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Sequence of UGPA_HUMAN

EC Number:2.7.7.9

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
UTP-glucose-1-phosphate uridylyltransferase
Q16851
Homo sapiens
508
56940
Reaction
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Other sequences found for EC No. 2.7.7.9

General information:

Sequence
show sequence in fasta format
  0 MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH TKKDLDGFRK
 60 LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
120 MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
180 CRVKIYTFNQ SRYPRINKES LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
240 GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
300 KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNAKTLD
360 GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
420 KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
480 NHGDRIDIPP GAVLENKIVS GNLRILDH
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
498096
Peng H.-L.,Chang H.-Y.
Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by complementation of the bacterial galU mutation.
FEBS Lett.
329
153-158
1993
498097
Duggleby R.G.,Chao Y.C.,Huang J.G.,Peng H.-L.,Chang H.-Y.
Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli.
Eur. J. Biochem.
235
173-179
1996
498098
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
498099
Chang H.-Y.,Peng H.-L.,Chao Y.C.,Duggleby R.G.
The importance of conserved residues in human liver UDPglucose pyrophosphorylase.
Eur. J. Biochem.
236
723-728
1996
498100
Choudhary C.,Kumar C.,Gnad F.,Nielsen M.L.,Rehman M.,Walther T.C.,Olsen J.V.,Mann M.
Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Science
325
834-840
2009
498101
Olsen J.V.,Vermeulen M.,Santamaria A.,Kumar C.,Miller M.L.,Jensen L.J.,Gnad F.,Cox J.,Jensen T.S.,Nigg E.A.,Brunak S.,Mann M.
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Sci. Signal.
3
0-0
2010
498102
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
498103
Rigbolt K.T.,Prokhorova T.A.,Akimov V.,Henningsen J.,Johansen P.T.,Kratchmarova I.,Kassem M.,Mann M.,Olsen J.V.,Blagoev B.
System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
Sci. Signal.
4
0-0
2011
498104
Bienvenut W.V.,Sumpton D.,Martinez A.,Lilla S.,Espagne C.,Meinnel T.,Giglione C.
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
Mol. Cell. Proteomics
11
0-0
2012
498105
Van Damme P.,Lasa M.,Polevoda B.,Gazquez C.,Elosegui-Artola A.,Kim D.S.,De Juan-Pardo E.,Demeyer K.,Hole K.,Larrea E.,Timmerman E.,Prieto J.,Arnesen T.,Sherman F.,Gevaert K.,Aldabe R.
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
2012
498106
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
498107
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
498108
Perenthaler E.,Nikoncuk A.,Yousefi S.,Berdowski W.M.,Alsagob M.,Capo I.,van der Linde H.C.,van den Berg P.,Jacobs E.H.,Putar D.,Ghazvini M.,Aronica E.,van Ijcken W.F.J.,de Valk W.G.,Medici-van den Herik E.,van Slegtenhorst M.,Brick L.,Kozenko M.,Kohler J.N.,Bernstein J.A.,Monaghan K.G.,Begtrup A.,Torene R.,Al Futaisi A.,Al Murshedi F.,Mani R.,Al Azri F.,Kamsteeg E.J.,Mojarrad M.,Eslahi A.,Khazaei Z.,Darmiyan F.M.,Doosti M.,Karimiani E.G.,Vandrovcova J.,Zafar F.,Rana N.,Kandaswamy K.K.,Hertecant J.,Bauer P.,Almuhaizea M.A.,Salih M.A.,Aldosary M.,Almass R.,Al-Quait L.,Qubbaj W.,Coskun S.,Alahmadi K.O.,Hamad M.H.A.,Alwadaee S.,Awartani K.,Dababo A.M.,Almohanna F.,Colak D.,Dehghani M.,Mehrjardi M.Y.V.,Gunel M.,Ercan-Sencicek A.G.,Passi G.R.,Cheema H.A.,Efthymiou S.,Houlden H.,Bertoli-Avella A.M.,Brooks A.S.,Retterer K.,Maroofian R.,Kaya N.,van Ham T.J.,Barakat T.S.
Loss of UGP2 in brain leads to a severe epileptic encephalopathy, emphasizing that bi-allelic isoform-specific start-loss mutations of essential genes can cause genetic diseases.
Acta Neuropathol.
139
415-442
2020
498109
Yu Q.,Zheng X.
The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity.
Biochem. J.
442
283-291
2012
498110
Fuhring J.I.,Cramer J.T.,Schneider J.,Baruch P.,Gerardy-Schahn R.,Fedorov R.
A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.
Sci. Rep.
5
9618-9618
2015