Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7Z7M9

- GALT5_HUMAN

UniProt

Q7Z7M9 - GALT5_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

GALNT5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei536 – 5361SubstrateBy similarity
    Binding sitei565 – 5651SubstrateBy similarity
    Metal bindingi588 – 5881ManganeseBy similarity
    Binding sitei589 – 5891SubstrateBy similarity
    Metal bindingi590 – 5901ManganeseBy similarity
    Binding sitei695 – 6951SubstrateBy similarity
    Metal bindingi723 – 7231ManganeseBy similarity
    Binding sitei726 – 7261SubstrateBy similarity
    Binding sitei731 – 7311SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. glycosaminoglycan biosynthetic process Source: UniProtKB
    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

    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 5 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 5
    Short name:
    GalNAc-T5
    Short name:
    pp-GaNTase 5
    Protein-UDP acetylgalactosaminyltransferase 5
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
    Gene namesi
    Name:GALNT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4127. GALNT5.

    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

    PharmGKBiPA28540.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 940940Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059110Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi486 ↔ 718PROSITE-ProRule annotation
    Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi709 ↔ 789PROSITE-ProRule annotation
    Glycosylationi776 – 7761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi822 ↔ 835PROSITE-ProRule annotation
    Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi845 – 8451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi858 ↔ 873PROSITE-ProRule annotation
    Disulfide bondi908 ↔ 923PROSITE-ProRule annotation
    Glycosylationi912 – 9121N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ7Z7M9.
    PaxDbiQ7Z7M9.
    PRIDEiQ7Z7M9.

    PTM databases

    PhosphoSiteiQ7Z7M9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7Z7M9.
    BgeeiQ7Z7M9.
    CleanExiHS_GALNT5.
    GenevestigatoriQ7Z7M9.

    Organism-specific databases

    HPAiHPA008963.
    HPA009035.

    Interactioni

    Subunit structurei

    Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3.1 Publication

    Protein-protein interaction databases

    BioGridi116394. 2 interactions.
    STRINGi9606.ENSP00000259056.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z7M9.
    SMRiQ7Z7M9. Positions 439-935.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 940905LumenalSequence 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
    Domaini804 – 935132Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni495 – 604110Catalytic subdomain AAdd
    BLAST
    Regioni664 – 72663Catalytic 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

    eggNOGiNOG307550.
    HOGENOMiHOG000231869.
    HOVERGENiHBG051698.
    InParanoidiQ7Z7M9.
    KOiK00710.
    OMAiSHVVIIT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ7Z7M9.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q7Z7M9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV    50
    RRERIGFRVQ PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK 100
    VEVDLDQTQR ERKMQNALGR GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK 150
    PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ VVKISVHMGR VSLKQEPRKS 200
    HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH PASTAVPKSG 250
    EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS 300
    LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV 350
    LGKSQSKHIS RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA 400
    PSTEYNQSHI KALLPEDSGT HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG 450
    KEKEAERRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNNLPTTSV 500
    IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK DYLKDNLDKY 550
    MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP 600
    LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP 650
    PDVIAKNRIK ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM 700
    ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE 750
    VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLENVF 800
    PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE LQQFNYTWLR 850
    LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF 900
    ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA 940
    Length:940
    Mass (Da):106,266
    Last modified:October 1, 2003 - v1
    Checksum:iDB2DFACDCACD0F6A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti273 – 2753NTS → AEG1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771P → L.
    Corresponds to variant rs3739112 [ dbSNP | Ensembl ].
    VAR_019578
    Natural varianti489 – 4891Q → H.
    Corresponds to variant rs6759356 [ dbSNP | Ensembl ].
    VAR_019579
    Natural varianti507 – 5071E → D in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035991
    Natural varianti692 – 6921L → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035992

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY277591 mRNA. Translation: AAP34404.1.
    AK292154 mRNA. Translation: BAF84843.1.
    CH471058 Genomic DNA. Translation: EAX11449.1.
    BC142676 mRNA. Translation: AAI42677.1.
    AJ245539 mRNA. Translation: CAB65104.1.
    AF154107 mRNA. Translation: AAF15313.1.
    CCDSiCCDS2203.1.
    RefSeqiNP_055383.1. NM_014568.1.
    UniGeneiHs.269027.

    Genome annotation databases

    EnsembliENST00000259056; ENSP00000259056; ENSG00000136542.
    GeneIDi11227.
    KEGGihsa:11227.
    UCSCiuc002tzg.3. human.

    Polymorphism databases

    DMDMi51315940.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 5

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY277591 mRNA. Translation: AAP34404.1 .
    AK292154 mRNA. Translation: BAF84843.1 .
    CH471058 Genomic DNA. Translation: EAX11449.1 .
    BC142676 mRNA. Translation: AAI42677.1 .
    AJ245539 mRNA. Translation: CAB65104.1 .
    AF154107 mRNA. Translation: AAF15313.1 .
    CCDSi CCDS2203.1.
    RefSeqi NP_055383.1. NM_014568.1.
    UniGenei Hs.269027.

    3D structure databases

    ProteinModelPortali Q7Z7M9.
    SMRi Q7Z7M9. Positions 439-935.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116394. 2 interactions.
    STRINGi 9606.ENSP00000259056.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q7Z7M9.

    Polymorphism databases

    DMDMi 51315940.

    Proteomic databases

    MaxQBi Q7Z7M9.
    PaxDbi Q7Z7M9.
    PRIDEi Q7Z7M9.

    Protocols and materials databases

    DNASUi 11227.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259056 ; ENSP00000259056 ; ENSG00000136542 .
    GeneIDi 11227.
    KEGGi hsa:11227.
    UCSCi uc002tzg.3. human.

    Organism-specific databases

    CTDi 11227.
    GeneCardsi GC02P158079.
    HGNCi HGNC:4127. GALNT5.
    HPAi HPA008963.
    HPA009035.
    neXtProti NX_Q7Z7M9.
    PharmGKBi PA28540.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307550.
    HOGENOMi HOG000231869.
    HOVERGENi HBG051698.
    InParanoidi Q7Z7M9.
    KOi K00710.
    OMAi SHVVIIT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q7Z7M9.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi GALNT5. human.
    GenomeRNAii 11227.
    NextBioi 42730.
    PROi Q7Z7M9.

    Gene expression databases

    ArrayExpressi Q7Z7M9.
    Bgeei Q7Z7M9.
    CleanExi HS_GALNT5.
    Genevestigatori Q7Z7M9.

    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. Huang C.Q., Wu S.L., Cheng Z.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Synovium.
    3. 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].
    5. Bennett E.P.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 273-940.
    6. "A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses."
      Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.
      Hum. Mol. Genet. 8:2155-2164(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-940, INTERACTION WITH EXT2.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-507 AND PHE-692.

    Entry informationi

    Entry nameiGALT5_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z7M9
    Secondary accession number(s): A5PKZ1, Q9UGK7, Q9UHL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 97 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

    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3