Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8N3T1 (GLT15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 15

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase-like protein 2
Short name=GalNAc-T-like protein 2
Short name=pp-GaNTase-like protein 2
Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Protein-UDP acetylgalactosaminyltransferase-like protein 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Gene names
Name:GALNT15
Synonyms:GALNTL2
ORF Names:UNQ770/PRO1564
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate.

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. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage. Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage. Ref.1 Ref.2

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

Was originally (Ref.1) termed Galnt15/pp-GaNTase 15.

Sequence caution

The sequence CAD89983.1 differs from that shown. Reason: Frameshift at positions 169, 192, 206, 222 and 270.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639Polypeptide N-acetylgalactosaminyltransferase 15
PRO_0000059137

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3423Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 639605Lumenal Potential
Domain504 – 631128Ricin B-type lectin
Region190 – 299110Catalytic subdomain A
Region358 – 42063Catalytic subdomain B

Sites

Metal binding2831Manganese By similarity
Metal binding2851Manganese By similarity
Metal binding4171Manganese By similarity
Binding site2311Substrate By similarity
Binding site2601Substrate By similarity

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Disulfide bond181 ↔ 412 By similarity
Disulfide bond403 ↔ 482 By similarity
Disulfide bond517 ↔ 536 By similarity
Disulfide bond562 ↔ 575 By similarity
Disulfide bond603 ↔ 620 By similarity

Natural variations

Natural variant681V → G.
Corresponds to variant rs36026882 [ dbSNP | Ensembl ].
VAR_049243
Natural variant1511P → L.
Corresponds to variant rs11715981 [ dbSNP | Ensembl ].
VAR_049244
Natural variant3241P → A.
Corresponds to variant rs12634179 [ dbSNP | Ensembl ].
VAR_049245
Natural variant4321A → T. Ref.5 Ref.7
Corresponds to variant rs17851238 [ dbSNP | Ensembl ].
VAR_049246
Natural variant5101H → Y.
Corresponds to variant rs2271077 [ dbSNP | Ensembl ].
VAR_019593

Experimental info

Sequence conflict441V → D in CAD38585. Ref.5
Sequence conflict3261K → R in CAD89983. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8N3T1 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: F5DCA523AF4965DA

FASTA63973,063
        10         20         30         40         50         60 
MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK HSPEARYRLD 

        70         80         90        100        110        120 
FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA LPQARRNQSQ GRRGGSYRLI 

       130        140        150        160        170        180 
KQPRRQDKEA PKRDWGADED GEVSEEEELT PFSLDPRGLQ EALSARIPLQ RALPEVRHPL 

       190        200        210        220        230        240 
CLQQHPQDSL PTASVILCFH DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS 

       250        260        270        280        290        300 
ALSEYVARLE GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 

       310        320        330        340        350        360 
AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK ALQSPISPIR 

       370        380        390        400        410        420 
SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA WLCGGSVEIL PCSRVGHIYQ 

       430        440        450        460        470        480 
NQDSHSPLDQ EATLRNRVRI AETWLGSFKE TFYKHSPEAF SLSKAEKPDC MERLQLQRRL 

       490        500        510        520        530        540 
GCRTFHWFLA NVYPELYPSE PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR 

       550        560        570        580        590        600 
QQQYLQHTSR KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS 

       610        620        630 
GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15."
Cheng L., Tachibana K., Iwasaki H., Kameyama A., Zhang Y., Kubota T., Hiruma T., Tachibana K., Kudo T., Guo J.-M., Narimatsu H.
FEBS Lett. 566:17-24(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
[2]"Identification and initial characterization of 5000 expressed sequenced tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA libraries."
Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J., Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M., Lark M.W.
Osteoarthritis Cartilage 9:641-653(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
Tissue: Osteoarthritic cartilage.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Tissue: Brain.
[5]"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], VARIANT THR-432.
Tissue: Adipose tissue and Spinal cord.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-432.
[8]"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.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase-like protein 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB078149 mRNA. Translation: BAD29961.1.
AY035399 mRNA. Translation: AAK63127.1.
AY358443 mRNA. Translation: AAQ88808.1.
AK312425 mRNA. Translation: BAG35335.1.
AL831925 mRNA. Translation: CAD38585.1.
AL832575 mRNA. Translation: CAD89983.1. Frameshift.
AC087858 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64266.1.
BC014789 mRNA. Translation: AAH14789.1.
CCDSCCDS33711.1.
RefSeqNP_473451.3. NM_054110.4.
UniGeneHs.411308.

3D structure databases

ProteinModelPortalQ8N3T1.
SMRQ8N3T1. Positions 595-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125583. 1 interaction.
IntActQ8N3T1. 1 interaction.
MINTMINT-4724072.
STRING9606.ENSP00000344260.

Protein family/group databases

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

PTM databases

PhosphoSiteQ8N3T1.

Polymorphism databases

DMDM51316023.

Proteomic databases

PaxDbQ8N3T1.
PRIDEQ8N3T1.

Protocols and materials databases

DNASU117248.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339732; ENSP00000344260; ENSG00000131386.
GeneID117248.
KEGGhsa:117248.
UCSCuc003caq.4. human.

Organism-specific databases

CTD117248.
GeneCardsGC03P016216.
HGNCHGNC:21531. GALNT15.
HPAHPA017076.
neXtProtNX_Q8N3T1.
PharmGKBPA134936170.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282033.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ8N3T1.
KOK00710.
OMAETWLGSF.
PhylomeDBQ8N3T1.
TreeFamTF313267.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8N3T1.
BgeeQ8N3T1.
CleanExHS_GALNTL2.
GenevestigatorQ8N3T1.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGALNTL2.
GenomeRNAi117248.
NextBio80182.
PROQ8N3T1.

Entry information

Entry nameGLT15_HUMAN
AccessionPrimary (citable) accession number: Q8N3T1
Secondary accession number(s): A6NMN1 expand/collapse secondary AC list , B2R638, F1LIP6, Q86T60, Q96C46, Q96DJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 106 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM