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Protein

Bisphosphoglycerate mutase

Gene

BPGM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Sitei29 – 291Not glycated
Sitei46 – 461Not glycated
Binding sitei62 – 621Substrate1 Publication
Binding sitei100 – 1001Substrate1 Publication
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

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • erythrocyte development Source: Ensembl
  • glycolytic process Source: UniProtKB-KW
  • respiratory gaseous exchange Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER.
BRENDAi3.1.3.13. 2681.
5.4.2.4. 2681.
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1093. BPGM.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Bisphosphoglycerate mutase deficiency (BPGMD)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.

See also OMIM:222800
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. 2 Publications
VAR_065368

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiBPGM.
DMDMi130350.

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
Modified residuei122 – 1221Phosphothreonine1 Publication
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, Phosphoprotein

Proteomic databases

MaxQBiP07738.
PaxDbiP07738.
PeptideAtlasiP07738.
PRIDEiP07738.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

PTM databases

DEPODiP07738.
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

BgeeiP07738.
CleanExiHS_BPGM.
ExpressionAtlasiP07738. baseline and differential.
GenevisibleiP07738. HS.

Organism-specific databases

HPAiHPA016493.
HPA028735.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi107137. 18 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 – 107Combined sources
Helixi15 – 184Combined sources
Helixi32 – 4716Combined sources
Beta strandi53 – 575Combined sources
Helixi61 – 7414Combined sources
Beta strandi81 – 833Combined sources
Helixi85 – 873Combined sources
Helixi93 – 953Combined sources
Helixi100 – 1078Combined sources
Helixi109 – 1179Combined sources
Helixi133 – 1375Combined sources
Helixi140 – 1423Combined sources
Beta strandi144 – 1474Combined sources
Helixi149 – 1513Combined sources
Helixi158 – 17215Combined sources
Helixi174 – 1785Combined sources
Beta strandi183 – 1875Combined sources
Helixi189 – 20012Combined sources
Helixi206 – 2094Combined sources
Beta strandi218 – 2225Combined sources
Beta strandi228 – 2303Combined sources
Helixi238 – 25013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Regioni10 – 178Substrate binding1 Publication
Regioni23 – 242Substrate binding1 Publication
Regioni89 – 924Substrate binding1 Publication
Regioni116 – 1172Substrate binding1 Publication
Regioni189 – 1902Substrate binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0588.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP07738.
KOiK01837.
OMAiNLHAVGP.
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

        10         20         30         40         50
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF
60 70 80 90 100
EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR
110 120 130 140 150
EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD
160 170 180 190 200
QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE
210 220 230 240 250
GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED

QGKVKQAKK
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. 2 Publications
VAR_065368

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001280014.1. NM_001293085.1.
NP_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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001280014.1. NM_001293085.1.
NP_001715.1. NM_001724.4.
NP_954655.1. NM_199186.2.
UniGeneiHs.198365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107137. 18 interactions.
IntActiP07738. 8 interactions.
STRINGi9606.ENSP00000342032.

PTM databases

DEPODiP07738.
PhosphoSiteiP07738.

Polymorphism and mutation databases

BioMutaiBPGM.
DMDMi130350.

2D gel databases

REPRODUCTION-2DPAGEIPI00215979.

Proteomic databases

MaxQBiP07738.
PaxDbiP07738.
PeptideAtlasiP07738.
PRIDEiP07738.

Protocols and materials databases

DNASUi669.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi669.
GeneCardsiGC07P134331.
HGNCiHGNC:1093. BPGM.
HPAiHPA016493.
HPA028735.
MIMi222800. phenotype.
613896. gene.
neXtProtiNX_P07738.
Orphaneti714. Hemolytic anemia due to diphosphoglycerate mutase deficiency.
PharmGKBiPA25401.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0588.
GeneTreeiENSGT00390000016700.
HOGENOMiHOG000221682.
HOVERGENiHBG027528.
InParanoidiP07738.
KOiK01837.
OMAiNLHAVGP.
OrthoDBiEOG7XM2ZV.
PhylomeDBiP07738.
TreeFamiTF300007.

Enzyme and pathway databases

BioCyciMetaCyc:HS10491-MONOMER.
BRENDAi3.1.3.13. 2681.
5.4.2.4. 2681.
SABIO-RKP07738.

Miscellaneous databases

ChiTaRSiBPGM. human.
EvolutionaryTraceiP07738.
GenomeRNAii669.
NextBioi2738.
PROiP07738.
SOURCEiSearch...

Gene expression databases

BgeeiP07738.
CleanExiHS_BPGM.
ExpressionAtlasiP07738. baseline and differential.
GenevisibleiP07738. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "Crystal structure of human bisphosphoglycerate mutase."
    Wang Y., Wei Z., Bian Q., Cheng Z., Wan M., Liu L., Gong W.
    J. Biol. Chem. 279:39132-39138(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-259, SUBUNIT.

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: June 24, 2015
This is version 164 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.