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Q8N4A0

- GALT4_HUMAN

UniProt

Q8N4A0 - GALT4_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 4

Gene

GALNT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (28 Jun 2011)
      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 highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.

    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 sitei175 – 1751SubstrateBy similarity
    Binding sitei204 – 2041SubstrateBy similarity
    Metal bindingi227 – 2271ManganeseBy similarity
    Metal bindingi229 – 2291ManganeseBy similarity
    Binding sitei334 – 3341SubstrateBy similarity
    Metal bindingi362 – 3621ManganeseBy similarity
    Binding sitei370 – 3701SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. O-glycan processing Source: Reactome
    4. post-translational protein modification Source: Reactome

    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 4 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 4
    Short name:
    GalNAc-T4
    Short name:
    pp-GaNTase 4
    Protein-UDP acetylgalactosaminyltransferase 4
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
    Gene namesi
    Name:GALNT4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4126. GALNT4.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi apparatus Source: ProtInc
    3. Golgi membrane Source: Reactome
    4. integral component of membrane Source: UniProtKB-KW
    5. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi459 – 4591D → H: Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC. 1 Publication

    Organism-specific databases

    PharmGKBiPA28539.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 578578Polypeptide N-acetylgalactosaminyltransferase 4PRO_0000059108Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi124 ↔ 357PROSITE-ProRule annotation
    Disulfide bondi348 ↔ 421PROSITE-ProRule annotation
    Disulfide bondi457 ↔ 477PROSITE-ProRule annotation
    Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi503 ↔ 518PROSITE-ProRule annotation
    Disulfide bondi547 ↔ 565PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8N4A0.
    PeptideAtlasiQ8N4A0.
    PRIDEiQ8N4A0.

    PTM databases

    PhosphoSiteiQ8N4A0.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in mucous cells.1 Publication

    Gene expression databases

    CleanExiHS_GALNT4.
    GenevestigatoriQ8N4A0.

    Interactioni

    Protein-protein interaction databases

    BioGridi114240. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N4A0.
    SMRiQ8N4A0. Positions 103-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 578543LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini444 – 577134Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 243110Catalytic subdomain AAdd
    BLAST
    Regioni303 – 36563Catalytic 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 directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG051699.
    KOiK00710.
    OMAiINAYEET.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8N4A0.
    TreeFamiTF352660.

    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N4A0-1) [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

    MAVRWTWAGK SCLLLAFLTV AYIFVELLVS TFHASAGAGR ARELGSRRLS    50
    DLQKNTEDLS RPLYKKPPAD SRALGEWGKA SKLQLNEDEL KQQEELIERY 100
    AINIYLSDRI SLHRHIEDKR MYECKSQKFN YRTLPTTSVI IAFYNEAWST 150
    LLRTIHSVLE TSPAVLLKEI ILVDDLSDRV YLKTQLETYI SNLDRVRLIR 200
    TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNSGWLEPL LERIGRDETA 250
    VVCPVIDTID WNTFEFYMQI GEPMIGGFDW RLTFQWHSVP KQERDRRISR 300
    IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG 350
    KLEIHPCSHV GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP 400
    ARKEAYGDIS ERKLLRERLR CKSFDWYLKN VFPNLHVPED RPGWHGAIRS 450
    RGISSECLDY NSPDNNPTGA NLSLFGCHGQ GGNQFFEYTS NKEIRFNSVT 500
    ELCAEVPEQK NYVGMQNCPK DGFPVPANII WHFKEDGTIF HPHSGLCLSA 550
    YRTPEGRPDV QMRTCDALDK NQIWSFEK 578
    Length:578
    Mass (Da):66,666
    Last modified:June 28, 2011 - v2
    Checksum:i6EEEF502A40CBD2E
    GO
    Isoform 2 (identifier: Q8N4A0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-120: MAVRWTWAGK...SLHRHIEDKR → MAWCVATADP...WTSAPTASNL
         121-292: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:406
    Mass (Da):45,702
    Checksum:iEB89E46BF360847D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111S → T in CAA69875. (PubMed:9804815)Curated
    Sequence conflicti227 – 2271D → Y in CAA69875. (PubMed:9804815)Curated
    Sequence conflicti247 – 2471D → Y in CAA69875. (PubMed:9804815)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511D → G.1 Publication
    Corresponds to variant rs17853610 [ dbSNP | Ensembl ].
    VAR_065257
    Natural varianti270 – 2701I → T.1 Publication
    Corresponds to variant rs2230281 [ dbSNP | Ensembl ].
    VAR_019576
    Natural varianti506 – 5061V → I.2 Publications
    Corresponds to variant rs2230283 [ dbSNP | Ensembl ].
    VAR_019577

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 120120MAVRW…IEDKR → MAWCVATADPAHTSRPLFTG LAVSRGSAGHAWSAGFDWAA VVVVTGRRCRSGQTVPGAAR SPLLPHPLPSPLRVPPPTGA LGRPLPRWPQPRRTPFWSVI SKATKLRSPPWTSAPTASNL in isoform 2. 1 PublicationVSP_045009Add
    BLAST
    Alternative sequencei121 – 292172Missing in isoform 2. 1 PublicationVSP_045010Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08564 Genomic DNA. Translation: CAA69875.1.
    AK297677 mRNA. Translation: BAG60038.1.
    AK312870 mRNA. Translation: BAG35722.1.
    AC010201 Genomic DNA. No translation available.
    AC025034 Genomic DNA. No translation available.
    BC036390 mRNA. Translation: AAH36390.1.
    CCDSiCCDS53817.1. [Q8N4A0-1]
    RefSeqiNP_001186711.1. NM_001199782.1. [Q8N4A0-2]
    NP_003765.2. NM_003774.4. [Q8N4A0-1]
    UniGeneiHs.25130.

    Genome annotation databases

    EnsembliENST00000529983; ENSP00000436604; ENSG00000257594. [Q8N4A0-1]
    GeneIDi100528030.
    8693.
    KEGGihsa:100528030.
    hsa:8693.
    UCSCiuc001tbd.3. human. [Q8N4A0-1]
    uc010suo.2. human.

    Polymorphism databases

    DMDMi338817878.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 4

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08564 Genomic DNA. Translation: CAA69875.1 .
    AK297677 mRNA. Translation: BAG60038.1 .
    AK312870 mRNA. Translation: BAG35722.1 .
    AC010201 Genomic DNA. No translation available.
    AC025034 Genomic DNA. No translation available.
    BC036390 mRNA. Translation: AAH36390.1 .
    CCDSi CCDS53817.1. [Q8N4A0-1 ]
    RefSeqi NP_001186711.1. NM_001199782.1. [Q8N4A0-2 ]
    NP_003765.2. NM_003774.4. [Q8N4A0-1 ]
    UniGenei Hs.25130.

    3D structure databases

    ProteinModelPortali Q8N4A0.
    SMRi Q8N4A0. Positions 103-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114240. 2 interactions.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8N4A0.

    Polymorphism databases

    DMDMi 338817878.

    Proteomic databases

    MaxQBi Q8N4A0.
    PeptideAtlasi Q8N4A0.
    PRIDEi Q8N4A0.

    Protocols and materials databases

    DNASUi 8693.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000529983 ; ENSP00000436604 ; ENSG00000257594 . [Q8N4A0-1 ]
    GeneIDi 100528030.
    8693.
    KEGGi hsa:100528030.
    hsa:8693.
    UCSCi uc001tbd.3. human. [Q8N4A0-1 ]
    uc010suo.2. human.

    Organism-specific databases

    CTDi 100528030.
    8693.
    GeneCardsi GC12M089913.
    HGNCi HGNC:4126. GALNT4.
    MIMi 603565. gene.
    neXtProti NX_Q8N4A0.
    PharmGKBi PA28539.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG051699.
    KOi K00710.
    OMAi INAYEET.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8N4A0.
    TreeFami TF352660.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 32603.
    PROi Q8N4A0.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_GALNT4.
    Genevestigatori Q8N4A0.

    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 of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat."
      Bennett E.P., Hassan H., Mandel U., Mirgorodskaya E., Roepstorff P., Burchell J., Taylor-Papadimitriou J., Hollingsworth M.A., Merkx G., van Kessel A.G., Eiberg H., Steffensen R., Clausen H.
      J. Biol. Chem. 273:30472-30481(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ILE-506.
    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), VARIANTS THR-270 AND ILE-506.
      Tissue: Kidney and Trachea.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANT GLY-51.
      Tissue: Brain.
    5. "The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities."
      Hassan H., Reis C.A., Bennett E.P., Mirgorodskaya E., Roepstorff P., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
      J. Biol. Chem. 275:38197-38205(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF ASP-459.

    Entry informationi

    Entry nameiGALT4_HUMAN
    AccessioniPrimary (citable) accession number: Q8N4A0
    Secondary accession number(s): B2R775, B4DMX6, O00208
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 103 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 12
      Human chromosome 12: 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