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P16662

- UD2B7_HUMAN

UniProt

P16662 - UD2B7_HUMAN

Protein

UDP-glucuronosyltransferase 2B7

Gene

UGT2B7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    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

    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 membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: ProtInc

    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.
    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.
    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

    MSVKWTSVIL LIQLSFCFSS GNCGKVLVWA AEYSHWMNIK TILDELIQRG    50
    HEVTVLASSA SILFDPNNSS ALKIEIYPTS LTKTELENFI MQQIKRWSDL 100
    PKDTFWLYFS QVQEIMSIFG DITRKFCKDV VSNKKFMKKV QESRFDVIFA 150
    DAIFPCSELL AELFNIPFVY SLSFSPGYTF EKHSGGFIFP PSYVPVVMSE 200
    LTDQMTFMER VKNMIYVLYF DFWFEIFDMK KWDQFYSEVL GRPTTLSETM 250
    GKADVWLIRN SWNFQFPHPL LPNVDFVGGL HCKPAKPLPK EMEDFVQSSG 300
    ENGVVVFSLG SMVSNMTEER ANVIASALAQ IPQKVLWRFD GNKPDTLGLN 350
    TRLYKWIPQN DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGIPLFADQP 400
    DNIAHMKARG AAVRVDFNTM SSTDLLNALK RVINDPSYKE NVMKLSRIQH 450
    DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA HDLTWFQYHS LDVIGFLLVC 500
    VATVIFIVTK CCLFCFWKFA RKAKKGKND 529
    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.

    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.
    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.
    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

    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 1, 2014
    This is version 141 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