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Q8C7U7

- GALT6_MOUSE

UniProt

Q8C7U7 - GALT6_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 6

Gene

Galnt6

Organism
Mus musculus (Mouse)
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 (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

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: MGI

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198517. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1891640. Galnt6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini29 – 622594LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Polypeptide N-acetylgalactosaminyltransferase 6PRO_0000059115Add
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

MaxQBiQ8C7U7.
PaxDbiQ8C7U7.
PRIDEiQ8C7U7.

PTM databases

PhosphoSiteiQ8C7U7.

Expressioni

Gene expression databases

BgeeiQ8C7U7.
GenevestigatoriQ8C7U7.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056705.

Structurei

3D structure databases

ProteinModelPortaliQ8C7U7.
SMRiQ8C7U7. Positions 131-604.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8C7U7.
KOiK00710.
OMAiNQCLDVG.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8C7U7.
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.

Q8C7U7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK
60 70 80 90 100
DQVLDFMLGA VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK
110 120 130 140 150
PFWDRPPQDP NSPGADGKAF QKKEWTNLET KEKEEGYKKH CFNAFASDRI
160 170 180 190 200
SLQRSLGPDT RPPECVDQKF RRCPPLPTTS VIIVFHNEAW STLLRTVYSV
210 220 230 240 250
LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV VRQRERKGLI
260 270 280 290 300
TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT
310 320 330 340 350
IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK
360 370 380 390 400
SPTFAGGLFS ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII
410 420 430 440 450
PCSVVGHVFR TKSPHTFPKG TSVIARNQVR LAEVWMDDYK KIFYRRNLQA
460 470 480 490 500
AKMVQENNFG DISERLRLRE QLRCHNFSWY LHNVYPEMFV PDLNPTFYGA
510 520 530 540 550
IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS QRDLRHNIGK
560 570 580 590 600
QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS
610 620
QDKKPAMAPC NPRDPYQLWL FV
Length:622
Mass (Da):71,537
Last modified:March 1, 2003 - v1
Checksum:i6DBCA3A2CCFDBDAA
GO

Sequence cautioni

The sequence CAB55352.1 differs from that shown. Reason: Frameshift at position 622. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → T in CAB55352. (PubMed:10464263)Curated
Sequence conflicti100 – 1001K → R in CAB55352. (PubMed:10464263)Curated
Sequence conflicti210 – 2101K → N in BAC25984. (PubMed:16141072)Curated
Sequence conflicti215 – 2151V → M in BAC25984. (PubMed:16141072)Curated
Sequence conflicti247 – 2471K → G in BAC25984. (PubMed:16141072)Curated
Sequence conflicti263 – 27513EVLTF…HCECF → KGAHVSWTPTVSVS(PubMed:10464263)CuratedAdd
BLAST
Sequence conflicti292 – 2921A → P in CAB55352. (PubMed:10464263)Curated
Sequence conflicti336 – 3361E → Q in CAB55352. (PubMed:10464263)Curated
Sequence conflicti398 – 3981E → G in BAC25984. (PubMed:16141072)Curated
Sequence conflicti467 – 4671R → Q in CAB55352. (PubMed:10464263)Curated
Sequence conflicti562 – 5621G → S in CAB55352. (PubMed:10464263)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133523 mRNA. Translation: CAB55352.1. Frameshift.
AK028506 mRNA. Translation: BAC25984.1.
AK049222 mRNA. Translation: BAC33618.1.
AK155008 mRNA. Translation: BAE32989.1.
AK159721 mRNA. Translation: BAE35316.1.
BC119324 mRNA. Translation: AAI19325.1.
BC119326 mRNA. Translation: AAI19327.1.
CCDSiCCDS27843.1.
RefSeqiNP_001155239.1. NM_001161767.1.
NP_001155240.1. NM_001161768.1.
NP_766039.2. NM_172451.3.
UniGeneiMm.22969.

Genome annotation databases

EnsembliENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
GeneIDi207839.
KEGGimmu:207839.
UCSCiuc007xrz.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133523 mRNA. Translation: CAB55352.1 . Frameshift.
AK028506 mRNA. Translation: BAC25984.1 .
AK049222 mRNA. Translation: BAC33618.1 .
AK155008 mRNA. Translation: BAE32989.1 .
AK159721 mRNA. Translation: BAE35316.1 .
BC119324 mRNA. Translation: AAI19325.1 .
BC119326 mRNA. Translation: AAI19327.1 .
CCDSi CCDS27843.1.
RefSeqi NP_001155239.1. NM_001161767.1.
NP_001155240.1. NM_001161768.1.
NP_766039.2. NM_172451.3.
UniGenei Mm.22969.

3D structure databases

ProteinModelPortali Q8C7U7.
SMRi Q8C7U7. Positions 131-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000056705.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8C7U7.

Proteomic databases

MaxQBi Q8C7U7.
PaxDbi Q8C7U7.
PRIDEi Q8C7U7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000052069 ; ENSMUSP00000056705 ; ENSMUSG00000037280 .
ENSMUST00000159715 ; ENSMUSP00000123848 ; ENSMUSG00000037280 .
ENSMUST00000161514 ; ENSMUSP00000124793 ; ENSMUSG00000037280 .
GeneIDi 207839.
KEGGi mmu:207839.
UCSCi uc007xrz.2. mouse.

Organism-specific databases

CTDi 11226.
MGIi MGI:1891640. Galnt6.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8C7U7.
KOi K00710.
OMAi NQCLDVG.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8C7U7.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 372071.
PROi Q8C7U7.
SOURCEi Search...

Gene expression databases

Bgeei Q8C7U7.
Genevestigatori Q8C7U7.

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].
    Tissue: Gastric carcinoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Skin.
  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: Brain.

Entry informationi

Entry nameiGALT6_MOUSE
AccessioniPrimary (citable) accession number: Q8C7U7
Secondary accession number(s): Q0VE84
, Q3TWF0, Q8CED2, Q9QZ16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3