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P07738

- PMGE_HUMAN

UniProt

P07738 - PMGE_HUMAN

Protein

Bisphosphoglycerate mutase

Gene

BPGM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.

    Catalytic activityi

    3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
    2-phospho-D-glycerate = 3-phospho-D-glycerate.
    2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate.

    Enzyme regulationi

    At alkaline pH BPGM favors the synthase reaction; however, at lower pH the phosphatase reaction is dominant. Inhibited by citrate.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Tele-phosphohistidine intermediate1 Publication
    Binding sitei17 – 1712,3-bisphospho-D-glycerate
    Sitei29 – 291Not glycated
    Sitei46 – 461Not glycated
    Binding sitei62 – 6212,3-bisphospho-D-glycerate
    Binding sitei100 – 10012,3-bisphospho-D-glycerate
    Sitei143 – 1431Not glycated
    Sitei181 – 1811Not glycated
    Active sitei188 – 18811 Publication
    Sitei246 – 2461Not glycated
    Sitei247 – 2471Not glycated
    Sitei253 – 2531Not glycated
    Sitei258 – 2581Not glycated
    Sitei259 – 2591Not glycated

    GO - Molecular functioni

    1. bisphosphoglycerate 2-phosphatase activity Source: UniProtKB-EC
    2. bisphosphoglycerate mutase activity Source: ProtInc
    3. phosphoglycerate mutase activity Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. erythrocyte development Source: Ensembl
    3. glycolytic process Source: UniProtKB-KW
    4. respiratory gaseous exchange Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Isomerase

    Keywords - Biological processi

    Glycolysis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10491-MONOMER.
    SABIO-RKP07738.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bisphosphoglycerate mutase (EC:5.4.2.4)
    Short name:
    BPGM
    Alternative name(s):
    2,3-bisphosphoglycerate mutase, erythrocyte
    2,3-bisphosphoglycerate synthase (EC:3.1.3.13, EC:5.4.2.11)
    2,3-diphosphoglycerate mutase
    Short name:
    DPGM
    BPG-dependent PGAM
    Gene namesi
    Name:BPGM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1093. BPGM.

    Pathology & Biotechi

    Involvement in diseasei

    Bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]: A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → Q in BPGMD. 1 Publication
    VAR_065367
    Natural varianti90 – 901R → C in BPGMD; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity. 1 Publication
    VAR_065368

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi222800. phenotype.
    Orphaneti714. Hemolytic anemia due to diphosphoglycerate mutase deficiency.
    PharmGKBiPA25401.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 259258Bisphosphoglycerate mutasePRO_0000179834Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Glycosylationi3 – 31N-linked (Glc) (glycation); in vitro
    Glycosylationi5 – 51N-linked (Glc) (glycation); in vitro
    Glycosylationi18 – 181N-linked (Glc) (glycation); in vitro
    Glycosylationi43 – 431N-linked (Glc) (glycation); in vitro
    Glycosylationi159 – 1591N-linked (Glc) (glycation)
    Glycosylationi197 – 1971N-linked (Glc) (glycation); in vitro

    Post-translational modificationi

    Glycation of Lys-159 in diabetic patients inactivates the enzyme.

    Keywords - PTMi

    Acetylation, Glycation, Glycoprotein

    Proteomic databases

    MaxQBiP07738.
    PaxDbiP07738.
    PeptideAtlasiP07738.
    PRIDEiP07738.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00215979.

    PTM databases

    PhosphoSiteiP07738.

    Expressioni

    Tissue specificityi

    Expressed in red blood cells. Expressed in non-erythroid cells of the placenta; present in the syncytiotrophoblast layer of the placental villi at the feto-maternal interface (at protein level).3 Publications

    Gene expression databases

    ArrayExpressiP07738.
    BgeeiP07738.
    CleanExiHS_BPGM.
    GenevestigatoriP07738.

    Organism-specific databases

    HPAiHPA016493.
    HPA028735.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi107137. 10 interactions.
    IntActiP07738. 8 interactions.
    STRINGi9606.ENSP00000342032.

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi15 – 184
    Helixi32 – 4716
    Beta strandi53 – 575
    Helixi61 – 7414
    Beta strandi81 – 833
    Helixi85 – 873
    Helixi93 – 953
    Helixi100 – 1078
    Helixi109 – 1179
    Helixi133 – 1375
    Helixi140 – 1423
    Beta strandi144 – 1474
    Helixi149 – 1513
    Helixi158 – 17215
    Helixi174 – 1785
    Beta strandi183 – 1875
    Helixi189 – 20012
    Helixi206 – 2094
    Beta strandi218 – 2225
    Beta strandi228 – 2303
    Helixi238 – 25013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T8PX-ray2.50A/B1-259[»]
    2A9JX-ray2.00A/B1-259[»]
    2F90X-ray2.00A/B1-259[»]
    2H4XX-ray1.85A/B1-259[»]
    2H4ZX-ray2.00A/B1-259[»]
    2H52X-ray2.00A/B1-259[»]
    2HHJX-ray1.50A/B1-259[»]
    3NFYX-ray1.94A/B1-259[»]
    ProteinModelPortaliP07738.
    SMRiP07738. Positions 2-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07738.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 2422,3-bisphospho-D-glycerate binding
    Regioni89 – 9242,3-bisphospho-D-glycerate binding
    Regioni116 – 11722,3-diphosphoglyceric acid binding
    Regioni188 – 19032,3-bisphospho-D-glycerate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0588.
    HOGENOMiHOG000221682.
    HOVERGENiHBG027528.
    InParanoidiP07738.
    KOiK01837.
    OMAiIKEAQNC.
    OrthoDBiEOG7XM2ZV.
    PhylomeDBiP07738.
    TreeFamiTF300007.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    HAMAPiMF_01039. PGAM_GpmA.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view]
    PANTHERiPTHR11931. PTHR11931. 1 hit.
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    TIGRFAMsiTIGR01258. pgm_1. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07738-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF    50
    EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR 100
    EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD 150
    QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE 200
    GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED 250
    QGKVKQAKK 259
    Length:259
    Mass (Da):30,005
    Last modified:January 23, 2007 - v2
    Checksum:iA2AF1D6F2985A3B5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → Q in BPGMD. 1 Publication
    VAR_065367
    Natural varianti90 – 901R → C in BPGMD; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity. 1 Publication
    VAR_065368

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04327 mRNA. Translation: CAA27858.1.
    M23068, M23067 Genomic DNA. Translation: AAA51840.1.
    AK315439 mRNA. Translation: BAG37827.1.
    CH236950 Genomic DNA. Translation: EAL24067.1.
    CH471070 Genomic DNA. Translation: EAW83821.1.
    BC017050 mRNA. Translation: AAH17050.1.
    CCDSiCCDS5833.1.
    PIRiA31999. PMHUBM.
    RefSeqiNP_001715.1. NM_001724.4.
    NP_954655.1. NM_199186.2.
    UniGeneiHs.198365.

    Genome annotation databases

    EnsembliENST00000344924; ENSP00000342032; ENSG00000172331.
    ENST00000393132; ENSP00000376840; ENSG00000172331.
    ENST00000418040; ENSP00000399838; ENSG00000172331.
    GeneIDi669.
    KEGGihsa:669.
    UCSCiuc003vrv.3. human.

    Polymorphism databases

    DMDMi130350.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04327 mRNA. Translation: CAA27858.1 .
    M23068 , M23067 Genomic DNA. Translation: AAA51840.1 .
    AK315439 mRNA. Translation: BAG37827.1 .
    CH236950 Genomic DNA. Translation: EAL24067.1 .
    CH471070 Genomic DNA. Translation: EAW83821.1 .
    BC017050 mRNA. Translation: AAH17050.1 .
    CCDSi CCDS5833.1.
    PIRi A31999. PMHUBM.
    RefSeqi NP_001715.1. NM_001724.4.
    NP_954655.1. NM_199186.2.
    UniGenei Hs.198365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T8P X-ray 2.50 A/B 1-259 [» ]
    2A9J X-ray 2.00 A/B 1-259 [» ]
    2F90 X-ray 2.00 A/B 1-259 [» ]
    2H4X X-ray 1.85 A/B 1-259 [» ]
    2H4Z X-ray 2.00 A/B 1-259 [» ]
    2H52 X-ray 2.00 A/B 1-259 [» ]
    2HHJ X-ray 1.50 A/B 1-259 [» ]
    3NFY X-ray 1.94 A/B 1-259 [» ]
    ProteinModelPortali P07738.
    SMRi P07738. Positions 2-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107137. 10 interactions.
    IntActi P07738. 8 interactions.
    STRINGi 9606.ENSP00000342032.

    PTM databases

    PhosphoSitei P07738.

    Polymorphism databases

    DMDMi 130350.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00215979.

    Proteomic databases

    MaxQBi P07738.
    PaxDbi P07738.
    PeptideAtlasi P07738.
    PRIDEi P07738.

    Protocols and materials databases

    DNASUi 669.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344924 ; ENSP00000342032 ; ENSG00000172331 .
    ENST00000393132 ; ENSP00000376840 ; ENSG00000172331 .
    ENST00000418040 ; ENSP00000399838 ; ENSG00000172331 .
    GeneIDi 669.
    KEGGi hsa:669.
    UCSCi uc003vrv.3. human.

    Organism-specific databases

    CTDi 669.
    GeneCardsi GC07P134331.
    HGNCi HGNC:1093. BPGM.
    HPAi HPA016493.
    HPA028735.
    MIMi 222800. phenotype.
    613896. gene.
    neXtProti NX_P07738.
    Orphaneti 714. Hemolytic anemia due to diphosphoglycerate mutase deficiency.
    PharmGKBi PA25401.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0588.
    HOGENOMi HOG000221682.
    HOVERGENi HBG027528.
    InParanoidi P07738.
    KOi K01837.
    OMAi IKEAQNC.
    OrthoDBi EOG7XM2ZV.
    PhylomeDBi P07738.
    TreeFami TF300007.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS10491-MONOMER.
    SABIO-RK P07738.

    Miscellaneous databases

    ChiTaRSi BPGM. human.
    EvolutionaryTracei P07738.
    GenomeRNAii 669.
    NextBioi 2738.
    PROi P07738.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07738.
    Bgeei P07738.
    CleanExi HS_BPGM.
    Genevestigatori P07738.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    HAMAPi MF_01039. PGAM_GpmA.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR001345. PG/BPGM_mutase_AS.
    IPR005952. Phosphogly_mut1.
    [Graphical view ]
    PANTHERi PTHR11931. PTHR11931. 1 hit.
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    TIGRFAMsi TIGR01258. pgm_1. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation, characterization, and structure of a mutant 89 ArgTO: bisphosphoglycerate mutase. Implication of the active site in the mutation."
      Rosa R., Blouquit Y., Calvin M.C., Prome D., Prome J.C., Rosa J.
      J. Biol. Chem. 264:7837-7843(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF VARIANT BPGMD CYS-90, CHARACTERIZATION OF VARIANT BPGMD CYS-90.
    2. "The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase."
      Haggarty N.W., Dunbar B., Fothergill L.A.
      EMBO J. 2:1213-1220(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-259, CLEAVAGE OF INITIATOR METHIONINE, TISSUE SPECIFICITY.
    3. "Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence."
      Joulin V., Peduzzi J., Romeo P.-H., Rosa R., Valentin C., Dubart A., Lapeyre B., Blouquit Y., Garel M.-C., Goossens M., Rosa J., Cohen-Solal M.
      EMBO J. 5:2275-2283(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    4. "Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence."
      Cohen-Solal M., Joulin V., Romeo P.-H., Rosa R., Valentin C., Garel M.-C., Rosa J.
      Biomed. Biochim. Acta 46:S126-S130(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene."
      Joulin V., Garel M.-C., le Boulch P., Valentin C., Rosa R., Rosa J., Cohen-Solal M.
      J. Biol. Chem. 263:15785-15790(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.
    7. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    10. "Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro."
      Fujita T., Suzuki K., Tada T., Yoshihara Y., Hamaoka R., Uchida K., Matuo Y., Sasaki T., Hanafusa T., Taniguchi N.
      J. Biochem. 124:1237-1244(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-46; 144-168 AND 182-206, GLYCATION AT LYS-3; LYS-5; LYS-18; LYS-43; LYS-159 AND LYS-197, LACK OF GLYCATION AT LYS-29; LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
    11. "The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties."
      Stafforini D.M., Rollins E.N., Prescott S.M., McIntyre T.M.
      J. Biol. Chem. 268:3857-3865(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 104-114.
    12. "Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: equations and parameter refinement."
      Mulquiney P.J., Kuchel P.W.
      Biochem. J. 342:581-596(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "Novel placental expression of 2,3-bisphosphoglycerate mutase."
      Pritlove D.C., Gu M., Boyd C.A., Randeva H.S., Vatish M.
      Placenta 27:924-927(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Structural modeling of the human erythrocyte bisphosphoglycerate mutase."
      Craescu C.T., Schaad O., Garel M.-C., Rosa R., Edelstein S.J.
      Biochimie 74:519-526(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    17. "Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase."
      Wang Y., Liu L., Wei Z., Cheng Z., Lin Y., Gong W.
      J. Biol. Chem. 281:39642-39648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-258 IN COMPLEXES WITH 3-PHOSPHO-D-GLYCERATE AND 2,3-BISPHOSPHO-D-GLYCERATE, SUBUNIT, ACTIVE SITE.
    18. "Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding."
      Patterson A., Price N.C., Nairn J.
      Acta Crystallogr. F 66:1415-1420(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), ENZYME REGULATION.
    19. "Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency."
      Lemarchandel V., Joulin V., Valentin C., Rosa R., Galacteros F., Rosa J., Cohen-Solal M.
      Blood 80:2643-2649(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BPGMD CYS-90.
    20. "Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency."
      Hoyer J.D., Allen S.L., Beutler E., Kubik K., West C., Fairbanks V.F.
      Am. J. Hematol. 75:205-208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BPGMD GLN-62.

    Entry informationi

    Entry nameiPMGE_HUMAN
    AccessioniPrimary (citable) accession number: P07738
    Secondary accession number(s): A4D1N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3