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Q9NS00 (C1GLT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1

EC=2.4.1.122
Alternative name(s):
B3Gal-T8
Core 1 O-glycan T-synthase
Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1
Short name=Beta-1,3-galactosyltransferase
Core 1 beta1,3-galactosyltransferase 1
Short name=C1GalT1
Short name=Core 1 beta3-Gal-T1
Gene names
Name:C1GALT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Catalytic activity

UDP-alpha-D-galactose + glycoprotein N-acetyl-D-galactosamine = UDP + glycoprotein D-galactosyl-(1->3)-N-acetyl-D-galactosamine. Ref.1

Cofactor

Magnesium By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; disulfide-linked By similarity. Interacts with the C1GALT1C1 chaperone; required for galactosyltransferase activity. Ref.6

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Widely expressed. Highly expressed in kidney, heart, placenta and liver. Ref.1

Miscellaneous

Aberrant O-galactosylation of IgA1 molecules plays a role in the development and progression of IgA nephropathy (IgAN). Genetic interactions of C1GALT1 and ST6GALNAC2 variants influence IgA1 O-glycosylation, disease predisposition, and disease severity, and may contribute to the polygenic nature of IgAN.

Sequence similarities

Belongs to the glycosyltransferase 31 family. Beta3-Gal-T subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C1GALT1C1Q96EU74EBI-8628584,EBI-2837343

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NS00-1)

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.
Isoform 2 (identifier: Q9NS00-2)

The sequence of this isoform differs from the canonical sequence as follows:
     297-363: GPGCCSDLAV...EDTKVKLGNP → VSLEILLLCQYLD
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 363362Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
PRO_0000285064

Regions

Topological domain2 – 65Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 363334Lumenal Potential

Amino acid modifications

Modified residue2351Phosphoserine By similarity

Natural variations

Alternative sequence297 – 36367GPGCC…KLGNP → VSLEILLLCQYLD in isoform 2.
VSP_024809

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 01F472B55C5F526F

FASTA36342,203
        10         20         30         40         50         60 
MASKSWLNFL TFLCGSAIGF LLCSQLFSIL LGEKVDTQPN VLHNDPHARH SDDNGQNHLE 

        70         80         90        100        110        120 
GQMNFNADSS QHKDENTDIA ENLYQKVRIL CWVMTGPQNL EKKAKHVKAT WAQRCNKVLF 

       130        140        150        160        170        180 
MSSEENKDFP AVGLKTKEGR DQLYWKTIKA FQYVHEHYLE DADWFLKADD DTYVILDNLR 

       190        200        210        220        230        240 
WLLSKYDPEE PIYFGRRFKP YVKQGYMSGG AGYVLSKEAL KRFVDAFKTD KCTHSSSIED 

       250        260        270        280        290        300 
LALGRCMEIM NVEAGDSRDT IGKETFHPFV PEHHLIKGYL PRTFWYWNYN YYPPVEGPGC 

       310        320        330        340        350        360 
CSDLAVSFHY VDSTTMYELE YLVYHLRPYG YLYRYQPTLP ERILKEISQA NKNEDTKVKL 


GNP 

« Hide

Isoform 2 [UniParc].

Checksum: 8FF6B139ED96421D
Show »

FASTA30935,935

References

« Hide 'large scale' references
[1]"Cloning and expression of human core 1 beta1,3-galactosyltransferase."
Ju T., Brewer K., D'Souza A., Cummings R.D., Canfield W.M.
J. Biol. Chem. 277:178-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
[2]"Cloning and expression of a novel beta-1,3-galactosyltransferase."
Jensen M.P.A.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
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] OF 79-363 (ISOFORM 1).
Tissue: Kidney.
[6]"A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase."
Ju T., Cummings R.D.
Proc. Natl. Acad. Sci. U.S.A. 99:16613-16618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C1GALT1C1.
[7]"Variants of C1GALT1 gene are associated with the genetic susceptibility to IgA nephropathy."
Li G.-S., Zhang H., Lv J.-C., Shen Y., Wang H.-Y.
Kidney Int. 71:448-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IGA NEPHROPATHY.
[8]"Interaction between variants of two glycosyltransferase genes in IgA nephropathy."
Zhu L., Tang W., Li G., Lv J., Ding J., Yu L., Zhao M., Li Y., Zhang X., Shen Y., Zhang H., Wang H.
Kidney Int. 76:190-198(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IGA NEPHROPATHY.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Core1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155582 mRNA. Translation: AAF81981.1.
AJ132443 mRNA. Translation: CAC45046.1.
AJ278960 mRNA. Translation: CAC82373.1.
AJ243256 mRNA. Translation: CAC80435.1.
AC005532 Genomic DNA. Translation: AAQ96887.1.
CH236948 Genomic DNA. Translation: EAL24308.1.
BC003174 mRNA. Translation: AAH03174.1.
RefSeqNP_064541.1. NM_020156.4.
XP_005249870.1. XM_005249813.1.
UniGeneHs.239666.

3D structure databases

ProteinModelPortalQ9NS00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121241. 3 interactions.
IntActQ9NS00. 1 interaction.
MINTMINT-2819104.
STRING9606.ENSP00000223122.

Chemistry

ChEMBLCHEMBL2321633.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteQ9NS00.

Polymorphism databases

DMDM74719147.

Proteomic databases

PaxDbQ9NS00.
PeptideAtlasQ9NS00.
PRIDEQ9NS00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223122; ENSP00000223122; ENSG00000106392. [Q9NS00-1]
ENST00000402468; ENSP00000384550; ENSG00000106392. [Q9NS00-2]
ENST00000436587; ENSP00000389176; ENSG00000106392. [Q9NS00-1]
GeneID56913.
KEGGhsa:56913.
UCSCuc003sra.4. human. [Q9NS00-1]
uc010kto.2. human. [Q9NS00-2]

Organism-specific databases

CTD56913.
GeneCardsGC07P007196.
HGNCHGNC:24337. C1GALT1.
HPAHPA011294.
HPA012819.
MIM610555. gene.
neXtProtNX_Q9NS00.
PharmGKBPA134971259.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254346.
HOGENOMHOG000021316.
HOVERGENHBG097900.
InParanoidQ9NS00.
KOK00731.
OMATTGKETF.
PhylomeDBQ9NS00.
TreeFamTF317293.

Enzyme and pathway databases

BRENDA2.4.1.122. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9NS00.
BgeeQ9NS00.
CleanExHS_C1GALT1.
GenevestigatorQ9NS00.

Family and domain databases

InterProIPR026842. C1GALT1.
IPR003378. Fringe-like.
[Graphical view]
PANTHERPTHR23033:SF1. PTHR23033:SF1. 1 hit.
PfamPF02434. Fringe. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi56913.
NextBio62395.
PROQ9NS00.
SOURCESearch...

Entry information

Entry nameC1GLT_HUMAN
AccessionPrimary (citable) accession number: Q9NS00
Secondary accession number(s): Q96QH4, Q9BTU1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 88 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM