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Protein

Polypeptide N-acetylgalactosaminyltransferase 9

Gene

GALNT9

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. Does not glycosylate apomucin or SDC3.2 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.1 Publication
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
Metal bindingi247ManganeseBy similarity1
Metal bindingi377ManganeseBy similarity1
Binding sitei380SubstrateBy similarity1
Binding sitei385SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • O-glycan processing Source: Reactome
  • protein O-linked glycosylation Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
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 9 (EC:2.4.1.411 Publication)
Alternative name(s):
Polypeptide GalNAc transferase 9
Short name:
GalNAc-T9
Short name:
pp-GaNTase 9
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Gene namesi
Name:GALNT9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000182870.12.
HGNCiHGNC:4131. GALNT9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 603LumenalSequence analysisAdd BLAST574

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi50614.
OpenTargetsiENSG00000182870.
PharmGKBiPA28544.

Polymorphism and mutation databases

BioMutaiGALNT9.
DMDMi143811393.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591201 – 603Polypeptide N-acetylgalactosaminyltransferase 9Add BLAST603

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi141 ↔ 372PROSITE-ProRule annotation
Disulfide bondi363 ↔ 442PROSITE-ProRule annotation
Glycosylationi460N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi477 ↔ 493PROSITE-ProRule annotation
Disulfide bondi525 ↔ 540PROSITE-ProRule annotation
Disulfide bondi567 ↔ 587PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9HCQ5.
PeptideAtlasiQ9HCQ5.
PRIDEiQ9HCQ5.

PTM databases

iPTMnetiQ9HCQ5.
PhosphoSitePlusiQ9HCQ5.

Expressioni

Tissue specificityi

Specifically expressed in brain. Not expressed in heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocyte. In brain, it is expressed in cerebellum, frontal lobe, temporal lobe, putamen and spinal cord, weakly expressed in cerebral cortex. Not expressed in medulla and occipital pole.1 Publication

Gene expression databases

BgeeiENSG00000182870.
CleanExiHS_GALNT9.
ExpressionAtlasiQ9HCQ5. baseline and differential.
GenevisibleiQ9HCQ5. HS.

Organism-specific databases

HPAiHPA075016.

Interactioni

Protein-protein interaction databases

BioGridi119094. 1 interactor.
IntActiQ9HCQ5. 1 interactor.
STRINGi9606.ENSP00000380488.

Structurei

3D structure databases

ProteinModelPortaliQ9HCQ5.
SMRiQ9HCQ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini464 – 600Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 261Catalytic subdomain AAdd BLAST112
Regioni318 – 380Catalytic 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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00900000140827.
HOGENOMiHOG000038228.
HOVERGENiHBG051699.
InParanoidiQ9HCQ5.
KOiK00710.
PhylomeDBiQ9HCQ5.
TreeFamiTF313267.

Family and domain databases

CDDicd00161. RICIN. 1 hit.
Gene3Di3.90.550.10. 1 hit.
InterProiView protein in InterPro
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR035992. Ricin_B-like_lectins.
IPR000772. Ricin_B_lectin.
IPR001202. WW_dom.
PfamiView protein in Pfam
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
SMARTiView protein in SMART
SM00458. RICIN. 1 hit.
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiView protein in PROSITE
PS50231. RICIN_B_LECTIN. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9HCQ5-1) [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
MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR
60 70 80 90 100
HAKVGTLGDR EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA
110 120 130 140 150
ATLRDDGQEA EGKYEEYGYN AQLSDRISLD RSIPDYRPRK CRQMSYAQDL
160 170 180 190 200
PQVSVVFIFV NEALSVILRS VHSVVNHTPS QLLKEVILVD DNSDNVELKF
210 220 230 240 250
NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV VGFFDAHVEF
260 270 280 290 300
NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC
310 320 330 340 350
MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG
360 370 380 390 400
GENVELGMRV WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA
410 420 430 440 450
AEVWMDDFKS HVYMAWNIPM SNPGVDFGDV SERLALRQRL KCRSFKWYLE
460 470 480 490 500
NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ GAEDGDRAIL YPCHGMSSQL
510 520 530 540 550
VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC EDVARPTQRL
560 570 580 590 600
WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH

ARH
Length:603
Mass (Da):68,359
Last modified:April 3, 2007 - v3
Checksum:i4B5888733D8577CF
GO
Isoform 2 (identifier: Q9HCQ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-366: Missing.

Show »
Length:237
Mass (Da):27,211
Checksum:i5484F64E65F6F6DA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti539K → R in BAB13699 (PubMed:10978536).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0112061 – 366Missing in isoform 2. 2 PublicationsAdd BLAST366

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040672 mRNA. Translation: BAB13699.2.
AF458594 mRNA. Translation: AAM49722.1.
BC093817 mRNA. Translation: AAH93817.2.
BC093819 mRNA. Translation: AAH93819.2.
CCDSiCCDS41866.1. [Q9HCQ5-2]
CCDS81755.1. [Q9HCQ5-1]
RefSeqiNP_001116108.1. NM_001122636.1.
NP_068580.2. NM_021808.3. [Q9HCQ5-2]
UniGeneiHs.301062.
Hs.658249.

Genome annotation databases

EnsembliENST00000397325; ENSP00000380488; ENSG00000182870. [Q9HCQ5-2]
ENST00000541995; ENSP00000440544; ENSG00000182870. [Q9HCQ5-2]
GeneIDi50614.
KEGGihsa:50614.
UCSCiuc001uka.3. human. [Q9HCQ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiGALT9_HUMAN
AccessioniPrimary (citable) accession number: Q9HCQ5
Secondary accession number(s): Q52LR8, Q6NT54, Q8NFR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: April 3, 2007
Last modified: October 25, 2017
This is version 135 of the entry and version 3 of the sequence. See 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 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families