位置:首页 > 蛋白库 > PMGE_HUMAN
PMGE_HUMAN
ID   PMGE_HUMAN              Reviewed;         259 AA.
AC   P07738; A4D1N9;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 212.
DE   RecName: Full=Bisphosphoglycerate mutase;
DE            Short=BPGM;
DE            EC=5.4.2.4 {ECO:0000269|PubMed:21045285};
DE   AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE   AltName: Full=2,3-bisphosphoglycerate synthase;
DE            EC=5.4.2.11 {ECO:0000269|PubMed:21045285};
DE   AltName: Full=2,3-diphosphoglycerate mutase;
DE            Short=DPGM;
DE   AltName: Full=BPG-dependent PGAM;
GN   Name=BPGM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
RP   IDENTIFICATION OF VARIANT ECYT8 CYS-90, CHARACTERIZATION OF VARIANT ECYT8
RP   CYS-90, AND INVOLVEMENT IN ECYT8.
RX   PubMed=2542247; DOI=10.1016/s0021-9258(18)83118-0;
RA   Rosa R., Blouquit Y., Calvin M.C., Prome D., Prome J.C., Rosa J.;
RT   "Isolation, characterization, and structure of a mutant 89 ArgTO:
RT   bisphosphoglycerate mutase. Implication of the active site in the
RT   mutation.";
RL   J. Biol. Chem. 264:7837-7843(1989).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-259, CLEAVAGE OF INITIATOR METHIONINE,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=6313356; DOI=10.1002/j.1460-2075.1983.tb01569.x;
RA   Haggarty N.W., Dunbar B., Fothergill L.A.;
RT   "The complete amino acid sequence of human erythrocyte diphosphoglycerate
RT   mutase.";
RL   EMBO J. 2:1213-1220(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=3023066; DOI=10.1002/j.1460-2075.1986.tb04495.x;
RA   Joulin V., Peduzzi J., Romeo P.-H., Rosa R., Valentin C., Dubart A.,
RA   Lapeyre B., Blouquit Y., Garel M.-C., Goossens M., Rosa J., Cohen-Solal M.;
RT   "Molecular cloning and sequencing of the human erythrocyte 2,3-
RT   bisphosphoglycerate mutase cDNA: revised amino acid sequence.";
RL   EMBO J. 5:2275-2283(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3036106;
RA   Cohen-Solal M., Joulin V., Romeo P.-H., Rosa R., Valentin C., Garel M.-C.,
RA   Rosa J.;
RT   "Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and
RT   revised amino acid sequence.";
RL   Biomed. Biochim. Acta 46:S126-S130(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2844822; DOI=10.1016/s0021-9258(19)37657-4;
RA   Joulin V., Garel M.-C., le Boulch P., Valentin C., Rosa R., Rosa J.,
RA   Cohen-Solal M.;
RT   "Isolation and characterization of the human 2,3-bisphosphoglycerate mutase
RT   gene.";
RL   J. Biol. Chem. 263:15785-15790(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-46; 144-168 AND 182-206, GLYCATION AT LYS-3; LYS-5;
RP   LYS-18; LYS-43; LYS-159 AND LYS-197, AND LACK OF GLYCATION AT LYS-29;
RP   LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
RX   PubMed=9832630; DOI=10.1093/oxfordjournals.jbchem.a022243;
RA   Fujita T., Suzuki K., Tada T., Yoshihara Y., Hamaoka R., Uchida K.,
RA   Matuo Y., Sasaki T., Hanafusa T., Taniguchi N.;
RT   "Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in
RT   vivo and in vitro.";
RL   J. Biochem. 124:1237-1244(1998).
RN   [11]
RP   PROTEIN SEQUENCE OF 104-114.
RX   PubMed=8440681; DOI=10.1016/s0021-9258(18)53552-3;
RA   Stafforini D.M., Rollins E.N., Prescott S.M., McIntyre T.M.;
RT   "The platelet-activating factor acetylhydrolase from human erythrocytes.
RT   Purification and properties.";
RL   J. Biol. Chem. 268:3857-3865(1993).
RN   [12]
RP   ACTIVITY REGULATION.
RX   PubMed=10477269; DOI=10.1042/bj3420581;
RA   Mulquiney P.J., Kuchel P.W.;
RT   "Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based
RT   on detailed enzyme kinetic equations: equations and parameter refinement.";
RL   Biochem. J. 342:581-596(1999).
RN   [13]
RP   TISSUE SPECIFICITY.
RX   PubMed=16246416; DOI=10.1016/j.placenta.2005.08.010;
RA   Pritlove D.C., Gu M., Boyd C.A., Randeva H.S., Vatish M.;
RT   "Novel placental expression of 2,3-bisphosphoglycerate mutase.";
RL   Placenta 27:924-927(2006).
RN   [14]
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., Buerckstuemmer T.,
RA   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   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   3D-STRUCTURE MODELING.
RX   PubMed=1387804; DOI=10.1016/0300-9084(92)90149-9;
RA   Craescu C.T., Schaad O., Garel M.-C., Rosa R., Edelstein S.J.;
RT   "Structural modeling of the human erythrocyte bisphosphoglycerate mutase.";
RL   Biochimie 74:519-526(1992).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-259, AND SUBUNIT.
RX   PubMed=15258155; DOI=10.1074/jbc.m405982200;
RA   Wang Y., Wei Z., Bian Q., Cheng Z., Wan M., Liu L., Gong W.;
RT   "Crystal structure of human bisphosphoglycerate mutase.";
RL   J. Biol. Chem. 279:39132-39138(2004).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-258 IN COMPLEXES WITH
RP   3-PHOSPHO-D-GLYCERATE AND 2,3-BISPHOSPHO-D-GLYCERATE, SUBUNIT, AND ACTIVE
RP   SITE.
RX   PubMed=17052986; DOI=10.1074/jbc.m606421200;
RA   Wang Y., Liu L., Wei Z., Cheng Z., Lin Y., Gong W.;
RT   "Seeing the process of histidine phosphorylation in human
RT   bisphosphoglycerate mutase.";
RL   J. Biol. Chem. 281:39642-39648(2006).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RX   PubMed=21045285; DOI=10.1107/s1744309110035475;
RA   Patterson A., Price N.C., Nairn J.;
RT   "Unliganded structure of human bisphosphoglycerate mutase reveals side-
RT   chain movements induced by ligand binding.";
RL   Acta Crystallogr. F 66:1415-1420(2010).
RN   [21]
RP   VARIANT ECYT8 CYS-90.
RX   PubMed=1421379;
RA   Lemarchandel V., Joulin V., Valentin C., Rosa R., Galacteros F., Rosa J.,
RA   Cohen-Solal M.;
RT   "Compound heterozygosity in a complete erythrocyte bisphosphoglycerate
RT   mutase deficiency.";
RL   Blood 80:2643-2649(1992).
RN   [22]
RP   VARIANT ECYT8 GLN-62.
RX   PubMed=15054810; DOI=10.1002/ajh.20014;
RA   Hoyer J.D., Allen S.L., Beutler E., Kubik K., West C., Fairbanks V.F.;
RT   "Erythrocytosis due to bisphosphoglycerate mutase deficiency with
RT   concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency.";
RL   Am. J. Hematol. 75:205-208(2004).
CC   -!- FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity
CC       by controlling the levels of its allosteric effector 2,3-
CC       bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11)
CC       activity. {ECO:0000269|PubMed:21045285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC         bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC         Evidence={ECO:0000269|PubMed:21045285};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.11; Evidence={ECO:0000269|PubMed:21045285};
CC   -!- ACTIVITY REGULATION: At alkaline pH BPGM favors the synthase reaction;
CC       however, at lower pH the phosphatase reaction is dominant. Inhibited by
CC       citrate. {ECO:0000269|PubMed:10477269, ECO:0000269|PubMed:21045285}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15258155,
CC       ECO:0000269|PubMed:17052986}.
CC   -!- INTERACTION:
CC       P07738; P15259: PGAM2; NbExp=4; IntAct=EBI-2115835, EBI-2511669;
CC   -!- TISSUE SPECIFICITY: Expressed in red blood cells. Expressed in non-
CC       erythroid cells of the placenta; present in the syncytiotrophoblast
CC       layer of the placental villi at the feto-maternal interface (at protein
CC       level). {ECO:0000269|PubMed:16246416, ECO:0000269|PubMed:3023066,
CC       ECO:0000269|PubMed:6313356}.
CC   -!- PTM: Glycation of Lys-159 in diabetic patients inactivates the enzyme.
CC   -!- DISEASE: Erythrocytosis, familial, 8 (ECYT8) [MIM:222800]: An autosomal
CC       recessive disorder characterized by elevated serum hemoglobin and
CC       hematocrit, and biphosphoglycerate mutase deficiency. ECYT8 affected
CC       individuals manifest hemolytic anemia and splenomegaly.
CC       {ECO:0000269|PubMed:1421379, ECO:0000269|PubMed:15054810,
CC       ECO:0000269|PubMed:2542247}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X04327; CAA27858.1; -; mRNA.
DR   EMBL; M23068; AAA51840.1; -; Genomic_DNA.
DR   EMBL; M23067; AAA51840.1; JOINED; Genomic_DNA.
DR   EMBL; AK315439; BAG37827.1; -; mRNA.
DR   EMBL; CH236950; EAL24067.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83821.1; -; Genomic_DNA.
DR   EMBL; BC017050; AAH17050.1; -; mRNA.
DR   CCDS; CCDS5833.1; -.
DR   PIR; A31999; PMHUBM.
DR   RefSeq; NP_001280014.1; NM_001293085.1.
DR   RefSeq; NP_001715.1; NM_001724.4.
DR   RefSeq; NP_954655.1; NM_199186.2.
DR   RefSeq; XP_011514829.1; XM_011516527.1.
DR   PDB; 1T8P; X-ray; 2.50 A; A/B=1-259.
DR   PDB; 2A9J; X-ray; 2.00 A; A/B=1-259.
DR   PDB; 2F90; X-ray; 2.00 A; A/B=1-259.
DR   PDB; 2H4X; X-ray; 1.85 A; A/B=1-259.
DR   PDB; 2H4Z; X-ray; 2.00 A; A/B=1-259.
DR   PDB; 2H52; X-ray; 2.00 A; A/B=1-259.
DR   PDB; 2HHJ; X-ray; 1.50 A; A/B=1-259.
DR   PDB; 3NFY; X-ray; 1.94 A; A/B=1-259.
DR   PDB; 7N3R; X-ray; 2.25 A; A/B=1-259.
DR   PDB; 7N3S; X-ray; 2.48 A; A/B=1-259.
DR   PDB; 7THI; X-ray; 1.33 A; A/B=1-259.
DR   PDBsum; 1T8P; -.
DR   PDBsum; 2A9J; -.
DR   PDBsum; 2F90; -.
DR   PDBsum; 2H4X; -.
DR   PDBsum; 2H4Z; -.
DR   PDBsum; 2H52; -.
DR   PDBsum; 2HHJ; -.
DR   PDBsum; 3NFY; -.
DR   PDBsum; 7N3R; -.
DR   PDBsum; 7N3S; -.
DR   PDBsum; 7THI; -.
DR   AlphaFoldDB; P07738; -.
DR   SMR; P07738; -.
DR   BioGRID; 107137; 27.
DR   IntAct; P07738; 18.
DR   STRING; 9606.ENSP00000376840; -.
DR   DEPOD; BPGM; -.
DR   iPTMnet; P07738; -.
DR   MetOSite; P07738; -.
DR   PhosphoSitePlus; P07738; -.
DR   BioMuta; BPGM; -.
DR   DMDM; 130350; -.
DR   REPRODUCTION-2DPAGE; IPI00215979; -.
DR   EPD; P07738; -.
DR   jPOST; P07738; -.
DR   MassIVE; P07738; -.
DR   MaxQB; P07738; -.
DR   PaxDb; P07738; -.
DR   PeptideAtlas; P07738; -.
DR   PRIDE; P07738; -.
DR   ProteomicsDB; 52025; -.
DR   Antibodypedia; 2975; 265 antibodies from 28 providers.
DR   DNASU; 669; -.
DR   Ensembl; ENST00000344924.8; ENSP00000342032.3; ENSG00000172331.12.
DR   Ensembl; ENST00000393132.2; ENSP00000376840.2; ENSG00000172331.12.
DR   Ensembl; ENST00000418040.5; ENSP00000399838.1; ENSG00000172331.12.
DR   GeneID; 669; -.
DR   KEGG; hsa:669; -.
DR   MANE-Select; ENST00000344924.8; ENSP00000342032.3; NM_001724.5; NP_001715.1.
DR   UCSC; uc003vrv.4; human.
DR   CTD; 669; -.
DR   DisGeNET; 669; -.
DR   GeneCards; BPGM; -.
DR   HGNC; HGNC:1093; BPGM.
DR   HPA; ENSG00000172331; Tissue enhanced (bone).
DR   MalaCards; BPGM; -.
DR   MIM; 222800; phenotype.
DR   MIM; 613896; gene.
DR   neXtProt; NX_P07738; -.
DR   OpenTargets; ENSG00000172331; -.
DR   Orphanet; 247378; Autosomal recessive secondary polycythemia not associated with VHL gene.
DR   Orphanet; 714; Hemolytic anemia due to diphosphoglycerate mutase deficiency.
DR   PharmGKB; PA25401; -.
DR   VEuPathDB; HostDB:ENSG00000172331; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   GeneTree; ENSGT00950000182926; -.
DR   HOGENOM; CLU_033323_1_1_1; -.
DR   InParanoid; P07738; -.
DR   OMA; ITESHPY; -.
DR   OrthoDB; 1112626at2759; -.
DR   PhylomeDB; P07738; -.
DR   TreeFam; TF300007; -.
DR   BioCyc; MetaCyc:HS10491-MON; -.
DR   BRENDA; 5.4.2.4; 2681.
DR   PathwayCommons; P07738; -.
DR   Reactome; R-HSA-70171; Glycolysis.
DR   SABIO-RK; P07738; -.
DR   SignaLink; P07738; -.
DR   BioGRID-ORCS; 669; 17 hits in 1084 CRISPR screens.
DR   ChiTaRS; BPGM; human.
DR   EvolutionaryTrace; P07738; -.
DR   GenomeRNAi; 669; -.
DR   Pharos; P07738; Tbio.
DR   PRO; PR:P07738; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P07738; protein.
DR   Bgee; ENSG00000172331; Expressed in secondary oocyte and 195 other tissues.
DR   ExpressionAtlas; P07738; baseline and differential.
DR   Genevisible; P07738; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; TAS:Reactome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; TAS:Reactome.
DR   GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR   GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR   GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR   GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0150076; P:neuroinflammatory response; IEA:Ensembl.
DR   GO; GO:0015671; P:oxygen transport; IEA:Ensembl.
DR   GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Congenital erythrocytosis;
KW   Direct protein sequencing; Disease variant; Glycation; Glycolysis;
KW   Glycoprotein; Hereditary hemolytic anemia; Hydrolase; Isomerase;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6313356,
FT                   ECO:0000269|PubMed:9832630, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..259
FT                   /note="Bisphosphoglycerate mutase"
FT                   /id="PRO_0000179834"
FT   ACT_SITE        11
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         10..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         23..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         89..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         116..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   SITE            29
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            46
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            143
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            181
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            188
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000269|PubMed:17052986"
FT   SITE            246
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            247
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            253
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            258
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   SITE            259
FT                   /note="Not glycated"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         122
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CARBOHYD        3
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   CARBOHYD        5
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   CARBOHYD        18
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   CARBOHYD        43
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   CARBOHYD        159
FT                   /note="N-linked (Glc) (glycation) lysine"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   CARBOHYD        197
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:9832630"
FT   VARIANT         62
FT                   /note="R -> Q (in ECYT8; dbSNP:rs751972865)"
FT                   /evidence="ECO:0000269|PubMed:15054810"
FT                   /id="VAR_065367"
FT   VARIANT         90
FT                   /note="R -> C (in ECYT8; mutation identified at protein
FT                   level; marked decrease in synthase and mutase activities;
FT                   no effect on phosphatase activity; dbSNP:rs121964925)"
FT                   /evidence="ECO:0000269|PubMed:1421379,
FT                   ECO:0000269|PubMed:2542247"
FT                   /id="VAR_065368"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           15..19
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           32..47
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           61..74
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           100..107
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           109..117
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           133..137
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           158..171
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           174..178
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           189..200
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           206..209
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:7THI"
FT   HELIX           238..250
FT                   /evidence="ECO:0007829|PDB:7THI"
SQ   SEQUENCE   259 AA;  30005 MW;  A2AF1D6F2985A3B5 CRC64;
     MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
     NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN
     VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
     KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
     IQAAIKKVED QGKVKQAKK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024