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P54855 (UDB15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucuronosyltransferase 2B15

Short name=UDPGT 2B15
EC=2.4.1.17
Alternative name(s):
HLUG4
UDP-glucuronosyltransferase 2B8
Short name=UDPGT 2B8
UDPGTh-3
Gene names
Name:UGT2B15
Synonyms:UGT2B8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward several classes of xenobiotic substrates, including simple phenolic compounds, 7-hydroxylated coumarins, flavonoids, anthraquinones, and certain drugs and their hydroxylated metabolites. It also catalyzes the glucuronidation of endogenous estrogens and androgens.

Catalytic activity

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

Subcellular location

Microsome membrane; Single-pass membrane protein Potential. Endoplasmic reticulum membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in many tissues. Present in liver, prostate and testis. Ref.1

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Caution

Ref.6 thought that this was a separate form (UGT2B8). The name UGT2B8 has now been reused for a rat enzyme.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 530507UDP-glucuronosyltransferase 2B15
PRO_0000036039

Regions

Transmembrane495 – 51521Helical; Potential

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Ref.7
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential

Natural variations

Natural variant851Y → D. Ref.1 Ref.2
Corresponds to variant rs1902023 [ dbSNP | Ensembl ].
VAR_007713
Natural variant5231K → T. Ref.1 Ref.2 Ref.3 Ref.8
Corresponds to variant rs4148269 [ dbSNP | Ensembl ].
VAR_018348

Experimental info

Sequence conflict1191E → A in AAA83406. Ref.6
Sequence conflict1451K → R in AAA83406. Ref.6
Sequence conflict150 – 1556LADALN → PGDPVF in AAA83406. Ref.6
Sequence conflict1621A → S in AAA83406. Ref.6
Sequence conflict1651F → L in AAA83406. Ref.6
Sequence conflict170 – 1778LYSLRFSV → VYRSRISR in AAA83406. Ref.6
Sequence conflict1811F → I in AAA83406. Ref.6
Sequence conflict2031S → I in AAA83406. Ref.6
Sequence conflict2931M → L in AAA83406. Ref.6
Sequence conflict4011H → D in AAA83406. Ref.6
Sequence conflict4431V → A in AAA83406. Ref.6
Sequence conflict5011C → W in AAA83406. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P54855 [UniParc].

Last modified May 3, 2011. Version 3.
Checksum: EB2DAE838769C955

FASTA53061,036
        10         20         30         40         50         60 
MSLKWTSVFL LIQLSCYFSS GSCGKVLVWP TEYSHWINMK TILEELVQRG HEVTVLTSSA 

        70         80         90        100        110        120 
STLVNASKSS AIKLEVYPTS LTKNYLEDSL LKILDRWIYG VSKNTFWSYF SQLQELCWEY 

       130        140        150        160        170        180 
YDYSNKLCKD AVLNKKLMMK LQESKFDVIL ADALNPCGEL LAELFNIPFL YSLRFSVGYT 

       190        200        210        220        230        240 
FEKNGGGFLF PPSYVPVVMS ELSDQMIFME RIKNMIHMLY FDFWFQIYDL KKWDQFYSEV 

       250        260        270        280        290        300 
LGRPTTLFET MGKAEMWLIR TYWDFEFPRP FLPNVDFVGG LHCKPAKPLP KEMEEFVQSS 

       310        320        330        340        350        360 
GENGIVVFSL GSMISNMSEE SANMIASALA QIPQKVLWRF DGKKPNTLGS NTRLYKWLPQ 

       370        380        390        400        410        420 
NDLLGHPKTK AFITHGGTNG IYEAIYHGIP MVGIPLFADQ HDNIAHMKAK GAALSVDIRT 

       430        440        450        460        470        480 
MSSRDLLNAL KSVINDPVYK ENVMKLSRIH HDQPMKPLDR AVFWIEFVMR HKGAKHLRVA 

       490        500        510        520        530 
AHNLTWIQYH SLDVIAFLLA CVATVIFIIT KFCLFCFRKL AKKGKKKKRD 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a cloned human dihydrotestosterone/androstanediol UDP-glucuronosyltransferase and its comparison to other steroid isoforms."
Chen F., Ritter J.K., Wang M.G., McBride O.W., Lubet R.A., Owens I.S.
Biochemistry 32:10648-10657(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, VARIANTS ASP-85 AND THR-523.
Tissue: Liver.
[2]"Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) with activity toward steroid and xenobiotic substrates."
Green M.D., Oturu E.M., Tephly T.R.
Drug Metab. Dispos. 22:799-805(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-85 AND THR-523.
Tissue: Liver.
[3]"Isolation and characterization of UGT2B15(Y85): a UDP-glucuronosyltransferase encoded by a polymorphic gene."
Levesque E., Beaulieu M., Green M.D., Tephly T.R., Belanger A., Hum D.W.
Pharmacogenetics 7:317-325(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-523.
[4]"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. expand/collapse author list , 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].
[5]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].
[6]"Characterization and primary sequence of a human hepatic microsomal estriol UDPglucuronosyltransferase."
Coffman B.L., Tephly T.R., Irshaid Y.M., Green M.D., Smith C., Jackson M.R., Wooster R., Burchell B.
Arch. Biochem. Biophys. 281:170-175(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-530, PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65.
Tissue: Liver.
[8]"A major genotype in UDP-glucuronosyltransferase 2B15."
Toide K., Umeda S., Yamazaki H., Takahashi Y., Terauchi Y., Fujii T., Kamataki T.
Drug Metab. Pharmacokinet. 17:164-166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-523.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF548389 mRNA. Translation: AAN40695.1.
U08854 mRNA. Translation: AAC50077.1.
AF180322 mRNA. Translation: AAD55093.1.
AC019173 Genomic DNA. No translation available.
AC147055 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05574.1.
U06641 mRNA. Translation: AAA83406.1.
PIRA48633.
S11309.
RefSeqNP_001067.2. NM_001076.3.
UniGeneHs.150207.

3D structure databases

ProteinModelPortalP54855.
SMRP54855. Positions 286-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000341045.

Chemistry

ChEMBLCHEMBL6161.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteP54855.

Polymorphism databases

DMDM332278237.

Proteomic databases

PaxDbP54855.
PRIDEP54855.

Protocols and materials databases

DNASU7366.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338206; ENSP00000341045; ENSG00000196620.
GeneID7366.
KEGGhsa:7366.
UCSCuc021xow.1. human.

Organism-specific databases

CTD7366.
GeneCardsGC04M069561.
H-InvDBHIX0031375.
HIX0164240.
HGNCHGNC:12546. UGT2B15.
HPAHPA045108.
MIM600069. gene.
neXtProtNX_P54855.
PharmGKBPA37188.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1819.
HOGENOMHOG000220831.
HOVERGENHBG004033.
InParanoidP54855.
KOK00699.
OMAKEQSAMI.
OrthoDBEOG7GBFWS.
PhylomeDBP54855.
TreeFamTF315472.

Enzyme and pathway databases

BRENDA2.4.1.17. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP54855.

Gene expression databases

BgeeP54855.
CleanExHS_UGT2B15.
GenevestigatorP54855.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. PTHR11926. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUGT2B15.
GenomeRNAi7366.
NextBio28842.
PROP54855.
SOURCESearch...

Entry information

Entry nameUDB15_HUMAN
AccessionPrimary (citable) accession number: P54855
Secondary accession number(s): A6NDX0 expand/collapse secondary AC list , A6NNJ4, P23765, Q9UK63
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 128 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM