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Protein

Sialin

Gene

SLC17A5

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

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. cellular protein metabolic process Source: Reactome
  4. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  5. ion transport Source: Reactome
  6. post-translational protein modification Source: Reactome
  7. protein N-linked glycosylation via asparagine Source: Reactome
  8. proton transport Source: GOC
  9. sialic acid transport Source: MGI
  10. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Symport, Transport

Enzyme and pathway databases

ReactomeiREACT_19372. Organic anion transporters.
REACT_264366. 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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10933. SLC17A5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4141CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei42 – 6221HelicalSequence AnalysisAdd
BLAST
Topological domaini63 – 10947LumenalSequence AnalysisAdd
BLAST
Transmembranei110 – 13021HelicalSequence AnalysisAdd
BLAST
Topological domaini131 – 1366CytoplasmicSequence Analysis
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 1581LumenalSequence Analysis
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 20021CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei201 – 22121HelicalSequence AnalysisAdd
BLAST
Topological domaini222 – 2276LumenalSequence Analysis
Transmembranei228 – 24821HelicalSequence AnalysisAdd
BLAST
Topological domaini249 – 27931CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei280 – 30021HelicalSequence AnalysisAdd
BLAST
Topological domaini301 – 32828LumenalSequence AnalysisAdd
BLAST
Transmembranei329 – 34921HelicalSequence AnalysisAdd
BLAST
Topological domaini350 – 36516CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei366 – 38621HelicalSequence AnalysisAdd
BLAST
Topological domaini387 – 3915LumenalSequence Analysis
Transmembranei392 – 41221HelicalSequence AnalysisAdd
BLAST
Topological domaini413 – 42311CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei424 – 44421HelicalSequence AnalysisAdd
BLAST
Topological domaini445 – 45713LumenalSequence AnalysisAdd
BLAST
Transmembranei458 – 47821HelicalSequence AnalysisAdd
BLAST
Topological domaini479 – 49517CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Salla disease (SD)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionSialic 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.

See also OMIM:604369
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. 2 Publications
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)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionSevere 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.

See also OMIM:269920
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831H → R in ISSD. 2 Publications
VAR_018686
Natural varianti268 – 2725Missing in ISSD. 2 Publications
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. 1 Publication

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

BgeeiQ9NRA2.
CleanExiHS_SLC17A5.
ExpressionAtlasiQ9NRA2. baseline and differential.
GenevestigatoriQ9NRA2.

Organism-specific databases

HPAiHPA044479.

Interactioni

Protein-protein interaction databases

BioGridi117710. 4 interactions.
IntActiQ9NRA2. 1 interaction.
STRINGi9606.ENSP00000348019.

Structurei

3D structure databases

ProteinModelPortaliQ9NRA2.
SMRiQ9NRA2. Positions 421-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000119079.
HOGENOMiHOG000230811.
HOVERGENiHBG008834.
InParanoidiQ9NRA2.
KOiK12301.
OMAiVYDWDSE.
OrthoDBiEOG789C9Z.
PhylomeDBiQ9NRA2.
TreeFamiTF313535.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
[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. AlignAdd to basket

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

        10         20         30         40         50
MRSPVRDLAR NDGEESTDRT PLLPGAPRAE AAPVCCSARY NLAILAFFGF
60 70 80 90 100
FIVYALRVNL SVALVDMVDS NTTLEDNRTS KACPEHSAPI KVHHNQTGKK
110 120 130 140 150
YQWDAETQGW ILGSFFYGYI ITQIPGGYVA SKIGGKMLLG FGILGTAVLT
160 170 180 190 200
LFTPIAADLG VGPLIVLRAL EGLGEGVTFP AMHAMWSSWA PPLERSKLLS
210 220 230 240 250
ISYAGAQLGT VISLPLSGII CYYMNWTYVF YFFGTIGIFW FLLWIWLVSD
260 270 280 290 300
TPQKHKRISH YEKEYILSSL RNQLSSQKSV PWVPILKSLP LWAIVVAHFS
310 320 330 340 350
YNWTFYTLLT LLPTYMKEIL RFNVQENGFL SSLPYLGSWL CMILSGQAAD
360 370 380 390 400
NLRAKWNFST LCVRRIFSLI GMIGPAVFLV AAGFIGCDYS LAVAFLTIST
410 420 430 440 450
TLGGFCSSGF SINHLDIAPS YAGILLGITN TFATIPGMVG PVIAKSLTPD
460 470 480 490
NTVGEWQTVF YIAAAINVFG AIFFTLFAKG EVQNWALNDH HGHRH
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. Curated

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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9NRA2.
SMRiQ9NRA2. Positions 421-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117710. 4 interactions.
IntActiQ9NRA2. 1 interaction.
STRINGi9606.ENSP00000348019.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ9NRA2.

Polymorphism databases

DMDMi48428688.

Proteomic databases

MaxQBiQ9NRA2.
PaxDbiQ9NRA2.
PRIDEiQ9NRA2.

Protocols and materials databases

DNASUi26503.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26503.
GeneCardsiGC06M074303.
GeneReviewsiSLC17A5.
HGNCiHGNC:10933. SLC17A5.
HPAiHPA044479.
MIMi269920. phenotype.
604322. gene.
604369. phenotype.
neXtProtiNX_Q9NRA2.
Orphaneti309324. Free sialic acid storage disease, infantile form.
309331. Intermediate severe Salla disease.
309334. Salla disease.
PharmGKBiPA35824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000119079.
HOGENOMiHOG000230811.
HOVERGENiHBG008834.
InParanoidiQ9NRA2.
KOiK12301.
OMAiVYDWDSE.
OrthoDBiEOG789C9Z.
PhylomeDBiQ9NRA2.
TreeFamiTF313535.

Enzyme and pathway databases

ReactomeiREACT_19372. Organic anion transporters.
REACT_264366. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiSLC17A5. human.
GeneWikiiHP59.
SLC17A5.
GenomeRNAii26503.
NextBioi48778.
PROiQ9NRA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRA2.
CleanExiHS_SLC17A5.
ExpressionAtlasiQ9NRA2. baseline and differential.
GenevestigatoriQ9NRA2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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(2000) [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(2003) [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(2002) [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(2003) [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(2003) [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(2009) [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(2010) [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(1999) [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(2002) [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: April 1, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.