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Protein

UDP-glucuronosyltransferase 2A3

Gene

UGT2A3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

  • glucuronosyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.17. 2681.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronosyltransferase 2A3 (EC:2.4.1.17)
Short name:
UDPGT 2A3
Gene namesi
Name:UGT2A3
ORF Names:UNQ2559/PRO6239
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:28528. UGT2A3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 491468ExtracellularSequence AnalysisAdd
BLAST
Transmembranei492 – 51221HelicalSequence AnalysisAdd
BLAST
Topological domaini513 – 52715CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670641.

Polymorphism and mutation databases

BioMutaiUGT2A3.
DMDMi296452855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 527504UDP-glucuronosyltransferase 2A3PRO_0000299146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6UWM9.
PaxDbiQ6UWM9.
PRIDEiQ6UWM9.

PTM databases

PhosphoSiteiQ6UWM9.

Expressioni

Gene expression databases

BgeeiQ6UWM9.
CleanExiHS_UGT2A3.
ExpressionAtlasiQ6UWM9. baseline and differential.
GenevisibleiQ6UWM9. HS.

Organism-specific databases

HPAiHPA045108.

Interactioni

Protein-protein interaction databases

BioGridi122896. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ6UWM9.
SMRiQ6UWM9. Positions 283-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1819.
GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220831.
HOVERGENiHBG004033.
InParanoidiQ6UWM9.
KOiK00699.
OMAiCESFIYN.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ6UWM9.
TreeFamiTF315472.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UWM9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSDKSALVF LLLQLFCVGC GFCGKVLVWP CDMSHWLNVK VILEELIVRG
60 70 80 90 100
HEVTVLTHSK PSLIDYRKPS ALKFEVVHMP QDRTEENEIF VDLALNVLPG
110 120 130 140 150
LSTWQSVIKL NDFFVEIRGT LKMMCESFIY NQTLMKKLQE TNYDVMLIDP
160 170 180 190 200
VIPCGDLMAE LLAVPFVLTL RISVGGNMER SCGKLPAPLS YVPVPMTGLT
210 220 230 240 250
DRMTFLERVK NSMLSVLFHF WIQDYDYHFW EEFYSKALGR PTTLCETVGK
260 270 280 290 300
AEIWLIRTYW DFEFPQPYQP NFEFVGGLHC KPAKALPKEM ENFVQSSGED
310 320 330 340 350
GIVVFSLGSL FQNVTEEKAN IIASALAQIP QKVLWRYKGK KPSTLGANTR
360 370 380 390 400
LYDWIPQNDL LGHPKTKAFI THGGMNGIYE AIYHGVPMVG VPIFGDQLDN
410 420 430 440 450
IAHMKAKGAA VEINFKTMTS EDLLRALRTV ITDSSYKENA MRLSRIHHDQ
460 470 480 490 500
PVKPLDRAVF WIEFVMRHKG AKHLRSAAHD LTWFQHYSID VIGFLLACVA
510 520
TAIFLFTKCF LFSCQKFNKT RKIEKRE
Length:527
Mass (Da):60,254
Last modified:May 18, 2010 - v2
Checksum:i801C8F886B4DF80F
GO

Sequence cautioni

The sequence BAB15179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti497 – 4971A → T in AAS48425 (Ref. 1) Curated
Sequence conflicti497 – 4971A → T in AAQ89089 (PubMed:12975309).Curated
Sequence conflicti497 – 4971A → T in AAI30534 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542891 mRNA. Translation: AAS48425.1.
AY358727 mRNA. Translation: AAQ89089.1.
AC021146 Genomic DNA. No translation available.
BC130533 mRNA. Translation: AAI30534.1.
AK025587 mRNA. Translation: BAB15179.1. Different initiation.
CCDSiCCDS3525.1.
RefSeqiNP_079019.3. NM_024743.3.
UniGeneiHs.122583.

Genome annotation databases

EnsembliENST00000251566; ENSP00000251566; ENSG00000135220.
ENST00000611042; ENSP00000479283; ENSG00000278216.
GeneIDi79799.
KEGGihsa:79799.
UCSCiuc003hef.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY542891 mRNA. Translation: AAS48425.1.
AY358727 mRNA. Translation: AAQ89089.1.
AC021146 Genomic DNA. No translation available.
BC130533 mRNA. Translation: AAI30534.1.
AK025587 mRNA. Translation: BAB15179.1. Different initiation.
CCDSiCCDS3525.1.
RefSeqiNP_079019.3. NM_024743.3.
UniGeneiHs.122583.

3D structure databases

ProteinModelPortaliQ6UWM9.
SMRiQ6UWM9. Positions 283-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122896. 2 interactions.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteiQ6UWM9.

Polymorphism and mutation databases

BioMutaiUGT2A3.
DMDMi296452855.

Proteomic databases

MaxQBiQ6UWM9.
PaxDbiQ6UWM9.
PRIDEiQ6UWM9.

Protocols and materials databases

DNASUi79799.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251566; ENSP00000251566; ENSG00000135220.
ENST00000611042; ENSP00000479283; ENSG00000278216.
GeneIDi79799.
KEGGihsa:79799.
UCSCiuc003hef.2. human.

Organism-specific databases

CTDi79799.
GeneCardsiGC04M069828.
H-InvDBHIX0163946.
HIX0164239.
HGNCiHGNC:28528. UGT2A3.
HPAiHPA045108.
MIMi616382. gene.
neXtProtiNX_Q6UWM9.
PharmGKBiPA142670641.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1819.
GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220831.
HOVERGENiHBG004033.
InParanoidiQ6UWM9.
KOiK00699.
OMAiCESFIYN.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ6UWM9.
TreeFamiTF315472.

Enzyme and pathway databases

BRENDAi2.4.1.17. 2681.

Miscellaneous databases

GenomeRNAii79799.
NextBioi69352.
PROiQ6UWM9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UWM9.
CleanExiHS_UGT2A3.
ExpressionAtlasiQ6UWM9. baseline and differential.
GenevisibleiQ6UWM9. HS.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of novel human UGTs."
    Court M.H.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "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] OF 56-527.

Entry informationi

Entry nameiUD2A3_HUMAN
AccessioniPrimary (citable) accession number: Q6UWM9
Secondary accession number(s): Q9H6S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 94 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.