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Protein

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase

Gene

Gcnt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine moiety onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. Mucin-type core 2 O-glycans play an important role in leukocyte extravasation as they serve as scaffolds for the display of the selectin ligand sialyl Lewis X by leukocytes.1 Publication

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R.

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei320 – 32011 Publication

GO - Molecular functioni

GO - Biological processi

  • cell adhesion molecule production Source: UniProtKB
  • glycoprotein biosynthetic process Source: UniProtKB
  • kidney morphogenesis Source: MGI
  • leukocyte tethering or rolling Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway
  • response to insulin Source: Ensembl
  • tissue morphogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.102. 3474.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT14. Glycosyltransferase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase (EC:2.4.1.102)
Alternative name(s):
Core 2-branching enzyme
Core2-GlcNAc-transferase
Short name:
C2GNT
Gene namesi
Name:Gcnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:95676. Gcnt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence analysis
Transmembranei10 – 3223Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini33 – 428396LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferasePRO_0000191396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...)1 Publication
Disulfide bondi59 ↔ 413
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
Disulfide bondi100 ↔ 172
Disulfide bondi151 ↔ 199
Disulfide bondi372 ↔ 381

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ09324.
PaxDbiQ09324.
PRIDEiQ09324.

PTM databases

iPTMnetiQ09324.
PhosphoSiteiQ09324.

Expressioni

Tissue specificityi

Expressed in kidney, liver, stomach, spleen, lung and brain.1 Publication

Gene expression databases

BgeeiQ09324.
CleanExiMM_GCNT1.
GenevisibleiQ09324. MM.

Interactioni

Subunit structurei

Interacts with GOLPH3; may control GCNT1 retention in the Golgi.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069023.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 635Combined sources
Helixi67 – 7812Combined sources
Helixi80 – 834Combined sources
Helixi90 – 967Combined sources
Helixi100 – 1078Combined sources
Helixi116 – 1194Combined sources
Beta strandi123 – 1297Combined sources
Helixi133 – 14311Combined sources
Beta strandi148 – 1547Combined sources
Helixi160 – 17112Combined sources
Beta strandi176 – 1783Combined sources
Helixi190 – 20617Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi221 – 2244Combined sources
Helixi226 – 23510Combined sources
Turni236 – 2383Combined sources
Beta strandi244 – 2463Combined sources
Helixi249 – 2513Combined sources
Helixi253 – 2564Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi290 – 2923Combined sources
Helixi293 – 3019Combined sources
Helixi303 – 31210Combined sources
Beta strandi315 – 3173Combined sources
Helixi318 – 3203Combined sources
Helixi322 – 3265Combined sources
Helixi340 – 3423Combined sources
Turni346 – 3483Combined sources
Beta strandi349 – 3546Combined sources
Turni357 – 3593Combined sources
Helixi363 – 3653Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi380 – 3823Combined sources
Helixi385 – 3873Combined sources
Helixi388 – 3914Combined sources
Beta strandi397 – 4004Combined sources
Turni404 – 4063Combined sources
Helixi408 – 42316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GAKX-ray2.00A/B38-428[»]
2GAMX-ray2.70A/B/C/D38-428[»]
3OTKX-ray2.30A/B/C/D38-428[»]
ProteinModelPortaliQ09324.
SMRiQ09324. Positions 56-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09324.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 95Mediates interaction with GOLPH3 and is necessary and sufficient for localization to the GolgiBy similarity
Regioni33 – 12189Stem regionAdd
BLAST
Regioni122 – 428307CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 14 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0799. Eukaryota.
ENOG410XQ7M. LUCA.
GeneTreeiENSGT00760000119183.
HOGENOMiHOG000293251.
HOVERGENiHBG051711.
InParanoidiQ09324.
KOiK00727.
OMAiGIHVRSV.

Family and domain databases

InterProiIPR003406. Glyco_trans_14.
[Graphical view]
PfamiPF02485. Branch. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRNLFRRRL FSCPTKYYFM LLVLSLITFS VLRIHQKPEF FSVRHLELAG
60 70 80 90 100
DDPYSNVNCT KILQGDPEEI QKVKLEILTV QFKKRPRRTP HDYINMTRDC
110 120 130 140 150
ASFIRTRKYI VEPLTKEEVG FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY
160 170 180 190 200
CIHVDRKAEE SFLAAVQGIA SCFDNVFVAS QLESVVYASW SRVKADLNCM
210 220 230 240 250
KDLYRMNANW KYLINLCGMD FPIKTNLEIV RKLKCSTGEN NLETEKMPPN
260 270 280 290 300
KEERWKKRYT VVDGKLTNTG IVKAPPPLKT PLFSGSAYFV VTREYVGYVL
310 320 330 340 350
ENENIQKLME WAQDTYSPDE FLWATIQRIP EVPGSFPSSN KYDLSDMNAI
360 370 380 390 400
ARFVKWQYFE GHVSNGAPYP PCSGVHVRSV CVFGAGDLSW MLRQHHLFAN
410 420
KFDMDVDPFA IQCLDEHLRH KALENLEH
Length:428
Mass (Da):49,839
Last modified:July 27, 2011 - v2
Checksum:i57E54F07AFFE640B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881R → W in AAA60948 (Ref. 1) Curated
Sequence conflicti88 – 881R → W in BAA22998 (PubMed:9341170).Curated
Sequence conflicti88 – 881R → W in BAA22999 (PubMed:9341170).Curated
Sequence conflicti191 – 1911S → T in AAA60948 (Ref. 1) Curated
Sequence conflicti238 – 2381G → A in BAA22998 (PubMed:9341170).Curated
Sequence conflicti238 – 2381G → A in BAA22999 (PubMed:9341170).Curated
Sequence conflicti260 – 2601T → A in AAA60948 (Ref. 1) Curated
Sequence conflicti260 – 2601T → A in BAA22998 (PubMed:9341170).Curated
Sequence conflicti260 – 2601T → A in BAA22999 (PubMed:9341170).Curated
Sequence conflicti362 – 3621H → D in AAA60948 (Ref. 1) Curated
Sequence conflicti362 – 3621H → D in BAA22998 (PubMed:9341170).Curated
Sequence conflicti362 – 3621H → D in BAA22999 (PubMed:9341170).Curated
Sequence conflicti404 – 4041M → I in BAA22998 (PubMed:9341170).Curated
Sequence conflicti404 – 4041M → I in BAA22999 (PubMed:9341170).Curated
Sequence conflicti420 – 4201H → R in AAA60948 (Ref. 1) Curated
Sequence conflicti420 – 4201H → R in BAA22998 (PubMed:9341170).Curated
Sequence conflicti420 – 4201H → R in BAA22999 (PubMed:9341170).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19265 mRNA. Translation: AAA60948.1.
D87332 mRNA. Translation: BAA22998.1.
D87333 mRNA. Translation: BAA22999.1.
AK045216 mRNA. Translation: BAC32265.1.
CCDSiCCDS29687.1.
RefSeqiNP_001129956.3. NM_001136484.3.
NP_034395.4. NM_010265.5.
NP_775618.3. NM_173442.5.
UniGeneiMm.244825.

Genome annotation databases

EnsembliENSMUST00000169897; ENSMUSP00000127835; ENSMUSG00000038843.
ENSMUST00000174236; ENSMUSP00000133935; ENSMUSG00000038843.
GeneIDi14537.
KEGGimmu:14537.
UCSCiuc008gxm.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

core 2 beta 6 GlcNAc T1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19265 mRNA. Translation: AAA60948.1.
D87332 mRNA. Translation: BAA22998.1.
D87333 mRNA. Translation: BAA22999.1.
AK045216 mRNA. Translation: BAC32265.1.
CCDSiCCDS29687.1.
RefSeqiNP_001129956.3. NM_001136484.3.
NP_034395.4. NM_010265.5.
NP_775618.3. NM_173442.5.
UniGeneiMm.244825.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GAKX-ray2.00A/B38-428[»]
2GAMX-ray2.70A/B/C/D38-428[»]
3OTKX-ray2.30A/B/C/D38-428[»]
ProteinModelPortaliQ09324.
SMRiQ09324. Positions 56-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069023.

Protein family/group databases

CAZyiGT14. Glycosyltransferase Family 14.

PTM databases

iPTMnetiQ09324.
PhosphoSiteiQ09324.

Proteomic databases

MaxQBiQ09324.
PaxDbiQ09324.
PRIDEiQ09324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000169897; ENSMUSP00000127835; ENSMUSG00000038843.
ENSMUST00000174236; ENSMUSP00000133935; ENSMUSG00000038843.
GeneIDi14537.
KEGGimmu:14537.
UCSCiuc008gxm.2. mouse.

Organism-specific databases

CTDi2650.
MGIiMGI:95676. Gcnt1.

Phylogenomic databases

eggNOGiKOG0799. Eukaryota.
ENOG410XQ7M. LUCA.
GeneTreeiENSGT00760000119183.
HOGENOMiHOG000293251.
HOVERGENiHBG051711.
InParanoidiQ09324.
KOiK00727.
OMAiGIHVRSV.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.102. 3474.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGcnt1. mouse.
EvolutionaryTraceiQ09324.
PROiQ09324.
SOURCEiSearch...

Gene expression databases

BgeeiQ09324.
CleanExiMM_GCNT1.
GenevisibleiQ09324. MM.

Family and domain databases

InterProiIPR003406. Glyco_trans_14.
[Graphical view]
PfamiPF02485. Branch. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Warren C.E., Smookler D.S., Dennis J.W.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2J.
  2. "Tissue-specific regulation of mouse core 2 beta-1,6-N-acetylglucosaminyltransferase."
    Sekine M., Nara K., Suzuki A.
    J. Biol. Chem. 272:27246-27252(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Kidney and Submandibular gland.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-GlcNAc transferase from mouse kidney."
    Sekine M., Hashimoto Y., Suzuki M., Inagaki F., Takio K., Suzuki A.
    J. Biol. Chem. 269:31143-31148(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 62-72; 109-116; 225-232 AND 258-265, FUNCTION.
    Tissue: Kidney.
  5. "Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity."
    Yen T.Y., Macher B.A., Bryson S., Chang X., Tvaroska I., Tse R., Takeshita S., Lew A.M., Datti A.
    J. Biol. Chem. 278:45864-45881(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Pancreas.
  7. "X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism."
    Pak J.E., Arnoux P., Zhou S., Sivarajah P., Satkunarajah M., Xing X., Rini J.M.
    J. Biol. Chem. 281:26693-26701(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-428 ALONE AND IN COMPLEX WITH GALBETA1-3GALNAC, DISULFIDE BOND, ACTIVE SITE, GLYCOSYLATION AT ASN-58 AND ASN-95.

Entry informationi

Entry nameiGCNT1_MOUSE
AccessioniPrimary (citable) accession number: Q09324
Secondary accession number(s): O35981, Q8BRB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.