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Q9HCQ5 (GALT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 9

EC=2.4.1.41
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 names
Name:GALNT9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.4

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

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. Ref.1

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCQ5-1)

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.
Isoform 2 (identifier: Q9HCQ5-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Polypeptide N-acetylgalactosaminyltransferase 9
PRO_0000059120

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 603574Lumenal Potential
Domain464 – 600137Ricin B-type lectin
Region150 – 261112Catalytic subdomain A
Region318 – 38063Catalytic subdomain B

Sites

Metal binding2451Manganese By similarity
Metal binding2471Manganese By similarity
Metal binding3771Manganese By similarity
Binding site1911Substrate By similarity
Binding site2221Substrate By similarity
Binding site3801Substrate By similarity
Binding site3851Substrate By similarity

Amino acid modifications

Glycosylation4601N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 372 By similarity
Disulfide bond363 ↔ 442 By similarity
Disulfide bond477 ↔ 493 By similarity
Disulfide bond525 ↔ 540 By similarity
Disulfide bond567 ↔ 587 By similarity

Natural variations

Alternative sequence1 – 366366Missing in isoform 2.
VSP_011206

Experimental info

Sequence conflict5391K → R in BAB13699. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 4B5888733D8577CF

FASTA60368,359
        10         20         30         40         50         60 
MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR HAKVGTLGDR 

        70         80         90        100        110        120 
EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA ATLRDDGQEA EGKYEEYGYN 

       130        140        150        160        170        180 
AQLSDRISLD RSIPDYRPRK CRQMSYAQDL PQVSVVFIFV NEALSVILRS VHSVVNHTPS 

       190        200        210        220        230        240 
QLLKEVILVD DNSDNVELKF NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV 

       250        260        270        280        290        300 
VGFFDAHVEF NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC 

       310        320        330        340        350        360 
MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG GENVELGMRV 

       370        380        390        400        410        420 
WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA AEVWMDDFKS HVYMAWNIPM 

       430        440        450        460        470        480 
SNPGVDFGDV SERLALRQRL KCRSFKWYLE NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ 

       490        500        510        520        530        540 
GAEDGDRAIL YPCHGMSSQL VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC 

       550        560        570        580        590        600 
EDVARPTQRL WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH 


ARH 

« Hide

Isoform 2 [UniParc].

Checksum: 5484F64E65F6F6DA
Show »

FASTA23727,211

References

« Hide 'large scale' references
[1]"Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)."
Toba S., Tenno M., Konishi M., Mikami T., Itoh N., Kurosaka A.
Biochim. Biophys. Acta 1493:264-268(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[2]Guo J.H., Zan Q., Yu L.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon.
[4]"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 9

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040672 mRNA. Translation: BAB13699.2.
AF458594 mRNA. Translation: AAM49722.1.
BC093817 mRNA. Translation: AAH93817.2.
BC093819 mRNA. Translation: AAH93819.2.
CCDSCCDS41866.1. [Q9HCQ5-2]
RefSeqNP_001116108.1. NM_001122636.1.
NP_068580.2. NM_021808.3. [Q9HCQ5-2]
UniGeneHs.301062.
Hs.658249.

3D structure databases

ProteinModelPortalQ9HCQ5.
SMRQ9HCQ5. Positions 105-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000380488.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Polymorphism databases

DMDM143811393.

Proteomic databases

PaxDbQ9HCQ5.
PRIDEQ9HCQ5.

Protocols and materials databases

DNASU50614.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397325; ENSP00000380488; ENSG00000182870. [Q9HCQ5-2]
ENST00000541995; ENSP00000440544; ENSG00000182870. [Q9HCQ5-2]
ENST00000562730; ENSP00000455804; ENSG00000259919. [Q9HCQ5-2]
ENST00000566342; ENSP00000457483; ENSG00000259919. [Q9HCQ5-2]
GeneID50614.
KEGGhsa:50614.
UCSCuc001uka.3. human. [Q9HCQ5-2]

Organism-specific databases

CTD50614.
GeneCardsGC12M132680.
HGNCHGNC:4131. GALNT9.
MIM606251. gene.
neXtProtNX_Q9HCQ5.
PharmGKBPA28544.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250827.
HOGENOMHOG000038228.
HOVERGENHBG051699.
InParanoidQ9HCQ5.
KOK00710.
PhylomeDBQ9HCQ5.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9HCQ5.
BgeeQ9HCQ5.
CleanExHS_GALNT9.
GenevestigatorQ9HCQ5.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
IPR001202. WW_dom.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi50614.
NextBio53114.
PROQ9HCQ5.
SOURCESearch...

Entry information

Entry nameGALT9_HUMAN
AccessionPrimary (citable) accession number: Q9HCQ5
Secondary accession number(s): Q52LR8, Q6NT54, Q8NFR1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM