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Q8N3T1

- GLT15_HUMAN

UniProt

Q8N3T1 - GLT15_HUMAN

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Protein

Polypeptide N-acetylgalactosaminyltransferase 15

Gene

GALNT15

Organism
Homo sapiens (Human)
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. 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 activityi

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

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311SubstrateBy similarity
Binding sitei260 – 2601SubstrateBy similarity
Metal bindingi283 – 2831ManganeseBy similarity
Metal bindingi285 – 2851ManganeseBy similarity
Metal bindingi417 – 4171ManganeseBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. O-glycan processing Source: Reactome
  3. post-translational protein modification Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_115606. 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 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 namesi
Name:GALNT15
Synonyms:GALNTL2
ORF Names:UNQ770/PRO1564
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:21531. GALNT15.

Subcellular locationi

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. transport vesicle Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134936170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639Polypeptide N-acetylgalactosaminyltransferase 15PRO_0000059137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi181 ↔ 412PROSITE-ProRule annotation
Disulfide bondi403 ↔ 482PROSITE-ProRule annotation
Disulfide bondi517 ↔ 536PROSITE-ProRule annotation
Disulfide bondi562 ↔ 575PROSITE-ProRule annotation
Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi603 ↔ 620PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8N3T1.
PRIDEiQ8N3T1.

PTM databases

PhosphoSiteiQ8N3T1.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ8N3T1.
CleanExiHS_GALNTL2.
ExpressionAtlasiQ8N3T1. baseline and differential.
GenevestigatoriQ8N3T1.

Organism-specific databases

HPAiHPA017076.

Interactioni

Protein-protein interaction databases

BioGridi125583. 1 interaction.
IntActiQ8N3T1. 1 interaction.
MINTiMINT-4724072.
STRINGi9606.ENSP00000344260.

Structurei

3D structure databases

ProteinModelPortaliQ8N3T1.
SMRiQ8N3T1. Positions 144-632.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini35 – 639605LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3423Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 631128Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 299110Catalytic subdomain AAdd
BLAST
Regioni358 – 42063Catalytic 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

eggNOGiNOG282033.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8N3T1.
KOiK00710.
OMAiETWLGSF.
PhylomeDBiQ8N3T1.
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.

Q8N3T1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK
60 70 80 90 100
HSPEARYRLD FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA
110 120 130 140 150
LPQARRNQSQ GRRGGSYRLI KQPRRQDKEA PKRDWGADED GEVSEEEELT
160 170 180 190 200
PFSLDPRGLQ EALSARIPLQ RALPEVRHPL CLQQHPQDSL PTASVILCFH
210 220 230 240 250
DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS ALSEYVARLE
260 270 280 290 300
GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
310 320 330 340 350
AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK
360 370 380 390 400
ALQSPISPIR SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA
410 420 430 440 450
WLCGGSVEIL PCSRVGHIYQ NQDSHSPLDQ EATLRNRVRI AETWLGSFKE
460 470 480 490 500
TFYKHSPEAF SLSKAEKPDC MERLQLQRRL GCRTFHWFLA NVYPELYPSE
510 520 530 540 550
PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR QQQYLQHTSR
560 570 580 590 600
KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS
610 620 630
GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER
Length:639
Mass (Da):73,063
Last modified:August 16, 2004 - v2
Checksum:iF5DCA523AF4965DA
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441V → D in CAD38585. (PubMed:17974005)Curated
Sequence conflicti326 – 3261K → R in CAD89983. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681V → G.
Corresponds to variant rs36026882 [ dbSNP | Ensembl ].
VAR_049243
Natural varianti151 – 1511P → L.
Corresponds to variant rs11715981 [ dbSNP | Ensembl ].
VAR_049244
Natural varianti324 – 3241P → A.
Corresponds to variant rs12634179 [ dbSNP | Ensembl ].
VAR_049245
Natural varianti432 – 4321A → T.2 Publications
Corresponds to variant rs17851238 [ dbSNP | Ensembl ].
VAR_049246
Natural varianti510 – 5101H → Y.
Corresponds to variant rs2271077 [ dbSNP | Ensembl ].
VAR_019593

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33711.1.
RefSeqiNP_473451.3. NM_054110.4.
UniGeneiHs.411308.

Genome annotation databases

EnsembliENST00000339732; ENSP00000344260; ENSG00000131386.
GeneIDi117248.
KEGGihsa:117248.
UCSCiuc003caq.4. human.

Polymorphism databases

DMDMi51316023.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase-like protein 2

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33711.1.
RefSeqi NP_473451.3. NM_054110.4.
UniGenei Hs.411308.

3D structure databases

ProteinModelPortali Q8N3T1.
SMRi Q8N3T1. Positions 144-632.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125583. 1 interaction.
IntActi Q8N3T1. 1 interaction.
MINTi MINT-4724072.
STRINGi 9606.ENSP00000344260.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8N3T1.

Polymorphism databases

DMDMi 51316023.

Proteomic databases

PaxDbi Q8N3T1.
PRIDEi Q8N3T1.

Protocols and materials databases

DNASUi 117248.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339732 ; ENSP00000344260 ; ENSG00000131386 .
GeneIDi 117248.
KEGGi hsa:117248.
UCSCi uc003caq.4. human.

Organism-specific databases

CTDi 117248.
GeneCardsi GC03P016216.
HGNCi HGNC:21531. GALNT15.
HPAi HPA017076.
neXtProti NX_Q8N3T1.
PharmGKBi PA134936170.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282033.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8N3T1.
KOi K00710.
OMAi ETWLGSF.
PhylomeDBi Q8N3T1.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

GeneWikii GALNTL2.
GenomeRNAii 117248.
NextBioi 80182.
PROi Q8N3T1.

Gene expression databases

Bgeei Q8N3T1.
CleanExi HS_GALNTL2.
ExpressionAtlasi Q8N3T1. baseline and differential.
Genevestigatori Q8N3T1.

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. 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. 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.
    , 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. 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.
    , 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. 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.

Entry informationi

Entry nameiGLT15_HUMAN
AccessioniPrimary (citable) accession number: Q8N3T1
Secondary accession number(s): A6NMN1
, B2R638, F1LIP6, Q86T60, Q96C46, Q96DJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was originally termed Galnt15/pp-GaNTase 15.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3