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UDB11_HUMAN
ID   UDB11_HUMAN             Reviewed;         529 AA.
AC   O75310; Q3KNV9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=UDP-glucuronosyltransferase 2B11;
DE            Short=UDPGT 2B11;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B11;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9675083; DOI=10.1006/bbrc.1998.8908;
RA   Beaulieu M., Levesque E., Hum D.W., Belanger A.;
RT   "Isolation and characterization of a human orphan UDP-
RT   glucuronosyltransferase, UGT2B11.";
RL   Biochem. Biophys. Res. Commun. 248:44-50(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC   -!- INTERACTION:
CC       O75310; Q12797-6: ASPH; NbExp=3; IntAct=EBI-12891746, EBI-12092171;
CC       O75310; P55061: TMBIM6; NbExp=3; IntAct=EBI-12891746, EBI-1045825;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF016492; AAC27891.1; -; mRNA.
DR   EMBL; BC069441; AAH69441.1; -; mRNA.
DR   EMBL; BC107059; AAI07060.1; -; mRNA.
DR   EMBL; BC107060; AAI07061.1; -; mRNA.
DR   CCDS; CCDS3527.1; -.
DR   PIR; JE0200; JE0200.
DR   RefSeq; NP_001064.1; NM_001073.2.
DR   AlphaFoldDB; O75310; -.
DR   SMR; O75310; -.
DR   BioGRID; 115945; 6.
DR   IntAct; O75310; 2.
DR   STRING; 9606.ENSP00000387683; -.
DR   ChEMBL; CHEMBL4523985; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyGen; O75310; 1 site.
DR   iPTMnet; O75310; -.
DR   PhosphoSitePlus; O75310; -.
DR   BioMuta; UGT2B11; -.
DR   jPOST; O75310; -.
DR   MassIVE; O75310; -.
DR   PaxDb; O75310; -.
DR   PeptideAtlas; O75310; -.
DR   PRIDE; O75310; -.
DR   ProteomicsDB; 49886; -.
DR   Antibodypedia; 57751; 56 antibodies from 13 providers.
DR   DNASU; 10720; -.
DR   Ensembl; ENST00000446444.2; ENSP00000387683.1; ENSG00000213759.10.
DR   GeneID; 10720; -.
DR   KEGG; hsa:10720; -.
DR   MANE-Select; ENST00000446444.2; ENSP00000387683.1; NM_001073.3; NP_001064.1.
DR   UCSC; uc003heh.5; human.
DR   CTD; 10720; -.
DR   DisGeNET; 10720; -.
DR   GeneCards; UGT2B11; -.
DR   HGNC; HGNC:12545; UGT2B11.
DR   HPA; ENSG00000213759; Tissue enriched (breast).
DR   MIM; 603064; gene.
DR   neXtProt; NX_O75310; -.
DR   OpenTargets; ENSG00000213759; -.
DR   PharmGKB; PA37187; -.
DR   VEuPathDB; HostDB:ENSG00000213759; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000165281; -.
DR   HOGENOM; CLU_012949_0_2_1; -.
DR   InParanoid; O75310; -.
DR   OMA; WINNALY; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; O75310; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 2681.
DR   PathwayCommons; O75310; -.
DR   Reactome; R-HSA-156588; Glucuronidation.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   SignaLink; O75310; -.
DR   BioGRID-ORCS; 10720; 23 hits in 988 CRISPR screens.
DR   ChiTaRS; UGT2B11; human.
DR   GenomeRNAi; 10720; -.
DR   Pharos; O75310; Tbio.
DR   PRO; PR:O75310; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O75310; protein.
DR   Bgee; ENSG00000213759; Expressed in liver and 43 other tissues.
DR   Genevisible; O75310; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR   GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR   GO; GO:0052697; P:xenobiotic glucuronidation; IDA:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:ProtInc.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Microsome; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..529
FT                   /note="UDP-glucuronosyltransferase 2B11"
FT                   /id="PRO_0000036035"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  61038 MW;  CE4AC3C71CFC2AB4 CRC64;
     MTLKWTSVLL LIHLSCYFSS GSCGKVLVWA AEYSHWMNMK TILKELVQRG HEVTVLASSA
     SILFDPNDAS TLKFEVYPTS LTKTEFENII MQQVKRWSDI RKDSFWLYFS QEQEILWELY
     DIFRNFCKDV VSNKKVMKKL QESRFDIVFA DAVFPCGELL AALLNIRFVY SLRFTPGYTI
     ERHSGGLIFP PSYIPIVMSK LSDQMTFMER VKNMIYVLYF DFWFQMSDMK KWDQFYSEVL
     GRPTTLFETM GKADIWLMRN SWSFQFPHPF LPNVDFVGGF HCKPAKPLPK EMEEFVQSSG
     ENGVVVFSLG SVISNMTAER ANVIATALAK IPQKVLWRFD GNKPDALGLN TRLYKWIPQN
     DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGIPLFFDQP DNIAHMKAKG AAVRLDFNTM
     SSTDLLNALK TVINDPLYKE NIMKLSRIQH DQPVKPLDRA VFWIEFVMPH KGAKHLRVAA
     HDLTWFQYHS LDVIGFLLAC VATVIFIITK FCLFCFWKFA RKGKKGKRD
 
 
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