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Q8NCW6 (GLT11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 11

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name=GalNAc-T11
Short name=pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene names
Name:GALNT11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO). Ref.1 Ref.7

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.

Subunit structure

Interacts with NOTCH1. Ref.7

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.1.

Tissue specificity

Highly expressed in kidney. Expressed at intermediate level in brain, heart and skeletal muscle. Weakly expressed other tissues. In kidney, it is strongly expressed in tubules but not expressed in glomeruli. 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.

Involvement in disease

Defects in GALNT11 may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning (Ref.6).

Sequence similarities

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

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence BAB15338.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseHeterotaxy
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
Manganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch receptor processing

Inferred from sequence or structural similarity. Source: UniProtKB

Notch signaling involved in heart development

Inferred from sequence or structural similarity. Source: UniProtKB

O-glycan processing

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

determination of left/right symmetry

Inferred from sequence or structural similarity. Source: UniProtKB

post-translational protein modification

Traceable author statement. Source: Reactome

protein O-linked glycosylation via threonine

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of Notch signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNotch binding

Inferred from direct assay Ref.7. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polypeptide N-acetylgalactosaminyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NCW6-1)

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: Q8NCW6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     196-202: DDLKGEL → GKECCTW
     203-608: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Polypeptide N-acetylgalactosaminyltransferase 11
PRO_0000059125

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 608579Lumenal Potential
Domain476 – 607132Ricin B-type lectin
Region150 – 261112Catalytic subdomain A
Region319 – 38163Catalytic subdomain B

Sites

Metal binding2451Manganese By similarity
Metal binding2471Manganese By similarity
Metal binding3781Manganese By similarity
Binding site1911Substrate By similarity
Binding site2221Substrate By similarity
Binding site2461Substrate By similarity
Binding site3501Substrate By similarity
Binding site3811Substrate By similarity
Binding site3861Substrate By similarity

Amino acid modifications

Glycosylation4281N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 373 By similarity
Disulfide bond364 ↔ 441 By similarity
Disulfide bond493 ↔ 512 By similarity
Disulfide bond536 ↔ 553 By similarity
Disulfide bond578 ↔ 596 By similarity

Natural variations

Alternative sequence196 – 2027DDLKGEL → GKECCTW in isoform 2.
VSP_011215
Alternative sequence203 – 608406Missing in isoform 2.
VSP_011216
Natural variant1511P → S.
Corresponds to variant rs6464201 [ dbSNP | Ensembl ].
VAR_019589
Natural variant1971D → Y. Ref.8
Corresponds to variant rs3778922 [ dbSNP | Ensembl ].
VAR_019590

Experimental info

Mutagenesis2471H → A: Abolishes glycosyltransferase activity and ability to rescue left-right patterning defects induced by galnt11 knockdown in X.tropicalis. Ref.7
Sequence conflict941F → L in BAG54116. Ref.3
Sequence conflict5511M → V in BAB15105. Ref.3
Sequence conflict5771Q → L in BAB15105. Ref.3

Sequences

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

Last modified August 16, 2004. Version 2.
Checksum: 075D7B839A8D5607

FASTA60868,919
        10         20         30         40         50         60 
MGSVTVRYFC YGCLFTSATW TVLLFVYFNF SEVTQPLKNV PVKGSGPHGP SPKKFYPRFT 

        70         80         90        100        110        120 
RGPSRVLEPQ FKANKIDDVI DSRVEDPEEG HLKFSSELGM IFNERDQELR DLGYQKHAFN 

       130        140        150        160        170        180 
MLISDRLGYH RDVPDTRNAA CKEKFYPPDL PAASVVICFY NEAFSALLRT VHSVIDRTPA 

       190        200        210        220        230        240 
HLLHEIILVD DDSDFDDLKG ELDEYVQKYL PGKIKVIRNT KREGLIRGRM IGAAHATGEV 

       250        260        270        280        290        300 
LVFLDSHCEV NVMWLQPLLA AIREDRHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF 

       310        320        330        340        350        360 
KWDLVPLSEL GRAEGATAPI KSPTMAGGLF AMNRQYFHEL GQYDSGMDIW GGENLEISFR 

       370        380        390        400        410        420 
IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD 

       430        440        450        460        470        480 
LKTKSYGNIS ERVELRKKLG CKSFKWYLDN VYPEMQISGS HAKPQQPIFV NRGPKRPKVL 

       490        500        510        520        530        540 
QRGRLYHLQT NKCLVAQGRP SQKGGLVVLK ACDYSDPNQI WIYNEEHELV LNSLLCLDMS 

       550        560        570        580        590        600 
ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR AVDPLGQKGS VAMAICDGSS 


SQQWHLEG 

« Hide

Isoform 2 [UniParc].

Checksum: A2B98F18AB31C370
Show »

FASTA20223,090

References

« Hide 'large scale' references
[1]"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]Bennett E.P.
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 14-15; 119; 295; 310; 365 AND 369.
[3]"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] (ISOFORM 1).
Tissue: Colon, Kidney epithelium and Subthalamic nucleus.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Placenta.
[6]"Rare copy number variations in congenital heart disease patients identify unique genes in left-right patterning."
Fakhro K.A., Choi M., Ware S.M., Belmont J.W., Towbin J.A., Lifton R.P., Khokha M.K., Brueckner M.
Proc. Natl. Acad. Sci. U.S.A. 108:2915-2920(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN HETEROTAXY.
[7]"The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-247, INTERACTION WITH NOTCH1.
[8]"A Japanese-specific allele in the GALNT11 gene."
Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S., Fukumori Y., Saitou N., Jin F., Chattopadhyay P.K., Henke L., Henke J.
Leg. Med. 12:208-211(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-197.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 11

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12434 mRNA. Translation: CAC79625.3.
AK025287 mRNA. Translation: BAB15105.1.
AK026056 mRNA. Translation: BAB15338.1. Different initiation.
AK124934 mRNA. Translation: BAG54116.1.
AC006017 Genomic DNA. Translation: AAD45821.1.
BC059377 mRNA. Translation: AAH59377.1.
CCDSCCDS5930.1. [Q8NCW6-1]
RefSeqNP_071370.2. NM_022087.2. [Q8NCW6-1]
XP_006716145.1. XM_006716082.1. [Q8NCW6-1]
XP_006716146.1. XM_006716083.1. [Q8NCW6-1]
XP_006716147.1. XM_006716084.1. [Q8NCW6-1]
UniGeneHs.647109.

3D structure databases

ProteinModelPortalQ8NCW6.
SMRQ8NCW6. Positions 130-606.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121988. 1 interaction.
STRING9606.ENSP00000315835.

Protein family/group databases

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

PTM databases

PhosphoSiteQ8NCW6.

Polymorphism databases

DMDM51316030.

Proteomic databases

MaxQBQ8NCW6.
PaxDbQ8NCW6.
PRIDEQ8NCW6.

Protocols and materials databases

DNASU63917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320311; ENSP00000315835; ENSG00000178234. [Q8NCW6-1]
ENST00000415421; ENSP00000410093; ENSG00000178234. [Q8NCW6-2]
ENST00000430044; ENSP00000395122; ENSG00000178234. [Q8NCW6-1]
ENST00000434507; ENSP00000416787; ENSG00000178234. [Q8NCW6-1]
GeneID63917.
KEGGhsa:63917.
UCSCuc003wku.2. human. [Q8NCW6-1]
uc003wkv.1. human. [Q8NCW6-2]

Organism-specific databases

CTD63917.
GeneCardsGC07P151722.
H-InvDBHIX0007236.
HGNCHGNC:19875. GALNT11.
HPAHPA039330.
MIM615130. gene.
neXtProtNX_Q8NCW6.
PharmGKBPA134911149.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ8NCW6.
KOK00710.
OMAMIFNERD.
OrthoDBEOG7J9VP2.
PhylomeDBQ8NCW6.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 2681.
ReactomeREACT_17015. Metabolism of proteins.
SABIO-RKQ8NCW6.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8NCW6.
BgeeQ8NCW6.
CleanExHS_GALNT11.
GenevestigatorQ8NCW6.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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

ChiTaRSGALNT11. human.
GenomeRNAi63917.
NextBio65642.
PROQ8NCW6.
SOURCESearch...

Entry information

Entry nameGLT11_HUMAN
AccessionPrimary (citable) accession number: Q8NCW6
Secondary accession number(s): B3KWF4 expand/collapse secondary AC list , Q6PCD1, Q9H6C2, Q9H6Z5, Q9UDR8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 107 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 7

Human chromosome 7: entries, gene names and cross-references to MIM