
    604369. phenotype.
    Orphaneti309324. Free sialic acid storage disease, infantile form.
    309331. Intermediate severe Salla disease.
    309334. Salla disease.
    PharmGKBiPA35824.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 495495SialinPRO_0000220947Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9NRA2.
    PaxDbiQ9NRA2.
    PRIDEiQ9NRA2.

    PTM databases

    PhosphoSiteiQ9NRA2.

    Expressioni

    Tissue specificityi

    Found in fetal lung and small intestine, and at lower level in fetal skin and muscle. In the adult, detected in placenta, kidney and pancreas. Abundant in the endothelial cells of tumors from ovary, colon, breast and lung, but is not detected in endothelial cells from the corresponding normal tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9NRA2.
    BgeeiQ9NRA2.
    CleanExiHS_SLC17A5.
    GenevestigatoriQ9NRA2.

    Organism-specific databases

    HPAiHPA044479.

    Interactioni

    Protein-protein interaction databases

    BioGridi117710. 2 interactions.
    IntActiQ9NRA2. 1 interaction.
    STRINGi9606.ENSP00000348019.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRA2.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4141CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini63 – 10947LumenalSequence AnalysisAdd
    BLAST
    Topological domaini131 – 1366CytoplasmicSequence Analysis
    Topological domaini158 – 1581LumenalSequence Analysis
    Topological domaini180 – 20021CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini222 – 2276LumenalSequence Analysis
    Topological domaini249 – 27931CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini301 – 32828LumenalSequence AnalysisAdd
    BLAST
    Topological domaini350 – 36516CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini387 – 3915LumenalSequence Analysis
    Topological domaini413 – 42311CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini445 – 45713LumenalSequence AnalysisAdd
    BLAST
    Topological domaini479 – 49517CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei42 – 6221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei110 – 13021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei137 – 15721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei159 – 17921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei201 – 22121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei228 – 24821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei280 – 30021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei329 – 34921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei366 – 38621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei392 – 41221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei424 – 44421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei458 – 47821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi22 – 232Dileucine internalization motif

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0477.
    HOGENOMiHOG000230811.
    HOVERGENiHBG008834.
    InParanoidiQ9NRA2.
    KOiK12301.
    OMAiKHKRISH.
    OrthoDBiEOG789C9Z.
    PhylomeDBiQ9NRA2.
    TreeFamiTF313535.

    Family and domain databases

    InterProiIPR011701. MFS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view]
    PfamiPF07690. MFS_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 2 hits.
    PROSITEiPS50850. MFS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRA2-1) [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

    MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF    50
    FIVYALRVNL SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK 100
    YQWDAETQGW ILGSFFYGYI ITQIPGGYVA SKIGGKMLLG FGILGTAVLT 150
    LFTPIAADLG VGPLIVLRAL EGLGEGVTFP AMHAMWSSWA PPLERSKLLS 200
    ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW FLLWIWLVSD 250
    TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS 300
    YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD 350
    NLRAKWNFST LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST 400
    TLGGFCSSGF SINHLDIAPS YAGILLGITN TFATIPGMVG PVIAKSLTPD 450
    NTVGEWQTVF YIAAAINVFG AIFFTLFAKG EVQNWALNDH HGHRH 495
    Length:495
    Mass (Da):54,640
    Last modified:June 7, 2004 - v2
    Checksum:i5C6C154B3E93A19E
    GO
    Isoform 2 (identifier: Q9NRA2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         274-276: LSS → AGV
         278-495: Missing.

    Show »
    Length:277
    Mass (Da):30,667
    Checksum:i1BF03EA560AB80DB
    GO

    Sequence cautioni

    The sequence AAF97769.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391R → C in SD; completely devoid of aspartate and glutamate transport activity, but retains appreciable H(+)/sialic acid cotransport activity, frequent mutation in Finland. 4 Publications
    VAR_018684
    Natural varianti136 – 1361K → E in SD. 1 Publication
    VAR_018685
    Natural varianti183 – 1831H → R in ISSD. 2 Publications
    VAR_018686
    Natural varianti268 – 2725Missing in ISSD.
    VAR_018687
    Natural varianti296 – 2961V → I.
    Corresponds to variant rs16883930 [ dbSNP | Ensembl ].
    VAR_034746
    Natural varianti334 – 3341P → R in ISSD. 2 Publications
    VAR_018688
    Natural varianti371 – 3711G → V in ISSD. 1 Publication
    VAR_018689

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei274 – 2763LSS → AGV in isoform 2. 2 PublicationsVSP_010482
    Alternative sequencei278 – 495218Missing in isoform 2. 2 PublicationsVSP_010483Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF244577 mRNA. Translation: AAF97769.1. Different initiation.
    AJ387747 mRNA. Translation: CAB62540.1.
    AK075320 mRNA. Translation: BAC11546.1.
    AL590428, AL121972 Genomic DNA. Translation: CAI15635.1.
    AL121972, AL590428 Genomic DNA. Translation: CAI20417.1.
    BC020961 mRNA. Translation: AAH20961.1.
    CCDSiCCDS4981.1. [Q9NRA2-1]
    RefSeqiNP_036566.1. NM_012434.4. [Q9NRA2-1]
    UniGeneiHs.597422.

    Genome annotation databases

    EnsembliENST00000355773; ENSP00000348019; ENSG00000119899. [Q9NRA2-1]
    GeneIDi26503.
    KEGGihsa:26503.
    UCSCiuc003phn.4. human. [Q9NRA2-1]

    Polymorphism databases

    DMDMi48428688.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF244577 mRNA. Translation: AAF97769.1 . Different initiation.
    AJ387747 mRNA. Translation: CAB62540.1 .
    AK075320 mRNA. Translation: BAC11546.1 .
    AL590428 , AL121972 Genomic DNA. Translation: CAI15635.1 .
    AL121972 , AL590428 Genomic DNA. Translation: CAI20417.1 .
    BC020961 mRNA. Translation: AAH20961.1 .
    CCDSi CCDS4981.1. [Q9NRA2-1 ]
    RefSeqi NP_036566.1. NM_012434.4. [Q9NRA2-1 ]
    UniGenei Hs.597422.

    3D structure databases

    ProteinModelPortali Q9NRA2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117710. 2 interactions.
    IntActi Q9NRA2. 1 interaction.
    STRINGi 9606.ENSP00000348019.

    Protein family/group databases

    TCDBi 2.A.1.14.10. the major facilitator superfamily (mfs).

    PTM databases

    PhosphoSitei Q9NRA2.

    Polymorphism databases

    DMDMi 48428688.

    Proteomic databases

    MaxQBi Q9NRA2.
    PaxDbi Q9NRA2.
    PRIDEi Q9NRA2.

    Protocols and materials databases

    DNASUi 26503.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355773 ; ENSP00000348019 ; ENSG00000119899 . [Q9NRA2-1 ]
    GeneIDi 26503.
    KEGGi hsa:26503.
    UCSCi uc003phn.4. human. [Q9NRA2-1 ]

    Organism-specific databases

    CTDi 26503.
    GeneCardsi GC06M074359.
    GeneReviewsi SLC17A5.
    HGNCi HGNC:10933. SLC17A5.
    HPAi HPA044479.
    MIMi 269920. phenotype.
    604322. gene.
    604369. phenotype.
    neXtProti NX_Q9NRA2.
    Orphaneti 309324. Free sialic acid storage disease, infantile form.
    309331. Intermediate severe Salla disease.
    309334. Salla disease.
    PharmGKBi PA35824.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0477.
    HOGENOMi HOG000230811.
    HOVERGENi HBG008834.
    InParanoidi Q9NRA2.
    KOi K12301.
    OMAi KHKRISH.
    OrthoDBi EOG789C9Z.
    PhylomeDBi Q9NRA2.
    TreeFami TF313535.

    Enzyme and pathway databases

    Reactomei REACT_19372. Organic anion transporters.
    REACT_200874. Sialic acid metabolism.

    Miscellaneous databases

    GeneWikii HP59.
    SLC17A5.
    GenomeRNAii 26503.
    NextBioi 48778.
    PROi Q9NRA2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRA2.
    Bgeei Q9NRA2.
    CleanExi HS_SLC17A5.
    Genevestigatori Q9NRA2.

    Family and domain databases

    InterProi IPR011701. MFS.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view ]
    Pfami PF07690. MFS_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103473. SSF103473. 2 hits.
    PROSITEi PS50850. MFS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel membrane protein, HP59, with therapeutic potential as a target of tumor angiogenesis."
      Fu C., Bardhan S., Cetateanu N.D., Wamil B.D., Wang Y., Yan H.-P., Shi E., Carter C., Venkov C., Yakes F.M., Page D.L., Lloyd R.S., Mernaugh R.L., Hellerqvist C.G.
      Clin. Cancer Res. 7:4182-4194(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT SD CYS-39, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183 AND ARG-334.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Colon.
    6. "Functional characterization of wild-type and mutant human sialin."
      Morin P., Sagne C., Gasnier B.
      EMBO J. 23:4560-4570(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DILEUCINE MOTIF, MUTAGENESIS OF 22-LEU--LEU-23.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    8. "Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes."
      Courville P., Quick M., Reimer R.J.
      J. Biol. Chem. 285:19316-19323(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, MUTAGENESIS OF PHE-179.
    9. "Functional characterization of vesicular excitatory amino acid transport by human sialin."
      Miyaji T., Omote H., Moriyama Y.
      J. Neurochem. 119:1-5(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT SD CYS-39.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation."
      Aula N., Salomaeki P., Timonen R., Verheijen F., Mancini G.M.S., Maensson J.-E., Aula P., Peltonen L.
      Am. J. Hum. Genet. 67:832-840(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SD CYS-39 AND GLU-136, VARIANTS ISSD 268-SER--ASN-272 DEL; ARG-183; ARG-334 AND VAL-371.
    12. "Sialic acid storage disease of the Salla phenotype in American monozygous twin female sibs."
      Martin R.A., Slaugh R., Natowicz M., Pearlman K., Orvisky E., Krasnewich D., Kleta R., Huizing M., Gahl W.A.
      Am. J. Med. Genet. A 120:23-27(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SD CYS-39.

    Entry informationi

    Entry nameiS17A5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRA2
    Secondary accession number(s): Q5SZ76, Q8NBR5, Q9UGH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 111 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 6
      Human chromosome 6: 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