UDP-glucuronosyltransferase 2B15 precursor

Names and origin

Protein names

Recommended name:
    UDP-glucuronosyltransferase 2B15
      Short name=UDPGT 2B15
    EC=2.4.1.17
Alternative name(s):
    UDPGTh-3
    HLUG4

Gene names

Name:	UGT2B15
Synonyms:	UGT2B8

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	steroid metabolic process Ref.2 Traceable author statement. Source: ProtInc xenobiotic metabolic process Ref.2 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glucuronosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 530

507

UDP-glucuronosyltransferase 2B15

PRO_0000036039

Regions

Transmembrane

495 – 515

21

Potential

Amino acid modifications

Glycosylation

65

1

N-linked (GlcNAc...)

Glycosylation

316

1

N-linked (GlcNAc...) Potential

Glycosylation

483

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

85

1

D → Y: dbSNP rs1902023. Ref.3 Ref.6

VAR_007713

Natural variant

523

1

K → T: dbSNP rs4148269. Ref.1 Ref.3 Ref.2 Ref.8

VAR_018348

Experimental info

Sequence conflict

119

1

E → A in AAA83406. Ref.6

Sequence conflict

145

1

K → R in AAA83406. Ref.6

Sequence conflict

150 – 155

6

LADALN → PGDPVF in AAA83406. Ref.6

Sequence conflict

162

1

A → S in AAA83406. Ref.6

Sequence conflict

165

1

F → L in AAA83406. Ref.6

Sequence conflict

170 – 177

8

LYSLRFSV → VYRSRISR in AAA83406. Ref.6

Sequence conflict

181

1

F → I in AAA83406. Ref.6

Sequence conflict

203

1

S → I in AAA83406. Ref.6

Sequence conflict

293

1

M → L in AAA83406. Ref.6

Sequence conflict

401

1

H → D in AAA83406. Ref.6

Sequence conflict

443

1

V → A in AAA83406. Ref.6

Sequence conflict

501

1

C → W in AAA83406. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P54855-1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: E0DDA4B99687ECA6
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FASTA

530

60,988

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

        70         80         90        100        110        120 
STLVNASKSS AIKLEVYPTS LTKNDLEDSL 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

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References

	« Hide 'large scale' referencesShow '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: 8399210] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT 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: 7835232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 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: 9295060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TYR-85 AND 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. Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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. 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: 2116769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-530, PARTIAL PROTEIN SEQUENCE, VARIANT TYR-85. 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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65, MASS SPECTROMETRY. 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: 15618667] [Abstract] Cited for: VARIANT THR-523.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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.
IPI	IPI00008905.
PIR	A48633. S11309.
RefSeq	NP_001067.2.
UniGene	Hs.150207 Hs.714028
3D structure databases
SMR	P54855. Positions 286-447.
ModBase	Search...
Protein family/group databases
CAZy	GT1. Glycosyltransferase Family 1.
PTM databases
PhosphoSite	P54855.
Genome annotation databases
Ensembl	ENSG00000197592. Homo sapiens. [Contig view]
GeneID	7366.
KEGG	hsa:7366.
UCSC	uc003hed.1. human.
Organism-specific databases
GeneCards	GC04M069546. GC04M069561.
H-InvDB	HIX0031375. HIX0057366.
HGNC	HGNC:12546. UGT2B15.
MIM	600069. gene.
PharmGKB	PA37188.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P54855.
HOVERGEN	P54855.
Enzyme and pathway databases
BRENDA	2.4.1.17. 247.
Reactome	REACT_13433. Biological oxidations.
Gene expression databases
CleanEx	HS_UGT2B15.
GermOnline	ENSG00000197592. Homo sapiens.
Family and domain databases
InterPro	IPR002213. UDP_glucos_trans. [Graphical view]
PANTHER	PTHR11926. UDP_glucos_trans. 1 hit.
Pfam	PF00201. UDPGT. 1 hit. [Graphical view]
PROSITE	PS00375. UDPGT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	28842.
SOURCE	Search...

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Entry information

Entry name

UDB15_HUMAN

Accession

Primary (citable) accession number: P54855
Secondary accession number(s): A6NDX0

Q9UK63

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 3, 2007
Last modified:	July 7, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 4

Human chromosome 4: 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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents