Full text data of PGM2
PGM2
[Confidence: low (only semi-automatic identification from reviews)]
Phosphoglucomutase-2; PGM 2; 5.4.2.2 (Glucose phosphomutase 2; Phosphodeoxyribomutase; Phosphopentomutase; 5.4.2.7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoglucomutase-2; PGM 2; 5.4.2.2 (Glucose phosphomutase 2; Phosphodeoxyribomutase; Phosphopentomutase; 5.4.2.7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96G03
ID PGM2_HUMAN Reviewed; 612 AA.
AC Q96G03; Q53FP5; Q5QTR0; Q9H0P9; Q9NV22;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Phosphoglucomutase-2;
DE Short=PGM 2;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase 2;
DE AltName: Full=Phosphodeoxyribomutase;
DE AltName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
GN Name=PGM2; ORFNames=MSTP006;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-10.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-10.
RC TISSUE=Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: Catalyzes the conversion of the nucleoside breakdown
CC products ribose-1-phosphate and deoxyribose-1-phosphate to the
CC corresponding 5-phosphopentoses. May also catalyze the
CC interconversion of glucose-1-phosphate and glucose-6-phosphate.
CC Has low glucose 1,6-bisphosphate synthase activity.
CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
CC 6-phosphate.
CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC alpha-D-ribose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.7 uM for alpha-D-ribose 1-phosphate;
CC KM=4.1 uM for 2-deoxy-alpha-D-ribose 1-phosphate;
CC KM=114 uM for alpha-D-glucose 1-phosphate;
CC Vmax=104.3 umol/min/mg enzyme with alpha-D-ribose 1-phosphate as
CC substrate;
CC Vmax=20.8 umol/min/mg enzyme with 2-deoxy-alpha-D-ribose 1-
CC phosphate as substrate;
CC Vmax=22.8 umol/min/mg enzyme with alpha-D-glucose 1-phosphate as
CC substrate;
CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC deoxy-alpha-D-ribose 1-phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR EMBL; AL136705; CAB66640.1; -; mRNA.
DR EMBL; AK001845; BAA91938.1; -; mRNA.
DR EMBL; AF109360; AAQ13508.1; -; mRNA.
DR EMBL; CR457274; CAG33555.1; -; mRNA.
DR EMBL; AK223237; BAD96957.1; -; mRNA.
DR EMBL; BC010087; AAH10087.1; -; mRNA.
DR RefSeq; NP_060760.2; NM_018290.3.
DR UniGene; Hs.23363; -.
DR UniGene; Hs.607816; -.
DR ProteinModelPortal; Q96G03; -.
DR SMR; Q96G03; 57-205.
DR STRING; 9606.ENSP00000371393; -.
DR PhosphoSite; Q96G03; -.
DR DMDM; 116242708; -.
DR PaxDb; Q96G03; -.
DR PeptideAtlas; Q96G03; -.
DR PRIDE; Q96G03; -.
DR Ensembl; ENST00000381967; ENSP00000371393; ENSG00000169299.
DR GeneID; 55276; -.
DR KEGG; hsa:55276; -.
DR UCSC; uc011byb.1; human.
DR CTD; 55276; -.
DR GeneCards; GC04P037828; -.
DR HGNC; HGNC:8906; PGM2.
DR MIM; 172000; gene.
DR neXtProt; NX_Q96G03; -.
DR PharmGKB; PA33243; -.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268676; -.
DR HOVERGEN; HBG056917; -.
DR InParanoid; Q96G03; -.
DR KO; K15779; -.
DR OMA; HRSVNRE; -.
DR OrthoDB; EOG715Q3R; -.
DR PhylomeDB; Q96G03; -.
DR BioCyc; MetaCyc:HS09924-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00002; UER00467.
DR GeneWiki; PGM2; -.
DR GenomeRNAi; 55276; -.
DR NextBio; 59409; -.
DR PRO; PR:Q96G03; -.
DR ArrayExpress; Q96G03; -.
DR Bgee; Q96G03; -.
DR CleanEx; HS_PGM2; -.
DR Genevestigator; Q96G03; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:RefGenome.
DR GO; GO:0008973; F:phosphopentomutase activity; IDA:UniProtKB.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019388; P:galactose catabolic process; 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:0005980; P:glycogen catabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
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 InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Glucose metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 612 Phosphoglucomutase-2.
FT /FTId=PRO_0000147781.
FT ACT_SITE 165 165 Phosphoserine intermediate (By
FT similarity).
FT METAL 165 165 Magnesium; via phosphate group (By
FT similarity).
FT METAL 322 322 Magnesium (By similarity).
FT METAL 324 324 Magnesium (By similarity).
FT METAL 326 326 Magnesium (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 165 165 Phosphoserine.
FT VARIANT 10 10 G -> D (in dbSNP:rs17856324).
FT /FTId=VAR_027968.
FT VARIANT 488 488 E -> D (in dbSNP:rs10001580).
FT /FTId=VAR_027969.
FT CONFLICT 114 114 G -> A (in Ref. 5; BAD96957).
FT CONFLICT 162 162 I -> V (in Ref. 2; BAA91938).
FT CONFLICT 282 282 K -> R (in Ref. 1; CAB66640).
FT CONFLICT 495 495 E -> G (in Ref. 5; BAD96957).
SQ SEQUENCE 612 AA; 68283 MW; 82234DDE810D1F52 CRC64;
MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC FGARMEFGTA
GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG IVISFDARAH PSSGGSSRRF
ARLAATTFIS QGIPVYLFSD ITPTPFVPFT VSHLKLCAGI MITASHNPKQ DNGYKVYWDN
GAQIISPHDK GISQAIEENL EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR
SVNRETKVKF VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK
GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL LGWWLFTSWK
EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT GFKWMGNRAK QLIDQGKTVL
FAFEEAIGYM CCPFVLDKDG VSAAVISAEL ASFLATKNLS LSQQLKAIYV EYGYHITKAS
YFICHDQETI KKLFENLRNY DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK
SSQMITFTFA NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF
QPQKYNLQPK AD
//
ID PGM2_HUMAN Reviewed; 612 AA.
AC Q96G03; Q53FP5; Q5QTR0; Q9H0P9; Q9NV22;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Phosphoglucomutase-2;
DE Short=PGM 2;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase 2;
DE AltName: Full=Phosphodeoxyribomutase;
DE AltName: Full=Phosphopentomutase;
DE EC=5.4.2.7;
GN Name=PGM2; ORFNames=MSTP006;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
RA Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
RA Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-10.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-10.
RC TISSUE=Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: Catalyzes the conversion of the nucleoside breakdown
CC products ribose-1-phosphate and deoxyribose-1-phosphate to the
CC corresponding 5-phosphopentoses. May also catalyze the
CC interconversion of glucose-1-phosphate and glucose-6-phosphate.
CC Has low glucose 1,6-bisphosphate synthase activity.
CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
CC 6-phosphate.
CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
CC phosphate.
CC -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
CC alpha-D-ribose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.7 uM for alpha-D-ribose 1-phosphate;
CC KM=4.1 uM for 2-deoxy-alpha-D-ribose 1-phosphate;
CC KM=114 uM for alpha-D-glucose 1-phosphate;
CC Vmax=104.3 umol/min/mg enzyme with alpha-D-ribose 1-phosphate as
CC substrate;
CC Vmax=20.8 umol/min/mg enzyme with 2-deoxy-alpha-D-ribose 1-
CC phosphate as substrate;
CC Vmax=22.8 umol/min/mg enzyme with alpha-D-glucose 1-phosphate as
CC substrate;
CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC deoxy-alpha-D-ribose 1-phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR EMBL; AL136705; CAB66640.1; -; mRNA.
DR EMBL; AK001845; BAA91938.1; -; mRNA.
DR EMBL; AF109360; AAQ13508.1; -; mRNA.
DR EMBL; CR457274; CAG33555.1; -; mRNA.
DR EMBL; AK223237; BAD96957.1; -; mRNA.
DR EMBL; BC010087; AAH10087.1; -; mRNA.
DR RefSeq; NP_060760.2; NM_018290.3.
DR UniGene; Hs.23363; -.
DR UniGene; Hs.607816; -.
DR ProteinModelPortal; Q96G03; -.
DR SMR; Q96G03; 57-205.
DR STRING; 9606.ENSP00000371393; -.
DR PhosphoSite; Q96G03; -.
DR DMDM; 116242708; -.
DR PaxDb; Q96G03; -.
DR PeptideAtlas; Q96G03; -.
DR PRIDE; Q96G03; -.
DR Ensembl; ENST00000381967; ENSP00000371393; ENSG00000169299.
DR GeneID; 55276; -.
DR KEGG; hsa:55276; -.
DR UCSC; uc011byb.1; human.
DR CTD; 55276; -.
DR GeneCards; GC04P037828; -.
DR HGNC; HGNC:8906; PGM2.
DR MIM; 172000; gene.
DR neXtProt; NX_Q96G03; -.
DR PharmGKB; PA33243; -.
DR eggNOG; COG1109; -.
DR HOGENOM; HOG000268676; -.
DR HOVERGEN; HBG056917; -.
DR InParanoid; Q96G03; -.
DR KO; K15779; -.
DR OMA; HRSVNRE; -.
DR OrthoDB; EOG715Q3R; -.
DR PhylomeDB; Q96G03; -.
DR BioCyc; MetaCyc:HS09924-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00002; UER00467.
DR GeneWiki; PGM2; -.
DR GenomeRNAi; 55276; -.
DR NextBio; 59409; -.
DR PRO; PR:Q96G03; -.
DR ArrayExpress; Q96G03; -.
DR Bgee; Q96G03; -.
DR CleanEx; HS_PGM2; -.
DR Genevestigator; Q96G03; -.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:RefGenome.
DR GO; GO:0008973; F:phosphopentomutase activity; IDA:UniProtKB.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019388; P:galactose catabolic process; 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:0005980; P:glycogen catabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
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 InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Glucose metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 612 Phosphoglucomutase-2.
FT /FTId=PRO_0000147781.
FT ACT_SITE 165 165 Phosphoserine intermediate (By
FT similarity).
FT METAL 165 165 Magnesium; via phosphate group (By
FT similarity).
FT METAL 322 322 Magnesium (By similarity).
FT METAL 324 324 Magnesium (By similarity).
FT METAL 326 326 Magnesium (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 165 165 Phosphoserine.
FT VARIANT 10 10 G -> D (in dbSNP:rs17856324).
FT /FTId=VAR_027968.
FT VARIANT 488 488 E -> D (in dbSNP:rs10001580).
FT /FTId=VAR_027969.
FT CONFLICT 114 114 G -> A (in Ref. 5; BAD96957).
FT CONFLICT 162 162 I -> V (in Ref. 2; BAA91938).
FT CONFLICT 282 282 K -> R (in Ref. 1; CAB66640).
FT CONFLICT 495 495 E -> G (in Ref. 5; BAD96957).
SQ SEQUENCE 612 AA; 68283 MW; 82234DDE810D1F52 CRC64;
MAAPEGSGLG EDARLDQETA QWLRWDKNSL TLEAVKRLIA EGNKEELRKC FGARMEFGTA
GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG IVISFDARAH PSSGGSSRRF
ARLAATTFIS QGIPVYLFSD ITPTPFVPFT VSHLKLCAGI MITASHNPKQ DNGYKVYWDN
GAQIISPHDK GISQAIEENL EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR
SVNRETKVKF VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK
GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL LGWWLFTSWK
EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT GFKWMGNRAK QLIDQGKTVL
FAFEEAIGYM CCPFVLDKDG VSAAVISAEL ASFLATKNLS LSQQLKAIYV EYGYHITKAS
YFICHDQETI KKLFENLRNY DGKNNYPKAC GKFEISAIRD LTTGYDDSQP DKKAVLPTSK
SSQMITFTFA NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF
QPQKYNLQPK AD
//
MIM
172000
*RECORD*
*FIELD* NO
172000
*FIELD* TI
*172000 PHOSPHOGLUCOMUTASE 2; PGM2
*FIELD* TX
CLONING
Hopkinson and Harris (1965) presented evidence for a second structural
read morelocus controlling phosphoglucomutase; see PGM1 (171900).
Maliekal et al. (2007) isolated phosphopentomutase from human
erythrocytes and found that it copurified with a 68-kD (612-amino acid)
protein that was identified by mass spectrometry as phosphoglucomutase-2
(PGM2), a protein of the alpha-D-phosphohexomutase family. The PGM2
protein shares about 20% identity with mammalian PGM1. Sequence analysis
suggested that PGM2 is a cytosolic protein. Quantitative RT-PCR of mouse
tissues detected the highest expression levels of PGM2 in lung, spleen,
and thymus.
GENE FUNCTION
Maliekal et al. (2007) overexpressed and purified PGM2 and PGM2L1
(611610) in E. coli and 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. Maliekal et al. (2007)
speculated that PGM2 may play a role in congenital immunodeficiencies.
They noted that phosphopentomutase uses ribose 1-phosphate and
deoxyribose 1-phosphate, which are formed by purine nucleoside
phosphorylase and uridine phosphorylase, and that the absence of
phosphopentomutase should result in the accumulation of ribose
1-phosphate and deoxyribose 1-phosphate and therefore in a functional
block of purine nucleoside phosphorylase.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
MAPPING
By cell hybrid studies, PGM2 was assigned to chromosome 4 (McAlpine et
al., 1975). The smallest region of overlap (SRO) derived from hybrid
cell studies by Francke and Brown (1978), Sparkes et al. (1978, 1978),
and Wijnen et al. (1977) was 4p14-q12.
*FIELD* RF
1. Francke, U.; Brown, S.: Regional assignment of genes for phosphoglucomutase-2
and peptidase S to 4pter-4q21 in man. Cytogenet. Cell Genet. 22:
401-405, 1978.
2. Hopkinson, D. A.; Harris, H.: Evidence for a second 'structural'
locus determining human phosphoglucomutase. Nature 208: 410-412,
1965.
3. 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.
4. McAlpine, P. J.; Mohandas, T.; Komarnicki, L.; Niewczas-Late, V.;
Vust, A.; Hamerton, J. L.: Further data on the assignment of the
phosphoglucomutase (2) (PGM-2) gene locus to chromosome 4 in man. Birth
Defects Orig. Art. Ser. 11(3): 198-199, 1975. Note: Alternate: Cytogenet.
Cell Genet. 14: 368-369, 1975.
5. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
6. Sparkes, R. S.; Mohandas, T.; Sparkes, M. C.; Shulkin, J. D.:
Human PGM-2 locus mapped to 4pter-q25. Exp. Cell Res. 111: 492-495,
1978.
7. Sparkes, R. S.; Mohandas, T.; Sparkes, M. C.; Shulkin, J. D.:
Human PGM-2 (EC 3.7.5.1) mapped to 4pter-4q25. Cytogenet. Cell Genet. 22:
406-407, 1978.
8. Wijnen, L. M. M.; Grzeschik, K.-H.; Pearson, P. L.; Meera Khan,
P.: The human PGM-2 and its chromosomal localization in man-mouse
hybrids. Hum. Genet. 37: 271-278, 1977.
*FIELD* CN
Alan F. Scott - updated: 11/21/2007
Alan F. Scott - updated: 11/20/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 11/21/2007
terry: 11/20/2007
dkim: 7/7/1998
mimadm: 4/1/1994
warfield: 3/29/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
carol: 4/20/1989
*RECORD*
*FIELD* NO
172000
*FIELD* TI
*172000 PHOSPHOGLUCOMUTASE 2; PGM2
*FIELD* TX
CLONING
Hopkinson and Harris (1965) presented evidence for a second structural
read morelocus controlling phosphoglucomutase; see PGM1 (171900).
Maliekal et al. (2007) isolated phosphopentomutase from human
erythrocytes and found that it copurified with a 68-kD (612-amino acid)
protein that was identified by mass spectrometry as phosphoglucomutase-2
(PGM2), a protein of the alpha-D-phosphohexomutase family. The PGM2
protein shares about 20% identity with mammalian PGM1. Sequence analysis
suggested that PGM2 is a cytosolic protein. Quantitative RT-PCR of mouse
tissues detected the highest expression levels of PGM2 in lung, spleen,
and thymus.
GENE FUNCTION
Maliekal et al. (2007) overexpressed and purified PGM2 and PGM2L1
(611610) in E. coli and 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. Maliekal et al. (2007)
speculated that PGM2 may play a role in congenital immunodeficiencies.
They noted that phosphopentomutase uses ribose 1-phosphate and
deoxyribose 1-phosphate, which are formed by purine nucleoside
phosphorylase and uridine phosphorylase, and that the absence of
phosphopentomutase should result in the accumulation of ribose
1-phosphate and deoxyribose 1-phosphate and therefore in a functional
block of purine nucleoside phosphorylase.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
MAPPING
By cell hybrid studies, PGM2 was assigned to chromosome 4 (McAlpine et
al., 1975). The smallest region of overlap (SRO) derived from hybrid
cell studies by Francke and Brown (1978), Sparkes et al. (1978, 1978),
and Wijnen et al. (1977) was 4p14-q12.
*FIELD* RF
1. Francke, U.; Brown, S.: Regional assignment of genes for phosphoglucomutase-2
and peptidase S to 4pter-4q21 in man. Cytogenet. Cell Genet. 22:
401-405, 1978.
2. Hopkinson, D. A.; Harris, H.: Evidence for a second 'structural'
locus determining human phosphoglucomutase. Nature 208: 410-412,
1965.
3. 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.
4. McAlpine, P. J.; Mohandas, T.; Komarnicki, L.; Niewczas-Late, V.;
Vust, A.; Hamerton, J. L.: Further data on the assignment of the
phosphoglucomutase (2) (PGM-2) gene locus to chromosome 4 in man. Birth
Defects Orig. Art. Ser. 11(3): 198-199, 1975. Note: Alternate: Cytogenet.
Cell Genet. 14: 368-369, 1975.
5. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
6. Sparkes, R. S.; Mohandas, T.; Sparkes, M. C.; Shulkin, J. D.:
Human PGM-2 locus mapped to 4pter-q25. Exp. Cell Res. 111: 492-495,
1978.
7. Sparkes, R. S.; Mohandas, T.; Sparkes, M. C.; Shulkin, J. D.:
Human PGM-2 (EC 3.7.5.1) mapped to 4pter-4q25. Cytogenet. Cell Genet. 22:
406-407, 1978.
8. Wijnen, L. M. M.; Grzeschik, K.-H.; Pearson, P. L.; Meera Khan,
P.: The human PGM-2 and its chromosomal localization in man-mouse
hybrids. Hum. Genet. 37: 271-278, 1977.
*FIELD* CN
Alan F. Scott - updated: 11/21/2007
Alan F. Scott - updated: 11/20/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 11/21/2007
terry: 11/20/2007
dkim: 7/7/1998
mimadm: 4/1/1994
warfield: 3/29/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
carol: 4/20/1989