SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8N3T1

- GLT15_HUMAN

UniProt

Q8N3T1 - GLT15_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Polypeptide N-acetylgalactosaminyltransferase 15
Gene
GALNT15, GALNTL2, UNQ770/PRO1564
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 – 2311Substrate By similarity
Binding sitei260 – 2601Substrate By similarity
Metal bindingi283 – 2831Manganese By similarity
Metal bindingi285 – 2851Manganese By similarity
Metal bindingi417 – 4171Manganese By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. O-glycan processing Source: Reactome
  2. cellular protein metabolic process 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei12 – 3423Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini35 – 639605Lumenal Reviewed prediction
Add
BLAST

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 15
PRO_0000059137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi107 – 1071N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi181 ↔ 412 By similarity
Disulfide bondi403 ↔ 482 By similarity
Disulfide bondi517 ↔ 536 By similarity
Disulfide bondi562 ↔ 575 By similarity
Glycosylationi574 – 5741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi603 ↔ 620 By similarity

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

ArrayExpressiQ8N3T1.
BgeeiQ8N3T1.
CleanExiHS_GALNTL2.
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 595-631.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 631128Ricin B-type lectin
Add
BLAST

Region

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282033.
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

MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK    50
HSPEARYRLD FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA 100
LPQARRNQSQ GRRGGSYRLI KQPRRQDKEA PKRDWGADED GEVSEEEELT 150
PFSLDPRGLQ EALSARIPLQ RALPEVRHPL CLQQHPQDSL PTASVILCFH 200
DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS ALSEYVARLE 250
GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 300
AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK 350
ALQSPISPIR SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA 400
WLCGGSVEIL PCSRVGHIYQ NQDSHSPLDQ EATLRNRVRI AETWLGSFKE 450
TFYKHSPEAF SLSKAEKPDC MERLQLQRRL GCRTFHWFLA NVYPELYPSE 500
PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR QQQYLQHTSR 550
KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS 600
GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER 639
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441V → D in CAD38585. 1 Publication
Sequence conflicti326 – 3261K → R in CAD89983. 1 Publication

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 595-631.
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.
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

ArrayExpressi Q8N3T1.
Bgeei Q8N3T1.
CleanExi HS_GALNTL2.
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: September 3, 2014
This is version 107 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 (1 Publication) termed Galnt15/pp-GaNTase 15.

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

Similar proteinsi