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Q8NCL4 (GALT6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 6

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 6
Short name=GalNAc-T6
Short name=pp-GaNTase 6
Protein-UDP acetylgalactosaminyltransferase 6
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Gene names
Name:GALNT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length622 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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides.

Catalytic activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Tissue specificity

Expressed in placenta and trachea. Weakly expressed in brain and pancreas. Expressed in fibroblast. Weakly or not expressed in lung, liver, muscle, kidney, spleen, thymus, prostate, testis, ovary, intestine, colon, leukocyte, stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland and bone marrow. 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.

Sequence caution

The sequence BAB15297.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Polypeptide N-acetylgalactosaminyltransferase 6
PRO_0000059114

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 622594Lumenal Potential
Domain496 – 622127Ricin B-type lectin
Region176 – 285110Catalytic subdomain A
Region348 – 41063Catalytic subdomain B

Sites

Metal binding2691Manganese By similarity
Metal binding2711Manganese By similarity
Metal binding4071Manganese By similarity
Binding site2171Substrate By similarity
Binding site2461Substrate By similarity
Binding site3791Substrate By similarity
Binding site4101Substrate By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Disulfide bond165 ↔ 402 By similarity
Disulfide bond393 ↔ 474 By similarity
Disulfide bond509 ↔ 527 By similarity
Disulfide bond553 ↔ 566 By similarity
Disulfide bond597 ↔ 610 By similarity

Natural variations

Natural variant4231V → I.
Corresponds to variant rs747300 [ dbSNP | Ensembl ].
VAR_019580

Experimental info

Sequence conflict3621S → P in CAA69876. Ref.1
Sequence conflict4541A → T in BAC11118. Ref.2
Sequence conflict5511Q → R in BAC11118. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8NCL4 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 38E63FF2AFB486EF

FASTA62271,159
        10         20         30         40         50         60 
MRLLRRRHMP LRLAMVGCAF VLFLFLLHRD VSSREEATEK PWLKSLVSRK DHVLDLMLEA 

        70         80         90        100        110        120 
MNNLRDSMPK LQIRAPEAQQ TLFSINQSCL PGFYTPAELK PFWERPPQDP NAPGADGKAF 

       130        140        150        160        170        180 
QKSKWTPLET QEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLATTS 

       190        200        210        220        230        240 
VIIVFHNEAW STLLRTVYSV LHTTPAILLK EIILVDDAST EEHLKEKLEQ YVKQLQVVRV 

       250        260        270        280        290        300 
VRQEERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TVVVSPDIVT 

       310        320        330        340        350        360 
IDLNTFEFAK PVQRGRVHSR GNFDWSLTFG WETLPPHEKQ RRKDETYPIK SPTFAGGLFS 

       370        380        390        400        410        420 
ISKSYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG 

       430        440        450        460        470        480 
TSVIARNQVR LAEVWMDSYK KIFYRRNLQA AKMAQEKSFG DISERLQLRE QLHCHNFSWY 

       490        500        510        520        530        540 
LHNVYPEMFV PDLTPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYSCHGL GGNQYFEYTT 

       550        560        570        580        590        600 
QRDLRHNIAK QLCLHVSKGA LGLGSCHFTG KNSQVPKDEE WELAQDQLIR NSGSGTCLTS 

       610        620 
QDKKPAMAPC NPSDPHQLWL FV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a close homologue of human UDP-N-acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy."
Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N., Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.
J. Biol. Chem. 274:25362-25370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Gastric carcinoma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney epithelium and Mammary gland.
[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].
Tissue: Lymph.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 6

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08565 mRNA. Translation: CAA69876.1.
AK025961 mRNA. Translation: BAB15297.1. Different initiation.
AK074658 mRNA. Translation: BAC11118.1.
BC035822 mRNA. Translation: AAH35822.2.
RefSeqNP_009141.2. NM_007210.3.
XP_005268664.1. XM_005268607.1.
XP_005268665.1. XM_005268608.1.
UniGeneHs.505575.

3D structure databases

ProteinModelPortalQ8NCL4.
SMRQ8NCL4. Positions 142-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116393. 4 interactions.
IntActQ8NCL4. 4 interactions.
MINTMINT-5006466.
STRING9606.ENSP00000348668.

Protein family/group databases

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

PTM databases

PhosphoSiteQ8NCL4.

Polymorphism databases

DMDM51316028.

Proteomic databases

PaxDbQ8NCL4.
PRIDEQ8NCL4.

Protocols and materials databases

DNASU11226.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356317; ENSP00000348668; ENSG00000139629.
ENST00000543196; ENSP00000444171; ENSG00000139629.
GeneID11226.
KEGGhsa:11226.
UCSCuc001ryk.2. human.

Organism-specific databases

CTD11226.
GeneCardsGC12M051769.
HGNCHGNC:4128. GALNT6.
HPAHPA011762.
HPA017086.
MIM605148. gene.
neXtProtNX_Q8NCL4.
PharmGKBPA28541.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ8NCL4.
KOK00710.
OMANQCLDVG.
OrthoDBEOG7J9VP2.
PhylomeDBQ8NCL4.
TreeFamTF313267.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ8NCL4.
BgeeQ8NCL4.
CleanExHS_GALNT6.
GenevestigatorQ8NCL4.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[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.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT6. human.
GeneWikiGALNT6.
GenomeRNAi11226.
NextBio42726.
PROQ8NCL4.
SOURCESearch...

Entry information

Entry nameGALT6_HUMAN
AccessionPrimary (citable) accession number: Q8NCL4
Secondary accession number(s): Q8IYH4, Q9H6G2, Q9UIV5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: February 19, 2014
This is version 101 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

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