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P22732

- GTR5_HUMAN

UniProt

P22732 - GTR5_HUMAN

Protein

Solute carrier family 2, facilitated glucose transporter member 5

Gene

SLC2A5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Cytochalasin B-sensitive carrier. Seems to function primarily as a fructose transporter.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei325 – 3251MonosaccharideBy similarity

    GO - Molecular functioni

    1. fructose transmembrane transporter activity Source: ProtInc
    2. glucose transmembrane transporter activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular response to fructose stimulus Source: UniProtKB
    3. fructose transport Source: ProtInc
    4. glucose transport Source: ProtInc
    5. hexose transport Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Sugar transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_19281. Class II GLUTs.
    REACT_9441. Hexose transport.

    Protein family/group databases

    TCDBi2.A.1.1.13. the major facilitator superfamily (mfs).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Solute carrier family 2, facilitated glucose transporter member 5
    Alternative name(s):
    Fructose transporter
    Glucose transporter type 5, small intestine
    Short name:
    GLUT-5
    Gene namesi
    Name:SLC2A5
    Synonyms:GLUT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11010. SLC2A5.

    Subcellular locationi

    Apical cell membrane By similarity; Multi-pass membrane protein By similarity. Membrane; Multi-pass membrane protein
    Note: Localized on the apical membrane of the small intestine and the proximal tubule of the kidney.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Solute carrier family 2, facilitated glucose transporter member 5PRO_0000050369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    PaxDbiP22732.
    PeptideAtlasiP22732.
    PRIDEiP22732.

    PTM databases

    PhosphoSiteiP22732.

    Expressioni

    Tissue specificityi

    Expressed in small intestine, and at much lower levels in kidney, skeletal muscle, and adipose tissue.

    Inductioni

    By forskolin in Caco-2 cells.1 Publication

    Gene expression databases

    ArrayExpressiP22732.
    BgeeiP22732.
    CleanExiHS_SLC2A5.
    GenevestigatoriP22732.

    Organism-specific databases

    HPAiCAB026176.
    HPA005449.

    Interactioni

    Protein-protein interaction databases

    BioGridi112409. 2 interactions.
    IntActiP22732. 3 interactions.
    STRINGi9606.ENSP00000366641.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YG1model-A1-501[»]
    ProteinModelPortaliP22732.
    SMRiP22732. Positions 63-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 6835ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini90 – 989CytoplasmicSequence Analysis
    Topological domaini120 – 1201ExtracellularSequence Analysis
    Topological domaini142 – 16120CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini183 – 19210ExtracellularSequence Analysis
    Topological domaini214 – 27764CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini299 – 31820ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini340 – 3423CytoplasmicSequence Analysis
    Topological domaini364 – 3685ExtracellularSequence Analysis
    Topological domaini390 – 41223CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini434 – 4396ExtracellularSequence Analysis
    Topological domaini461 – 50141CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei69 – 8921Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei99 – 11921Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei121 – 14121Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei162 – 18221Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei193 – 21321Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei278 – 29821Helical; Name=7Sequence AnalysisAdd
    BLAST
    Transmembranei319 – 33921Helical; Name=8Sequence AnalysisAdd
    BLAST
    Transmembranei343 – 36321Helical; Name=9Sequence AnalysisAdd
    BLAST
    Transmembranei369 – 38921Helical; Name=10Sequence AnalysisAdd
    BLAST
    Transmembranei413 – 43321Helical; Name=11Sequence AnalysisAdd
    BLAST
    Transmembranei440 – 46021Helical; Name=12Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni288 – 2947Monosaccharide bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0477.
    HOGENOMiHOG000202871.
    HOVERGENiHBG014816.
    InParanoidiP22732.
    KOiK08143.
    OMAiILMGCSE.
    OrthoDBiEOG7QVM2R.
    PhylomeDBiP22732.
    TreeFamiTF313762.

    Family and domain databases

    InterProiIPR002442. Fru_transpt_5.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR003663. Sugar/inositol_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view]
    PfamiPF00083. Sugar_tr. 1 hit.
    [Graphical view]
    PRINTSiPR01194. GLUCTRSPORT5.
    PR00171. SUGRTRNSPORT.
    SUPFAMiSSF103473. SSF103473. 1 hit.
    TIGRFAMsiTIGR00879. SP. 1 hit.
    PROSITEiPS50850. MFS. 1 hit.
    PS00216. SUGAR_TRANSPORT_1. 1 hit.
    PS00217. SUGAR_TRANSPORT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22732-1) [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

    MEQQDQSMKE GRLTLVLALA TLIAAFGSSF QYGYNVAAVN SPALLMQQFY    50
    NETYYGRTGE FMEDFPLTLL WSVTVSMFPF GGFIGSLLVG PLVNKFGRKG 100
    ALLFNNIFSI VPAILMGCSR VATSFELIII SRLLVGICAG VSSNVVPMYL 150
    GELAPKNLRG ALGVVPQLFI TVGILVAQIF GLRNLLANVD GWPILLGLTG 200
    VPAALQLLLL PFFPESPRYL LIQKKDEAAA KKALQTLRGW DSVDREVAEI 250
    RQEDEAEKAA GFISVLKLFR MRSLRWQLLS IIVLMGGQQL SGVNAIYYYA 300
    DQIYLSAGVP EEHVQYVTAG TGAVNVVMTF CAVFVVELLG RRLLLLLGFS 350
    ICLIACCVLT AALALQDTVS WMPYISIVCV ISYVIGHALG PSPIPALLIT 400
    EIFLQSSRPS AFMVGGSVHW LSNFTVGLIF PFIQEGLGPY SFIVFAVICL 450
    LTTIYIFLIV PETKAKTFIE INQIFTKMNK VSEVYPEKEE LKELPPVTSE 500
    Q 501
    Length:501
    Mass (Da):54,974
    Last modified:August 1, 1991 - v1
    Checksum:i090B12F529C7B857
    GO
    Isoform 2 (identifier: P22732-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         192-501: WPILLGLTGV...KELPPVTSEQ → EFRTSREHPH...LGGPSCPEPT

    Show »
    Length:244
    Mass (Da):26,519
    Checksum:i310B5F011D6CEA71
    GO

    Sequence cautioni

    The sequence AAB60641.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2021P → G in AAB60641. (PubMed:8037665)Curated

    Mass spectrometryi

    Molecular mass is 54973.98 Da from positions 1 - 501. Determined by MALDI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei192 – 501310WPILL…VTSEQ → EFRTSREHPHPFTTTLGPLL VFQSHHHRTGLSADWSLLTG WMSLGGPSCPEPT in isoform 2. 2 PublicationsVSP_042031Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55531 mRNA. Translation: AAA52570.1.
    U11843
    , U05344, U11839, U11840, U11841, U11842 Genomic DNA. Translation: AAB60641.1. Sequence problems.
    AK289849 mRNA. Translation: BAF82538.1.
    AK290398 mRNA. Translation: BAF83087.1.
    AL158048 Genomic DNA. Translation: CAI23457.1.
    AL158048 Genomic DNA. Translation: CAI23458.1.
    CH471130 Genomic DNA. Translation: EAW71610.1.
    BC001692 mRNA. Translation: AAH01692.1.
    BC001820 mRNA. Translation: AAH01820.1.
    BC035878 mRNA. Translation: AAH35878.1.
    CCDSiCCDS44054.1. [P22732-2]
    CCDS99.1. [P22732-1]
    PIRiA36629.
    G02864.
    RefSeqiNP_001129057.1. NM_001135585.1. [P22732-2]
    NP_003030.1. NM_003039.2. [P22732-1]
    XP_005263548.1. XM_005263491.1. [P22732-1]
    UniGeneiHs.530003.

    Genome annotation databases

    EnsembliENST00000377414; ENSP00000366631; ENSG00000142583. [P22732-2]
    ENST00000377424; ENSP00000366641; ENSG00000142583. [P22732-1]
    GeneIDi6518.
    KEGGihsa:6518.
    UCSCiuc001apo.3. human. [P22732-1]
    uc001app.4. human. [P22732-2]

    Polymorphism databases

    DMDMi121764.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55531 mRNA. Translation: AAA52570.1 .
    U11843
    , U05344 , U11839 , U11840 , U11841 , U11842 Genomic DNA. Translation: AAB60641.1 . Sequence problems.
    AK289849 mRNA. Translation: BAF82538.1 .
    AK290398 mRNA. Translation: BAF83087.1 .
    AL158048 Genomic DNA. Translation: CAI23457.1 .
    AL158048 Genomic DNA. Translation: CAI23458.1 .
    CH471130 Genomic DNA. Translation: EAW71610.1 .
    BC001692 mRNA. Translation: AAH01692.1 .
    BC001820 mRNA. Translation: AAH01820.1 .
    BC035878 mRNA. Translation: AAH35878.1 .
    CCDSi CCDS44054.1. [P22732-2 ]
    CCDS99.1. [P22732-1 ]
    PIRi A36629.
    G02864.
    RefSeqi NP_001129057.1. NM_001135585.1. [P22732-2 ]
    NP_003030.1. NM_003039.2. [P22732-1 ]
    XP_005263548.1. XM_005263491.1. [P22732-1 ]
    UniGenei Hs.530003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YG1 model - A 1-501 [» ]
    ProteinModelPortali P22732.
    SMRi P22732. Positions 63-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112409. 2 interactions.
    IntActi P22732. 3 interactions.
    STRINGi 9606.ENSP00000366641.

    Chemistry

    BindingDBi P22732.
    ChEMBLi CHEMBL5875.

    Protein family/group databases

    TCDBi 2.A.1.1.13. the major facilitator superfamily (mfs).

    PTM databases

    PhosphoSitei P22732.

    Polymorphism databases

    DMDMi 121764.

    Proteomic databases

    PaxDbi P22732.
    PeptideAtlasi P22732.
    PRIDEi P22732.

    Protocols and materials databases

    DNASUi 6518.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377414 ; ENSP00000366631 ; ENSG00000142583 . [P22732-2 ]
    ENST00000377424 ; ENSP00000366641 ; ENSG00000142583 . [P22732-1 ]
    GeneIDi 6518.
    KEGGi hsa:6518.
    UCSCi uc001apo.3. human. [P22732-1 ]
    uc001app.4. human. [P22732-2 ]

    Organism-specific databases

    CTDi 6518.
    GeneCardsi GC01M009095.
    HGNCi HGNC:11010. SLC2A5.
    HPAi CAB026176.
    HPA005449.
    MIMi 138230. gene.
    neXtProti NX_P22732.
    PharmGKBi PA35880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0477.
    HOGENOMi HOG000202871.
    HOVERGENi HBG014816.
    InParanoidi P22732.
    KOi K08143.
    OMAi ILMGCSE.
    OrthoDBi EOG7QVM2R.
    PhylomeDBi P22732.
    TreeFami TF313762.

    Enzyme and pathway databases

    Reactomei REACT_19281. Class II GLUTs.
    REACT_9441. Hexose transport.

    Miscellaneous databases

    ChiTaRSi SLC2A5. human.
    GenomeRNAii 6518.
    NextBioi 25345.
    PROi P22732.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22732.
    Bgeei P22732.
    CleanExi HS_SLC2A5.
    Genevestigatori P22732.

    Family and domain databases

    InterProi IPR002442. Fru_transpt_5.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR003663. Sugar/inositol_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view ]
    Pfami PF00083. Sugar_tr. 1 hit.
    [Graphical view ]
    PRINTSi PR01194. GLUCTRSPORT5.
    PR00171. SUGRTRNSPORT.
    SUPFAMi SSF103473. SSF103473. 1 hit.
    TIGRFAMsi TIGR00879. SP. 1 hit.
    PROSITEi PS50850. MFS. 1 hit.
    PS00216. SUGAR_TRANSPORT_1. 1 hit.
    PS00217. SUGAR_TRANSPORT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human facilitative glucose transporters. Isolation, functional characterization, and gene localization of cDNAs encoding an isoform (GLUT5) expressed in small intestine, kidney, muscle, and adipose tissue and an unusual glucose transporter pseudogene-like sequence (GLUT6)."
      Kayano T., Burant C.F., Fukumoto H., Gould G.W., Fan Y.-S., Eddy R.L., Byers M.G., Shows T.B., Seino S., Bell G.I.
      J. Biol. Chem. 265:13276-13282(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Jejunum.
    2. "Regulation of expression of the human fructose transporter (GLUT5) by cyclic AMP."
      Mahraoui L., Takeda J., Mesonero J., Chantret I., Dussaulx E., Bell G.I., Brot-Laroche E.
      Biochem. J. 301:169-175(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Tissue: Fetal liver.
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Umbilical cord blood.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: Lymph and Prostate.
    7. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGTR5_HUMAN
    AccessioniPrimary (citable) accession number: P22732
    Secondary accession number(s): Q14770, Q5T977, Q8IVB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 152 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3