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Q86SR1 (GLT10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. 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 10

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name=GalNAc-T10
Short name=pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene names
Name:GALNT10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Has activity toward Muc5Ac and EA2 peptide substrates.

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

Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues. 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.

Caution

According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.

Sequence caution

The sequence BAB14676.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86SR1-1)

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: Q86SR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-251: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86SR1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     354-366: WMCGGRMEDIPCS → SQLSRRPVLGTAS
     367-603: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86SR1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-329: Missing.
     330-352: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ
     389-389: N → VRT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000059122

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3120Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 603572Lumenal Potential
Domain458 – 590133Ricin B-type lectin
Region144 – 253110Catalytic subdomain A
Region311 – 37363Catalytic subdomain B
Region373 – 38412Flexible loop

Sites

Metal binding2371Manganese
Metal binding2391Manganese
Metal binding3701Manganese
Binding site1541Substrate
Binding site1561Substrate
Binding site1851Substrate
Binding site2141Substrate
Binding site2381Substrate
Binding site3421Substrate
Binding site3731Substrate
Binding site3781Substrate

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Ref.7
Glycosylation1461N-linked (GlcNAc...) Ref.7
Glycosylation5931N-linked (GlcNAc...) Ref.7
Disulfide bond135 ↔ 365 Ref.7
Disulfide bond356 ↔ 432 Ref.7
Disulfide bond471 ↔ 488 Ref.7
Disulfide bond523 ↔ 538 Ref.7
Disulfide bond563 ↔ 578 Ref.7

Natural variations

Alternative sequence1 – 329329Missing in isoform 4.
VSP_011207
Alternative sequence190 – 25162Missing in isoform 2.
VSP_011209
Alternative sequence330 – 35223WELGG…EISFK → MLAWRDGELEAETSSSLFLL AMQ in isoform 4.
VSP_011208
Alternative sequence354 – 36613WMCGG…DIPCS → SQLSRRPVLGTAS in isoform 3.
VSP_011212
Alternative sequence367 – 603237Missing in isoform 3.
VSP_011213
Alternative sequence3891N → VRT in isoform 4.
VSP_011214

Experimental info

Sequence conflict5181H → Y in BAC56890. Ref.1
Sequence conflict5181H → Y in BAB14676. Ref.3

Secondary structure

......................................................................................................... 603
Helix Strand Turn

Details...

Sequences

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

Last modified August 16, 2004. Version 2.
Checksum: EE176F6139B92573

FASTA60368,992
        10         20         30         40         50         60 
MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA AGQGSHSRQK 

        70         80         90        100        110        120 
KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD AERVDQAYRE NGFNIYVSDK 

       130        140        150        160        170        180 
ISLNRSLPDI RHPNCNSKRY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 

       190        200        210        220        230        240 
VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC 

       250        260        270        280        290        300 
EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 

       310        320        330        340        350        360 
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM 

       370        380        390        400        410        420 
EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV 

       430        440        450        460        470        480 
AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CADTKHGALG 

       490        500        510        520        530        540 
SPLRLEGCVR GRGEAAWNNM QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS 

       550        560        570        580        590        600 
MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF 


NRN 

« Hide

Isoform 2 [UniParc].

Checksum: 4216612D314EA82B
Show »

FASTA54161,947
Isoform 3 [UniParc].

Checksum: 52AB23ABC6F797FE
Show »

FASTA36641,452
Isoform 4 [UniParc].

Checksum: F357AFF828E57DC7
Show »

FASTA27631,833

References

« Hide 'large scale' references
[1]"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10."
Cheng L., Tachibana K., Zhang Y., Guo J.-M., Tachibana K.K., Kameyama A., Wang H., Hiruma T., Iwasaki H., Togayachi A., Kudo T., Narimatsu H.
FEBS Lett. 531:115-121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Colon cancer.
[2]Bennett E.P.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-603 (ISOFORM 2).
Tissue: Brain and Placenta.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterus.
[5]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-366 (ISOFORM 3).
Tissue: Spleen.
[6]"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] OF 191-603 (ISOFORM 1).
Tissue: Kidney and Skin.
[7]"Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)."
Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R., Wakatsuki S., Narimatsu H.
J. Mol. Biol. 359:708-727(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITH UDP-GALNAC AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES, GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB078145 mRNA. Translation: BAC56890.1.
AJ505950 mRNA. Translation: CAD44532.1.
AK023782 mRNA. Translation: BAB14676.1. Different initiation.
AK127135 mRNA. Translation: BAG54441.1.
AL096739 mRNA. Translation: CAB46378.1.
AK074132 mRNA. Translation: BAB84958.1.
BC007224 mRNA. Translation: AAH07224.2.
BC072450 mRNA. Translation: AAH72450.1.
PIRT12552.
RefSeqNP_938080.1. NM_198321.3.
UniGeneHs.631797.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D7IX-ray2.50A40-603[»]
2D7RX-ray2.80A40-603[»]
ProteinModelPortalQ86SR1.
SMRQ86SR1. Positions 68-603.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120723. 1 interaction.
IntActQ86SR1. 1 interaction.
MINTMINT-2808648.

Protein family/group databases

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

PTM databases

PhosphoSiteQ86SR1.

Polymorphism databases

DMDM51315962.

Proteomic databases

PaxDbQ86SR1.
PRIDEQ86SR1.

Protocols and materials databases

DNASU55568.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297107; ENSP00000297107; ENSG00000164574. [Q86SR1-1]
ENST00000377661; ENSP00000366889; ENSG00000164574. [Q86SR1-2]
ENST00000425427; ENSP00000415210; ENSG00000164574. [Q86SR1-3]
GeneID55568.
KEGGhsa:55568.
UCSCuc003lvg.1. human. [Q86SR1-3]
uc003lvh.3. human. [Q86SR1-1]
uc010jid.3. human. [Q86SR1-2]

Organism-specific databases

CTD55568.
GeneCardsGC05P153550.
HGNCHGNC:19873. GALNT10.
HPAHPA007525.
MIM608043. gene.
neXtProtNX_Q86SR1.
PharmGKBPA134870832.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOVERGENHBG051699.
InParanoidQ86SR1.
KOK00710.
OMAQKKTFFL.
OrthoDBEOG7J9VP2.
PhylomeDBQ86SR1.
TreeFamTF313267.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ86SR1.
BgeeQ86SR1.
GenevestigatorQ86SR1.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
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

ChiTaRSGALNT10. human.
EvolutionaryTraceQ86SR1.
GenomeRNAi55568.
NextBio60056.
PROQ86SR1.
SOURCESearch...

Entry information

Entry nameGLT10_HUMAN
AccessionPrimary (citable) accession number: Q86SR1
Secondary accession number(s): B3KXC9 expand/collapse secondary AC list , Q6IN56, Q86VP8, Q8IXJ2, Q8TEJ2, Q96IV2, Q9H8E1, Q9Y4M4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 109 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM