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Protein

Equilibrative nucleoside transporter 1

Gene

SLC29A1

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

Functioni

Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs).

Kineticsi

Vmax for adenosine uptake is about the same for SLC29A1 and SLC29A2.

  1. KM=0.62 mM for adenosine1 Publication

    GO - Molecular functioni

    • nucleoside transmembrane transporter activity Source: ProtInc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_1206. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

    Protein family/group databases

    TCDBi2.A.57.1.1. the equilibrative nucleoside transporter (ent) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Equilibrative nucleoside transporter 1
    Alternative name(s):
    Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter
    Short name:
    Equilibrative NBMPR-sensitive nucleoside transporter
    Nucleoside transporter, es-type
    Solute carrier family 29 member 1
    Gene namesi
    Name:SLC29A1
    Synonyms:ENT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11003. SLC29A1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 1211CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei13 – 2917HelicalSequence AnalysisAdd
    BLAST
    Topological domaini30 – 8253ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei83 – 10725HelicalSequence AnalysisAdd
    BLAST
    Topological domaini108 – 1114CytoplasmicSequence Analysis
    Transmembranei112 – 13019HelicalSequence AnalysisAdd
    BLAST
    Topological domaini131 – 1388ExtracellularSequence Analysis
    Transmembranei139 – 15719HelicalSequence AnalysisAdd
    BLAST
    Topological domaini158 – 17417CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei175 – 19925HelicalSequence AnalysisAdd
    BLAST
    Topological domaini200 – 2067ExtracellularSequence Analysis
    Transmembranei207 – 22721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini228 – 29164CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei292 – 31120HelicalSequence AnalysisAdd
    BLAST
    Topological domaini312 – 32312ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei324 – 34219HelicalSequence AnalysisAdd
    BLAST
    Topological domaini343 – 35917CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei360 – 37819HelicalSequence AnalysisAdd
    BLAST
    Topological domaini379 – 39315ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei394 – 41320HelicalSequence AnalysisAdd
    BLAST
    Topological domaini414 – 43118CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei432 – 45221HelicalSequence AnalysisAdd
    BLAST
    Topological domaini453 – 4564ExtracellularSequence Analysis

    GO - Cellular componenti

    • apical plasma membrane Source: UniProtKB
    • basolateral plasma membrane Source: UniProtKB
    • integral component of plasma membrane Source: ProtInc
    • membrane Source: UniProtKB
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi453 – 4564Missing : No effect on subcellular localization and inosine transport. 1 Publication
    Mutagenesisi453 – 4531R → A: No effect on subcellular localization and inosine transport. 1 Publication

    Organism-specific databases

    PharmGKBiPA154.

    Chemistry

    DrugBankiDB00987. Cytarabine.
    DB00900. Didanosine.
    DB01073. Fludarabine.
    DB00544. Fluorouracil.
    DB00441. Gemcitabine.
    DB01033. Mercaptopurine.
    DB00642. Pemetrexed.
    DB00811. Ribavirin.
    DB00943. Zalcitabine.

    Polymorphism and mutation databases

    BioMutaiSLC29A1.
    DMDMi9296956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 456455Equilibrative nucleoside transporter 1PRO_0000209337Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ99808.
    PaxDbiQ99808.
    PRIDEiQ99808.

    PTM databases

    PhosphoSiteiQ99808.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level). Expressed in heart, brain, mammary gland, erythrocytes and placenta, and also in fetal liver and spleen.2 Publications

    Gene expression databases

    BgeeiQ99808.
    CleanExiHS_SLC29A1.
    GenevisibleiQ99808. HS.

    Organism-specific databases

    HPAiHPA012383.
    HPA012384.

    Interactioni

    Subunit structurei

    Identified in a complex with STOM.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STK19P498421EBI-347907,EBI-347581

    Protein-protein interaction databases

    BioGridi108344. 15 interactions.
    IntActiQ99808. 3 interactions.
    MINTiMINT-1034227.
    STRINGi9606.ENSP00000360773.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99808.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG249415.
    GeneTreeiENSGT00390000002232.
    HOGENOMiHOG000007684.
    HOVERGENiHBG074626.
    InParanoidiQ99808.
    KOiK15014.
    OMAiSTWERYF.
    OrthoDBiEOG7PP56W.
    PhylomeDBiQ99808.
    TreeFamiTF313950.

    Family and domain databases

    InterProiIPR030195. ENT1.
    IPR002259. Eqnu_transpt.
    IPR020846. MFS_dom.
    [Graphical view]
    PANTHERiPTHR10332. PTHR10332. 1 hit.
    PTHR10332:SF9. PTHR10332:SF9. 1 hit.
    PfamiPF01733. Nucleoside_tran. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016379. ENT. 1 hit.
    PRINTSiPR01130. DERENTRNSPRT.
    SUPFAMiSSF103473. SSF103473. 3 hits.
    TIGRFAMsiTIGR00939. 2a57. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q99808-1) [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
    MTTSHQPQDR YKAVWLIFFM LGLGTLLPWN FFMTATQYFT NRLDMSQNVS
    60 70 80 90 100
    LVTAELSKDA QASAAPAAPL PERNSLSAIF NNVMTLCAML PLLLFTYLNS
    110 120 130 140 150
    FLHQRIPQSV RILGSLVAIL LVFLITAILV KVQLDALPFF VITMIKIVLI
    160 170 180 190 200
    NSFGAILQGS LFGLAGLLPA SYTAPIMSGQ GLAGFFASVA MICAIASGSE
    210 220 230 240 250
    LSESAFGYFI TACAVIILTI ICYLGLPRLE FYRYYQQLKL EGPGEQETKL
    260 270 280 290 300
    DLISKGEEPR AGKEESGVSV SNSQPTNESH SIKAILKNIS VLAFSVCFIF
    310 320 330 340 350
    TITIGMFPAV TVEVKSSIAG SSTWERYFIP VSCFLTFNIF DWLGRSLTAV
    360 370 380 390 400
    FMWPGKDSRW LPSLVLARLV FVPLLLLCNI KPRRYLTVVF EHDAWFIFFM
    410 420 430 440 450
    AAFAFSNGYL ASLCMCFGPK KVKPAEAETA GAIMAFFLCL GLALGAVFSF

    LFRAIV
    Length:456
    Mass (Da):50,219
    Last modified:January 23, 2007 - v3
    Checksum:iF18535A95DEBC95D
    GO
    Isoform 2 (identifier: Q99808-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRRERTRGPQ...PGKTENTITM

    Note: No experimental confirmation available.
    Show »
    Length:535
    Mass (Da):58,963
    Checksum:iE58D6674A3C519D7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti216 – 2161I → T.
    Corresponds to variant rs45573936 [ dbSNP | Ensembl ].
    VAR_053668
    Natural varianti293 – 2931A → T in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036221
    Natural varianti391 – 3911E → K.
    Corresponds to variant rs45458701 [ dbSNP | Ensembl ].
    VAR_053669
    Natural varianti455 – 4551I → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036222

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRRERTRGPQAWEFPSPTKS GCSLQSLSRDLRELREGEKP EDQAETEESWQGLARKTPGK ACAPEGGSCQPGKTENTITM in isoform 2. 1 PublicationVSP_056579

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U81375 mRNA. Translation: AAC51103.1.
    AF190884 Genomic DNA. Translation: AAF02777.1.
    AF079117 mRNA. Translation: AAC62495.1.
    AF495730 Genomic DNA. Translation: AAM11785.1.
    AK090491 mRNA. Translation: BAG52169.1.
    AK090615 mRNA. Translation: BAG52197.1.
    AL139392 Genomic DNA. Translation: CAI20093.1.
    CH471081 Genomic DNA. Translation: EAX04255.1.
    BC001382 mRNA. Translation: AAH01382.1.
    BC008954 mRNA. Translation: AAH08954.1.
    CCDSiCCDS4908.1. [Q99808-1]
    RefSeqiNP_001071643.1. NM_001078175.2. [Q99808-1]
    NP_001071645.1. NM_001078177.1. [Q99808-1]
    XP_005248935.1. XM_005248878.3. [Q99808-1]
    XP_005248936.1. XM_005248879.3. [Q99808-1]
    XP_005248937.1. XM_005248880.3. [Q99808-1]
    XP_005248938.1. XM_005248881.3. [Q99808-1]
    XP_005248939.1. XM_005248882.3. [Q99808-1]
    UniGeneiHs.25450.

    Genome annotation databases

    EnsembliENST00000371708; ENSP00000360773; ENSG00000112759. [Q99808-1]
    ENST00000371713; ENSP00000360778; ENSG00000112759. [Q99808-1]
    ENST00000371724; ENSP00000360789; ENSG00000112759. [Q99808-1]
    ENST00000371731; ENSP00000360796; ENSG00000112759. [Q99808-1]
    ENST00000371740; ENSP00000360805; ENSG00000112759. [Q99808-1]
    ENST00000371755; ENSP00000360820; ENSG00000112759. [Q99808-1]
    ENST00000393841; ENSP00000377424; ENSG00000112759. [Q99808-1]
    ENST00000393844; ENSP00000377427; ENSG00000112759. [Q99808-1]
    ENST00000427851; ENSP00000392668; ENSG00000112759. [Q99808-1]
    GeneIDi2030.
    KEGGihsa:2030.
    UCSCiuc003owu.1. human. [Q99808-1]
    uc003oww.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U81375 mRNA. Translation: AAC51103.1.
    AF190884 Genomic DNA. Translation: AAF02777.1.
    AF079117 mRNA. Translation: AAC62495.1.
    AF495730 Genomic DNA. Translation: AAM11785.1.
    AK090491 mRNA. Translation: BAG52169.1.
    AK090615 mRNA. Translation: BAG52197.1.
    AL139392 Genomic DNA. Translation: CAI20093.1.
    CH471081 Genomic DNA. Translation: EAX04255.1.
    BC001382 mRNA. Translation: AAH01382.1.
    BC008954 mRNA. Translation: AAH08954.1.
    CCDSiCCDS4908.1. [Q99808-1]
    RefSeqiNP_001071643.1. NM_001078175.2. [Q99808-1]
    NP_001071645.1. NM_001078177.1. [Q99808-1]
    XP_005248935.1. XM_005248878.3. [Q99808-1]
    XP_005248936.1. XM_005248879.3. [Q99808-1]
    XP_005248937.1. XM_005248880.3. [Q99808-1]
    XP_005248938.1. XM_005248881.3. [Q99808-1]
    XP_005248939.1. XM_005248882.3. [Q99808-1]
    UniGeneiHs.25450.

    3D structure databases

    ProteinModelPortaliQ99808.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108344. 15 interactions.
    IntActiQ99808. 3 interactions.
    MINTiMINT-1034227.
    STRINGi9606.ENSP00000360773.

    Chemistry

    BindingDBiQ99808.
    ChEMBLiCHEMBL1997.
    DrugBankiDB00987. Cytarabine.
    DB00900. Didanosine.
    DB01073. Fludarabine.
    DB00544. Fluorouracil.
    DB00441. Gemcitabine.
    DB01033. Mercaptopurine.
    DB00642. Pemetrexed.
    DB00811. Ribavirin.
    DB00943. Zalcitabine.
    GuidetoPHARMACOLOGYi1117.

    Protein family/group databases

    TCDBi2.A.57.1.1. the equilibrative nucleoside transporter (ent) family.

    PTM databases

    PhosphoSiteiQ99808.

    Polymorphism and mutation databases

    BioMutaiSLC29A1.
    DMDMi9296956.

    Proteomic databases

    MaxQBiQ99808.
    PaxDbiQ99808.
    PRIDEiQ99808.

    Protocols and materials databases

    DNASUi2030.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000371708; ENSP00000360773; ENSG00000112759. [Q99808-1]
    ENST00000371713; ENSP00000360778; ENSG00000112759. [Q99808-1]
    ENST00000371724; ENSP00000360789; ENSG00000112759. [Q99808-1]
    ENST00000371731; ENSP00000360796; ENSG00000112759. [Q99808-1]
    ENST00000371740; ENSP00000360805; ENSG00000112759. [Q99808-1]
    ENST00000371755; ENSP00000360820; ENSG00000112759. [Q99808-1]
    ENST00000393841; ENSP00000377424; ENSG00000112759. [Q99808-1]
    ENST00000393844; ENSP00000377427; ENSG00000112759. [Q99808-1]
    ENST00000427851; ENSP00000392668; ENSG00000112759. [Q99808-1]
    GeneIDi2030.
    KEGGihsa:2030.
    UCSCiuc003owu.1. human. [Q99808-1]
    uc003oww.1. human.

    Organism-specific databases

    CTDi2030.
    GeneCardsiGC06P044187.
    HGNCiHGNC:11003. SLC29A1.
    HPAiHPA012383.
    HPA012384.
    MIMi602193. gene.
    neXtProtiNX_Q99808.
    PharmGKBiPA154.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG249415.
    GeneTreeiENSGT00390000002232.
    HOGENOMiHOG000007684.
    HOVERGENiHBG074626.
    InParanoidiQ99808.
    KOiK15014.
    OMAiSTWERYF.
    OrthoDBiEOG7PP56W.
    PhylomeDBiQ99808.
    TreeFamiTF313950.

    Enzyme and pathway databases

    ReactomeiREACT_1206. Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.

    Miscellaneous databases

    ChiTaRSiSLC29A1. human.
    GeneWikiiEquilibrative_nucleoside_transporter_1.
    GenomeRNAii2030.
    NextBioi35469417.
    PROiQ99808.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ99808.
    CleanExiHS_SLC29A1.
    GenevisibleiQ99808. HS.

    Family and domain databases

    InterProiIPR030195. ENT1.
    IPR002259. Eqnu_transpt.
    IPR020846. MFS_dom.
    [Graphical view]
    PANTHERiPTHR10332. PTHR10332. 1 hit.
    PTHR10332:SF9. PTHR10332:SF9. 1 hit.
    PfamiPF01733. Nucleoside_tran. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016379. ENT. 1 hit.
    PRINTSiPR01130. DERENTRNSPRT.
    SUPFAMiSSF103473. SSF103473. 3 hits.
    TIGRFAMsiTIGR00939. 2a57. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of a human nucleoside transporter implicated in the cellular uptake of adenosine and chemotherapeutic drugs."
      Griffiths M., Beaumont N., Yao S.Y.M., Sundaram M., Boumah C.E., Davies A., Kwong F.Y.P., Coe I., Cass C.E., Young J.D., Baldwin S.A.
      Nat. Med. 3:89-93(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-22.
      Tissue: Placenta.
    2. "Genomic sequence of the human equilibrative nucleoside transporter 1 (hENT1)."
      Graham K.A., Coe I.R., Carpenter P., Baldwin S.A., Young J.D., Cass C.E.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Human intestinal es nucleoside transporter: molecular characterization and nucleoside inhibitory profiles."
      Lum P.Y., Ngo L.Y., Bakken A.H., Unadkat J.D.
      Cancer Chemother. Pharmacol. 45:273-278(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Jejunum and Small intestine.
    4. "Comparative genomic analysis of equilibrative nucleoside transporters suggests conserved protein structure despite limited sequence identity."
      Sankar N., Machado J., Abdulla P., Hilliker A.J., Coe I.R.
      Nucleic Acids Res. 30:4339-4350(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Localization of human equilibrative nucleoside transporters, hENT1 and hENT2, in renal epithelial cells."
      Mangravite L.M., Xiao G., Giacomini K.M.
      Am. J. Physiol. 284:F902-F910(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-453 AND 453-ARG--VAL-456.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Adrenal gland.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Colon and Muscle.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48.
      Tissue: Leukemic T-cell.
    12. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
      Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
      Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH STOM, SUBUNIT.
    13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-293 AND VAL-455.

    Entry informationi

    Entry nameiS29A1_HUMAN
    AccessioniPrimary (citable) accession number: Q99808
    Secondary accession number(s): B3KQV7
    , B3KQY5, Q5T9W9, Q9UJY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 141 of the entry and version 3 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, Direct protein sequencing, 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.