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Q86SR1

- GLT10_HUMAN

UniProt

Q86SR1 - GLT10_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

GALNT10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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 activity toward Muc5Ac and EA2 peptide substrates.

    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 sitei154 – 1541Substrate
    Binding sitei156 – 1561Substrate
    Binding sitei185 – 1851Substrate
    Binding sitei214 – 2141Substrate
    Metal bindingi237 – 2371Manganese
    Binding sitei238 – 2381Substrate
    Metal bindingi239 – 2391Manganese
    Binding sitei342 – 3421Substrate
    Metal bindingi370 – 3701Manganese
    Binding sitei373 – 3731Substrate
    Binding sitei378 – 3781Substrate

    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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    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 10 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 10
    Short name:
    GalNAc-T10
    Short name:
    pp-GaNTase 10
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
    Gene namesi
    Name:GALNT10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:19873. GALNT10.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134870832.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603Polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059122Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
    Disulfide bondi135 ↔ 3651 PublicationPROSITE-ProRule annotation
    Glycosylationi146 – 1461N-linked (GlcNAc...)1 Publication
    Disulfide bondi356 ↔ 4321 PublicationPROSITE-ProRule annotation
    Disulfide bondi471 ↔ 4881 PublicationPROSITE-ProRule annotation
    Disulfide bondi523 ↔ 5381 PublicationPROSITE-ProRule annotation
    Disulfide bondi563 ↔ 5781 PublicationPROSITE-ProRule annotation
    Glycosylationi593 – 5931N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ86SR1.
    PaxDbiQ86SR1.
    PRIDEiQ86SR1.

    PTM databases

    PhosphoSiteiQ86SR1.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ86SR1.
    BgeeiQ86SR1.
    GenevestigatoriQ86SR1.

    Organism-specific databases

    HPAiHPA007525.

    Interactioni

    Protein-protein interaction databases

    BioGridi120723. 1 interaction.
    IntActiQ86SR1. 1 interaction.
    MINTiMINT-2808648.

    Structurei

    Secondary structure

    1
    603
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi77 – 848
    Helixi91 – 933
    Turni100 – 1034
    Helixi106 – 1094
    Helixi115 – 1195
    Helixi133 – 1364
    Beta strandi140 – 1434
    Beta strandi147 – 1559
    Helixi158 – 17114
    Helixi174 – 1763
    Beta strandi177 – 1848
    Helixi190 – 1923
    Helixi194 – 2007
    Beta strandi206 – 2105
    Helixi217 – 22711
    Beta strandi230 – 2356
    Beta strandi238 – 2425
    Helixi248 – 2569
    Beta strandi260 – 26910
    Turni271 – 2733
    Beta strandi285 – 2884
    Beta strandi294 – 2974
    Turni301 – 3033
    Beta strandi319 – 3257
    Helixi326 – 3316
    Beta strandi341 – 3444
    Helixi345 – 35511
    Beta strandi359 – 37012
    Helixi386 – 39712
    Helixi399 – 4013
    Helixi402 – 4065
    Helixi410 – 4123
    Helixi421 – 43010
    Helixi435 – 4417
    Helixi446 – 4494
    Beta strandi458 – 4658
    Turni466 – 4683
    Turni478 – 4803
    Helixi495 – 4973
    Beta strandi503 – 5053
    Turni507 – 5093
    Beta strandi511 – 5144
    Beta strandi521 – 5255
    Beta strandi528 – 5325
    Beta strandi534 – 5374
    Beta strandi540 – 5434
    Beta strandi548 – 5503
    Turni551 – 5533
    Beta strandi554 – 5563
    Turni558 – 5603
    Beta strandi563 – 5664
    Turni568 – 5703
    Beta strandi573 – 5764
    Beta strandi587 – 5915
    Helixi594 – 5974
    Turni598 – 6014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D7IX-ray2.50A40-603[»]
    2D7RX-ray2.80A40-603[»]
    ProteinModelPortaliQ86SR1.
    SMRiQ86SR1. Positions 68-603.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86SR1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 603572LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 590133Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 253110Catalytic subdomain AAdd
    BLAST
    Regioni311 – 37363Catalytic subdomain BAdd
    BLAST
    Regioni373 – 38412Flexible loopAdd
    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.
    HOVERGENiHBG051699.
    InParanoidiQ86SR1.
    KOiK00710.
    OMAiHSRQKKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ86SR1.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86SR1-1) [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

    MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA    50
    AGQGSHSRQK KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD 100
    AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKRY LETLPNTSII 150
    IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM 200
    ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC EANVNWLPPL 250
    LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 300
    PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS 350
    FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE 400
    YAEYIYQRRP EYRHLSAGDV AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY 450
    PPVEPPAAAW GEIRNVGTGL CADTKHGALG SPLRLEGCVR GRGEAAWNNM 500
    QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS MKGNQLWKYR 550
    KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF 600
    NRN 603
    Length:603
    Mass (Da):68,992
    Last modified:August 16, 2004 - v2
    Checksum:iEE176F6139B92573
    GO
    Isoform 2 (identifier: Q86SR1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         190-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:541
    Mass (Da):61,947
    Checksum:i4216612D314EA82B
    GO
    Isoform 3 (identifier: Q86SR1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         354-366: WMCGGRMEDIPCS → SQLSRRPVLGTAS
         367-603: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:366
    Mass (Da):41,452
    Checksum:i52AB23ABC6F797FE
    GO
    Isoform 4 (identifier: Q86SR1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-329: Missing.
         330-352: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ
         389-389: N → VRT

    Note: No experimental confirmation available.

    Show »
    Length:276
    Mass (Da):31,833
    Checksum:iF357AFF828E57DC7
    GO

    Sequence cautioni

    The sequence BAB14676.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti518 – 5181H → Y in BAC56890. (PubMed:12417297)Curated
    Sequence conflicti518 – 5181H → Y in BAB14676. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 329329Missing in isoform 4. 1 PublicationVSP_011207Add
    BLAST
    Alternative sequencei190 – 25162Missing in isoform 2. 1 PublicationVSP_011209Add
    BLAST
    Alternative sequencei330 – 35223WELGG…EISFK → MLAWRDGELEAETSSSLFLL AMQ in isoform 4. 1 PublicationVSP_011208Add
    BLAST
    Alternative sequencei354 – 36613WMCGG…DIPCS → SQLSRRPVLGTAS in isoform 3. 1 PublicationVSP_011212Add
    BLAST
    Alternative sequencei367 – 603237Missing in isoform 3. 1 PublicationVSP_011213Add
    BLAST
    Alternative sequencei389 – 3891N → VRT in isoform 4. 1 PublicationVSP_011214

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078145 mRNA. Translation: BAC56890.1.
    AJ505950 mRNA. Translation: CAD44532.1.
    AK023782 mRNA. Translation: BAB14676.1. Different initiation.
    AK127135 mRNA. Translation: BAG54441.1.
    AL096739 mRNA. Translation: CAB46378.1.
    AK074132 mRNA. Translation: BAB84958.1.
    BC007224 mRNA. Translation: AAH07224.2.
    BC072450 mRNA. Translation: AAH72450.1.
    CCDSiCCDS4325.1. [Q86SR1-1]
    PIRiT12552.
    RefSeqiNP_938080.1. NM_198321.3. [Q86SR1-1]
    UniGeneiHs.631797.

    Genome annotation databases

    EnsembliENST00000297107; ENSP00000297107; ENSG00000164574. [Q86SR1-1]
    ENST00000377661; ENSP00000366889; ENSG00000164574. [Q86SR1-2]
    ENST00000425427; ENSP00000415210; ENSG00000164574. [Q86SR1-3]
    GeneIDi55568.
    KEGGihsa:55568.
    UCSCiuc003lvg.1. human. [Q86SR1-3]
    uc003lvh.3. human. [Q86SR1-1]
    uc010jid.3. human. [Q86SR1-2]

    Polymorphism databases

    DMDMi51315962.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 10

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 10

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078145 mRNA. Translation: BAC56890.1 .
    AJ505950 mRNA. Translation: CAD44532.1 .
    AK023782 mRNA. Translation: BAB14676.1 . Different initiation.
    AK127135 mRNA. Translation: BAG54441.1 .
    AL096739 mRNA. Translation: CAB46378.1 .
    AK074132 mRNA. Translation: BAB84958.1 .
    BC007224 mRNA. Translation: AAH07224.2 .
    BC072450 mRNA. Translation: AAH72450.1 .
    CCDSi CCDS4325.1. [Q86SR1-1 ]
    PIRi T12552.
    RefSeqi NP_938080.1. NM_198321.3. [Q86SR1-1 ]
    UniGenei Hs.631797.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D7I X-ray 2.50 A 40-603 [» ]
    2D7R X-ray 2.80 A 40-603 [» ]
    ProteinModelPortali Q86SR1.
    SMRi Q86SR1. Positions 68-603.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120723. 1 interaction.
    IntActi Q86SR1. 1 interaction.
    MINTi MINT-2808648.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q86SR1.

    Polymorphism databases

    DMDMi 51315962.

    Proteomic databases

    MaxQBi Q86SR1.
    PaxDbi Q86SR1.
    PRIDEi Q86SR1.

    Protocols and materials databases

    DNASUi 55568.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297107 ; ENSP00000297107 ; ENSG00000164574 . [Q86SR1-1 ]
    ENST00000377661 ; ENSP00000366889 ; ENSG00000164574 . [Q86SR1-2 ]
    ENST00000425427 ; ENSP00000415210 ; ENSG00000164574 . [Q86SR1-3 ]
    GeneIDi 55568.
    KEGGi hsa:55568.
    UCSCi uc003lvg.1. human. [Q86SR1-3 ]
    uc003lvh.3. human. [Q86SR1-1 ]
    uc010jid.3. human. [Q86SR1-2 ]

    Organism-specific databases

    CTDi 55568.
    GeneCardsi GC05P153550.
    HGNCi HGNC:19873. GALNT10.
    HPAi HPA007525.
    MIMi 608043. gene.
    neXtProti NX_Q86SR1.
    PharmGKBi PA134870832.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOVERGENi HBG051699.
    InParanoidi Q86SR1.
    KOi K00710.
    OMAi HSRQKKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q86SR1.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT10. human.
    EvolutionaryTracei Q86SR1.
    GenomeRNAii 55568.
    NextBioi 60056.
    PROi Q86SR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86SR1.
    Bgeei Q86SR1.
    Genevestigatori Q86SR1.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Colon cancer.
    2. Bennett E.P.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-603 (ISOFORM 2).
      Tissue: Brain and Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Uterus.
    5. "Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
      Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
      DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-366 (ISOFORM 3).
      Tissue: Spleen.
    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] OF 191-603 (ISOFORM 1).
      Tissue: Kidney and Skin.
    7. "Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)."
      Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R., Wakatsuki S., Narimatsu H.
      J. Mol. Biol. 359:708-727(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITH UDP-GALNAC AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES, GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.

    Entry informationi

    Entry nameiGLT10_HUMAN
    AccessioniPrimary (citable) accession number: Q86SR1
    Secondary accession number(s): B3KXC9
    , Q6IN56, Q86VP8, Q8IXJ2, Q8TEJ2, Q96IV2, Q9H8E1, Q9Y4M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3