Reviewed, UniProtKB/Swiss-Prot P16662 (UD2B7_HUMAN)

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
    UDPGTh-2

Gene names

Name:	UGT2B7
Synonyms:	UGTB2B9

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

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. 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.
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.
Sequence similarities	Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	lipid metabolic process Ref.1 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...

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

Potential

Amino acid modifications

Glycosylation

67

1

N-linked (GlcNAc...) Potential

Glycosylation

68

1

N-linked (GlcNAc...)

Glycosylation

315

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

71

1

A → S: dbSNP rs12233719.

VAR_057327

Natural variant

268

1

H → Y in allele UGT2B7*2. dbSNP rs7439366. Ref.2 Ref.3 Ref.4 Ref.5 Ref.7

VAR_012342

Natural variant

378

1

N → S: dbSNP rs35590824.

VAR_057328

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

Turn

448 – 450

3

Sequences

	Sequence		Length	Mass (Da)
	P16662-1 [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: 2159463] [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: 14702039] [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: 15815621] [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: 15489334] [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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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: 11186130] [Abstract] Cited for: VARIANT UGT2B7*2 TYR-268.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.654424

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein family/group databases

CAZy

GT1. Glycosyltransferase Family 1.

Proteomic databases

PRIDE

P16662.

Genome annotation databases

Ensembl

ENSG00000171234. Homo sapiens. [Contig view]

GeneID

7364.

KEGG

hsa:7364.

Organism-specific databases

GeneCards

GC04P070010.

H-InvDB

HIX0004256.

HGNC

HGNC:12554. UGT2B7.

MIM

600068. gene.

PharmGKB

PA361.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P16662.

HOVERGEN

P16662.

Enzyme and pathway databases

BRENDA

2.4.1.17. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

P16662.

Bgee

P16662.

CleanEx

HS_UGT2B7.

GermOnline

ENSG00000171234. 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

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:	July 7, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)