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P16662

- UD2B7_HUMAN

UniProt

P16662 - UD2B7_HUMAN

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Protein

UDP-glucuronosyltransferase 2B7

Gene

UGT2B7

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

Functioni

UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.1 Publication
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).1 Publication

Catalytic activityi

UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei398 – 3981UDP-glucuronic acidCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi373 – 3797UDP-glucuronic acidCurated

GO - Molecular functioni

  1. glucuronosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. androgen metabolic process Source: UniProtKB
  2. cellular glucuronidation Source: UniProtKB
  3. lipid metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS10272-MONOMER.
BRENDAi2.4.1.17. 2681.
ReactomeiREACT_6784. Glucuronidation.
SABIO-RKP16662.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronosyltransferase 2B7 (EC:2.4.1.17)
Short name:
UDPGT 2B7
Alternative name(s):
3,4-catechol estrogen-specific UDPGT
UDP-glucuronosyltransferase 2B9
Short name:
UDPGT 2B9
UDPGTh-2
Gene namesi
Name:UGT2B7
Synonyms:UGTB2B9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:12554. UGT2B7.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151S → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi35 – 351H → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi151 – 1511D → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi373 – 3731T → V: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi374 – 3741H → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi378 – 3781N → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi379 – 3791G → D: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi398 – 3981D → A or N: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi399 – 3991Q → A: Abolishes enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA361.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323By similarityAdd
BLAST
Chaini24 – 529506UDP-glucuronosyltransferase 2B7PRO_0000036031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi68 – 681N-linked (GlcNAc...)1 Publication
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP16662.
PaxDbiP16662.
PRIDEiP16662.

PTM databases

PhosphoSiteiP16662.

Expressioni

Gene expression databases

BgeeiP16662.
CleanExiHS_UGT2B7.
ExpressionAtlasiP16662. baseline and differential.
GenevestigatoriP16662.

Interactioni

Protein-protein interaction databases

BioGridi113211. 1 interaction.
IntActiP16662. 1 interaction.
STRINGi9606.ENSP00000304811.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi290 – 2978
Turni298 – 3025
Beta strandi304 – 3085
Helixi318 – 32811
Beta strandi331 – 3388
Beta strandi351 – 3566
Helixi359 – 3635
Beta strandi368 – 3736
Helixi377 – 38610
Beta strandi390 – 3923
Helixi399 – 4079
Turni408 – 4103
Beta strandi411 – 4144
Turni417 – 4193
Helixi422 – 43413
Helixi436 – 44510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O6LX-ray1.80A/B285-451[»]
ProteinModelPortaliP16662.
SMRiP16662. Positions 285-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16662.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei493 – 50917HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1819.
GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220831.
HOVERGENiHBG004033.
InParanoidiP16662.
KOiK00699.
PhylomeDBiP16662.
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.

P16662-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVKWTSVIL LIQLSFCFSS GNCGKVLVWA AEYSHWMNIK TILDELIQRG
60 70 80 90 100
HEVTVLASSA SILFDPNNSS ALKIEIYPTS LTKTELENFI MQQIKRWSDL
110 120 130 140 150
PKDTFWLYFS QVQEIMSIFG DITRKFCKDV VSNKKFMKKV QESRFDVIFA
160 170 180 190 200
DAIFPCSELL AELFNIPFVY SLSFSPGYTF EKHSGGFIFP PSYVPVVMSE
210 220 230 240 250
LTDQMTFMER VKNMIYVLYF DFWFEIFDMK KWDQFYSEVL GRPTTLSETM
260 270 280 290 300
GKADVWLIRN SWNFQFPHPL LPNVDFVGGL HCKPAKPLPK EMEDFVQSSG
310 320 330 340 350
ENGVVVFSLG SMVSNMTEER ANVIASALAQ IPQKVLWRFD GNKPDTLGLN
360 370 380 390 400
TRLYKWIPQN DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGIPLFADQP
410 420 430 440 450
DNIAHMKARG AAVRVDFNTM SSTDLLNALK RVINDPSYKE NVMKLSRIQH
460 470 480 490 500
DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA HDLTWFQYHS LDVIGFLLVC
510 520
VATVIFIVTK CCLFCFWKFA RKAKKGKND
Length:529
Mass (Da):60,695
Last modified:August 1, 1990 - v1
Checksum:i94B1CA6CE92F1446
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711A → S.
Corresponds to variant rs12233719 [ dbSNP | Ensembl ].
VAR_057327
Natural varianti268 – 2681H → Y in allele UGT2B7*2. 5 Publications
Corresponds to variant rs7439366 [ dbSNP | Ensembl ].
VAR_012342
Natural varianti378 – 3781N → S.
Corresponds to variant rs35590824 [ dbSNP | Ensembl ].
VAR_057328

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3526.1.
PIRiA35366.
RefSeqiNP_001065.2. NM_001074.2.
UniGeneiHs.654424.

Genome annotation databases

EnsembliENST00000305231; ENSP00000304811; ENSG00000171234.
GeneIDi7364.
KEGGihsa:7364.
UCSCiuc003heg.4. human.

Polymorphism databases

DMDMi136727.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3526.1.
PIRi A35366.
RefSeqi NP_001065.2. NM_001074.2.
UniGenei Hs.654424.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O6L X-ray 1.80 A/B 285-451 [» ]
ProteinModelPortali P16662.
SMRi P16662. Positions 285-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113211. 1 interaction.
IntActi P16662. 1 interaction.
STRINGi 9606.ENSP00000304811.

Chemistry

BindingDBi P16662.
ChEMBLi CHEMBL4370.
DrugBanki DB01076. Atorvastatin.
DB00564. Carbamazepine.
DB06777. Chenodeoxycholic acid.
DB00318. Codeine.
DB06695. Dabigatran etexilate.
DB06292. Dapagliflozin.
DB00586. Diclofenac.
DB00445. Epirubicin.
DB00749. Etodolac.
DB00973. Ezetimibe.
DB01544. Flunitrazepam.
DB00712. Flurbiprofen.
DB01095. Fluvastatin.
DB01050. Ibuprofen.
DB00328. Indomethacin.
DB00678. Losartan.
DB00227. Lovastatin.
DB01252. Mitiglinide.
DB00295. Morphine.
DB00688. Mycophenolate mofetil.
DB01024. Mycophenolic acid.
DB00788. Naproxen.
DB00842. Oxazepam.
DB08860. Pitavastatin.
DB06207. Silodosin.
DB00641. Simvastatin.
DB00870. Suprofen.
DB06204. Tapentadol.
DB00313. Valproic Acid.
DB00495. Zidovudine.

Protein family/group databases

CAZyi GT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSitei P16662.

Polymorphism databases

DMDMi 136727.

Proteomic databases

MaxQBi P16662.
PaxDbi P16662.
PRIDEi P16662.

Protocols and materials databases

DNASUi 7364.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305231 ; ENSP00000304811 ; ENSG00000171234 .
GeneIDi 7364.
KEGGi hsa:7364.
UCSCi uc003heg.4. human.

Organism-specific databases

CTDi 7364.
GeneCardsi GC04P069917.
HGNCi HGNC:12554. UGT2B7.
MIMi 600068. gene.
neXtProti NX_P16662.
PharmGKBi PA361.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1819.
GeneTreei ENSGT00760000118949.
HOGENOMi HOG000220831.
HOVERGENi HBG004033.
InParanoidi P16662.
KOi K00699.
PhylomeDBi P16662.
TreeFami TF315472.

Enzyme and pathway databases

BioCyci MetaCyc:HS10272-MONOMER.
BRENDAi 2.4.1.17. 2681.
Reactomei REACT_6784. Glucuronidation.
SABIO-RK P16662.

Miscellaneous databases

EvolutionaryTracei P16662.
GeneWikii UGT2B7.
GenomeRNAii 7364.
NextBioi 28832.
PROi P16662.
SOURCEi Search...

Gene expression databases

Bgeei P16662.
CleanExi HS_UGT2B7.
ExpressionAtlasi P16662. baseline and differential.
Genevestigatori P16662.

Family and domain databases

InterProi IPR002213. UDP_glucos_trans.
[Graphical view ]
PANTHERi PTHR11926. PTHR11926. 1 hit.
Pfami PF00201. UDPGT. 1 hit.
[Graphical view ]
PROSITEi PS00375. UDPGT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    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.

Entry informationi

Entry nameiUD2B7_HUMAN
AccessioniPrimary (citable) accession number: P16662
Secondary accession number(s): B2R810, Q6GTW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 142 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3