Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Bisphosphoglycerate mutase  

UniProtKB / Swiss-Prot ID :  PMGE_HUMAN

Gene Name (Synonyms) : 
BPGM  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

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

Protein Sequence MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLI...
Predicted Secondary Structure CCCEEEEEEECCCCHHCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCEEEECCHHHHHHHHHHH...
Protein Variant
LocationDescription
62R -> Q (in BPGMD). VAR_065367
90R -> C (in BPGMD; mutation identified atprotein level; marked decrease in
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3N-linked (Glc) (glycation)--MSKYKLI
--CCCEEEE
45.14HPRD
Link
3N-linked (Glc) (glycation); in vitro.--MSKYKLI
--CCCEEEE
45.14UniProtKB
Link
5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MSKYKLIML
CCCEEEEEE
34.96Phosphositeplus
Link
5N-linked (Glc) (glycation)MSKYKLIML
CCCEEEEEE
34.96HPRD
Link
5N-linked (Glc) (glycation); in vitro.MSKYKLIML
CCCEEEEEE
34.96UniProtKB
Link
18N-linked (Glc) (glycation)GAWNKENRF
CHHCCCCCC
45.74HPRD
Link
18N-linked (Glc) (glycation); in vitro.GAWNKENRF
CHHCCCCCC
45.74UniProtKB
Link
43N-linked (Glc) (glycation)RNCGKQLKA
HHHHHHHHH
55.44HPRD
Link
43N-linked (Glc) (glycation); in vitro.RNCGKQLKA
HHHHHHHHH
55.44UniProtKB
Link
92PhosphotyrosineNERHYGALI
CHHHCCHHC
15.43Phosphositeplus
Link
159N-linked (Glc) (glycation)SESLKDVLE
CCCHHHHHH
55.88HPRD
Link
159N-linked (Glc) (glycation).SESLKDVLE
CCCHHHHHH
55.88UniProtKB
Link
197N-linked (Glc) (glycation)RALLKHLEG
HHHHHHHHC
47.17HPRD
Link
197N-linked (Glc) (glycation); in vitro.RALLKHLEG
HHHHHHHHC
47.17UniProtKB
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
G3P_HUMANin vitroHPRD:01961HPRD9308888
- top -

Disease Reference
Kegg disease
OMIM disease
222800Bisphosphoglycerate mutase deficiency (BPGMD)
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human erythrocyte bisphosphoglycerate mutase: inactivation byglycation 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).
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, AND LACK OF GLYCATION ATLYS-29; LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258AND LYS-259.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures