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Q10471

- GALT2_HUMAN

UniProt

Q10471 - GALT2_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

GALNT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region.4 Publications

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.2 Publications

    Cofactori

    Manganese.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei143 – 1431Substrate
    Binding sitei176 – 1761Substrate
    Binding sitei201 – 2011Substrate
    Metal bindingi224 – 2241Manganese1 Publication
    Binding sitei225 – 2251Substrate
    Metal bindingi226 – 2261Manganese1 Publication
    Binding sitei331 – 3311Substrate
    Metal bindingi359 – 3591Manganese1 Publication
    Binding sitei362 – 3621Substrate
    Binding sitei365 – 3651Substrate
    Binding sitei367 – 3671Substrate
    Sitei516 – 5161Not glycosylated

    GO - Molecular functioni

    1. manganese ion binding Source: UniProtKB
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. immunoglobulin biosynthetic process Source: BHF-UCL
    3. O-glycan processing Source: Reactome
    4. post-translational protein modification Source: Reactome
    5. protein O-linked glycosylation Source: UniProtKB
    6. protein O-linked glycosylation via serine Source: BHF-UCL
    7. protein O-linked glycosylation via threonine Source: BHF-UCL

    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 2 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 2
    Short name:
    GalNAc-T2
    Short name:
    pp-GaNTase 2
    Protein-UDP acetylgalactosaminyltransferase 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
    Cleaved into the following chain:
    Gene namesi
    Name:GALNT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4124. GALNT2.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Secreted 1 Publication
    Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi apparatus Source: BHF-UCL
    3. Golgi cisterna membrane Source: UniProtKB-SubCell
    4. Golgi membrane Source: Reactome
    5. Golgi stack Source: BHF-UCL
    6. integral component of Golgi membrane Source: BHF-UCL
    7. membrane Source: UniProtKB
    8. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28537.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 571571Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000223391Add
    BLAST
    Chaini52 – 571520Polypeptide N-acetylgalactosaminyltransferase 2 soluble formPRO_0000012265Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi126 ↔ 3541 PublicationPROSITE-ProRule annotation
    Disulfide bondi345 ↔ 4231 PublicationPROSITE-ProRule annotation
    Disulfide bondi456 ↔ 4731 PublicationPROSITE-ProRule annotation
    Disulfide bondi496 ↔ 5131 PublicationPROSITE-ProRule annotation
    Disulfide bondi539 ↔ 5551 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ10471.
    PaxDbiQ10471.
    PeptideAtlasiQ10471.
    PRIDEiQ10471.

    PTM databases

    PhosphoSiteiQ10471.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ10471.
    BgeeiQ10471.
    CleanExiHS_GALNT2.
    GenevestigatoriQ10471.

    Organism-specific databases

    HPAiHPA011222.

    Interactioni

    Protein-protein interaction databases

    BioGridi108862. 8 interactions.
    MINTiMINT-3026412.
    STRINGi9606.ENSP00000355632.

    Structurei

    Secondary structure

    1
    571
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi78 – 803
    Helixi83 – 886
    Turni98 – 1025
    Helixi106 – 1116
    Helixi124 – 1285
    Beta strandi138 – 1469
    Helixi149 – 16214
    Helixi165 – 1673
    Beta strandi168 – 1758
    Helixi182 – 1854
    Helixi186 – 1894
    Beta strandi193 – 1975
    Helixi203 – 21412
    Beta strandi217 – 2226
    Beta strandi225 – 2295
    Helixi234 – 24310
    Beta strandi247 – 25610
    Turni258 – 2603
    Beta strandi268 – 2747
    Beta strandi280 – 2845
    Helixi287 – 2926
    Beta strandi308 – 3147
    Helixi315 – 3206
    Beta strandi330 – 3334
    Helixi334 – 34411
    Beta strandi348 – 35912
    Turni366 – 3683
    Helixi373 – 38816
    Helixi390 – 3923
    Helixi393 – 3997
    Helixi401 – 4055
    Helixi412 – 4209
    Helixi426 – 4327
    Beta strandi447 – 4526
    Beta strandi455 – 4584
    Turni463 – 4653
    Beta strandi469 – 4724
    Helixi478 – 4803
    Beta strandi482 – 4843
    Beta strandi490 – 4923
    Beta strandi495 – 4984
    Beta strandi509 – 5124
    Helixi518 – 5203
    Beta strandi522 – 5254
    Turni526 – 5294
    Beta strandi530 – 5334
    Beta strandi536 – 5416
    Helixi545 – 5473
    Beta strandi551 – 5544
    Helixi559 – 5613
    Beta strandi564 – 5674

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FFUX-ray1.64A75-571[»]
    2FFVX-ray2.75A/B75-571[»]
    4D0TX-ray2.45A/B/C/D/E/F1-571[»]
    4D0ZX-ray2.20A/B/C/D/E/F1-571[»]
    4D11X-ray2.85A/B/C/D/E/F1-571[»]
    ProteinModelPortaliQ10471.
    SMRiQ10471. Positions 75-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ10471.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini25 – 571547LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini443 – 566124Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni135 – 240106Catalytic subdomain AAdd
    BLAST
    Regioni300 – 36263Catalytic 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.
    InParanoidiQ10471.
    KOiK00710.
    OMAiDDYSDNP.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ10471.
    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 (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. Align

    Isoform 1 (identifier: Q10471-1) [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

    MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP    50
    IKKKDLHHSN GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA 100
    RNKFNQVESD KLRMDRAIPD TRHDQCQRKQ WRVDLPATSV VITFHNEARS 150
    ALLRTVVSVL KKSPPHLIKE IILVDDYSND PEDGALLGKI EKVRVLRNDR 200
    REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER VAEDRTRVVS 250
    PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP 300
    IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE 350
    IIPCSRVGHV FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV 400
    PSARNVPYGN IQSRLELRKK LSCKPFKWYL ENVYPELRVP DHQDIAFGAL 450
    QQGTNCLDTL GHFADGVVGV YECHNAGGNQ EWALTKEKSV KHMDLCLTVV 500
    DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL DSRTAKSGGL 550
    SVEVCGPALS QQWKFTLNLQ Q 571
    Length:571
    Mass (Da):64,733
    Last modified:November 1, 1996 - v1
    Checksum:iD9A0F5D17C55BAF2
    GO
    Isoform 2 (identifier: Q10471-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-90: Missing.
         303-355: TPMIAGGLFV...GGSLEIIPCS → DLVPRVAVWW...HPPGSRGLDG
         356-571: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:265
    Mass (Da):30,256
    Checksum:i02CD3D8D4652ED95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701T → G AA sequence (PubMed:7592619)Curated
    Sequence conflicti78 – 781W → D AA sequence (PubMed:7592619)Curated
    Sequence conflicti93 – 931R → G AA sequence (PubMed:7592619)Curated
    Sequence conflicti210 – 2101R → W AA sequence (PubMed:7592619)Curated
    Sequence conflicti290 – 2912RR → SC AA sequence (PubMed:7592619)Curated
    Sequence conflicti293 – 2931R → Q AA sequence (PubMed:7592619)Curated
    Sequence conflicti300 – 3001P → H AA sequence (PubMed:7592619)Curated
    Sequence conflicti522 – 5221W → A AA sequence (PubMed:7592619)Curated
    Sequence conflicti533 – 5331H → M AA sequence (PubMed:7592619)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti245 – 2451R → H.
    Corresponds to variant rs1923950 [ dbSNP | Ensembl ].
    VAR_049240
    Natural varianti554 – 5541V → M.1 Publication
    Corresponds to variant rs2273970 [ dbSNP | Ensembl ].
    VAR_019575

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9090Missing in isoform 2. 1 PublicationVSP_056491Add
    BLAST
    Alternative sequencei303 – 35553TPMIA…IIPCS → DLVPRVAVWWQPGDHPVQPC GTRVPEAAPLHVPGWQWHCL CPKHPPGSRGLDG in isoform 2. 1 PublicationVSP_056492Add
    BLAST
    Alternative sequencei356 – 571216Missing in isoform 2. 1 PublicationVSP_056493Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85019 mRNA. Translation: CAA59381.1.
    AK290048 mRNA. Translation: BAF82737.1.
    AK304029 mRNA. Translation: BAH14094.1.
    AL592228 Genomic DNA. No translation available.
    AL078646, AL117349, AL136988 Genomic DNA. Translation: CAC00585.2.
    AL117349, AL078646, AL136988 Genomic DNA. Translation: CAI22902.1.
    AL136988, AL078646, AL117349 Genomic DNA. Translation: CAI23447.1.
    FJ515852 Genomic DNA. Translation: ACS13744.1.
    CH471098 Genomic DNA. Translation: EAW69911.1.
    BC041120 mRNA. Translation: AAH41120.1.
    CCDSiCCDS1582.1.
    PIRiI37405.
    RefSeqiNP_001278795.1. NM_001291866.1.
    NP_004472.1. NM_004481.4.
    UniGeneiHs.743964.

    Genome annotation databases

    EnsembliENST00000366672; ENSP00000355632; ENSG00000143641.
    ENST00000541865; ENSP00000444346; ENSG00000143641.
    GeneIDi2590.
    KEGGihsa:2590.
    UCSCiuc010pwa.1. human.

    Polymorphism databases

    DMDMi51315838.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85019 mRNA. Translation: CAA59381.1 .
    AK290048 mRNA. Translation: BAF82737.1 .
    AK304029 mRNA. Translation: BAH14094.1 .
    AL592228 Genomic DNA. No translation available.
    AL078646 , AL117349 , AL136988 Genomic DNA. Translation: CAC00585.2 .
    AL117349 , AL078646 , AL136988 Genomic DNA. Translation: CAI22902.1 .
    AL136988 , AL078646 , AL117349 Genomic DNA. Translation: CAI23447.1 .
    FJ515852 Genomic DNA. Translation: ACS13744.1 .
    CH471098 Genomic DNA. Translation: EAW69911.1 .
    BC041120 mRNA. Translation: AAH41120.1 .
    CCDSi CCDS1582.1.
    PIRi I37405.
    RefSeqi NP_001278795.1. NM_001291866.1.
    NP_004472.1. NM_004481.4.
    UniGenei Hs.743964.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FFU X-ray 1.64 A 75-571 [» ]
    2FFV X-ray 2.75 A/B 75-571 [» ]
    4D0T X-ray 2.45 A/B/C/D/E/F 1-571 [» ]
    4D0Z X-ray 2.20 A/B/C/D/E/F 1-571 [» ]
    4D11 X-ray 2.85 A/B/C/D/E/F 1-571 [» ]
    ProteinModelPortali Q10471.
    SMRi Q10471. Positions 75-568.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108862. 8 interactions.
    MINTi MINT-3026412.
    STRINGi 9606.ENSP00000355632.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q10471.

    Polymorphism databases

    DMDMi 51315838.

    Proteomic databases

    MaxQBi Q10471.
    PaxDbi Q10471.
    PeptideAtlasi Q10471.
    PRIDEi Q10471.

    Protocols and materials databases

    DNASUi 2590.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366672 ; ENSP00000355632 ; ENSG00000143641 .
    ENST00000541865 ; ENSP00000444346 ; ENSG00000143641 .
    GeneIDi 2590.
    KEGGi hsa:2590.
    UCSCi uc010pwa.1. human.

    Organism-specific databases

    CTDi 2590.
    GeneCardsi GC01P230193.
    H-InvDB HIX0001682.
    HGNCi HGNC:4124. GALNT2.
    HPAi HPA011222.
    MIMi 602274. gene.
    neXtProti NX_Q10471.
    PharmGKBi PA28537.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOGENOMi HOG000038227.
    HOVERGENi HBG051699.
    InParanoidi Q10471.
    KOi K00710.
    OMAi DDYSDNP.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q10471.
    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 GALNT2. human.
    EvolutionaryTracei Q10471.
    GeneWikii GALNT2.
    GenomeRNAii 2590.
    NextBioi 10245.
    PROi Q10471.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q10471.
    Bgeei Q10471.
    CleanExi HS_GALNT2.
    Genevestigatori Q10471.

    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. "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
      White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.
      J. Biol. Chem. 270:24156-24165(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 52-93; 104-120; 170-182; 193-218; 303-323; 421-424 AND 510-546, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Gastric carcinoma.
    2. "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), VARIANT MET-554.
      Tissue: Hippocampus and Trachea.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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] (ISOFORM 1).
      Tissue: Lymph.
    7. "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
      Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
      J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
      Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
      J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2."
      Iwasaki H., Zhang Y., Tachibana K., Gotoh M., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Kubota T., Narimatsu H.
      J. Biol. Chem. 278:5613-5621(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2."
      Fritz T.A., Raman J., Tabak L.A.
      J. Biol. Chem. 281:8613-8619(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 75-571 IN COMPLEX WITH UDP; PEPTIDE SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGALT2_HUMAN
    AccessioniPrimary (citable) accession number: Q10471
    Secondary accession number(s): A8K1Y3
    , B7Z8V8, C5HU00, Q9NPY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3