Full text data of UGP2
UGP2
(UGP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
UTP--glucose-1-phosphate uridylyltransferase; 2.7.7.9 (UDP-glucose pyrophosphorylase; UDPGP; UGPase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UTP--glucose-1-phosphate uridylyltransferase; 2.7.7.9 (UDP-glucose pyrophosphorylase; UDPGP; UGPase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00014919
IPI00014919 UTP--glucose-1-phosphate uridylyltransferase 1 Plays a central role as a glucosyl donor in cellular metabolic pathways soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00014919 UTP--glucose-1-phosphate uridylyltransferase 1 Plays a central role as a glucosyl donor in cellular metabolic pathways soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q16851
ID UGPA_HUMAN Reviewed; 508 AA.
AC Q16851; Q07131; Q0P6K2; Q86Y81; Q9BU15;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 5.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE EC=2.7.7.9;
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase;
GN Name=UGP2; Synonyms=UGP1;
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), SUBCELLULAR LOCATION, AND
RP VARIANT ILE-268.
RC TISSUE=Liver;
RX PubMed=8354390; DOI=10.1016/0014-5793(93)80213-E;
RA Peng H.-L., Chang H.-Y.;
RT "Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by
RT complementation of the bacterial galU mutation.";
RL FEBS Lett. 329:153-158(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-268.
RC TISSUE=Skeletal muscle;
RX PubMed=8631325; DOI=10.1111/j.1432-1033.1996.00173.x;
RA Duggleby R.G., Chao Y.C., Huang J.G., Peng H.-L., Chang H.-Y.;
RT "Sequence differences between human muscle and liver cDNAs for
RT UDPglucose pyrophosphorylase and kinetic properties of the recombinant
RT enzymes expressed in Escherichia coli.";
RL Eur. J. Biochem. 235:173-179(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Lymph, and Skin;
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 MUTAGENESIS.
RX PubMed=8612650; DOI=10.1111/j.1432-1033.1996.t01-1-00723.x;
RA Chang H.-Y., Peng H.-L., Chao Y.C., Duggleby R.G.;
RT "The importance of conserved residues in human liver UDPglucose
RT pyrophosphorylase.";
RL Eur. J. Biochem. 236:723-728(1996).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-438, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.57 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP 502-ASP--LEU-503.
RX PubMed=22132858; DOI=10.1042/BJ20111598;
RA Yu Q., Zheng X.;
RT "The crystal structure of human UDP-glucose pyrophosphorylase reveals
RT a latch effect that influences enzymatic activity.";
RL Biochem. J. 442:283-291(2012).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways.
CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate =
CC diphosphate + UDP-glucose.
CC -!- SUBUNIT: Homooctamer.
CC -!- INTERACTION:
CC P62993:GRB2; NbExp=2; IntAct=EBI-743729, EBI-401755;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16851-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16851-2; Sequence=VSP_012834;
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family.
CC -!- CAUTION: The human genome was initially thought to contain 2 genes
CC for UTP--glucose-1-phosphate uridylyltransferase: UGP1 and UGP2.
CC However, the sequence defined as UGP1 (PubMed:8354390) probably
CC does not exist and corresponds to UGP2.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U27460; AAB05640.1; -; mRNA.
DR EMBL; BC000173; AAH00173.2; -; mRNA.
DR EMBL; BC002954; AAH02954.1; -; mRNA.
DR EMBL; BC047004; AAH47004.1; -; mRNA.
DR PIR; S35692; S35692.
DR RefSeq; NP_001001521.1; NM_001001521.1.
DR RefSeq; NP_006750.3; NM_006759.3.
DR RefSeq; XP_005264594.1; XM_005264537.1.
DR RefSeq; XP_005264595.1; XM_005264538.1.
DR UniGene; Hs.516217; -.
DR PDB; 3R2W; X-ray; 3.60 A; A/B/C/D=1-508.
DR PDB; 3R3I; X-ray; 3.57 A; A/B/C/D=1-508.
DR PDBsum; 3R2W; -.
DR PDBsum; 3R3I; -.
DR ProteinModelPortal; Q16851; -.
DR SMR; Q16851; 22-500.
DR IntAct; Q16851; 6.
DR MINT; MINT-1468909; -.
DR STRING; 9606.ENSP00000338703; -.
DR PhosphoSite; Q16851; -.
DR DMDM; 59803098; -.
DR REPRODUCTION-2DPAGE; IPI00395676; -.
DR UCD-2DPAGE; Q16851; -.
DR PaxDb; Q16851; -.
DR PRIDE; Q16851; -.
DR DNASU; 7360; -.
DR Ensembl; ENST00000337130; ENSP00000338703; ENSG00000169764.
DR Ensembl; ENST00000394417; ENSP00000377939; ENSG00000169764.
DR Ensembl; ENST00000467648; ENSP00000420793; ENSG00000169764.
DR GeneID; 7360; -.
DR KEGG; hsa:7360; -.
DR UCSC; uc002scl.3; human.
DR CTD; 7360; -.
DR GeneCards; GC02P064068; -.
DR HGNC; HGNC:12527; UGP2.
DR HPA; HPA034696; -.
DR MIM; 191750; gene.
DR MIM; 191760; gene.
DR neXtProt; NX_Q16851; -.
DR PharmGKB; PA37172; -.
DR eggNOG; COG4284; -.
DR HOGENOM; HOG000113618; -.
DR HOVERGEN; HBG055396; -.
DR InParanoid; Q16851; -.
DR KO; K00963; -.
DR OrthoDB; EOG7ZPNK4; -.
DR PhylomeDB; Q16851; -.
DR BioCyc; MetaCyc:HS10006-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q16851; -.
DR ChiTaRS; UGP2; human.
DR GenomeRNAi; 7360; -.
DR NextBio; 28818; -.
DR PRO; PR:Q16851; -.
DR ArrayExpress; Q16851; -.
DR Bgee; Q16851; -.
DR CleanEx; HS_UGP2; -.
DR Genevestigator; Q16851; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; TAS:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; TAS:Reactome.
DR GO; GO:0006006; P:glucose metabolic process; TAS:Reactome.
DR GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; TAS:ProtInc.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR002618; UDPGP_trans.
DR InterPro; IPR016267; UDPGP_trans_subgr.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR PANTHER; PTHR11952:SF1; PTHR11952:SF1; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Phosphoprotein; Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 508 UTP--glucose-1-phosphate
FT uridylyltransferase.
FT /FTId=PRO_0000185752.
FT REGION 457 508 Oligomerization.
FT REGION 502 503 Critical for end-to-end subunit
FT interaction.
FT ACT_SITE 396 396 By similarity.
FT METAL 127 127 Magnesium (By similarity).
FT METAL 253 253 Magnesium (By similarity).
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 438 438 N6-acetyllysine.
FT VAR_SEQ 1 11 Missing (in isoform 2).
FT /FTId=VSP_012834.
FT VARIANT 268 268 M -> I (in dbSNP:rs1130982).
FT /FTId=VAR_033042.
FT MUTAGEN 123 123 C->S: No significant loss of activity.
FT MUTAGEN 218 218 W->S: No significant loss of activity.
FT MUTAGEN 266 266 H->R: No significant loss of activity.
FT MUTAGEN 333 333 W->S: Loss of activity; possibly due to
FT folding defect.
FT MUTAGEN 389 389 R->H: No significant loss of activity.
FT MUTAGEN 391 391 R->H: Loss of activity; possibly due to
FT folding defect.
FT MUTAGEN 422 422 R->H: No significant loss of activity.
FT MUTAGEN 445 445 R->H: No significant loss of activity.
FT MUTAGEN 502 503 NL->PE: Abolishes oligomerization and
FT significantly increases enzymatic
FT activity.
FT CONFLICT 25 25 R -> L (in Ref. 1).
FT CONFLICT 44 44 S -> T (in Ref. 1).
FT CONFLICT 48 48 F -> Y (in Ref. 1).
FT CONFLICT 62 62 F -> Y (in Ref. 1).
FT CONFLICT 152 152 T -> S (in Ref. 1).
FT CONFLICT 202 202 L -> R (in Ref. 1 and 2; AAB05640).
FT CONFLICT 210 210 Y -> S (in Ref. 1).
FT CONFLICT 214 214 N -> S (in Ref. 1).
FT CONFLICT 240 241 IG -> LE (in Ref. 1).
FT CONFLICT 356 356 A -> P (in Ref. 1).
SQ SEQUENCE 508 AA; 56940 MW; 60E54806807AB470 CRC64;
MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH TKKDLDGFRK
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
CRVKIYTFNQ SRYPRINKES LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNAKTLD
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
NHGDRIDIPP GAVLENKIVS GNLRILDH
//
ID UGPA_HUMAN Reviewed; 508 AA.
AC Q16851; Q07131; Q0P6K2; Q86Y81; Q9BU15;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 5.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE EC=2.7.7.9;
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase;
GN Name=UGP2; Synonyms=UGP1;
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), SUBCELLULAR LOCATION, AND
RP VARIANT ILE-268.
RC TISSUE=Liver;
RX PubMed=8354390; DOI=10.1016/0014-5793(93)80213-E;
RA Peng H.-L., Chang H.-Y.;
RT "Cloning of a human liver UDP-glucose pyrophosphorylase cDNA by
RT complementation of the bacterial galU mutation.";
RL FEBS Lett. 329:153-158(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-268.
RC TISSUE=Skeletal muscle;
RX PubMed=8631325; DOI=10.1111/j.1432-1033.1996.00173.x;
RA Duggleby R.G., Chao Y.C., Huang J.G., Peng H.-L., Chang H.-Y.;
RT "Sequence differences between human muscle and liver cDNAs for
RT UDPglucose pyrophosphorylase and kinetic properties of the recombinant
RT enzymes expressed in Escherichia coli.";
RL Eur. J. Biochem. 235:173-179(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, Lymph, and Skin;
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 MUTAGENESIS.
RX PubMed=8612650; DOI=10.1111/j.1432-1033.1996.t01-1-00723.x;
RA Chang H.-Y., Peng H.-L., Chao Y.C., Duggleby R.G.;
RT "The importance of conserved residues in human liver UDPglucose
RT pyrophosphorylase.";
RL Eur. J. Biochem. 236:723-728(1996).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-438, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.57 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP 502-ASP--LEU-503.
RX PubMed=22132858; DOI=10.1042/BJ20111598;
RA Yu Q., Zheng X.;
RT "The crystal structure of human UDP-glucose pyrophosphorylase reveals
RT a latch effect that influences enzymatic activity.";
RL Biochem. J. 442:283-291(2012).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways.
CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate =
CC diphosphate + UDP-glucose.
CC -!- SUBUNIT: Homooctamer.
CC -!- INTERACTION:
CC P62993:GRB2; NbExp=2; IntAct=EBI-743729, EBI-401755;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16851-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16851-2; Sequence=VSP_012834;
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family.
CC -!- CAUTION: The human genome was initially thought to contain 2 genes
CC for UTP--glucose-1-phosphate uridylyltransferase: UGP1 and UGP2.
CC However, the sequence defined as UGP1 (PubMed:8354390) probably
CC does not exist and corresponds to UGP2.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U27460; AAB05640.1; -; mRNA.
DR EMBL; BC000173; AAH00173.2; -; mRNA.
DR EMBL; BC002954; AAH02954.1; -; mRNA.
DR EMBL; BC047004; AAH47004.1; -; mRNA.
DR PIR; S35692; S35692.
DR RefSeq; NP_001001521.1; NM_001001521.1.
DR RefSeq; NP_006750.3; NM_006759.3.
DR RefSeq; XP_005264594.1; XM_005264537.1.
DR RefSeq; XP_005264595.1; XM_005264538.1.
DR UniGene; Hs.516217; -.
DR PDB; 3R2W; X-ray; 3.60 A; A/B/C/D=1-508.
DR PDB; 3R3I; X-ray; 3.57 A; A/B/C/D=1-508.
DR PDBsum; 3R2W; -.
DR PDBsum; 3R3I; -.
DR ProteinModelPortal; Q16851; -.
DR SMR; Q16851; 22-500.
DR IntAct; Q16851; 6.
DR MINT; MINT-1468909; -.
DR STRING; 9606.ENSP00000338703; -.
DR PhosphoSite; Q16851; -.
DR DMDM; 59803098; -.
DR REPRODUCTION-2DPAGE; IPI00395676; -.
DR UCD-2DPAGE; Q16851; -.
DR PaxDb; Q16851; -.
DR PRIDE; Q16851; -.
DR DNASU; 7360; -.
DR Ensembl; ENST00000337130; ENSP00000338703; ENSG00000169764.
DR Ensembl; ENST00000394417; ENSP00000377939; ENSG00000169764.
DR Ensembl; ENST00000467648; ENSP00000420793; ENSG00000169764.
DR GeneID; 7360; -.
DR KEGG; hsa:7360; -.
DR UCSC; uc002scl.3; human.
DR CTD; 7360; -.
DR GeneCards; GC02P064068; -.
DR HGNC; HGNC:12527; UGP2.
DR HPA; HPA034696; -.
DR MIM; 191750; gene.
DR MIM; 191760; gene.
DR neXtProt; NX_Q16851; -.
DR PharmGKB; PA37172; -.
DR eggNOG; COG4284; -.
DR HOGENOM; HOG000113618; -.
DR HOVERGEN; HBG055396; -.
DR InParanoid; Q16851; -.
DR KO; K00963; -.
DR OrthoDB; EOG7ZPNK4; -.
DR PhylomeDB; Q16851; -.
DR BioCyc; MetaCyc:HS10006-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q16851; -.
DR ChiTaRS; UGP2; human.
DR GenomeRNAi; 7360; -.
DR NextBio; 28818; -.
DR PRO; PR:Q16851; -.
DR ArrayExpress; Q16851; -.
DR Bgee; Q16851; -.
DR CleanEx; HS_UGP2; -.
DR Genevestigator; Q16851; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; TAS:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; TAS:Reactome.
DR GO; GO:0006006; P:glucose metabolic process; TAS:Reactome.
DR GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; TAS:ProtInc.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR002618; UDPGP_trans.
DR InterPro; IPR016267; UDPGP_trans_subgr.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR PANTHER; PTHR11952:SF1; PTHR11952:SF1; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Phosphoprotein; Polymorphism; Reference proteome; Transferase.
FT CHAIN 1 508 UTP--glucose-1-phosphate
FT uridylyltransferase.
FT /FTId=PRO_0000185752.
FT REGION 457 508 Oligomerization.
FT REGION 502 503 Critical for end-to-end subunit
FT interaction.
FT ACT_SITE 396 396 By similarity.
FT METAL 127 127 Magnesium (By similarity).
FT METAL 253 253 Magnesium (By similarity).
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 438 438 N6-acetyllysine.
FT VAR_SEQ 1 11 Missing (in isoform 2).
FT /FTId=VSP_012834.
FT VARIANT 268 268 M -> I (in dbSNP:rs1130982).
FT /FTId=VAR_033042.
FT MUTAGEN 123 123 C->S: No significant loss of activity.
FT MUTAGEN 218 218 W->S: No significant loss of activity.
FT MUTAGEN 266 266 H->R: No significant loss of activity.
FT MUTAGEN 333 333 W->S: Loss of activity; possibly due to
FT folding defect.
FT MUTAGEN 389 389 R->H: No significant loss of activity.
FT MUTAGEN 391 391 R->H: Loss of activity; possibly due to
FT folding defect.
FT MUTAGEN 422 422 R->H: No significant loss of activity.
FT MUTAGEN 445 445 R->H: No significant loss of activity.
FT MUTAGEN 502 503 NL->PE: Abolishes oligomerization and
FT significantly increases enzymatic
FT activity.
FT CONFLICT 25 25 R -> L (in Ref. 1).
FT CONFLICT 44 44 S -> T (in Ref. 1).
FT CONFLICT 48 48 F -> Y (in Ref. 1).
FT CONFLICT 62 62 F -> Y (in Ref. 1).
FT CONFLICT 152 152 T -> S (in Ref. 1).
FT CONFLICT 202 202 L -> R (in Ref. 1 and 2; AAB05640).
FT CONFLICT 210 210 Y -> S (in Ref. 1).
FT CONFLICT 214 214 N -> S (in Ref. 1).
FT CONFLICT 240 241 IG -> LE (in Ref. 1).
FT CONFLICT 356 356 A -> P (in Ref. 1).
SQ SEQUENCE 508 AA; 56940 MW; 60E54806807AB470 CRC64;
MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTASSHEFEH TKKDLDGFRK
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
CRVKIYTFNQ SRYPRINKES LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGKRCEFVM EVTNKTRADV KGGTLTQYEG
KLRLVEIAQV PKAHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNAKTLD
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIA
NHGDRIDIPP GAVLENKIVS GNLRILDH
//
MIM
191750
*RECORD*
*FIELD* NO
191750
*FIELD* TI
*191750 URIDYL DIPHOSPHATE GLUCOSE PYROPHOSPHORYLASE 1; UGP1
;;UGPP1
*FIELD* TX
The structural locus for this enzyme has been assigned to chromosome 1
read moreby somatic cell studies.
*FIELD* SA
Burgerhout et al. (1973); Van Someren et al. (1974)
*FIELD* RF
1. Burgerhout, W.; Van Someren, H.; Bootsma, D.: Cytological mapping
of the gene assigned to the human A1 chromosome by the use of radiation
induced chromosome breakage in a human-Chinese hamster hybrid cell
line. Humangenetik 20: 159-162, 1973.
2. Van Someren, H.; Van Henegouwen, H. B.; Westerveld, A.; Bootsma,
D.: Synteny of the human loci for fumarate hydratase and UDPG pyrophosphorylase
with chromosome 1 markers in somatic cell hybrids. Cytogenet. Cell
Genet. 13: 551-557, 1974.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
psherman: 07/21/1998
dkim: 7/16/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986
*RECORD*
*FIELD* NO
191750
*FIELD* TI
*191750 URIDYL DIPHOSPHATE GLUCOSE PYROPHOSPHORYLASE 1; UGP1
;;UGPP1
*FIELD* TX
The structural locus for this enzyme has been assigned to chromosome 1
read moreby somatic cell studies.
*FIELD* SA
Burgerhout et al. (1973); Van Someren et al. (1974)
*FIELD* RF
1. Burgerhout, W.; Van Someren, H.; Bootsma, D.: Cytological mapping
of the gene assigned to the human A1 chromosome by the use of radiation
induced chromosome breakage in a human-Chinese hamster hybrid cell
line. Humangenetik 20: 159-162, 1973.
2. Van Someren, H.; Van Henegouwen, H. B.; Westerveld, A.; Bootsma,
D.: Synteny of the human loci for fumarate hydratase and UDPG pyrophosphorylase
with chromosome 1 markers in somatic cell hybrids. Cytogenet. Cell
Genet. 13: 551-557, 1974.
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
psherman: 07/21/1998
dkim: 7/16/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986
MIM
191760
*RECORD*
*FIELD* NO
191760
*FIELD* TI
*191760 URIDYL DIPHOSPHATE GLUCOSE PYROPHOSPHORYLASE 2; UGP2
;;UGPP2;;
UDPG
*FIELD* TX
read more
DESCRIPTION
UDP-glucose pyrophosphorylase (UGP; EC 2.7.7.9) catalyzes the transfer
of a glucose moiety from glucose-1-phosphate to MgUTP, forming
UDP-glucose and MgPPi.
CLONING
Peng and Chang (1993) isolated a UGP cDNA, which they designated UDPG,
by screening a human liver cDNA library for complementation of an E.
coli galU mutation. The UDPG gene encodes a predicted 508-amino acid
protein with no homology to the bacterial protein, but with 47% identity
with potato UDPG. On Northern blots, the 2.2-kb UDPG mRNA is expressed
in all tissues tested, with the highest levels in skeletal muscle.
MAPPING
Shows et al. (1978) assigned UGPP2 to chromosome 2 by means of man-mouse
somatic cell hybrids. The linear order appears to be
(ACP1)-(UGPP2)-(MDH-S)-(IDH-S). Cheng et al. (1997) mapped the UGP2 gene
to 2p14-p13 by fluorescence in situ hybridization.
*FIELD* RF
1. Cheng, S.-D.; Peng, H.-L.; Chang, H.-Y.: Localization of the human
UGP2 gene encoding the muscle isoform of UDPglucose pyrophosphorylase
to 2p13-p14 by fluorescence in situ hybridization. Genomics 39:
414-416, 1997.
2. 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.
3. Shows, T. B.; Brown, J. A.; Goggin, A. P.; Haley, L. L.; Byers,
M. G.; Eddy, R. L.: Assignment of a molecular form of UDP glucose
pyrophosphorylase (UGPP-2) to chromosome 2 in man. Cytogenet. Cell
Genet. 22: 215-218, 1978.
*FIELD* CN
Rebekah S. Rasooly - updated: 3/5/1998
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/21/2010
dkim: 7/16/1998
alopez: 3/5/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986
*RECORD*
*FIELD* NO
191760
*FIELD* TI
*191760 URIDYL DIPHOSPHATE GLUCOSE PYROPHOSPHORYLASE 2; UGP2
;;UGPP2;;
UDPG
*FIELD* TX
read more
DESCRIPTION
UDP-glucose pyrophosphorylase (UGP; EC 2.7.7.9) catalyzes the transfer
of a glucose moiety from glucose-1-phosphate to MgUTP, forming
UDP-glucose and MgPPi.
CLONING
Peng and Chang (1993) isolated a UGP cDNA, which they designated UDPG,
by screening a human liver cDNA library for complementation of an E.
coli galU mutation. The UDPG gene encodes a predicted 508-amino acid
protein with no homology to the bacterial protein, but with 47% identity
with potato UDPG. On Northern blots, the 2.2-kb UDPG mRNA is expressed
in all tissues tested, with the highest levels in skeletal muscle.
MAPPING
Shows et al. (1978) assigned UGPP2 to chromosome 2 by means of man-mouse
somatic cell hybrids. The linear order appears to be
(ACP1)-(UGPP2)-(MDH-S)-(IDH-S). Cheng et al. (1997) mapped the UGP2 gene
to 2p14-p13 by fluorescence in situ hybridization.
*FIELD* RF
1. Cheng, S.-D.; Peng, H.-L.; Chang, H.-Y.: Localization of the human
UGP2 gene encoding the muscle isoform of UDPglucose pyrophosphorylase
to 2p13-p14 by fluorescence in situ hybridization. Genomics 39:
414-416, 1997.
2. 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.
3. Shows, T. B.; Brown, J. A.; Goggin, A. P.; Haley, L. L.; Byers,
M. G.; Eddy, R. L.: Assignment of a molecular form of UDP glucose
pyrophosphorylase (UGPP-2) to chromosome 2 in man. Cytogenet. Cell
Genet. 22: 215-218, 1978.
*FIELD* CN
Rebekah S. Rasooly - updated: 3/5/1998
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/21/2010
dkim: 7/16/1998
alopez: 3/5/1998
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
reenie: 6/2/1986