Full text data of UGGT1
UGGT1
(GT, UGCGL1, UGGT, UGT1, UGTR)
[Confidence: high (present in two of the MS resources)]
UDP-glucose:glycoprotein glucosyltransferase 1; UGT1; hUGT1; 2.4.1.- (UDP--Glc:glycoprotein glucosyltransferase; UDP-glucose ceramide glucosyltransferase-like 1; Flags: Precursor)
UDP-glucose:glycoprotein glucosyltransferase 1; UGT1; hUGT1; 2.4.1.- (UDP--Glc:glycoprotein glucosyltransferase; UDP-glucose ceramide glucosyltransferase-like 1; Flags: Precursor)
UniProt
Q9NYU2
ID UGGG1_HUMAN Reviewed; 1555 AA.
AC Q9NYU2; Q53QP2; Q53SL3; Q8IW30; Q9H8I4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE Short=UGT1;
DE Short=hUGT1;
DE EC=2.4.1.-;
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=UGGT1; Synonyms=GT, UGCGL1, UGGT, UGT1, UGTR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, INDUCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-1452;
RP GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND ASN-1457.
RC TISSUE=Fetal liver;
RX PubMed=10694380; DOI=10.1021/bi9916473;
RA Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J.;
RT "Two homologues encoding human UDP-glucose:glycoprotein
RT glucosyltransferase differ in mRNA expression and enzymatic
RT activity.";
RL Biochemistry 39:2149-2163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP INTERACTION WITH METTL23.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the
CC protein, thus providing quality control for protein folding in the
CC endoplasmic reticulum. Reglucosylated proteins are recognized by
CC calreticulin for recycling to the endoplasmic reticulum and
CC refolding or degradation.
CC -!- COFACTOR: Calcium or manganese.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Monomer as well as in a tight complex with SEP15 (By
CC similarity). Interacts with METTL23.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Endoplasmic
CC reticulum-Golgi intermediate compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYU2-2; Sequence=VSP_036508;
CC -!- TISSUE SPECIFICITY: Higher levels in pancreas, skeletal muscle,
CC kidney, and brain. Low levels in lung and heart.
CC -!- INDUCTION: By tunicamycin and A23187. Induced 3-4 fold 10 hours
CC after treatment.
CC -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects (By
CC similarity).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14885.1; Type=Erroneous gene model prediction;
CC Sequence=BAB14632.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
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DR EMBL; AF227905; AAF66232.1; -; mRNA.
DR EMBL; AC017079; AAY14735.1; -; Genomic_DNA.
DR EMBL; AC108059; AAY14885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041098; AAH41098.1; -; mRNA.
DR EMBL; AK023671; BAB14632.1; ALT_INIT; mRNA.
DR RefSeq; NP_064505.1; NM_020120.3.
DR UniGene; Hs.743306; -.
DR ProteinModelPortal; Q9NYU2; -.
DR IntAct; Q9NYU2; 2.
DR STRING; 9606.ENSP00000259253; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR PhosphoSite; Q9NYU2; -.
DR DMDM; 224471872; -.
DR PaxDb; Q9NYU2; -.
DR PRIDE; Q9NYU2; -.
DR Ensembl; ENST00000259253; ENSP00000259253; ENSG00000136731.
DR Ensembl; ENST00000375990; ENSP00000365158; ENSG00000136731.
DR GeneID; 56886; -.
DR KEGG; hsa:56886; -.
DR UCSC; uc002tpr.3; human.
DR CTD; 56886; -.
DR GeneCards; GC02P128848; -.
DR H-InvDB; HIX0002447; -.
DR HGNC; HGNC:15663; UGGT1.
DR HPA; HPA012761; -.
DR HPA; HPA015127; -.
DR MIM; 605897; gene.
DR neXtProt; NX_Q9NYU2; -.
DR PharmGKB; PA38014; -.
DR eggNOG; NOG320899; -.
DR HOGENOM; HOG000184622; -.
DR HOVERGEN; HBG079469; -.
DR InParanoid; Q9NYU2; -.
DR KO; K11718; -.
DR OMA; PAISWVN; -.
DR OrthoDB; EOG75J0M7; -.
DR PhylomeDB; Q9NYU2; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00378; -.
DR ChiTaRS; UGGT1; human.
DR GenomeRNAi; 56886; -.
DR NextBio; 62283; -.
DR PRO; PR:Q9NYU2; -.
DR ArrayExpress; Q9NYU2; -.
DR Bgee; Q9NYU2; -.
DR CleanEx; HS_UGCGL1; -.
DR Genevestigator; Q9NYU2; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Glycoprotein; Glycosyltransferase; Phosphoprotein; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1 42 By similarity.
FT CHAIN 43 1555 UDP-glucose:glycoprotein
FT glucosyltransferase 1.
FT /FTId=PRO_0000012271.
FT REGION 1244 1555 Glucosyltransferase (By similarity).
FT MOTIF 1552 1555 Prevents secretion from ER (Potential).
FT MOD_RES 1277 1277 Phosphoserine.
FT CARBOHYD 536 536 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1228 1228 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 24 Missing (in isoform 2).
FT /FTId=VSP_036508.
FT MUTAGEN 1452 1457 Missing: Inactive.
FT MUTAGEN 1452 1452 D->A: Inactive.
FT MUTAGEN 1453 1453 Q->A: 4% active.
FT MUTAGEN 1454 1454 D->A: Inactive.
FT MUTAGEN 1455 1455 L->A: 2% active.
FT MUTAGEN 1456 1456 P->A: 41% active.
FT MUTAGEN 1457 1457 N->A: 7% active.
FT CONFLICT 1487 1487 A -> T (in Ref. 4; BAB14632).
SQ SEQUENCE 1555 AA; 177190 MW; 0A5274A4A65152D3 CRC64;
MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS LTTKWFSTPL
LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH AILEAAFQFL SPLQQNLFKF
CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF FSVHGKKTCE SDTLEALLLT ASERPKPLLF
KGDHRYPSSN PESPVVIFYS EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS QNFPTKARAI
TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM DLDTQDIFSL FDVLRNEARV
MEGLHRLGIE GLSLHNVLKL NIQPSEADYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE LETITMHKIL
ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL TAERDYLDLT ASNNFFVDDY
ARFTILDSQG KTAAVANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIKHQKSSNN VRISMINNPA KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE
ALAAGADIAE FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA QRLAPLLLVL AQLINMNLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTSD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
VIVDTIVMAN LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF
KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ DKDDIINIFS
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMANEY NFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ KREEL
//
ID UGGG1_HUMAN Reviewed; 1555 AA.
AC Q9NYU2; Q53QP2; Q53SL3; Q8IW30; Q9H8I4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-MAR-2009, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE Short=UGT1;
DE Short=hUGT1;
DE EC=2.4.1.-;
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=UGGT1; Synonyms=GT, UGCGL1, UGGT, UGT1, UGTR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, INDUCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-1452;
RP GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND ASN-1457.
RC TISSUE=Fetal liver;
RX PubMed=10694380; DOI=10.1021/bi9916473;
RA Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J.;
RT "Two homologues encoding human UDP-glucose:glycoprotein
RT glucosyltransferase differ in mRNA expression and enzymatic
RT activity.";
RL Biochemistry 39:2149-2163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP INTERACTION WITH METTL23.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the
CC protein, thus providing quality control for protein folding in the
CC endoplasmic reticulum. Reglucosylated proteins are recognized by
CC calreticulin for recycling to the endoplasmic reticulum and
CC refolding or degradation.
CC -!- COFACTOR: Calcium or manganese.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Monomer as well as in a tight complex with SEP15 (By
CC similarity). Interacts with METTL23.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Endoplasmic
CC reticulum-Golgi intermediate compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYU2-2; Sequence=VSP_036508;
CC -!- TISSUE SPECIFICITY: Higher levels in pancreas, skeletal muscle,
CC kidney, and brain. Low levels in lung and heart.
CC -!- INDUCTION: By tunicamycin and A23187. Induced 3-4 fold 10 hours
CC after treatment.
CC -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects (By
CC similarity).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14885.1; Type=Erroneous gene model prediction;
CC Sequence=BAB14632.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
CC -----------------------------------------------------------------------
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DR EMBL; AF227905; AAF66232.1; -; mRNA.
DR EMBL; AC017079; AAY14735.1; -; Genomic_DNA.
DR EMBL; AC108059; AAY14885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041098; AAH41098.1; -; mRNA.
DR EMBL; AK023671; BAB14632.1; ALT_INIT; mRNA.
DR RefSeq; NP_064505.1; NM_020120.3.
DR UniGene; Hs.743306; -.
DR ProteinModelPortal; Q9NYU2; -.
DR IntAct; Q9NYU2; 2.
DR STRING; 9606.ENSP00000259253; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR PhosphoSite; Q9NYU2; -.
DR DMDM; 224471872; -.
DR PaxDb; Q9NYU2; -.
DR PRIDE; Q9NYU2; -.
DR Ensembl; ENST00000259253; ENSP00000259253; ENSG00000136731.
DR Ensembl; ENST00000375990; ENSP00000365158; ENSG00000136731.
DR GeneID; 56886; -.
DR KEGG; hsa:56886; -.
DR UCSC; uc002tpr.3; human.
DR CTD; 56886; -.
DR GeneCards; GC02P128848; -.
DR H-InvDB; HIX0002447; -.
DR HGNC; HGNC:15663; UGGT1.
DR HPA; HPA012761; -.
DR HPA; HPA015127; -.
DR MIM; 605897; gene.
DR neXtProt; NX_Q9NYU2; -.
DR PharmGKB; PA38014; -.
DR eggNOG; NOG320899; -.
DR HOGENOM; HOG000184622; -.
DR HOVERGEN; HBG079469; -.
DR InParanoid; Q9NYU2; -.
DR KO; K11718; -.
DR OMA; PAISWVN; -.
DR OrthoDB; EOG75J0M7; -.
DR PhylomeDB; Q9NYU2; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00378; -.
DR ChiTaRS; UGGT1; human.
DR GenomeRNAi; 56886; -.
DR NextBio; 62283; -.
DR PRO; PR:Q9NYU2; -.
DR ArrayExpress; Q9NYU2; -.
DR Bgee; Q9NYU2; -.
DR CleanEx; HS_UGCGL1; -.
DR Genevestigator; Q9NYU2; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Glycoprotein; Glycosyltransferase; Phosphoprotein; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1 42 By similarity.
FT CHAIN 43 1555 UDP-glucose:glycoprotein
FT glucosyltransferase 1.
FT /FTId=PRO_0000012271.
FT REGION 1244 1555 Glucosyltransferase (By similarity).
FT MOTIF 1552 1555 Prevents secretion from ER (Potential).
FT MOD_RES 1277 1277 Phosphoserine.
FT CARBOHYD 536 536 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1228 1228 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 24 Missing (in isoform 2).
FT /FTId=VSP_036508.
FT MUTAGEN 1452 1457 Missing: Inactive.
FT MUTAGEN 1452 1452 D->A: Inactive.
FT MUTAGEN 1453 1453 Q->A: 4% active.
FT MUTAGEN 1454 1454 D->A: Inactive.
FT MUTAGEN 1455 1455 L->A: 2% active.
FT MUTAGEN 1456 1456 P->A: 41% active.
FT MUTAGEN 1457 1457 N->A: 7% active.
FT CONFLICT 1487 1487 A -> T (in Ref. 4; BAB14632).
SQ SEQUENCE 1555 AA; 177190 MW; 0A5274A4A65152D3 CRC64;
MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS LTTKWFSTPL
LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH AILEAAFQFL SPLQQNLFKF
CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF FSVHGKKTCE SDTLEALLLT ASERPKPLLF
KGDHRYPSSN PESPVVIFYS EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS QNFPTKARAI
TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM DLDTQDIFSL FDVLRNEARV
MEGLHRLGIE GLSLHNVLKL NIQPSEADYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE LETITMHKIL
ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL TAERDYLDLT ASNNFFVDDY
ARFTILDSQG KTAAVANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIKHQKSSNN VRISMINNPA KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE
ALAAGADIAE FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA QRLAPLLLVL AQLINMNLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTSD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
VIVDTIVMAN LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF
KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ DKDDIINIFS
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMANEY NFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ KREEL
//
MIM
605897
*RECORD*
*FIELD* NO
605897
*FIELD* TI
*605897 UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; UGGT1
;;HUGT1
*FIELD* TX
DESCRIPTION
read more
UDP-glucose:glycoprotein glucosyltransferase (UGT) is a soluble protein
of the endoplasmic reticulum (ER) that selectively reglucosylates
unfolded glycoproteins, thus providing quality control for protein
transport out of the ER.
CLONING
Using a portion of Drosophila UGT to screen a human fetal liver cDNA
library, Arnold et al. (2000) isolated HUGT1. The assembled full-length
HUGT1 cDNA encodes a deduced 1,555-amino acid protein with a predicted
ER-targeting signal sequence, ER retrieval signal, 3 N-glycosylation
sites, and 2 disulfide loops. HUGT1 shares 55% sequence identity with
HUGT2 (605898) and 31 to 45% identity with Drosophila, C. elegans, and
S. pombe homologs. Northern blot analysis detected 3 HUGT1 transcripts
of 5.7, 8, and 10.6 kb in pancreas, heart, brain, placenta, lung, liver,
skeletal muscle, and kidney. Arnold et al. (2000) noted that HUGT1 and
HUGT2 differ slightly in their tissue distribution.
GENE FUNCTION
Using cell culture experiments, Arnold et al. (2000) demonstrated that
HUGT1 expression was induced upon disruption of protein folding in the
ER, whereas HUGT2 was not. By immunofluorescence microscopy, they
localized HUGT1 to the ER. Arnold et al. (2000) expressed HUGT1 in
transient transfection experiments and demonstrated UGT activity. Using
site-directed mutagenesis, they identified 4 residues of HUGT1 that are
essential for catalytic function.
MAPPING
Scott (2001) mapped the HUGT1 gene to chromosome 2 based on sequence
similarity between the HUGT1 sequence (GenBank GENBANK AF227905) and a
chromosome 2 clone (GenBank GENBANK AC017079).
*FIELD* RF
1. Arnold, S. M.; Fessler, L. I.; Fessler, J. H.; Kaufman, R. J.:
Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase
differ in mRNA expression and enzymatic activity. Biochemistry 39:
2149-2163, 2000.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 5/2/2001.
*FIELD* CD
Dawn Watkins-Chow: 5/2/2001
*FIELD* ED
carol: 10/30/2009
carol: 5/2/2001
*RECORD*
*FIELD* NO
605897
*FIELD* TI
*605897 UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; UGGT1
;;HUGT1
*FIELD* TX
DESCRIPTION
read more
UDP-glucose:glycoprotein glucosyltransferase (UGT) is a soluble protein
of the endoplasmic reticulum (ER) that selectively reglucosylates
unfolded glycoproteins, thus providing quality control for protein
transport out of the ER.
CLONING
Using a portion of Drosophila UGT to screen a human fetal liver cDNA
library, Arnold et al. (2000) isolated HUGT1. The assembled full-length
HUGT1 cDNA encodes a deduced 1,555-amino acid protein with a predicted
ER-targeting signal sequence, ER retrieval signal, 3 N-glycosylation
sites, and 2 disulfide loops. HUGT1 shares 55% sequence identity with
HUGT2 (605898) and 31 to 45% identity with Drosophila, C. elegans, and
S. pombe homologs. Northern blot analysis detected 3 HUGT1 transcripts
of 5.7, 8, and 10.6 kb in pancreas, heart, brain, placenta, lung, liver,
skeletal muscle, and kidney. Arnold et al. (2000) noted that HUGT1 and
HUGT2 differ slightly in their tissue distribution.
GENE FUNCTION
Using cell culture experiments, Arnold et al. (2000) demonstrated that
HUGT1 expression was induced upon disruption of protein folding in the
ER, whereas HUGT2 was not. By immunofluorescence microscopy, they
localized HUGT1 to the ER. Arnold et al. (2000) expressed HUGT1 in
transient transfection experiments and demonstrated UGT activity. Using
site-directed mutagenesis, they identified 4 residues of HUGT1 that are
essential for catalytic function.
MAPPING
Scott (2001) mapped the HUGT1 gene to chromosome 2 based on sequence
similarity between the HUGT1 sequence (GenBank GENBANK AF227905) and a
chromosome 2 clone (GenBank GENBANK AC017079).
*FIELD* RF
1. Arnold, S. M.; Fessler, L. I.; Fessler, J. H.; Kaufman, R. J.:
Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase
differ in mRNA expression and enzymatic activity. Biochemistry 39:
2149-2163, 2000.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 5/2/2001.
*FIELD* CD
Dawn Watkins-Chow: 5/2/2001
*FIELD* ED
carol: 10/30/2009
carol: 5/2/2001