Skip Header

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

Q8N428

- GLT16_HUMAN

UniProt

Q8N428 - GLT16_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 16

Gene

GALNT16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.1 Publication

Catalytic activityi

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

Cofactori

Mn2+By similarity

Kineticsi

  1. KM=251 µM for Muc5AC1 Publication
  2. KM=310 µM for Muc5AC-31 Publication
  3. KM=390 µM for Muc5AC-131 Publication
  4. KM=332 µM for EA21 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631SubstrateBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Metal bindingi213 – 2131ManganeseBy similarity
Binding sitei317 – 3171SubstrateBy similarity
Metal bindingi345 – 3451ManganeseBy similarity
Binding sitei348 – 3481SubstrateBy similarity
Binding sitei351 – 3511SubstrateBy similarity
Binding sitei353 – 3531SubstrateBy 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. protein glycosylation Source: UniProtKB-UniPathway
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 16 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 16
Short name:
GalNAc-T16
Polypeptide GalNAc transferase-like protein 1
Short name:
GalNAc-T-like protein 1
Short name:
pp-GaNTase-like protein 1
Polypeptide N-acetylgalactosaminyltransferase-like protein 1
Protein-UDP acetylgalactosaminyltransferase-like protein 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1
Gene namesi
Name:GALNT16
Synonyms:GALNTL1, KIAA1130
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:23233. GALNT16.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini27 – 558532LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. Golgi apparatus Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134991608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Polypeptide N-acetylgalactosaminyltransferase 16PRO_0000059135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi113 ↔ 340PROSITE-ProRule annotation
Disulfide bondi331 ↔ 409PROSITE-ProRule annotation
Disulfide bondi441 ↔ 460PROSITE-ProRule annotation
Disulfide bondi486 ↔ 506PROSITE-ProRule annotation
Disulfide bondi530 ↔ 543PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ8N428.
PaxDbiQ8N428.
PRIDEiQ8N428.

PTM databases

PhosphoSiteiQ8N428.

Expressioni

Gene expression databases

BgeeiQ8N428.
CleanExiHS_GALNTL1.
ExpressionAtlasiQ8N428. baseline and differential.
GenevestigatoriQ8N428.

Organism-specific databases

HPAiHPA059136.

Interactioni

Protein-protein interaction databases

BioGridi121524. 1 interaction.
STRINGi9606.ENSP00000336729.

Structurei

3D structure databases

ProteinModelPortaliQ8N428.
SMRiQ8N428. Positions 68-554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 555128Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 227106Catalytic subdomain AAdd
BLAST
Regioni286 – 34863Catalytic 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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8N428.
KOiK00710.
OMAiPEDCQLL.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8N428.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N428-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL
60 70 80 90 100
REDRTIPLIV TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS
110 120 130 140 150
PDRPIRDTRH YSCPSVSYSS DLPATSVIIT FHNEARSTLL RTVKSVLNRT
160 170 180 190 200
PANLIQEIIL VDDFSSDPED CLLLTRIPKV KCLRNDRREG LIRSRVRGAD
210 220 230 240 250
VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII DVISLDNFAY
260 270 280 290 300
LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID
310 320 330 340 350
KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR
360 370 380 390 400
HPYNFPEGNA LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR
410 420 430 440 450
IEQRKKMNCK SFRWYLENVY PELTVPVKEA LPGIIKQGVN CLESQGQNTA
460 470 480 490 500
GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI QQQGKCLAAT STLMSSPGSP
510 520 530 540 550
VILQMCNPRE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT SKCQADAQAQ

QWQLLPHT
Length:558
Mass (Da):63,074
Last modified:August 16, 2004 - v2
Checksum:iFF35C5606B5291B8
GO
Isoform 2 (identifier: Q8N428-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     514-558: KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT → VSLLASGPEAQQPEGPCLRVADLGRRAPD

Show »
Length:542
Mass (Da):60,972
Checksum:i1E517B517B2568A9
GO

Sequence cautioni

The sequence BAA86444.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011V → M.2 Publications
Corresponds to variant rs12879377 [ dbSNP | Ensembl ].
VAR_055848
Natural varianti497 – 4971P → S.
Corresponds to variant rs59840366 [ dbSNP | Ensembl ].
VAR_061195

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei514 – 55845KWRRK…LLPHT → VSLLASGPEAQQPEGPCLRV ADLGRRAPD in isoform 2. 2 PublicationsVSP_011231Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032956 mRNA. Translation: BAA86444.1. Different initiation.
AB078143 mRNA. Translation: BAD93178.1.
AK289745 mRNA. Translation: BAF82434.1.
CH471061 Genomic DNA. Translation: EAW80987.1.
BC036812 mRNA. Translation: AAH36812.2.
BC098578 mRNA. Translation: AAH98578.1.
CCDSiCCDS32107.1. [Q8N428-1]
RefSeqiNP_001161840.1. NM_001168368.1. [Q8N428-1]
NP_065743.2. NM_020692.2. [Q8N428-1]
UniGeneiHs.21035.

Genome annotation databases

EnsembliENST00000337827; ENSP00000336729; ENSG00000100626. [Q8N428-1]
ENST00000448469; ENSP00000402970; ENSG00000100626. [Q8N428-1]
ENST00000553471; ENSP00000451420; ENSG00000100626. [Q8N428-2]
ENST00000553669; ENSP00000451200; ENSG00000100626. [Q8N428-2]
GeneIDi57452.
KEGGihsa:57452.
UCSCiuc001xla.2. human.
uc001xlb.2. human. [Q8N428-1]

Polymorphism databases

DMDMi51316024.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032956 mRNA. Translation: BAA86444.1 . Different initiation.
AB078143 mRNA. Translation: BAD93178.1 .
AK289745 mRNA. Translation: BAF82434.1 .
CH471061 Genomic DNA. Translation: EAW80987.1 .
BC036812 mRNA. Translation: AAH36812.2 .
BC098578 mRNA. Translation: AAH98578.1 .
CCDSi CCDS32107.1. [Q8N428-1 ]
RefSeqi NP_001161840.1. NM_001168368.1. [Q8N428-1 ]
NP_065743.2. NM_020692.2. [Q8N428-1 ]
UniGenei Hs.21035.

3D structure databases

ProteinModelPortali Q8N428.
SMRi Q8N428. Positions 68-554.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121524. 1 interaction.
STRINGi 9606.ENSP00000336729.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8N428.

Polymorphism databases

DMDMi 51316024.

Proteomic databases

MaxQBi Q8N428.
PaxDbi Q8N428.
PRIDEi Q8N428.

Protocols and materials databases

DNASUi 57452.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337827 ; ENSP00000336729 ; ENSG00000100626 . [Q8N428-1 ]
ENST00000448469 ; ENSP00000402970 ; ENSG00000100626 . [Q8N428-1 ]
ENST00000553471 ; ENSP00000451420 ; ENSG00000100626 . [Q8N428-2 ]
ENST00000553669 ; ENSP00000451200 ; ENSG00000100626 . [Q8N428-2 ]
GeneIDi 57452.
KEGGi hsa:57452.
UCSCi uc001xla.2. human.
uc001xlb.2. human. [Q8N428-1 ]

Organism-specific databases

CTDi 57452.
GeneCardsi GC14P069725.
HGNCi HGNC:23233. GALNT16.
HPAi HPA059136.
neXtProti NX_Q8N428.
PharmGKBi PA134991608.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8N428.
KOi K00710.
OMAi PEDCQLL.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8N428.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii 57452.
NextBioi 63624.
PROi Q8N428.

Gene expression databases

Bgeei Q8N428.
CleanExi HS_GALNTL1.
ExpressionAtlasi Q8N428. baseline and differential.
Genevestigatori Q8N428.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
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. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Cloning and Characterization of New Member of Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, Designated GalNAc-T16."
    Guo J., Zhang Y., Chen L., Narimatsu H.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  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.
    , 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), VARIANT MET-201.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANT MET-201.
    Tissue: Brain and Chondrosarcoma.
  6. "UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree."
    Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.
    Glycobiology 22:768-777(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiGLT16_HUMAN
AccessioniPrimary (citable) accession number: Q8N428
Secondary accession number(s): Q4KMG3, Q58A55, Q9ULT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 26, 2014
This is version 114 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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