P16662 (UD2B7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glucuronosyltransferase 2B7
Short name=UDPGT 2B7
EC=2.4.1.17

Alternative name(s):
3,4-catechol estrogen-specific UDPGT
UDP-glucuronosyltransferase 2B9
Short name=UDPGT 2B9
UDPGTh-2

Gene names

Name:	UGT2B7
Synonyms:	UGTB2B9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Ref.7 Its unique specificity for 3,4-catechol estrogens and estriol suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites. Is also active with androsterone, hyodeoxycholic acid and tetrachlorocatechol (in vitro). Ref.7
Catalytic activity	UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside. Ref.7
Subcellular location	Microsome membrane; Single-pass membrane protein Potential. Endoplasmic reticulum membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen metabolic process Inferred from direct assay Ref.7. Source: UniProtKB cellular glucuronidation Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	glucuronosyltransferase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

By similarity

Chain

24 – 529

506

UDP-glucuronosyltransferase 2B7

PRO_0000036031

Regions

Transmembrane

493 – 509

17

Helical; Potential

Nucleotide binding

373 – 379

7

UDP-glucuronic acid Probable

Sites

Binding site

398

1

UDP-glucuronic acid Probable

Amino acid modifications

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

68

1

N-linked (GlcNAc...) Ref.6

Glycosylation

315

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

71

1

A → S.
Corresponds to variant rs12233719 [ dbSNP | Ensembl ].

VAR_057327

Natural variant

268

1

H → Y in allele UGT2B7*2. Ref.2 Ref.3 Ref.4 Ref.5 Ref.8
Corresponds to variant rs7439366 [ dbSNP | Ensembl ].

VAR_012342

Natural variant

378

1

N → S.
Corresponds to variant rs35590824 [ dbSNP | Ensembl ].

VAR_057328

Experimental info

Mutagenesis

15

1

S → A: Almost abolishes enzyme activity. Ref.7

Mutagenesis

35

1

H → A: Almost abolishes enzyme activity. Ref.7

Mutagenesis

151

1

D → A: Almost abolishes enzyme activity. Ref.7

Mutagenesis

373

1

T → V: Almost abolishes enzyme activity. Ref.7

Mutagenesis

374

1

H → A: Almost abolishes enzyme activity. Ref.7

Mutagenesis

378

1

N → A: Strongly reduced enzyme activity. Ref.7

Mutagenesis

379

1

G → D: Almost abolishes enzyme activity. Ref.7

Mutagenesis

398

1

D → A or N: Almost abolishes enzyme activity. Ref.7

Mutagenesis

399

1

Q → A: Abolishes enzyme activity. Ref.7

Secondary structure

1

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529

Helix Strand Turn

Details...

Helix

290 – 297

8

Turn

298 – 302

5

Beta strand

304 – 308

5

Helix

318 – 328

11

Beta strand

331 – 338

8

Beta strand

351 – 356

6

Helix

359 – 363

5

Beta strand

368 – 373

6

Helix

377 – 386

10

Beta strand

390 – 392

3

Helix

399 – 407

9

Turn

408 – 410

3

Beta strand

411 – 414

4

Turn

417 – 419

3

Helix

422 – 434

13

Helix

436 – 445

10

Sequences

	Sequence		Length	Mass (Da)
	P16662 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 94B1CA6CE92F1446	FASTA	529	60,695
	10 20 30 40 50 60 MSVKWTSVIL LIQLSFCFSS GNCGKVLVWA AEYSHWMNIK TILDELIQRG HEVTVLASSA 70 80 90 100 110 120 SILFDPNNSS ALKIEIYPTS LTKTELENFI MQQIKRWSDL PKDTFWLYFS QVQEIMSIFG 130 140 150 160 170 180 DITRKFCKDV VSNKKFMKKV QESRFDVIFA DAIFPCSELL AELFNIPFVY SLSFSPGYTF 190 200 210 220 230 240 EKHSGGFIFP PSYVPVVMSE LTDQMTFMER VKNMIYVLYF DFWFEIFDMK KWDQFYSEVL 250 260 270 280 290 300 GRPTTLSETM GKADVWLIRN SWNFQFPHPL LPNVDFVGGL HCKPAKPLPK EMEDFVQSSG 310 320 330 340 350 360 ENGVVVFSLG SMVSNMTEER ANVIASALAQ IPQKVLWRFD GNKPDTLGLN TRLYKWIPQN 370 380 390 400 410 420 DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGIPLFADQP DNIAHMKARG AAVRVDFNTM 430 440 450 460 470 480 SSTDLLNALK RVINDPSYKE NVMKLSRIQH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA 490 500 510 520 HDLTWFQYHS LDVIGFLLVC VATVIFIVTK CCLFCFWKFA RKAKKGKND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates." Ritter J.K., Sheen Y.Y., Owens I.S. J. Biol. Chem. 265:7900-7906(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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], VARIANT TYR-268. Tissue: Kidney.
[3]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-268. Tissue: Kidney.
[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. , 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], VARIANT TYR-268.
[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], VARIANT TYR-268. Tissue: Kidney.
[6]	"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-68, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7." Miley M.J., Zielinska A.K., Keenan J.E., Bratton S.M., Radominska-Pandya A., Redinbo M.R. J. Mol. Biol. 369:498-511(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 285-451, CATALYTIC ACTIVITY, FUNCTION TOWARDS STEROIDS, MUTAGENESIS OF SER-15; HIS-35; ASP-151; THR-373; HIS-374; ASN-378; GLY-379; ASP-398 AND GLN-399.
[8]	"Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance." Bhasker C.R., McKinnon W., Stone A., Lo A.C., Kubota T., Ishizaki T., Miners J.O. Pharmacogenetics 10:679-685(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT UGT2B7*2 TYR-268.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05428 mRNA. Translation: AAA36793.1.
AK313190 mRNA. Translation: BAG36007.1.
AK223142 mRNA. Translation: BAD96862.1.
AC111000 Genomic DNA. Translation: AAY41045.1.
BC030974 mRNA. Translation: AAH30974.1.

IPI

IPI00029784.

PIR

A35366.

RefSeq

NP_001065.2. NM_001074.2.

UniGene

Hs.654424.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O6L	X-ray	1.80	A/B	285-451	[»]

ProteinModelPortal

P16662.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16662. 1 interaction.

STRING

9606.ENSP00000304811.

Protein family/group databases

CAZy

GT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSite

P16662.

Polymorphism databases

DMDM

136727.

Proteomic databases

PaxDb

P16662.

PRIDE

P16662.

Protocols and materials databases

DNASU

7364.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000305231; ENSP00000304811; ENSG00000171234.

GeneID

7364.

KEGG

hsa:7364.

UCSC

uc003heg.4. human.

Organism-specific databases

CTD

7364.

GeneCards

GC04P069917.

HGNC

HGNC:12554. UGT2B7.

MIM

600068. gene.

neXtProt

NX_P16662.

PharmGKB

PA361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1819.

HOGENOM

HOG000220831.

HOVERGEN

HBG004033.

InParanoid

P16662.

KO

K00699.

Enzyme and pathway databases

BioCyc

MetaCyc:HS10272-MONOMER.

BRENDA

2.4.1.17. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P16662.

Gene expression databases

ArrayExpress

P16662.

Bgee

P16662.

CleanEx

HS_UGT2B7.

Genevestigator

P16662.

GermOnline

ENSG00000171234. Homo sapiens.

Family and domain databases

InterPro

IPR002213. UDP_glucos_trans.
[Graphical view]

PANTHER

PTHR11926. PTHR11926. 1 hit.

Pfam

PF00201. UDPGT. 1 hit.
[Graphical view]

PROSITE

PS00375. UDPGT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16662.

ChEMBL

CHEMBL4370.

EvolutionaryTrace

P16662.

GenomeRNAi

7364.

NextBio

28832.

SOURCE

Search...

Entry information

Entry name

UD2B7_HUMAN

Accession

Primary (citable) accession number: P16662
Secondary accession number(s): B2R810, Q6GTW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.