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Reviewed, UniProtKB/Swiss-Prot Q3SY77 (UD3A2_HUMAN)

Last modified July 7, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    UDP-glucuronosyltransferase 3A2
      Short name=UDPGT 3A2
    EC=2.4.1.17
Gene names
Name: UGT3A2
ORF Names: PSEC0073, UNQ842/PRO1780
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds By similarity.

Catalytic activity

UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucuronosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 523501UDP-glucuronosyltransferase 3A2
PRO_0000299153

Regions

Topological domain23 – 483461Extracellular Potential
Transmembrane484 – 50421 Potential
Topological domain505 – 52319Cytoplasmic Potential

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential

Natural variations

Natural variant741Y → N: dbSNP rs2197514.
VAR_057329
Natural variant5151R → H in a colorectal cancer sample; somatic mutation. Ref.4
VAR_036036

Experimental info

Sequence conflict2911G → E in BAC11583. Ref.2
Sequence conflict4861L → F in AAQ88782. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3SY77-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: DFE9CD92D1F5AF6F

FASTA52359,547
        10         20         30         40         50         60 
MAGQRVLLLV GFLLPGVLLS EAAKILTIST VGGSHYLLMD RVSQILQDHG HNVTMLNHKR 

        70         80         90        100        110        120 
GPFMPDFKKE EKSYQVISWL APEDHQREFK KSFDFFLEET LGGRGKFENL LNVLEYLALQ 

       130        140        150        160        170        180 
CSHFLNRKDI MDSLKNENFD MVIVETFDYC PFLIAEKLGK PFVAILSTSF GSLEFGLPIP 

       190        200        210        220        230        240 
LSYVPVFRSL LTDHMDFWGR VKNFLMFFSF CRRQQHMQST FDNTIKEHFT EGSRPVLSHL 

       250        260        270        280        290        300 
LLKAELWFIN SDFAFDFARP LLPNTVYVGG LMEKPIKPVP QDLENFIAKF GDSGFVLVTL 

       310        320        330        340        350        360 
GSMVNTCQNP EIFKEMNNAF AHLPQGVIWK CQCSHWPKDV HLAANVKIVD WLPQSDLLAH 

       370        380        390        400        410        420 
PSIRLFVTHG GQNSIMEAIQ HGVPMVGIPL FGDQPENMVR VEAKKFGVSI QLKKLKAETL 

       430        440        450        460        470        480 
ALKMKQIMED KRYKSAAVAA SVILRSHPLS PTQRLVGWID HVLQTGGATH LKPYVFQQPW 

       490        500        510        520 
HEQYLLDVFV FLLGLTLGTL WLCGKLLGMA VWWLRGARKV KET 

« Hide

References

[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-515.

Cross-references

Sequence databases

AY358416 mRNA. Translation: AAQ88782.1.
AK075383 mRNA. Translation: BAC11583.1.
BC103924 mRNA. Translation: AAI03925.1.
BC103925 mRNA. Translation: AAI03926.1.
IPIIPI00168291.
RefSeqNP_777574.1.
UniGeneHs.348941

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Proteomic databases

PRIDEQ3SY77.

Genome annotation databases

EnsemblENSG00000168671. Homo sapiens. [Contig view]
GeneID167127.
KEGGhsa:167127.
NMPDRfig|9606.3.peg.25144.
UCSCuc003jjz.1. human.

Organism-specific databases

GeneCardsGC05M036071.
HGNCHGNC:27266. UGT3A2.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ3SY77.
HOVERGENQ3SY77.
OMAQ3SY77. VISWLAP.

Enzyme and pathway databases

BRENDA2.4.1.17. 247.

Gene expression databases

ArrayExpressQ3SY77.
BgeeQ3SY77.
CleanExHS_UGT3A2.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. UDP_glucos_trans. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio88655.

Entry information

Entry nameUD3A2_HUMAN
AccessionPrimary (citable) accession number: Q3SY77
Secondary accession number(s): Q6UXC4, Q8NBP2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 11, 2005
Last modified: July 7, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

Human chromosome 5: 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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents