true
2005-06-21
2024-03-27
187
UGGG1_HUMAN
Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity.
Arnold S.M.
Fessler L.I.
Fessler J.H.
Kaufman R.J.
doi:10.1021/bi9916473
2000
Biochemistry
39
2149-2163
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
FUNCTION
CATALYTIC ACTIVITY
COFACTOR
INDUCTION
SUBCELLULAR LOCATION
TISSUE SPECIFICITY
MUTAGENESIS OF ASP-1452; GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND ASN-1457
Fetal liver
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.
doi:10.1038/nature03466
2005
Nature
434
724-731
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team
doi:10.1101/gr.2596504
2004
Genome Res.
14
2121-2127
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
Eye
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.
doi:10.1038/ng1285
2004
Nat. Genet.
36
40-45
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2)
Placenta
Initial characterization of the human central proteome.
Burkard T.R.
Planyavsky M.
Kaupe I.
Breitwieser F.P.
Buerckstuemmer T.
Bennett K.L.
Superti-Furga G.
Colinge J.
doi:10.1186/1752-0509-5-17
2011
BMC Syst. Biol.
5
17
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
Rigbolt K.T.
Prokhorova T.A.
Akimov V.
Henningsen J.
Johansen P.T.
Kratchmarova I.
Kassem M.
Mann M.
Olsen J.V.
Blagoev B.
doi:10.1126/scisignal.2001570
2011
Sci. Signal.
4
RS3
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
Cloutier P.
Lavallee-Adam M.
Faubert D.
Blanchette M.
Coulombe B.
doi:10.1371/journal.pgen.1003210
2013
PLoS Genet.
9
E1003210
INTERACTION WITH METTL23
Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active.
Takeda Y.
Seko A.
Hachisu M.
Daikoku S.
Izumi M.
Koizumi A.
Fujikawa K.
Kajihara Y.
Ito Y.
doi:10.1093/glycob/cwt163
2014
Glycobiology
24
344-350
FUNCTION
ACTIVITY REGULATION
INTERACTION WITH SELENOF
MUTAGENESIS OF ASP-1358
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
Bian Y.
Song C.
Cheng K.
Dong M.
Wang F.
Huang J.
Sun D.
Wang L.
Ye M.
Zou H.
doi:10.1016/j.jprot.2013.11.014
2014
J. Proteomics
96
253-262
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Liver
N-terminome analysis of the human mitochondrial proteome.
Vaca Jacome A.S.
Rabilloud T.
Schaeffer-Reiss C.
Rompais M.
Ayoub D.
Lane L.
Bairoch A.
Van Dorsselaer A.
Carapito C.
doi:10.1002/pmic.201400617
2015
Proteomics
15
2519-2524
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Sequence problems.
Different initiation.
217
70
Glycosyltransferase Family 24
6 N-Linked glycans (1 site)
4 sites, 7 glycans
7 sites, 7 N-linked glycans (1 site), 2 O-linked glycans (3 sites)
159 antibodies from 27 providers
human
UGGT1
Low tissue specificity
gene
Eukaryota
ER Quality Control Compartment (ERQC)
16 hits in 1161 CRISPR screens
human
Tbio
Protein
Expressed in calcaneal tendon and 189 other cell types or tissues
baseline and differential
GT8_HUGT1_C_like
Glyco_transf_24
Nucleotide-diphossugar_trans
UDP-g_GGtrans
UGGT_TRXL_1
UGGT_TRXL_2
UGGT_TRXL_3
UGGT_TRXL_4
UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE
UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1
Glyco_transf_24
Thioredoxin_12
Thioredoxin_13
Thioredoxin_14
Thioredoxin_15
UDP-g_GGTase
Nucleotide-diphospho-sugar transferases
ER_TARGET
HS
UDP-glucose:glycoprotein glucosyltransferase 1
UGT1
hUGT1
2.4.1.-
UDP--Glc:glycoprotein glucosyltransferase
UDP-glucose ceramide glucosyltransferase-like 1
UGGT1
GT
UGCGL1
UGGT
UGT1
UGTR
Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation.
Catalytic activity is enhanced by complex formation with SELENOF.
Monomer as well as in a tight complex with SELENOF (PubMed:24415556). Interacts with METTL23 (PubMed:23349634). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity).
Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart.
By tunicamycin and A23187. Induced 3-4 fold 10 hours after treatment.
The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects.
Belongs to the glycosyltransferase 8 family.
1
42
UDP-glucose:glycoprotein glucosyltransferase 1
173033
43
1555
Glucosyltransferase
1244
Disordered
1534
Prevents secretion from ER
1552
Phosphoserine
1277
N-linked (GlcNAc...) asparagine
536
N-linked (GlcNAc...) asparagine
1228
In isoform 2.
24
Loss of catalytic activity.
A
1358
Inactive.
1452
1457
Inactive.
A
4% active.
A
1453
Inactive.
A
1454
2% active.
A
1455
41% active.
A
1456
7% active.
A
T
1487
2009-03-03
3
true
177190
b2d2b452f852757b4ee355a502b0b7ff
1
MGCKGDASGACAAGALPVTGVCYKMGVLVVLTVLWLFSSVKADSKAITTSLTTKWFSTPLLLEASEFLAEDSQEKFWNFVEASQNIGSSDHDGTDYSYYHAILEAAFQFLSPLQQNLFKFCLSLRSYSATIQAFQQIAADEPPPEGCNSFFSVHGKKTCESDTLEALLLTASERPKPLLFKGDHRYPSSNPESPVVIFYSEIGSEEFSNFHRQLISKSNAGKINYVFRHYIFNPRKEPVYLSGYGVELAIKSTEYKAKDDTQVKGTEVNTTVIGENDPIDEVQGFLFGKLRDLHPDLEGQLKELRKHLVESTNEMAPLKVWQLQDLSFQTAARILASPVELALVVMKDLSQNFPTKARAITKTAVSSELRTEVEENQKYFKGTLGLQPGDSALFINGLHMDLDTQDIFSLFDVLRNEARVMEGLHRLGIEGLSLHNVLKLNIQPSEADYAVDIRSPAISWVNNLEVDSRYNSWPSSLQELLRPTFPGVIRQIRKNLHNMVFIVDPAHETTAELMNTAEMFLSNHIPLRIGFIFVVNDSEDVDGMQDAGVAVLRAYNYVAQEVDDYHAFQTLTHIYNKVRTGEKVKVEHVVSVLEKKYPYVEVNSILGIDSAYDRNRKEARGYYEQTGVGPLPVVLFNGMPFEREQLDPDELETITMHKILETTTFFQRAVYLGELPHDQDVVEYIMNQPNVVPRINSRILTAERDYLDLTASNNFFVDDYARFTILDSQGKTAAVANSMNYLTKKGMSSKEIYDDSFIRPVTFWIVGDFDSPSGRQLLYDAIKHQKSSNNVRISMINNPAKEISYENTQISRAIWAALQTQTSNAAKNFITKMAKEGAAEALAAGADIAEFSVGGMDFSLFKEVFESSKMDFILSHAVYCRDVLKLKKGQRAVISNGRIIGPLEDSELFNQDDFHLLENIILKTSGQKIKSHIQQLRVEEDVASDLVMKVDALLSAQPKGDPRIEYQFFEDRHSAIKLRPKEGETYFDVVAVVDPVTREAQRLAPLLLVLAQLINMNLRVFMNCQSKLSDMPLKSFYRYVLEPEISFTSDNSFAKGPIAKFLDMPQSPLFTLNLNTPESWMVESVRTPYDLDNIYLEEVDSVVAAEYELEYLLLEGHCYDITTGQPPRGLQFTLGTSANPVIVDTIVMANLGYFQLKANPGAWILRLRKGRSEDIYRIYSHDGTDSPPDADEVVIVLNNFKSKIIKVKVQKKADMVNEDLLSDGTSENESGFWDSFKWGFTGQKTEEVKQDKDDIINIFSVASGHLYERFLRIMMLSVLKNTKTPVKFWFLKNYLSPTFKEFIPYMANEYNFQYELVQYKWPRWLHQQTEKQRIIWGYKILFLDVLFPLVVDKFLFVDADQIVRTDLKELRDFNLDGAPYGYTPFCDSRREMDGYRFWKSGYWASHLAGRKYHISALYVVDLKKFRKIAAGDRLRGQYQGLSQDPNSLSNLDQDLPNNMIHQVPIKSLPQEWLWCETWCDDASKKRAKTIDLCNNPMTKEPKLEAAVRIVPEWQDYDQEIKQLQIRFQKEKETGALYKEKTKEPSREGPQKREEL
2
MGVLVVLTVLWLFSSVKADSKAITTSLTTKWFSTPLLLEASEFLAEDSQEKFWNFVEASQNIGSSDHDGTDYSYYHAILEAAFQFLSPLQQNLFKFCLSLRSYSATIQAFQQIAADEPPPEGCNSFFSVHGKKTCESDTLEALLLTASERPKPLLFKGDHRYPSSNPESPVVIFYSEIGSEEFSNFHRQLISKSNAGKINYVFRHYIFNPRKEPVYLSGYGVELAIKSTEYKAKDDTQVKGTEVNTTVIGENDPIDEVQGFLFGKLRDLHPDLEGQLKELRKHLVESTNEMAPLKVWQLQDLSFQTAARILASPVELALVVMKDLSQNFPTKARAITKTAVSSELRTEVEENQKYFKGTLGLQPGDSALFINGLHMDLDTQDIFSLFDVLRNEARVMEGLHRLGIEGLSLHNVLKLNIQPSEADYAVDIRSPAISWVNNLEVDSRYNSWPSSLQELLRPTFPGVIRQIRKNLHNMVFIVDPAHETTAELMNTAEMFLSNHIPLRIGFIFVVNDSEDVDGMQDAGVAVLRAYNYVAQEVDDYHAFQTLTHIYNKVRTGEKVKVEHVVSVLEKKYPYVEVNSILGIDSAYDRNRKEARGYYEQTGVGPLPVVLFNGMPFEREQLDPDELETITMHKILETTTFFQRAVYLGELPHDQDVVEYIMNQPNVVPRINSRILTAERDYLDLTASNNFFVDDYARFTILDSQGKTAAVANSMNYLTKKGMSSKEIYDDSFIRPVTFWIVGDFDSPSGRQLLYDAIKHQKSSNNVRISMINNPAKEISYENTQISRAIWAALQTQTSNAAKNFITKMAKEGAAEALAAGADIAEFSVGGMDFSLFKEVFESSKMDFILSHAVYCRDVLKLKKGQRAVISNGRIIGPLEDSELFNQDDFHLLENIILKTSGQKIKSHIQQLRVEEDVASDLVMKVDALLSAQPKGDPRIEYQFFEDRHSAIKLRPKEGETYFDVVAVVDPVTREAQRLAPLLLVLAQLINMNLRVFMNCQSKLSDMPLKSFYRYVLEPEISFTSDNSFAKGPIAKFLDMPQSPLFTLNLNTPESWMVESVRTPYDLDNIYLEEVDSVVAAEYELEYLLLEGHCYDITTGQPPRGLQFTLGTSANPVIVDTIVMANLGYFQLKANPGAWILRLRKGRSEDIYRIYSHDGTDSPPDADEVVIVLNNFKSKIIKVKVQKKADMVNEDLLSDGTSENESGFWDSFKWGFTGQKTEEVKQDKDDIINIFSVASGHLYERFLRIMMLSVLKNTKTPVKFWFLKNYLSPTFKEFIPYMANEYNFQYELVQYKWPRWLHQQTEKQRIIWGYKILFLDVLFPLVVDKFLFVDADQIVRTDLKELRDFNLDGAPYGYTPFCDSRREMDGYRFWKSGYWASHLAGRKYHISALYVVDLKKFRKIAAGDRLRGQYQGLSQDPNSLSNLDQDLPNNMIHQVPIKSLPQEWLWCETWCDDASKKRAKTIDLCNNPMTKEPKLEAAVRIVPEWQDYDQEIKQLQIRFQKEKETGALYKEKTKEPSREGPQKREEL
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true