Protein detail

GLT10

Polypeptide N-acetylgalactosaminyltransferase 10 (EC 2.4.1.41) (Polypeptide GalNAc transferase 10) (GalNAc-T10) (pp-GaNTase 10) (Protein-UDP acetylgalactosaminyltransferase 10) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10)

Protein symbol
GLT10
UniProt ID
Q86SR1
EVMP score
0.50
Frequency
2
Transmembrane count
1
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Polypeptide N-acetylgalactosaminyltransferase 10 (EC 2.4.1.41) (Polypeptide GalNAc transferase 10) (GalNAc-T10) (pp-GaNTase 10) (Protein-UDP acetylgalactosaminyltransferase 10) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10)
Protein Class
EnzymesMetabolic proteinsPredicted intracellular proteins
Protein Function
  • ENZYME proteins:Transferases
  • Enzymes
  • Predicted intracellular proteins
Transmembrane
12..31; Helical; Signal-anchor for type II membrane protein
Transmembrane Count
1
Ensembl
ENSG00000164574
Entrez Gene Symbol
GALNT10
Gene Synonym
GalNAc-T10
Gene Description
Polypeptide N-acetylgalactosaminyltransferase 10
Chromosome
5
Position
154190730-154420984
Frequency
2
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
  • ENZYME proteins:Transferases
  • Enzymes
  • Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
KEGG
Reactome
Mediation Categories
Metabolism mediation
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

11 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneOmniPathNoNoNoNoNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationWestern blottingFlow cytometryMORPH23303581438321535
Sequence, Structure & Domains

Sequences

Length
603
Mass
68,992
Sequence
MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKFNRN
Alternative Products
Event=Alternative splicing; Named isoforms=4; Name=1; IsoId=Q86SR1-1; Sequence=Displayed; Name=2; IsoId=Q86SR1-2; Sequence=VSP_011209; Name=3; IsoId=Q86SR1-3; Sequence=VSP_011212, VSP_011213; Name=4; IsoId=Q86SR1-4; Sequence=VSP_011207, VSP_011208, VSP_011214
Alternative Sequence
1..329; Missing (in isoform 4); 190..251; Missing (in isoform 2); 330..352; WELGGYDPGLEIWGGEQYEISFK -> MLAWRDGELEAETSSSLFLLAMQ (in isoform 4); 354..366; WMCGGRMEDIPCS -> SQLSRRPVLGTAS (in isoform 3); 367..603; Missing (in isoform 3); 389; N -> VRT (in isoform 4)

3D Structural Models

Turn
100..103; 271..273; 301..303; 466..468; 478..480; 507..509; 551..553; 558..560; 568..570; 598..601
Helix
77..84; 91..93; 106..109; 115..119; 133..136; 158..171; 174..176; 190..192; 194..200; 217..227; 248..256; 326..331; 345..355; 386..397; 399..401; 402..406; 410..412; 421..430; 435..441; 446..449; 495..497; 594..597
Beta Strand
140..143; 147..155; 177..184; 206..210; 230..235; 238..242; 260..269; 285..288; 294..297; 319..325; 341..344; 359..370; 458..465; 503..505; 511..514; 521..525; 528..532; 534..537; 540..543; 548..550; 554..556; 563..566; 573..576; 587..591
3D Structure
X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
45..55; Low complexity
Domain (CC)
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.; DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Domain (FT)
458..590; Ricin B-type lectin
Region
38..59; Disordered; 144..253; Catalytic subdomain A; 311..373; Catalytic subdomain B; 373..384; Flexible loop
Protein Families
  • Glycosyltransferase 2 family
  • GalNAc-T subfamily
Sequence Similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Clinical Relevance
Antibody
HPA007525