Full text data of PGM2L1
PGM2L1
(BM32A)
[Confidence: low (only semi-automatic identification from reviews)]
Glucose 1,6-bisphosphate synthase; 2.7.1.106 (PMMLP; Phosphoglucomutase-2-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Glucose 1,6-bisphosphate synthase; 2.7.1.106 (PMMLP; Phosphoglucomutase-2-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6PCE3
ID PGM2L_HUMAN Reviewed; 622 AA.
AC Q6PCE3; Q96MQ7; Q9UIK3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Glucose 1,6-bisphosphate synthase;
DE EC=2.7.1.106;
DE AltName: Full=PMMLP;
DE AltName: Full=Phosphoglucomutase-2-like 1;
GN Name=PGM2L1; Synonyms=BM32A;
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].
RC TISSUE=Brain;
RA Mori K., Miyoshi Y., Nakamura Y.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-531.
RC TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-14 AND
RP ILE-531.
RC TISSUE=Placenta;
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 [5]
RP FUNCTION.
RX PubMed=17804405; DOI=10.1074/jbc.M706818200;
RA Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Molecular identification of mammalian phosphopentomutase and glucose-
RT 1,6-bisphosphate synthase, two members of the alpha-D-
RT phosphohexomutase family.";
RL J. Biol. Chem. 282:31844-31851(2007).
RN [6]
RP FUNCTION.
RX PubMed=18927083; DOI=10.1074/jbc.M805224200;
RA Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G.,
RA Van Schaftingen E.;
RT "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-
RT 1,6-bisphosphatase.";
RL J. Biol. Chem. 283:33988-33993(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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).
CC -!- FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-
CC bisphosphoglycerate as a phosphate donor and a series of 1-
CC phosphate sugars as acceptors, including glucose 1-phosphate,
CC mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-
CC phosphate. 5 or 6-phosphosugars are bad substrates, with the
CC exception of glucose 6-phosphate. Also synthesizes ribose 1,5-
CC bisphosphate. Has only low phosphopentomutase and
CC phosphoglucomutase activities.
CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate + alpha-D-
CC glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-
CC bisphosphate.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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; AB019210; BAA82756.1; -; mRNA.
DR EMBL; AK056591; BAB71227.1; -; mRNA.
DR EMBL; AP001085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059360; AAH59360.1; -; mRNA.
DR RefSeq; NP_775853.2; NM_173582.3.
DR UniGene; Hs.26612; -.
DR ProteinModelPortal; Q6PCE3; -.
DR SMR; Q6PCE3; 67-207.
DR STRING; 9606.ENSP00000298198; -.
DR PhosphoSite; Q6PCE3; -.
DR DMDM; 71153044; -.
DR PaxDb; Q6PCE3; -.
DR PRIDE; Q6PCE3; -.
DR DNASU; 283209; -.
DR Ensembl; ENST00000298198; ENSP00000298198; ENSG00000165434.
DR GeneID; 283209; -.
DR KEGG; hsa:283209; -.
DR UCSC; uc001ovb.1; human.
DR CTD; 283209; -.
DR GeneCards; GC11M074041; -.
DR HGNC; HGNC:20898; PGM2L1.
DR MIM; 611610; gene.
DR neXtProt; NX_Q6PCE3; -.
DR PharmGKB; PA134938366; -.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268676; -.
DR HOVERGEN; HBG056917; -.
DR InParanoid; Q6PCE3; -.
DR KO; K11809; -.
DR OMA; NMTYNEV; -.
DR OrthoDB; EOG715Q3R; -.
DR PhylomeDB; Q6PCE3; -.
DR ChiTaRS; PGM2L1; human.
DR GenomeRNAi; 283209; -.
DR NextBio; 93718; -.
DR PRO; PR:Q6PCE3; -.
DR ArrayExpress; Q6PCE3; -.
DR Bgee; Q6PCE3; -.
DR CleanEx; HS_PGM2L1; -.
DR Genevestigator; Q6PCE3; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:RefGenome.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:RefGenome.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.120.10; -; 3.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR PROSITE; PS00710; PGM_PMM; FALSE_NEG.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Complete proteome; Glucose metabolism;
KW Isomerase; Phosphoprotein; Polymorphism; Reference proteome;
KW Transferase.
FT CHAIN 1 622 Glucose 1,6-bisphosphate synthase.
FT /FTId=PRO_0000147784.
FT ACT_SITE 175 175 Phosphoserine intermediate (By
FT similarity).
FT MOD_RES 175 175 Phosphoserine.
FT VARIANT 14 14 L -> P (in dbSNP:rs12049823).
FT /FTId=VAR_028094.
FT VARIANT 531 531 V -> I (in dbSNP:rs592644).
FT /FTId=VAR_028095.
FT VARIANT 608 608 N -> I (in dbSNP:rs36014178).
FT /FTId=VAR_056665.
FT CONFLICT 69 69 T -> A (in Ref. 2; BAB71227).
SQ SEQUENCE 622 AA; 70442 MW; 8AE00403B5D973CA CRC64;
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM
EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL
FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII
DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE
KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD VTTGYDSSQP
NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK
LIDALIENFL QPSKNGLIWR SV
//
ID PGM2L_HUMAN Reviewed; 622 AA.
AC Q6PCE3; Q96MQ7; Q9UIK3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=Glucose 1,6-bisphosphate synthase;
DE EC=2.7.1.106;
DE AltName: Full=PMMLP;
DE AltName: Full=Phosphoglucomutase-2-like 1;
GN Name=PGM2L1; Synonyms=BM32A;
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].
RC TISSUE=Brain;
RA Mori K., Miyoshi Y., Nakamura Y.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-531.
RC TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-14 AND
RP ILE-531.
RC TISSUE=Placenta;
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 [5]
RP FUNCTION.
RX PubMed=17804405; DOI=10.1074/jbc.M706818200;
RA Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Molecular identification of mammalian phosphopentomutase and glucose-
RT 1,6-bisphosphate synthase, two members of the alpha-D-
RT phosphohexomutase family.";
RL J. Biol. Chem. 282:31844-31851(2007).
RN [6]
RP FUNCTION.
RX PubMed=18927083; DOI=10.1074/jbc.M805224200;
RA Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G.,
RA Van Schaftingen E.;
RT "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-
RT 1,6-bisphosphatase.";
RL J. Biol. Chem. 283:33988-33993(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, 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).
CC -!- FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-
CC bisphosphoglycerate as a phosphate donor and a series of 1-
CC phosphate sugars as acceptors, including glucose 1-phosphate,
CC mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-
CC phosphate. 5 or 6-phosphosugars are bad substrates, with the
CC exception of glucose 6-phosphate. Also synthesizes ribose 1,5-
CC bisphosphate. Has only low phosphopentomutase and
CC phosphoglucomutase activities.
CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate + alpha-D-
CC glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-
CC bisphosphate.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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; AB019210; BAA82756.1; -; mRNA.
DR EMBL; AK056591; BAB71227.1; -; mRNA.
DR EMBL; AP001085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059360; AAH59360.1; -; mRNA.
DR RefSeq; NP_775853.2; NM_173582.3.
DR UniGene; Hs.26612; -.
DR ProteinModelPortal; Q6PCE3; -.
DR SMR; Q6PCE3; 67-207.
DR STRING; 9606.ENSP00000298198; -.
DR PhosphoSite; Q6PCE3; -.
DR DMDM; 71153044; -.
DR PaxDb; Q6PCE3; -.
DR PRIDE; Q6PCE3; -.
DR DNASU; 283209; -.
DR Ensembl; ENST00000298198; ENSP00000298198; ENSG00000165434.
DR GeneID; 283209; -.
DR KEGG; hsa:283209; -.
DR UCSC; uc001ovb.1; human.
DR CTD; 283209; -.
DR GeneCards; GC11M074041; -.
DR HGNC; HGNC:20898; PGM2L1.
DR MIM; 611610; gene.
DR neXtProt; NX_Q6PCE3; -.
DR PharmGKB; PA134938366; -.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268676; -.
DR HOVERGEN; HBG056917; -.
DR InParanoid; Q6PCE3; -.
DR KO; K11809; -.
DR OMA; NMTYNEV; -.
DR OrthoDB; EOG715Q3R; -.
DR PhylomeDB; Q6PCE3; -.
DR ChiTaRS; PGM2L1; human.
DR GenomeRNAi; 283209; -.
DR NextBio; 93718; -.
DR PRO; PR:Q6PCE3; -.
DR ArrayExpress; Q6PCE3; -.
DR Bgee; Q6PCE3; -.
DR CleanEx; HS_PGM2L1; -.
DR Genevestigator; Q6PCE3; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:RefGenome.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:RefGenome.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.120.10; -; 3.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR PROSITE; PS00710; PGM_PMM; FALSE_NEG.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Complete proteome; Glucose metabolism;
KW Isomerase; Phosphoprotein; Polymorphism; Reference proteome;
KW Transferase.
FT CHAIN 1 622 Glucose 1,6-bisphosphate synthase.
FT /FTId=PRO_0000147784.
FT ACT_SITE 175 175 Phosphoserine intermediate (By
FT similarity).
FT MOD_RES 175 175 Phosphoserine.
FT VARIANT 14 14 L -> P (in dbSNP:rs12049823).
FT /FTId=VAR_028094.
FT VARIANT 531 531 V -> I (in dbSNP:rs592644).
FT /FTId=VAR_028095.
FT VARIANT 608 608 N -> I (in dbSNP:rs36014178).
FT /FTId=VAR_056665.
FT CONFLICT 69 69 T -> A (in Ref. 2; BAB71227).
SQ SEQUENCE 622 AA; 70442 MW; 8AE00403B5D973CA CRC64;
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM
EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL
FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII
DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE
KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD VTTGYDSSQP
NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK
LIDALIENFL QPSKNGLIWR SV
//
MIM
611610
*RECORD*
*FIELD* NO
611610
*FIELD* TI
*611610 PHOSPHOGLUCOMUTASE 2-LIKE 1; PGM2L1
*FIELD* TX
By database searching with the sequence of PGM2 (172000) as query,
read moreMaliekal et al. (2007) identified PGM2L1. The deduced 622-amino acid
PGM2L1 protein has a molecular mass of 72 kD and shares 60% sequence
identity with the PGM2 protein. Sequence analysis suggested that PGM2L1
is a cytosolic protein. Quantitative RT-PCR of mouse tissues showed that
PGM2L1 was mainly expressed in brain where glucose-1,6-bisphosphate
synthase activity was previously shown to be particularly high. High
expression was also detected in testis, and intermediate expression was
found in thymus, spleen, lung, and skeletal muscle.
GENE FUNCTION
In studies with PGM2 and PGM2L1 in E. coli, Maliekal et al. (2007) found
that PGM2 acted more than 10-fold better as a phosphopentomutase (both
on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a
phosphoglucomutase, while PGM2L1 was about 5- to 20-fold better in
catalyzing the 1,3-bisphosphoglycerate-dependent synthesis of glucose
1,6-bisphosphate and other aldose-bisphosphates.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PGM2L1
gene to chromosome 11 (TMAP WI-15948). Scott (2007) mapped the gene to
11q13.4 based on an alignment of the PGM2L1 sequence (GenBank GENBANK
AB019210) with the genomic sequence (build 36.2).
*FIELD* RF
1. Maliekal, P.; Sokolova, T.; Vertommen, D.; Veiga-da-Cunha, M.;
Van Schaftingen, E.: Molecular identification of mammalian phosphopentomutase
and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase
family. J. Biol. Chem. 282: 31844-31851, 2007.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 11/20/2007.
*FIELD* CD
Alan F. Scott: 11/21/2007
*FIELD* ED
carol: 11/21/2007
*RECORD*
*FIELD* NO
611610
*FIELD* TI
*611610 PHOSPHOGLUCOMUTASE 2-LIKE 1; PGM2L1
*FIELD* TX
By database searching with the sequence of PGM2 (172000) as query,
read moreMaliekal et al. (2007) identified PGM2L1. The deduced 622-amino acid
PGM2L1 protein has a molecular mass of 72 kD and shares 60% sequence
identity with the PGM2 protein. Sequence analysis suggested that PGM2L1
is a cytosolic protein. Quantitative RT-PCR of mouse tissues showed that
PGM2L1 was mainly expressed in brain where glucose-1,6-bisphosphate
synthase activity was previously shown to be particularly high. High
expression was also detected in testis, and intermediate expression was
found in thymus, spleen, lung, and skeletal muscle.
GENE FUNCTION
In studies with PGM2 and PGM2L1 in E. coli, Maliekal et al. (2007) found
that PGM2 acted more than 10-fold better as a phosphopentomutase (both
on deoxyribose 1-phosphate and on ribose 1-phosphate) than as a
phosphoglucomutase, while PGM2L1 was about 5- to 20-fold better in
catalyzing the 1,3-bisphosphoglycerate-dependent synthesis of glucose
1,6-bisphosphate and other aldose-bisphosphates.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PGM2L1
gene to chromosome 11 (TMAP WI-15948). Scott (2007) mapped the gene to
11q13.4 based on an alignment of the PGM2L1 sequence (GenBank GENBANK
AB019210) with the genomic sequence (build 36.2).
*FIELD* RF
1. Maliekal, P.; Sokolova, T.; Vertommen, D.; Veiga-da-Cunha, M.;
Van Schaftingen, E.: Molecular identification of mammalian phosphopentomutase
and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase
family. J. Biol. Chem. 282: 31844-31851, 2007.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 11/20/2007.
*FIELD* CD
Alan F. Scott: 11/21/2007
*FIELD* ED
carol: 11/21/2007