Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

GALNT11

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

Functioni

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO).2 Publications

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 sitei191SubstrateBy similarity1
Binding sitei222SubstrateBy similarity1
Metal bindingi245ManganeseBy similarity1
Binding sitei246SubstrateBy similarity1
Metal bindingi247ManganeseBy similarity1
Binding sitei350SubstrateBy similarity1
Metal bindingi378ManganeseBy similarity1
Binding sitei381SubstrateBy similarity1
Binding sitei386SubstrateBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • Notch binding Source: UniProtKB
  • polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Notch signaling pathway

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS17020-MONOMER.
BRENDAi2.4.1.41. 2681.
ReactomeiR-HSA-913709. O-linked glycosylation of mucins.
SABIO-RKQ8NCW6.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 11 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name:
GalNAc-T11
Short name:
pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene namesi
Name:GALNT11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:19875. GALNT11.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 608LumenalSequence analysisAdd BLAST579

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in GALNT11 may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi247H → A: Abolishes glycosyltransferase activity and ability to rescue left-right patterning defects induced by galnt11 knockdown in X.tropicalis. 1 Publication1

Keywords - Diseasei

Heterotaxy

Organism-specific databases

DisGeNETi63917.
OpenTargetsiENSG00000178234.
PharmGKBiPA134911149.

Polymorphism and mutation databases

BioMutaiGALNT11.
DMDMi51316030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591251 – 608Polypeptide N-acetylgalactosaminyltransferase 11Add BLAST608

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphoserineBy similarity1
Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
Glycosylationi428N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi493 ↔ 512PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi578 ↔ 596PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8NCW6.
PaxDbiQ8NCW6.
PeptideAtlasiQ8NCW6.
PRIDEiQ8NCW6.

PTM databases

iPTMnetiQ8NCW6.
PhosphoSitePlusiQ8NCW6.

Expressioni

Tissue specificityi

Highly expressed in kidney. Expressed at intermediate level in brain, heart and skeletal muscle. Weakly expressed other tissues. In kidney, it is strongly expressed in tubules but not expressed in glomeruli.1 Publication

Gene expression databases

BgeeiENSG00000178234.
CleanExiHS_GALNT11.
ExpressionAtlasiQ8NCW6. baseline and differential.
GenevisibleiQ8NCW6. HS.

Organism-specific databases

HPAiHPA039330.

Interactioni

Subunit structurei

Interacts with NOTCH1.1 Publication

GO - Molecular functioni

  • Notch binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121988. 14 interactors.
STRINGi9606.ENSP00000315835.

Structurei

3D structure databases

ProteinModelPortaliQ8NCW6.
SMRiQ8NCW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini476 – 607Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 261Catalytic subdomain AAdd BLAST112
Regioni319 – 381Catalytic subdomain BAdd BLAST63

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.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8NCW6.
KOiK00710.
OMAiMIFNERD.
OrthoDBiEOG091G085O.
PhylomeDBiQ8NCW6.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NCW6-1) [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
MGSVTVRYFC YGCLFTSATW TVLLFVYFNF SEVTQPLKNV PVKGSGPHGP
60 70 80 90 100
SPKKFYPRFT RGPSRVLEPQ FKANKIDDVI DSRVEDPEEG HLKFSSELGM
110 120 130 140 150
IFNERDQELR DLGYQKHAFN MLISDRLGYH RDVPDTRNAA CKEKFYPPDL
160 170 180 190 200
PAASVVICFY NEAFSALLRT VHSVIDRTPA HLLHEIILVD DDSDFDDLKG
210 220 230 240 250
ELDEYVQKYL PGKIKVIRNT KREGLIRGRM IGAAHATGEV LVFLDSHCEV
260 270 280 290 300
NVMWLQPLLA AIREDRHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
310 320 330 340 350
KWDLVPLSEL GRAEGATAPI KSPTMAGGLF AMNRQYFHEL GQYDSGMDIW
360 370 380 390 400
GGENLEISFR IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL
410 420 430 440 450
RLAHVWLDEY KEQYFSLRPD LKTKSYGNIS ERVELRKKLG CKSFKWYLDN
460 470 480 490 500
VYPEMQISGS HAKPQQPIFV NRGPKRPKVL QRGRLYHLQT NKCLVAQGRP
510 520 530 540 550
SQKGGLVVLK ACDYSDPNQI WIYNEEHELV LNSLLCLDMS ETRSSDPPRL
560 570 580 590 600
MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR AVDPLGQKGS VAMAICDGSS

SQQWHLEG
Length:608
Mass (Da):68,919
Last modified:August 16, 2004 - v2
Checksum:i075D7B839A8D5607
GO
Isoform 2 (identifier: Q8NCW6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     196-202: DDLKGEL → GKECCTW
     203-608: Missing.

Note: No experimental confirmation available.
Show »
Length:202
Mass (Da):23,090
Checksum:iA2B98F18AB31C370
GO

Sequence cautioni

The sequence BAB15338 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94F → L in BAG54116 (PubMed:14702039).Curated1
Sequence conflicti551M → V in BAB15105 (PubMed:14702039).Curated1
Sequence conflicti577Q → L in BAB15105 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019589151P → S.Corresponds to variant rs6464201dbSNPEnsembl.1
Natural variantiVAR_019590197D → Y.1 PublicationCorresponds to variant rs3778922dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011215196 – 202DDLKGEL → GKECCTW in isoform 2. 1 Publication7
Alternative sequenceiVSP_011216203 – 608Missing in isoform 2. 1 PublicationAdd BLAST406

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12434 mRNA. Translation: CAC79625.3.
AK025287 mRNA. Translation: BAB15105.1.
AK026056 mRNA. Translation: BAB15338.1. Different initiation.
AK124934 mRNA. Translation: BAG54116.1.
AC006017 Genomic DNA. Translation: AAD45821.1.
BC059377 mRNA. Translation: AAH59377.1.
CCDSiCCDS5930.1. [Q8NCW6-1]
RefSeqiNP_071370.2. NM_022087.3. [Q8NCW6-1]
XP_006716145.1. XM_006716082.2. [Q8NCW6-1]
XP_006716146.1. XM_006716083.2. [Q8NCW6-1]
XP_006716147.1. XM_006716084.2. [Q8NCW6-1]
XP_016867989.1. XM_017012500.1.
UniGeneiHs.647109.

Genome annotation databases

EnsembliENST00000415421; ENSP00000410093; ENSG00000178234. [Q8NCW6-2]
ENST00000422997; ENSP00000389449; ENSG00000178234. [Q8NCW6-2]
ENST00000430044; ENSP00000395122; ENSG00000178234. [Q8NCW6-1]
ENST00000434507; ENSP00000416787; ENSG00000178234. [Q8NCW6-1]
GeneIDi63917.
KEGGihsa:63917.
UCSCiuc003wku.3. human. [Q8NCW6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12434 mRNA. Translation: CAC79625.3.
AK025287 mRNA. Translation: BAB15105.1.
AK026056 mRNA. Translation: BAB15338.1. Different initiation.
AK124934 mRNA. Translation: BAG54116.1.
AC006017 Genomic DNA. Translation: AAD45821.1.
BC059377 mRNA. Translation: AAH59377.1.
CCDSiCCDS5930.1. [Q8NCW6-1]
RefSeqiNP_071370.2. NM_022087.3. [Q8NCW6-1]
XP_006716145.1. XM_006716082.2. [Q8NCW6-1]
XP_006716146.1. XM_006716083.2. [Q8NCW6-1]
XP_006716147.1. XM_006716084.2. [Q8NCW6-1]
XP_016867989.1. XM_017012500.1.
UniGeneiHs.647109.

3D structure databases

ProteinModelPortaliQ8NCW6.
SMRiQ8NCW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121988. 14 interactors.
STRINGi9606.ENSP00000315835.

Protein family/group databases

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

PTM databases

iPTMnetiQ8NCW6.
PhosphoSitePlusiQ8NCW6.

Polymorphism and mutation databases

BioMutaiGALNT11.
DMDMi51316030.

Proteomic databases

MaxQBiQ8NCW6.
PaxDbiQ8NCW6.
PeptideAtlasiQ8NCW6.
PRIDEiQ8NCW6.

Protocols and materials databases

DNASUi63917.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000415421; ENSP00000410093; ENSG00000178234. [Q8NCW6-2]
ENST00000422997; ENSP00000389449; ENSG00000178234. [Q8NCW6-2]
ENST00000430044; ENSP00000395122; ENSG00000178234. [Q8NCW6-1]
ENST00000434507; ENSP00000416787; ENSG00000178234. [Q8NCW6-1]
GeneIDi63917.
KEGGihsa:63917.
UCSCiuc003wku.3. human. [Q8NCW6-1]

Organism-specific databases

CTDi63917.
DisGeNETi63917.
GeneCardsiGALNT11.
H-InvDBHIX0007236.
HGNCiHGNC:19875. GALNT11.
HPAiHPA039330.
MIMi615130. gene.
neXtProtiNX_Q8NCW6.
OpenTargetsiENSG00000178234.
PharmGKBiPA134911149.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8NCW6.
KOiK00710.
OMAiMIFNERD.
OrthoDBiEOG091G085O.
PhylomeDBiQ8NCW6.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciZFISH:HS17020-MONOMER.
BRENDAi2.4.1.41. 2681.
ReactomeiR-HSA-913709. O-linked glycosylation of mucins.
SABIO-RKQ8NCW6.

Miscellaneous databases

ChiTaRSiGALNT11. human.
GenomeRNAii63917.
PROiQ8NCW6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000178234.
CleanExiHS_GALNT11.
ExpressionAtlasiQ8NCW6. baseline and differential.
GenevisibleiQ8NCW6. 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 nameiGLT11_HUMAN
AccessioniPrimary (citable) accession number: Q8NCW6
Secondary accession number(s): B3KWF4
, Q6PCD1, Q9H6C2, Q9H6Z5, Q9UDR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 2, 2016
This is version 126 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 7
    Human chromosome 7: 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

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.