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Q02742 (GCNT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
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
Short name=Core 2 GNT
Gene names
Name:GCNT1
Synonyms:NACGT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Forms critical branches in O-glycans.

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein.

Tissue specificity

Highly expressed in activated T-lymphocytes and myeloid cells.

Sequence similarities

Belongs to the glycosyltransferase 14 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
PRO_0000191395

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3223Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 428396Lumenal Potential
Region33 – 12189Stem region By similarity
Region122 – 428307Catalytic By similarity

Sites

Active site3201 By similarity

Amino acid modifications

Modified residue2671Phosphothreonine By similarity
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation951N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 413 By similarity
Disulfide bond100 ↔ 172 By similarity
Disulfide bond151 ↔ 199 By similarity
Disulfide bond372 ↔ 381 By similarity

Natural variations

Natural variant1521I → V. Ref.1 Ref.2
Corresponds to variant rs2282683 [ dbSNP | Ensembl ].
VAR_048000
Natural variant1581S → C.
Corresponds to variant rs11546569 [ dbSNP | Ensembl ].
VAR_048001

Sequences

Sequence LengthMass (Da)Tools
Q02742 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 71D71A251874E1F0

FASTA42849,799
        10         20         30         40         50         60 
MLRTLLRRRL FSYPTKYYFM VLVLSLITFS VLRIHQKPEF VSVRHLELAG ENPSSDINCT 

        70         80         90        100        110        120 
KVLQGDVNEI QKVKLEILTV KFKKRPRWTP DDYINMTSDC SSFIKRRKYI VEPLSKEEAE 

       130        140        150        160        170        180 
FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDTKSED SYLAAVMGIA SCFSNVFVAS 

       190        200        210        220        230        240 
RLESVVYASW SRVQADLNCM KDLYAMSANW KYLINLCGMD FPIKTNLEIV RKLKLLMGEN 

       250        260        270        280        290        300 
NLETERMPSH KEERWKKRYE VVNGKLTNTG TVKMLPPLET PLFSGSAYFV VSREYVGYVL 

       310        320        330        340        350        360 
QNEKIQKLME WAQDTYSPDE YLWATIQRIP EVPGSLPASH KYDLSDMQAV ARFVKWQYFE 

       370        380        390        400        410        420 
GDVSKGAPYP PCDGVHVRSV CIFGAGDLNW MLRKHHLFAN KFDVDVDLFA IQCLDEHLRH 


KALETLKH 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of a cDNA encoding UDP-GlcNAc:Gal beta 1-3-GalNAc-R (GlcNAc to GalNAc) beta 1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen."
Bierhuizen M.F.A., Fukuda M.
Proc. Natl. Acad. Sci. U.S.A. 89:9326-9330(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-152.
[2]"Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family."
Bierhuizen M.F.A., Maemura K., Kudo S., Fukuda M.
Glycobiology 5:417-425(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-152.
Tissue: Placenta.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[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].
Tissue: Lung.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97347 mRNA. Translation: AAA35919.1.
L41415 Genomic DNA. Translation: AAA96661.1.
AL161626 Genomic DNA. Translation: CAI39746.1.
CH471089 Genomic DNA. Translation: EAW62580.1.
BC074885 mRNA. Translation: AAH74885.1.
BC074886 mRNA. Translation: AAH74886.1.
BC109101 mRNA. Translation: AAI09102.1.
BC109102 mRNA. Translation: AAI09103.1.
IPIIPI00295368.
PIRA46293.
RefSeqNP_001091102.1. NM_001097633.1.
NP_001091103.1. NM_001097634.1.
NP_001091104.1. NM_001097635.1.
NP_001091105.1. NM_001097636.1.
NP_001481.2. NM_001490.4.
UniGeneHs.521568.

3D structure databases

ProteinModelPortalQ02742.
SMRQ02742. Positions 56-424.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000365920.

Protein family/group databases

CAZyGT14. Glycosyltransferase Family 14.

PTM databases

PhosphoSiteQ02742.

Polymorphism databases

DMDM218512053.

Proteomic databases

PaxDbQ02742.
PRIDEQ02742.

Protocols and materials databases

DNASU2650.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376730; ENSP00000365920; ENSG00000187210.
ENST00000442371; ENSP00000415454; ENSG00000187210.
ENST00000444201; ENSP00000390703; ENSG00000187210.
ENST00000536223; ENSP00000440883; ENSG00000187210.
GeneID2650.
KEGGhsa:2650.
UCSCuc004akf.4. human.

Organism-specific databases

CTD2650.
GeneCardsGC09P079035.
H-InvDBHIX0008111.
HGNCHGNC:4203. GCNT1.
HPAHPA031151.
MIM600391. gene.
neXtProtNX_Q02742.
PharmGKBPA168.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253565.
HOGENOMHOG000293251.
HOVERGENHBG051711.
InParanoidQ02742.
KOK00727.
OMAYDYINMT.
OrthoDBEOG4W0XDC.
PhylomeDBQ02742.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

BgeeQ02742.
CleanExHS_GCNT1.
GenevestigatorQ02742.
GermOnlineENSG00000187210. Homo sapiens.

Family and domain databases

InterProIPR003406. Glyco_trans_14.
[Graphical view]
PfamPF02485. Branch. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi2650.
NextBio10460.
SOURCESearch...

Entry information

Entry nameGCNT1_HUMAN
AccessionPrimary (citable) accession number: Q02742
Secondary accession number(s): Q6DJZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 16, 2008
Last modified: April 3, 2013
This is version 114 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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families