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Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

GALNT10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Muc5Ac and EA2 peptide substrates.

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei154Substrate1
Binding sitei156Substrate1
Binding sitei185Substrate1
Binding sitei214Substrate1
Metal bindingi237Manganese1
Binding sitei238Substrate1
Metal bindingi239Manganese1
Binding sitei342Substrate1
Metal bindingi370Manganese1
Binding sitei373Substrate1
Binding sitei378Substrate1

GO - Molecular functioni

GO - Biological processi

  • O-glycan processing Source: GO_Central
  • protein O-linked glycosylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS15213-MONOMER.
ReactomeiR-HSA-913709. 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 10 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name:
GalNAc-T10
Short name:
pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:GALNT10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:19873. GALNT10.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 31Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini32 – 603LumenalSequence analysisAdd BLAST572

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi55568.
OpenTargetsiENSG00000164574.
PharmGKBiPA134870832.

Polymorphism and mutation databases

BioMutaiGALNT10.
DMDMi51315962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591221 – 603Polypeptide N-acetylgalactosaminyltransferase 10Add BLAST603

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi124N-linked (GlcNAc...)1 Publication1
Disulfide bondi135 ↔ 365PROSITE-ProRule annotation1 Publication
Glycosylationi146N-linked (GlcNAc...)1 Publication1
Disulfide bondi356 ↔ 432PROSITE-ProRule annotation1 Publication
Disulfide bondi471 ↔ 488PROSITE-ProRule annotation1 Publication
Disulfide bondi523 ↔ 538PROSITE-ProRule annotation1 Publication
Disulfide bondi563 ↔ 578PROSITE-ProRule annotation1 Publication
Glycosylationi593N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ86SR1.
PaxDbiQ86SR1.
PeptideAtlasiQ86SR1.
PRIDEiQ86SR1.

PTM databases

iPTMnetiQ86SR1.
PhosphoSitePlusiQ86SR1.
SwissPalmiQ86SR1.

Expressioni

Tissue specificityi

Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.1 Publication

Gene expression databases

BgeeiENSG00000164574.
ExpressionAtlasiQ86SR1. baseline and differential.
GenevisibleiQ86SR1. HS.

Organism-specific databases

HPAiHPA007525.

Interactioni

Protein-protein interaction databases

BioGridi120723. 4 interactors.
IntActiQ86SR1. 1 interactor.
MINTiMINT-2808648.
STRINGi9606.ENSP00000297107.

Structurei

Secondary structure

1603
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi77 – 84Combined sources8
Helixi91 – 93Combined sources3
Turni100 – 103Combined sources4
Helixi106 – 109Combined sources4
Helixi115 – 119Combined sources5
Helixi133 – 136Combined sources4
Beta strandi140 – 143Combined sources4
Beta strandi147 – 155Combined sources9
Helixi158 – 171Combined sources14
Helixi174 – 176Combined sources3
Beta strandi177 – 184Combined sources8
Helixi190 – 192Combined sources3
Helixi194 – 200Combined sources7
Beta strandi206 – 210Combined sources5
Helixi217 – 227Combined sources11
Beta strandi230 – 235Combined sources6
Beta strandi238 – 242Combined sources5
Helixi248 – 256Combined sources9
Beta strandi260 – 269Combined sources10
Turni271 – 273Combined sources3
Beta strandi285 – 288Combined sources4
Beta strandi294 – 297Combined sources4
Turni301 – 303Combined sources3
Beta strandi319 – 325Combined sources7
Helixi326 – 331Combined sources6
Beta strandi341 – 344Combined sources4
Helixi345 – 355Combined sources11
Beta strandi359 – 370Combined sources12
Helixi386 – 397Combined sources12
Helixi399 – 401Combined sources3
Helixi402 – 406Combined sources5
Helixi410 – 412Combined sources3
Helixi421 – 430Combined sources10
Helixi435 – 441Combined sources7
Helixi446 – 449Combined sources4
Beta strandi458 – 465Combined sources8
Turni466 – 468Combined sources3
Turni478 – 480Combined sources3
Helixi495 – 497Combined sources3
Beta strandi503 – 505Combined sources3
Turni507 – 509Combined sources3
Beta strandi511 – 514Combined sources4
Beta strandi521 – 525Combined sources5
Beta strandi528 – 532Combined sources5
Beta strandi534 – 537Combined sources4
Beta strandi540 – 543Combined sources4
Beta strandi548 – 550Combined sources3
Turni551 – 553Combined sources3
Beta strandi554 – 556Combined sources3
Turni558 – 560Combined sources3
Beta strandi563 – 566Combined sources4
Turni568 – 570Combined sources3
Beta strandi573 – 576Combined sources4
Beta strandi587 – 591Combined sources5
Helixi594 – 597Combined sources4
Turni598 – 601Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D7IX-ray2.50A40-603[»]
2D7RX-ray2.80A40-603[»]
ProteinModelPortaliQ86SR1.
SMRiQ86SR1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86SR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini458 – 590Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST133

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 253Catalytic subdomain AAdd BLAST110
Regioni311 – 373Catalytic subdomain BAdd BLAST63
Regioni373 – 384Flexible loopAdd BLAST12

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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ86SR1.
KOiK00710.
OMAiQKKTFFL.
OrthoDBiEOG091G085O.
PhylomeDBiQ86SR1.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86SR1-1) [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

        10         20         30         40         50
MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA
60 70 80 90 100
AGQGSHSRQK KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD
110 120 130 140 150
AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKRY LETLPNTSII
160 170 180 190 200
IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM
210 220 230 240 250
ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC EANVNWLPPL
260 270 280 290 300
LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
310 320 330 340 350
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS
360 370 380 390 400
FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE
410 420 430 440 450
YAEYIYQRRP EYRHLSAGDV AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY
460 470 480 490 500
PPVEPPAAAW GEIRNVGTGL CADTKHGALG SPLRLEGCVR GRGEAAWNNM
510 520 530 540 550
QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS MKGNQLWKYR
560 570 580 590 600
KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF

NRN
Length:603
Mass (Da):68,992
Last modified:August 16, 2004 - v2
Checksum:iEE176F6139B92573
GO
Isoform 2 (identifier: Q86SR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-251: Missing.

Note: No experimental confirmation available.
Show »
Length:541
Mass (Da):61,947
Checksum:i4216612D314EA82B
GO
Isoform 3 (identifier: Q86SR1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     354-366: WMCGGRMEDIPCS → SQLSRRPVLGTAS
     367-603: Missing.

Note: No experimental confirmation available.
Show »
Length:366
Mass (Da):41,452
Checksum:i52AB23ABC6F797FE
GO
Isoform 4 (identifier: Q86SR1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-329: Missing.
     330-352: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ
     389-389: N → VRT

Note: No experimental confirmation available.
Show »
Length:276
Mass (Da):31,833
Checksum:iF357AFF828E57DC7
GO

Sequence cautioni

The sequence BAB14676 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti518H → Y in BAC56890 (PubMed:12417297).Curated1
Sequence conflicti518H → Y in BAB14676 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0112071 – 329Missing in isoform 4. 1 PublicationAdd BLAST329
Alternative sequenceiVSP_011209190 – 251Missing in isoform 2. 1 PublicationAdd BLAST62
Alternative sequenceiVSP_011208330 – 352WELGG…EISFK → MLAWRDGELEAETSSSLFLL AMQ in isoform 4. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_011212354 – 366WMCGG…DIPCS → SQLSRRPVLGTAS in isoform 3. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_011213367 – 603Missing in isoform 3. 1 PublicationAdd BLAST237
Alternative sequenceiVSP_011214389N → VRT in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078145 mRNA. Translation: BAC56890.1.
AJ505950 mRNA. Translation: CAD44532.1.
AK023782 mRNA. Translation: BAB14676.1. Different initiation.
AK127135 mRNA. Translation: BAG54441.1.
AL096739 mRNA. Translation: CAB46378.1.
AK074132 mRNA. Translation: BAB84958.1.
BC007224 mRNA. Translation: AAH07224.2.
BC072450 mRNA. Translation: AAH72450.1.
CCDSiCCDS4325.1. [Q86SR1-1]
PIRiT12552.
RefSeqiNP_938080.1. NM_198321.3. [Q86SR1-1]
UniGeneiHs.631797.

Genome annotation databases

EnsembliENST00000297107; ENSP00000297107; ENSG00000164574. [Q86SR1-1]
ENST00000377661; ENSP00000366889; ENSG00000164574. [Q86SR1-2]
ENST00000425427; ENSP00000415210; ENSG00000164574. [Q86SR1-3]
GeneIDi55568.
KEGGihsa:55568.
UCSCiuc003lvg.2. human. [Q86SR1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB078145 mRNA. Translation: BAC56890.1.
AJ505950 mRNA. Translation: CAD44532.1.
AK023782 mRNA. Translation: BAB14676.1. Different initiation.
AK127135 mRNA. Translation: BAG54441.1.
AL096739 mRNA. Translation: CAB46378.1.
AK074132 mRNA. Translation: BAB84958.1.
BC007224 mRNA. Translation: AAH07224.2.
BC072450 mRNA. Translation: AAH72450.1.
CCDSiCCDS4325.1. [Q86SR1-1]
PIRiT12552.
RefSeqiNP_938080.1. NM_198321.3. [Q86SR1-1]
UniGeneiHs.631797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D7IX-ray2.50A40-603[»]
2D7RX-ray2.80A40-603[»]
ProteinModelPortaliQ86SR1.
SMRiQ86SR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120723. 4 interactors.
IntActiQ86SR1. 1 interactor.
MINTiMINT-2808648.
STRINGi9606.ENSP00000297107.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

iPTMnetiQ86SR1.
PhosphoSitePlusiQ86SR1.
SwissPalmiQ86SR1.

Polymorphism and mutation databases

BioMutaiGALNT10.
DMDMi51315962.

Proteomic databases

MaxQBiQ86SR1.
PaxDbiQ86SR1.
PeptideAtlasiQ86SR1.
PRIDEiQ86SR1.

Protocols and materials databases

DNASUi55568.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297107; ENSP00000297107; ENSG00000164574. [Q86SR1-1]
ENST00000377661; ENSP00000366889; ENSG00000164574. [Q86SR1-2]
ENST00000425427; ENSP00000415210; ENSG00000164574. [Q86SR1-3]
GeneIDi55568.
KEGGihsa:55568.
UCSCiuc003lvg.2. human. [Q86SR1-1]

Organism-specific databases

CTDi55568.
DisGeNETi55568.
GeneCardsiGALNT10.
HGNCiHGNC:19873. GALNT10.
HPAiHPA007525.
MIMi608043. gene.
neXtProtiNX_Q86SR1.
OpenTargetsiENSG00000164574.
PharmGKBiPA134870832.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ86SR1.
KOiK00710.
OMAiQKKTFFL.
OrthoDBiEOG091G085O.
PhylomeDBiQ86SR1.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciZFISH:HS15213-MONOMER.
ReactomeiR-HSA-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGALNT10. human.
EvolutionaryTraceiQ86SR1.
GenomeRNAii55568.
PROiQ86SR1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164574.
ExpressionAtlasiQ86SR1. baseline and differential.
GenevisibleiQ86SR1. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiGLT10_HUMAN
AccessioniPrimary (citable) accession number: Q86SR1
Secondary accession number(s): B3KXC9
, Q6IN56, Q86VP8, Q8IXJ2, Q8TEJ2, Q96IV2, Q9H8E1, Q9Y4M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 2, 2016
This is version 133 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

Caution

According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.