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Q8NCL4

- GALT6_HUMAN

UniProt

Q8NCL4 - GALT6_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 6

Gene

GALNT6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides.

Catalytic activityi

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

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei217 – 2171SubstrateBy similarity
Binding sitei246 – 2461SubstrateBy similarity
Metal bindingi269 – 2691ManganeseBy similarity
Metal bindingi271 – 2711ManganeseBy similarity
Binding sitei379 – 3791SubstrateBy similarity
Metal bindingi407 – 4071ManganeseBy similarity
Binding sitei410 – 4101SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. O-glycan processing Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein O-linked glycosylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. 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 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 namesi
Name:GALNT6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4128. GALNT6.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: BHF-UCL
  2. Golgi membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Polypeptide N-acetylgalactosaminyltransferase 6PRO_0000059114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi165 ↔ 402PROSITE-ProRule annotation
Disulfide bondi393 ↔ 474PROSITE-ProRule annotation
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi509 ↔ 527PROSITE-ProRule annotation
Disulfide bondi553 ↔ 566PROSITE-ProRule annotation
Disulfide bondi597 ↔ 610PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8NCL4.
PaxDbiQ8NCL4.
PRIDEiQ8NCL4.

PTM databases

PhosphoSiteiQ8NCL4.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ8NCL4.
CleanExiHS_GALNT6.
ExpressionAtlasiQ8NCL4. baseline and differential.
GenevestigatoriQ8NCL4.

Organism-specific databases

HPAiHPA011762.
HPA017086.

Interactioni

Protein-protein interaction databases

BioGridi116393. 4 interactions.
IntActiQ8NCL4. 4 interactions.
MINTiMINT-5006466.
STRINGi9606.ENSP00000348668.

Structurei

3D structure databases

ProteinModelPortaliQ8NCL4.
SMRiQ8NCL4. Positions 134-621.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Topological domaini29 – 622594LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 622127Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 285110Catalytic subdomain AAdd
BLAST
Regioni348 – 41063Catalytic subdomain BAdd
BLAST

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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8NCL4.
KOiK00710.
OMAiNQCLDVG.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8NCL4.
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.

Q8NCL4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLLRRRHMP LRLAMVGCAF VLFLFLLHRD VSSREEATEK PWLKSLVSRK
60 70 80 90 100
DHVLDLMLEA MNNLRDSMPK LQIRAPEAQQ TLFSINQSCL PGFYTPAELK
110 120 130 140 150
PFWERPPQDP NAPGADGKAF QKSKWTPLET QEKEEGYKKH CFNAFASDRI
160 170 180 190 200
SLQRSLGPDT RPPECVDQKF RRCPPLATTS VIIVFHNEAW STLLRTVYSV
210 220 230 240 250
LHTTPAILLK EIILVDDAST EEHLKEKLEQ YVKQLQVVRV VRQEERKGLI
260 270 280 290 300
TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TVVVSPDIVT
310 320 330 340 350
IDLNTFEFAK PVQRGRVHSR GNFDWSLTFG WETLPPHEKQ RRKDETYPIK
360 370 380 390 400
SPTFAGGLFS ISKSYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII
410 420 430 440 450
PCSVVGHVFR TKSPHTFPKG TSVIARNQVR LAEVWMDSYK KIFYRRNLQA
460 470 480 490 500
AKMAQEKSFG DISERLQLRE QLHCHNFSWY LHNVYPEMFV PDLTPTFYGA
510 520 530 540 550
IKNLGTNQCL DVGENNRGGK PLIMYSCHGL GGNQYFEYTT QRDLRHNIAK
560 570 580 590 600
QLCLHVSKGA LGLGSCHFTG KNSQVPKDEE WELAQDQLIR NSGSGTCLTS
610 620
QDKKPAMAPC NPSDPHQLWL FV
Length:622
Mass (Da):71,159
Last modified:August 16, 2004 - v2
Checksum:i38E63FF2AFB486EF
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti362 – 3621S → P in CAA69876. (PubMed:10464263)Curated
Sequence conflicti454 – 4541A → T in BAC11118. (PubMed:14702039)Curated
Sequence conflicti551 – 5511Q → R in BAC11118. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti423 – 4231V → I.
Corresponds to variant rs747300 [ dbSNP | Ensembl ].
VAR_019580

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08565 mRNA. Translation: CAA69876.1.
AK025961 mRNA. Translation: BAB15297.1. Different initiation.
AK074658 mRNA. Translation: BAC11118.1.
BC035822 mRNA. Translation: AAH35822.2.
CCDSiCCDS8813.1.
RefSeqiNP_009141.2. NM_007210.3.
XP_005268664.1. XM_005268607.1.
XP_005268665.1. XM_005268608.2.
XP_006719277.1. XM_006719214.1.
UniGeneiHs.505575.

Genome annotation databases

EnsembliENST00000356317; ENSP00000348668; ENSG00000139629.
ENST00000543196; ENSP00000444171; ENSG00000139629.
GeneIDi11226.
KEGGihsa:11226.
UCSCiuc001ryk.2. human.

Polymorphism databases

DMDMi51316028.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 6

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08565 mRNA. Translation: CAA69876.1 .
AK025961 mRNA. Translation: BAB15297.1 . Different initiation.
AK074658 mRNA. Translation: BAC11118.1 .
BC035822 mRNA. Translation: AAH35822.2 .
CCDSi CCDS8813.1.
RefSeqi NP_009141.2. NM_007210.3.
XP_005268664.1. XM_005268607.1.
XP_005268665.1. XM_005268608.2.
XP_006719277.1. XM_006719214.1.
UniGenei Hs.505575.

3D structure databases

ProteinModelPortali Q8NCL4.
SMRi Q8NCL4. Positions 134-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116393. 4 interactions.
IntActi Q8NCL4. 4 interactions.
MINTi MINT-5006466.
STRINGi 9606.ENSP00000348668.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSitei Q8NCL4.

Polymorphism databases

DMDMi 51316028.

Proteomic databases

MaxQBi Q8NCL4.
PaxDbi Q8NCL4.
PRIDEi Q8NCL4.

Protocols and materials databases

DNASUi 11226.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356317 ; ENSP00000348668 ; ENSG00000139629 .
ENST00000543196 ; ENSP00000444171 ; ENSG00000139629 .
GeneIDi 11226.
KEGGi hsa:11226.
UCSCi uc001ryk.2. human.

Organism-specific databases

CTDi 11226.
GeneCardsi GC12M051769.
HGNCi HGNC:4128. GALNT6.
HPAi HPA011762.
HPA017086.
MIMi 605148. gene.
neXtProti NX_Q8NCL4.
PharmGKBi PA28541.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8NCL4.
KOi K00710.
OMAi NQCLDVG.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8NCL4.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 2681.
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT6. human.
GeneWikii GALNT6.
GenomeRNAii 11226.
NextBioi 42726.
PROi Q8NCL4.
SOURCEi Search...

Gene expression databases

Bgeei Q8NCL4.
CleanExi HS_GALNT6.
ExpressionAtlasi Q8NCL4. baseline and differential.
Genevestigatori Q8NCL4.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGALT6_HUMAN
AccessioniPrimary (citable) accession number: Q8NCL4
Secondary accession number(s): Q8IYH4, Q9H6G2, Q9UIV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 108 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 12
    Human chromosome 12: 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

External Data

Dasty 3