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Q8IUC8

- GLT13_HUMAN

UniProt

Q8IUC8 - GLT13_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene

GALNT13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551SubstrateBy similarity
    Binding sitei185 – 1851SubstrateBy similarity
    Metal bindingi208 – 2081ManganeseBy similarity
    Metal bindingi210 – 2101ManganeseBy similarity
    Binding sitei315 – 3151SubstrateBy similarity
    Metal bindingi343 – 3431ManganeseBy similarity
    Binding sitei346 – 3461SubstrateBy similarity
    Binding sitei351 – 3511SubstrateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. O-glycan processing Source: Reactome
    3. post-translational protein modification Source: Reactome
    4. protein O-linked glycosylation Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.41. 2681.
    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 13 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 13
    Short name:
    GalNAc-T13
    Short name:
    pp-GaNTase 13
    Protein-UDP acetylgalactosaminyltransferase 13
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
    Gene namesi
    Name:GALNT13
    Synonyms:KIAA1918
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:23242. GALNT13.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-KW
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134887166.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi105 ↔ 338PROSITE-ProRule annotation
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi329 ↔ 407PROSITE-ProRule annotation
    Disulfide bondi441 ↔ 458PROSITE-ProRule annotation
    Disulfide bondi481 ↔ 496PROSITE-ProRule annotation
    Disulfide bondi522 ↔ 539PROSITE-ProRule annotation
    Glycosylationi551 – 5511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8IUC8.
    PaxDbiQ8IUC8.
    PRIDEiQ8IUC8.

    PTM databases

    PhosphoSiteiQ8IUC8.

    Expressioni

    Tissue specificityi

    Specifically expressed in neuronal cells. Expressed in fetal brain, whole adult brain, cerebral cortex and cerebellum. Not expressed in other tissues tested.1 Publication

    Gene expression databases

    ArrayExpressiQ8IUC8.
    BgeeiQ8IUC8.
    CleanExiHS_GALNT13.
    GenevestigatoriQ8IUC8.

    Organism-specific databases

    HPAiHPA060775.

    Interactioni

    Protein-protein interaction databases

    BioGridi125365. 3 interactions.
    STRINGi9606.ENSP00000376570.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IUC8.
    SMRiQ8IUC8. Positions 56-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini28 – 556529LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini428 – 550123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni114 – 224111Catalytic subdomain AAdd
    BLAST
    Regioni284 – 34663Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG239675.
    HOGENOMiHOG000038227.
    HOVERGENiHBG051699.
    KOiK00710.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8IUC8.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IUC8-1) [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

    MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI    50
    SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV 100
    RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV 150
    ILVDDASERD FLKLTLENYV KNLEVPVKII RMEERSGLIR ARLRGAAASK 200
    GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG 250
    SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 300
    YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP 350
    YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT 400
    LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN 450
    EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLNGP VIMLKCHHMR 500
    GNQLWEYDAE RLTLRHVNSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR 550
    NMTLGT 556
    Length:556
    Mass (Da):64,051
    Last modified:October 17, 2006 - v2
    Checksum:i00F3DCDDC4754D6F
    GO
    Isoform 2 (identifier: Q8IUC8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         466-486: VFSYTADKEIRTDDLCLDVSR → TQWTCNHVKMPPYERKSVMGI
         487-556: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:486
    Mass (Da):55,984
    Checksum:iCBD44DBD154E567D
    GO
    Isoform 3 (identifier: Q8IUC8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         511-556: RLTLRHVNSN...WLLRNMTLGT → SCLSVNKVAD...IFGNSTDYIL

    Note: No experimental confirmation available.

    Show »
    Length:561
    Mass (Da):64,624
    Checksum:i309A4A1B365D02B8
    GO

    Sequence cautioni

    The sequence BAC85542.1 differs from that shown. Reason: Chimera. Chimeric at the N-terminus.
    The sequence AAF19246.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41F → S in BAC54545. (PubMed:12407114)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591E → D.
    Corresponds to variant rs34086479 [ dbSNP | Ensembl ].
    VAR_049242

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei466 – 48621VFSYT…LDVSR → TQWTCNHVKMPPYERKSVMG I in isoform 2. 1 PublicationVSP_011218Add
    BLAST
    Alternative sequencei487 – 55670Missing in isoform 2. 1 PublicationVSP_011219Add
    BLAST
    Alternative sequencei511 – 55646RLTLR…MTLGT → SCLSVNKVADGSQHPTVETC NDSTLQKWLLRNYTRMEIFR NIFGNSTDYIL in isoform 3. 1 PublicationVSP_054411Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078142 mRNA. Translation: BAC54545.1.
    KJ534843 mRNA. Translation: AHW56483.1.
    AJ505991 mRNA. Translation: CAD44533.2.
    AC008166 Genomic DNA. No translation available.
    AC009227 Genomic DNA. Translation: AAF19246.1. Different initiation.
    AC009297 Genomic DNA. No translation available.
    AC092584 Genomic DNA. No translation available.
    AC092589 Genomic DNA. No translation available.
    AC133107 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11464.1.
    CH471058 Genomic DNA. Translation: EAX11465.1.
    BC101031 mRNA. Translation: AAI01032.1.
    BC101032 mRNA. Translation: AAI01033.1.
    BC101033 mRNA. Translation: AAI01034.1.
    BC101034 mRNA. Translation: AAI01035.1.
    AB067505 mRNA. Translation: BAB67811.1.
    AK123152 mRNA. Translation: BAC85542.1. Sequence problems.
    CCDSiCCDS2199.1. [Q8IUC8-1]
    RefSeqiNP_443149.2. NM_052917.2. [Q8IUC8-1]
    XP_006712293.1. XM_006712230.1. [Q8IUC8-1]
    UniGeneiHs.470277.

    Genome annotation databases

    EnsembliENST00000392825; ENSP00000376570; ENSG00000144278. [Q8IUC8-1]
    ENST00000409237; ENSP00000387239; ENSG00000144278. [Q8IUC8-3]
    GeneIDi114805.
    KEGGihsa:114805.
    UCSCiuc002tyr.4. human. [Q8IUC8-1]
    uc010foc.1. human. [Q8IUC8-2]

    Polymorphism databases

    DMDMi116242497.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 13

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078142 mRNA. Translation: BAC54545.1 .
    KJ534843 mRNA. Translation: AHW56483.1 .
    AJ505991 mRNA. Translation: CAD44533.2 .
    AC008166 Genomic DNA. No translation available.
    AC009227 Genomic DNA. Translation: AAF19246.1 . Different initiation.
    AC009297 Genomic DNA. No translation available.
    AC092584 Genomic DNA. No translation available.
    AC092589 Genomic DNA. No translation available.
    AC133107 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11464.1 .
    CH471058 Genomic DNA. Translation: EAX11465.1 .
    BC101031 mRNA. Translation: AAI01032.1 .
    BC101032 mRNA. Translation: AAI01033.1 .
    BC101033 mRNA. Translation: AAI01034.1 .
    BC101034 mRNA. Translation: AAI01035.1 .
    AB067505 mRNA. Translation: BAB67811.1 .
    AK123152 mRNA. Translation: BAC85542.1 . Sequence problems.
    CCDSi CCDS2199.1. [Q8IUC8-1 ]
    RefSeqi NP_443149.2. NM_052917.2. [Q8IUC8-1 ]
    XP_006712293.1. XM_006712230.1. [Q8IUC8-1 ]
    UniGenei Hs.470277.

    3D structure databases

    ProteinModelPortali Q8IUC8.
    SMRi Q8IUC8. Positions 56-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125365. 3 interactions.
    STRINGi 9606.ENSP00000376570.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    PTM databases

    PhosphoSitei Q8IUC8.

    Polymorphism databases

    DMDMi 116242497.

    Proteomic databases

    MaxQBi Q8IUC8.
    PaxDbi Q8IUC8.
    PRIDEi Q8IUC8.

    Protocols and materials databases

    DNASUi 114805.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392825 ; ENSP00000376570 ; ENSG00000144278 . [Q8IUC8-1 ]
    ENST00000409237 ; ENSP00000387239 ; ENSG00000144278 . [Q8IUC8-3 ]
    GeneIDi 114805.
    KEGGi hsa:114805.
    UCSCi uc002tyr.4. human. [Q8IUC8-1 ]
    uc010foc.1. human. [Q8IUC8-2 ]

    Organism-specific databases

    CTDi 114805.
    GeneCardsi GC02P154765.
    HGNCi HGNC:23242. GALNT13.
    HPAi HPA060775.
    MIMi 608369. gene.
    neXtProti NX_Q8IUC8.
    PharmGKBi PA134887166.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    KOi K00710.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8IUC8.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 2681.
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT13. human.
    GeneWikii GALNT13.
    GenomeRNAii 114805.
    NextBioi 79266.
    PROi Q8IUC8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IUC8.
    Bgeei Q8IUC8.
    CleanExi HS_GALNT13.
    Genevestigatori Q8IUC8.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
      Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
      J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
    2. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    3. "polypetide GalNAc-transferase 13, ppGalNAc-T13, GALNT13."
      Bennett E.P.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 3).
    7. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
      Nagase T., Kikuno R., Ohara O.
      DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-556 (ISOFORM 1).
      Tissue: Brain.
    8. "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] OF 262-556 (ISOFORM 2).
      Tissue: Cerebellum.

    Entry informationi

    Entry nameiGLT13_HUMAN
    AccessioniPrimary (citable) accession number: Q8IUC8
    Secondary accession number(s): Q08ER7
    , Q68VI8, Q6ZWG1, Q96PX0, Q9UIE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 114 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 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3