Chondroitin sulfate N-acetylgalactosaminyltransferase 2

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• 3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-seryl-[protein]

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  + UDP-N-acetyl-α-D-galactosamine

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  = 3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-seryl-[protein]

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  + H⁺

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  + UDP

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  EC:2.4.1.174
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  Source: Rhea

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  3-O-(β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-seryl-[protein]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  3-O-(β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine residue

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  zoom

  +

  UDP-N-acetyl-α-D-galactosamine

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  zoom

  =

  3-O-(β-D-GalNAc-(1→4)-β-D-GlcA-(1→3)-β-D-Gal-(1→3)-β-D-Gal-(1→4)-β-D-Xyl)-L-seryl-[protein]

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  

  O³-(N-acetyl-β-D-galactosaminyl-(1→4)-β-D-glucuronosyl-(1→3)-β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine residue

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  H⁺

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  • See the description of this molecule in ChEBI.

  

  +

  UDP

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Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• acetylgalactosaminyltransferase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]
• glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
• metal ion binding Source: UniProtKB-KW

GO - Biological processⁱ

• chondroitin sulfate biosynthetic process Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• chondroitin sulfate proteoglycan biosynthetic process Source: UniProtKBInferred from direct assayⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]
• chondroitin sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]
• dermatan sulfate proteoglycan biosynthetic process Source: UniProtKBInferred from direct assayⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]
• dermatan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Source: UniProtKBTraceable author statementⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]
• proteoglycan biosynthetic process Source: UniProtKBInferred from direct assayⁱ
  • "Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase: key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate."
    Uyama T., Kitagawa H., Tamura J., Sugahara K.
    J. Biol. Chem. 277:8841-8846(2002) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Topology

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Coiled coil

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MPRRGLILHT RTHWLLLGLA LLCSLVLFMY LLECAPQTDG NASLPGVVGE 
        60         70         80         90        100
NYGKEYYQAL LQEQEEHYQT RATSLKRQIA QLKQELQEMS EKMRSLQERR 
       110        120        130        140        150
NVGANGIGYQ SNKEQAPSDL LEFLHSQIDK AEVSIGAKLP SEYGVIPFES 
       160        170        180        190        200
FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL VEVIEAGLEV INNPDEDDEQ 
       210        220        230        240        250
EDEEGPLGEK LIFNENDFVE GYYRTERDKG TQYELFFKKA DLTEYRHVTL 
       260        270        280        290        300
FRPFGPLMKV KSEMIDITRS IINIIVPLAE RTEAFVQFMQ NFRDVCIHQD 
       310        320        330        340        350
KKIHLTVVYF GKEGLSKVKS ILESVTSESN FHNYTLVSLN EEFNRGRGLN 
       360        370        380        390        400
VGARAWDKGE VLMFFCDVDI YFSAEFLNSC RLNAEPGKKV FYPVVFSLYN 
       410        420        430        440        450
PAIVYANQEV PPPVEQQLVH KKDSGFWRDF GFGMTCQYRS DFLTIGGFDM 
       460        470        480        490        500
EVKGWGGEDV HLYRKYLHGD LIVIRTPVPG LFHLWHEKRC ADELTPEQYR 
       510        520        530        540 
MCIQSKAMNE ASHSHLGMLV FREEIETHLH KQAYRTNSEA VG         

        10         20         30         40         50
MPRRGLILHT RTHWLLLGLA LLCSLVLFMY LLECAPQTDG NASLPGVVGE 
        60         70         80         90        100
NYGKEYYQAL LQEQEEHYQT RATSLKRQIA QLKQELQEMS EKMRSLQERR 
       110        120        130        140        150
NVGANGIGYQ SNKEQAPSDL LEFLHSQIDK AEVSIGAKLP SEYGVIPFES 
       160        170        180        190        200
FTLMKVFQLE MGLTRHPEEK PVRKDKRDEL VEVIEAGLEV INNPDEDDEQ 
       210        220        230        240        250
EDEEGPLGEK LIFNENDFVE GYYRTERDKG TQYELFFKKA DLTEYRHVTL 
       260        270        280        290        300
FRPFGPLMKV KSEMIDITRS IINIIVPLAE RTEAFVQFMQ NFRDVCIHQD 
       310        320        330 
KKIHLTVVYF GKEGLSKVKS ILESVTRLAS STW                   

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 10
   Human chromosome 10: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. SIMILARITY comments
   Index of protein domains and families