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Q8NCW6 (GLT11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length608 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. Displays the same enzyme activity toward Muc1, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin.

Catalytic activity

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

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

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.

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

Amino acid modifications

Glycosylation4281N-linked (GlcNAc...) Potential
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.
Corresponds to variant rs3778922 [ dbSNP | Ensembl ].
VAR_019590

Experimental info

Sequence conflict14 – 152LF → FL in CAC79625. Ref.1
Sequence conflict1191F → L in CAC79625. Ref.1
Sequence conflict2951N → H in CAC79625. Ref.1
Sequence conflict3101L → F in CAC79625. Ref.1
Sequence conflict3651G → S in CAC79625. Ref.1
Sequence conflict3691F → S in CAC79625. Ref.1
Sequence conflict5511M → V in BAB15105. Ref.2
Sequence conflict5771Q → L in BAB15105. Ref.2

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: 11925450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon and Kidney epithelium.
[3]"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: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
+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: CAC79625.2.
AK025287 mRNA. Translation: BAB15105.1.
AK026056 mRNA. Translation: BAB15338.1. Different initiation.
AC006017 Genomic DNA. Translation: AAD45821.1.
BC059377 mRNA. Translation: AAH59377.1.
IPIIPI00456589.
IPI00456591.
RefSeqNP_071370.2. NM_022087.2.
UniGeneHs.647109.

3D structure databases

ProteinModelPortalQ8NCW6.
SMRQ8NCW6. Positions 101-607.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8NCW6.

Protein family/group databases

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

PTM databases

PhosphoSiteQ8NCW6.

Polymorphism databases

DMDM51316030.

Proteomic databases

PRIDEQ8NCW6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320311; ENSP00000315835; ENSG00000178234.
ENST00000430044; ENSP00000395122; ENSG00000178234.
ENST00000434507; ENSP00000416787; ENSG00000178234.
ENST00000443352; ENSP00000408155; ENSG00000178234.
GeneID63917.
KEGGhsa:63917.
UCSCuc003wku.2. human.
uc003wkv.1. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGprNOG10622.
GeneTreeENSGT00560000076662.
HOGENOMHBG715048.
HOVERGENHBG051699.
InParanoidQ8NCW6.
OMARDLGYQK.
OrthoDBEOG4JQ3X7.
PhylomeDBQ8NCW6.

Enzyme and pathway databases

BRENDA2.4.1.41. 2681.

Gene expression databases

ArrayExpressQ8NCW6.
BgeeQ8NCW6.
CleanExHS_GALNT11.
GenevestigatorQ8NCW6.
GermOnlineENSG00000178234. Homo sapiens.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR008997. Ricin_B-rel_lectin.
IPR000772. Ricin_B_lectin.
[Graphical view]
KOK00710.
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio65642.

Entry information

Entry nameGLT11_HUMAN
AccessionPrimary (citable) accession number: Q8NCW6
Secondary accession number(s): Q6PCD1 expand/collapse secondary AC list , Q9H6C2, Q9H6Z5, Q9UDR8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 84 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

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families