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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

GALNT5

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 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

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 sitei536SubstrateBy similarity1
Binding sitei565SubstrateBy similarity1
Metal bindingi588ManganeseBy similarity1
Binding sitei589SubstrateBy similarity1
Metal bindingi590ManganeseBy similarity1
Binding sitei695SubstrateBy similarity1
Metal bindingi723ManganeseBy similarity1
Binding sitei726SubstrateBy similarity1
Binding sitei731SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • glycosaminoglycan biosynthetic process Source: UniProtKB
  • O-glycan processing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS06180-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 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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4127. GALNT5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini36 – 940LumenalSequence analysisAdd BLAST905

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi11227.
OpenTargetsiENSG00000136542.
PharmGKBiPA28540.

Polymorphism and mutation databases

BioMutaiGALNT5.
DMDMi51315940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591101 – 940Polypeptide N-acetylgalactosaminyltransferase 5Add BLAST940

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi217N-linked (GlcNAc...)Sequence analysis1
Glycosylationi256N-linked (GlcNAc...)Sequence analysis1
Glycosylationi273N-linked (GlcNAc...)Sequence analysis1
Modified residuei292PhosphoserineCombined sources1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi486 ↔ 718PROSITE-ProRule annotation
Glycosylationi578N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi709 ↔ 789PROSITE-ProRule annotation
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi822 ↔ 835PROSITE-ProRule annotation
Glycosylationi827N-linked (GlcNAc...)Sequence analysis1
Glycosylationi845N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi858 ↔ 873PROSITE-ProRule annotation
Disulfide bondi908 ↔ 923PROSITE-ProRule annotation
Glycosylationi912N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ7Z7M9.
PaxDbiQ7Z7M9.
PeptideAtlasiQ7Z7M9.
PRIDEiQ7Z7M9.

PTM databases

iPTMnetiQ7Z7M9.
PhosphoSitePlusiQ7Z7M9.

Expressioni

Gene expression databases

BgeeiENSG00000136542.
CleanExiHS_GALNT5.
GenevisibleiQ7Z7M9. HS.

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 interactors.
IntActiQ7Z7M9. 4 interactors.
STRINGi9606.ENSP00000259056.

Structurei

3D structure databases

ProteinModelPortaliQ7Z7M9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini804 – 935Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni495 – 604Catalytic subdomain AAdd BLAST110
Regioni664 – 726Catalytic 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.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiQ7Z7M9.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG091G085O.
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

        10         20         30         40         50
MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV
60 70 80 90 100
RRERIGFRVQ PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK
110 120 130 140 150
VEVDLDQTQR ERKMQNALGR GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK
160 170 180 190 200
PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ VVKISVHMGR VSLKQEPRKS
210 220 230 240 250
HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH PASTAVPKSG
260 270 280 290 300
EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS
310 320 330 340 350
LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV
360 370 380 390 400
LGKSQSKHIS RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA
410 420 430 440 450
PSTEYNQSHI KALLPEDSGT HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG
460 470 480 490 500
KEKEAERRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNNLPTTSV
510 520 530 540 550
IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK DYLKDNLDKY
560 570 580 590 600
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP
610 620 630 640 650
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP
660 670 680 690 700
PDVIAKNRIK ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM
710 720 730 740 750
ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE
760 770 780 790 800
VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLENVF
810 820 830 840 850
PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE LQQFNYTWLR
860 870 880 890 900
LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF
910 920 930 940
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA
Length:940
Mass (Da):106,266
Last modified:October 1, 2003 - v1
Checksum:iDB2DFACDCACD0F6A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti273 – 275NTS → AEG (Ref. 5) Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01957877P → L.Corresponds to variant rs3739112dbSNPEnsembl.1
Natural variantiVAR_019579489Q → H.Corresponds to variant rs6759356dbSNPEnsembl.1
Natural variantiVAR_035991507E → D in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_035992692L → F in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001316797.1. NM_001329868.1.
NP_055383.1. NM_014568.2.
UniGeneiHs.269027.
Hs.560932.

Genome annotation databases

EnsembliENST00000259056; ENSP00000259056; ENSG00000136542.
GeneIDi11227.
KEGGihsa:11227.
UCSCiuc002tzg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001316797.1. NM_001329868.1.
NP_055383.1. NM_014568.2.
UniGeneiHs.269027.
Hs.560932.

3D structure databases

ProteinModelPortaliQ7Z7M9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116394. 2 interactors.
IntActiQ7Z7M9. 4 interactors.
STRINGi9606.ENSP00000259056.

Protein family/group databases

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

PTM databases

iPTMnetiQ7Z7M9.
PhosphoSitePlusiQ7Z7M9.

Polymorphism and mutation databases

BioMutaiGALNT5.
DMDMi51315940.

Proteomic databases

MaxQBiQ7Z7M9.
PaxDbiQ7Z7M9.
PeptideAtlasiQ7Z7M9.
PRIDEiQ7Z7M9.

Protocols and materials databases

DNASUi11227.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259056; ENSP00000259056; ENSG00000136542.
GeneIDi11227.
KEGGihsa:11227.
UCSCiuc002tzg.4. human.

Organism-specific databases

CTDi11227.
DisGeNETi11227.
GeneCardsiGALNT5.
HGNCiHGNC:4127. GALNT5.
HPAiHPA008963.
HPA009035.
MIMi615129. gene.
neXtProtiNX_Q7Z7M9.
OpenTargetsiENSG00000136542.
PharmGKBiPA28540.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiQ7Z7M9.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG091G085O.
PhylomeDBiQ7Z7M9.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciZFISH:HS06180-MONOMER.
ReactomeiR-HSA-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGALNT5. human.
GenomeRNAii11227.
PROiQ7Z7M9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136542.
CleanExiHS_GALNT5.
GenevisibleiQ7Z7M9. 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 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: November 30, 2016
This is version 117 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. 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.