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Protein

UDP-glucuronosyltransferase 1-8

Gene

UGT1A8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  • drug binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • enzyme inhibitor activity Source: BHF-UCL
  • fatty acid binding Source: BHF-UCL
  • glucuronosyltransferase activity Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid binding Source: BHF-UCL
  • steroid binding Source: BHF-UCL

GO - Biological processi

  • cellular glucuronidation Source: BHF-UCL
  • cellular response to hormone stimulus Source: GO_Central
  • coumarin metabolic process Source: BHF-UCL
  • drug metabolic process Source: BHF-UCL
  • fatty acid metabolic process Source: BHF-UCL
  • flavone metabolic process Source: BHF-UCL
  • flavonoid biosynthetic process Source: GO_Central
  • flavonoid glucuronidation Source: BHF-UCL
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of cellular glucuronidation Source: UniProtKB
  • negative regulation of fatty acid metabolic process Source: BHF-UCL
  • negative regulation of glucuronosyltransferase activity Source: BHF-UCL
  • negative regulation of steroid metabolic process Source: BHF-UCL
  • retinoic acid metabolic process Source: BHF-UCL
  • steroid metabolic process Source: BHF-UCL
  • xenobiotic glucuronidation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS10706-MONOMER.
BRENDAi2.4.1.17. 2681.
ReactomeiREACT_6784. Glucuronidation.
SABIO-RKQ9HAW9.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronosyltransferase 1-8 (EC:2.4.1.17)
Short name:
UDPGT 1-8
Short name:
UGT1*8
Short name:
UGT1-08
Short name:
UGT1.8
Alternative name(s):
UDP-glucuronosyltransferase 1-H
Short name:
UGT-1H
Short name:
UGT1H
UDP-glucuronosyltransferase 1A8
Gene namesi
Name:UGT1A8
Synonyms:GNT1, UGT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12540. UGT1A8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei488 – 50417HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37183.

Chemistry

DrugBankiDB00861. Diflunisal.
DB00295. Morphine.
DB00688. Mycophenolate mofetil.
DB00818. Propofol.
DB00313. Valproic Acid.

Polymorphism and mutation databases

BioMutaiUGT1A8.
DMDMi29839637.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 530505UDP-glucuronosyltransferase 1-8PRO_0000036007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication
Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9HAW9.

PTM databases

PhosphoSiteiQ9HAW9.

Expressioni

Tissue specificityi

Colon specific. Isoform 1 and 2 are expressed in liver, kidney, colon and small intestine; isoform 2 but not isoform 1 is expressed in liver (PubMed:18004212).2 Publications

Gene expression databases

BgeeiQ9HAW9.
ExpressionAtlasiQ9HAW9. baseline.
GenevisibleiQ9HAW9. HS.

Interactioni

Subunit structurei

Isoform 1 interacts with isoform 2/i2 suggesting that oligomerization is involved in negative regulation of transferase activity by isoform 2. Isoform 1 also interacts with respective i2 isoforms of UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A9 and UGT1A10.1 Publication

Protein-protein interaction databases

IntActiQ9HAW9. 7 interactions.
STRINGi9606.ENSP00000362549.

Structurei

3D structure databases

ProteinModelPortaliQ9HAW9.
SMRiQ9HAW9. Positions 280-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220832.
HOVERGENiHBG004033.
InParanoidiQ9HAW9.
KOiK00699.
OMAiFITEYEP.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ9HAW9.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HAW9-1) [UniParc]FASTAAdd to basket

Also known as: i1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARTGWTSPI PLCVSLLLTC GFAEAGKLLV VPMDGSHWFT MQSVVEKLIL
60 70 80 90 100
RGHEVVVVMP EVSWQLGKSL NCTVKTYSTS YTLEDLDREF MDFADAQWKA
110 120 130 140 150
QVRSLFSLFL SSSNGFFNLF FSHCRSLFND RKLVEYLKES SFDAVFLDPF
160 170 180 190 200
DACGLIVAKY FSLPSVVFAR GIACHYLEEG AQCPAPLSYV PRILLGFSDA
210 220 230 240 250
MTFKERVRNH IMHLEEHLFC QYFSKNALEI ASEILQTPVT AYDLYSHTSI
260 270 280 290 300
WLLRTDFVLD YPKPVMPNMI FIGGINCHQG KPLPMEFEAY INASGEHGIV
310 320 330 340 350
VFSLGSMVSE IPEKKAMAIA DALGKIPQTV LWRYTGTRPS NLANNTILVK
360 370 380 390 400
WLPQNDLLGH PMTRAFITHA GSHGVYESIC NGVPMVMMPL FGDQMDNAKR
410 420 430 440 450
METKGAGVTL NVLEMTSEDL ENALKAVIND KSYKENIMRL SSLHKDRPVE
460 470 480 490 500
PLDLAVFWVE FVMRHKGAPH LRPAAHDLTW YQYHSLDVIG FLLAVVLTVA
510 520 530
FITFKCCAYG YRKCLGKKGR VKKAHKSKTH
Length:530
Mass (Da):59,742
Last modified:March 1, 2001 - v1
Checksum:iAD838436940F4190
GO
Isoform 2 (identifier: Q9HAW9-2) [UniParc]FASTAAdd to basket

Also known as: i2, UGT1A8s

The sequence of this isoform differs from the canonical sequence as follows:
     432-530: SYKENIMRLS...VKKAHKSKTH → RKKQQSGRQM

Show »
Length:441
Mass (Da):49,518
Checksum:iCE3BAC9FD06D0565
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531H → N.
Corresponds to variant rs45504099 [ dbSNP | Ensembl ].
VAR_052463
Natural varianti132 – 1321K → R.2 Publications
VAR_015543
Natural varianti144 – 1441A → V.1 Publication
Corresponds to variant rs17862841 [ dbSNP | Ensembl ].
VAR_058585
Natural varianti154 – 1541G → A.2 Publications
VAR_015544
Natural varianti173 – 1731A → G in allele UGT1A8*2. 5 Publications
Corresponds to variant rs1042597 [ dbSNP | Ensembl ].
VAR_015545
Natural varianti173 – 1731A → V.
Corresponds to variant rs1042597 [ dbSNP | Ensembl ].
VAR_061871
Natural varianti202 – 2021T → A.2 Publications
VAR_015546
Natural varianti212 – 2121M → L.2 Publications
VAR_015547
Natural varianti231 – 2311A → T.1 Publication
VAR_058586
Natural varianti277 – 2771C → Y in allele UGT1A8*3; dramatic reduction in catalytic activity. 2 Publications
Corresponds to variant rs17863762 [ dbSNP | Ensembl ].
VAR_015549

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei432 – 53099SYKEN…KSKTH → RKKQQSGRQM in isoform 2. CuratedVSP_053964Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030310 mRNA. Translation: AAB84259.1.
AF297093 Genomic DNA. Translation: AAG30416.1.
AF462267 mRNA. Translation: AAL75963.1.
AF462268 mRNA. Translation: AAL75964.1.
AC006985 Genomic DNA. No translation available.
AC019072 Genomic DNA. No translation available.
AK313488 mRNA. Translation: BAG36270.1.
AF465198 Genomic DNA. Translation: AAL73506.1.
AF465199 Genomic DNA. Translation: AAL73507.1.
AF465200 Genomic DNA. Translation: AAL73508.1.
DQ364251 mRNA. Translation: ABC96775.1.
CCDSiCCDS33402.1. [Q9HAW9-1]
RefSeqiNP_061949.3. NM_019076.4. [Q9HAW9-1]
UniGeneiHs.554822.

Genome annotation databases

EnsembliENST00000373450; ENSP00000362549; ENSG00000242366.
GeneIDi54576.
KEGGihsa:54576.
UCSCiuc002vup.3. human. [Q9HAW9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030310 mRNA. Translation: AAB84259.1.
AF297093 Genomic DNA. Translation: AAG30416.1.
AF462267 mRNA. Translation: AAL75963.1.
AF462268 mRNA. Translation: AAL75964.1.
AC006985 Genomic DNA. No translation available.
AC019072 Genomic DNA. No translation available.
AK313488 mRNA. Translation: BAG36270.1.
AF465198 Genomic DNA. Translation: AAL73506.1.
AF465199 Genomic DNA. Translation: AAL73507.1.
AF465200 Genomic DNA. Translation: AAL73508.1.
DQ364251 mRNA. Translation: ABC96775.1.
CCDSiCCDS33402.1. [Q9HAW9-1]
RefSeqiNP_061949.3. NM_019076.4. [Q9HAW9-1]
UniGeneiHs.554822.

3D structure databases

ProteinModelPortaliQ9HAW9.
SMRiQ9HAW9. Positions 280-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9HAW9. 7 interactions.
STRINGi9606.ENSP00000362549.

Chemistry

ChEMBLiCHEMBL1743318.
DrugBankiDB00861. Diflunisal.
DB00295. Morphine.
DB00688. Mycophenolate mofetil.
DB00818. Propofol.
DB00313. Valproic Acid.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteiQ9HAW9.

Polymorphism and mutation databases

BioMutaiUGT1A8.
DMDMi29839637.

Proteomic databases

PRIDEiQ9HAW9.

Protocols and materials databases

DNASUi54576.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373450; ENSP00000362549; ENSG00000242366.
GeneIDi54576.
KEGGihsa:54576.
UCSCiuc002vup.3. human. [Q9HAW9-1]

Organism-specific databases

CTDi54576.
GeneCardsiGC02P234526.
HGNCiHGNC:12540. UGT1A8.
MIMi191740. gene.
606433. gene.
neXtProtiNX_Q9HAW9.
PharmGKBiPA37183.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118949.
HOGENOMiHOG000220832.
HOVERGENiHBG004033.
InParanoidiQ9HAW9.
KOiK00699.
OMAiFITEYEP.
OrthoDBiEOG7GBFWS.
PhylomeDBiQ9HAW9.
TreeFamiTF315472.

Enzyme and pathway databases

BioCyciMetaCyc:HS10706-MONOMER.
BRENDAi2.4.1.17. 2681.
ReactomeiREACT_6784. Glucuronidation.
SABIO-RKQ9HAW9.

Miscellaneous databases

ChiTaRSiUGT1A8. human.
GeneWikiiUGT1A8.
GenomeRNAii54576.
NextBioi35481514.
PROiQ9HAW9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAW9.
ExpressionAtlasiQ9HAW9. baseline.
GenevisibleiQ9HAW9. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8."
    Strassburg C.P., Manns M.P., Tukey R.H.
    J. Biol. Chem. 273:8719-8726(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS ARG-132; ALA-154; GLY-173; ALA-202 AND LEU-212.
  2. "Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1 gene complex locus."
    Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S., Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.
    Pharmacogenetics 11:357-368(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification and functional characterization of UDP-glucuronosyltransferases UGT1A8*1, UGT1A8*2 and UGT1A8*3."
    Huang Y.-H., Galijatovic A., Nguyen N., Geske D., Beaton D., Green J., Green M., Peters W.H., Tukey R.H.
    Pharmacogenetics 12:287-297(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-173 AND TYR-277.
    Tissue: Colon.
  4. "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] (ISOFORM 1), VARIANT GLY-173.
    Tissue: Tongue.
  5. "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].
  6. "Identification of genetic polymorphisms within the human extrahepatic UGT1A8 gene."
    Strassburg C.P., Vogel A., Manns M.P.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285, VARIANTS ARG-132; ALA-154; GLY-173; ALA-202 AND LEU-212.
  7. Guillemette C., Levesque E., Girard H., Bernard O.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  8. "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-292 AND ASN-344.
    Tissue: Liver.
  9. "Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity."
    Girard H., Levesque E., Bellemare J., Journault K., Caillier B., Guillemette C.
    Pharmacogenet. Genomics 17:1077-1089(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  10. "Structure and concentration changes affect characterization of UGT isoform-specific metabolism of isoflavones."
    Tang L., Singh R., Liu Z., Hu M.
    Mol. Pharm. 6:1466-1482(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro."
    Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.
    Drug Metab. Dispos. 38:1785-1789(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION (ISOFORM 2), SUBUNIT.
  12. "Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population."
    Menard V., Girard H., Harvey M., Perusse L., Guillemette C.
    Hum. Mutat. 30:677-687(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-144; GLY-173; THR-231 AND TYR-277.

Entry informationi

Entry nameiUD18_HUMAN
AccessioniPrimary (citable) accession number: Q9HAW9
Secondary accession number(s): B2R8S3
, B8K290, O14928, Q8TEX4, Q8WTQ9, Q8WX85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 126 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

Miscellaneous

The gene is part of the UGT1A complex locus which displays alternative use of promoters, first exons and terminal exons. The locus is defined by 13 first exons, which are alternatively spliced to 3 other common exons and 2 alternative terminal exons 5. From the 27 possible mRNA isoforms, 9 produce functionally active polypeptides (UGT1A1, 1A3, 1A4, 1A5, 1A6, 1A7, 1A8, 1A9 and 1A10) called isoforms 1 (i1). Use of an alternative exon 5 (5b) as terminal exon is leading to 9 additional alternatively spliced products termed isoforms i2 and which lack transferase activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.