PMGE_HUMAN - dbPTM
PMGE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMGE_HUMAN
UniProt AC P07738
Protein Name Bisphosphoglycerate mutase
Gene Name BPGM
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization
Protein Description 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 5.4.2.11) activity..
Protein Sequence MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSKYKLIML
------CCCEEEEEE		44.7022814378
3Glycation-----MSKYKLIMLR
-----CCCEEEEEEC		45.14-
3N-linked_Glycosylation-----MSKYKLIMLR
-----CCCEEEEEEC		45.149832630
5Glycation---MSKYKLIMLRHG
---CCCEEEEEECCC		34.96-
5Ubiquitination---MSKYKLIMLRHG
---CCCEEEEEECCC		34.9621890473
5Ubiquitination---MSKYKLIMLRHG
---CCCEEEEEECCC		34.9621890473
5N-linked_Glycosylation---MSKYKLIMLRHG
---CCCEEEEEECCC		34.969832630
11PhosphorylationYKLIMLRHGEGAWNK
EEEEEECCCCCCCCC		34.39-
18N-linked_GlycosylationHGEGAWNKENRFCSW
CCCCCCCCCCCCHHH		45.749832630
18GlycationHGEGAWNKENRFCSW
CCCCCCCCCCCCHHH		45.74-
24PhosphorylationNKENRFCSWVDQKLN
CCCCCCHHHHHHHHC		27.6728857561
32PhosphorylationWVDQKLNSEGMEEAR
HHHHHHCHHHHHHHH		46.0626437602
35SulfoxidationQKLNSEGMEEARNCG
HHHCHHHHHHHHHHH		3.5530846556
43N-linked_GlycosylationEEARNCGKQLKALNF
HHHHHHHHHHHHHCC		55.449832630
43GlycationEEARNCGKQLKALNF
HHHHHHHHHHHHHCC		55.44-
83PhosphorylationQEWVPVESSWRLNER
CCEEECHHCEECCHH		35.1222210691
84PhosphorylationEWVPVESSWRLNERH
CEEECHHCEECCHHH		11.6022210691
92PhosphorylationWRLNERHYGALIGLN
EECCHHHHHHEEECC		15.4322817900
118PhosphorylationQVRLWRRSYNVTPPP
HHHHHHHHCCCCCCC		16.7028857561
119PhosphorylationVRLWRRSYNVTPPPI
HHHHHHHCCCCCCCC		16.3127080861
122PhosphorylationWRRSYNVTPPPIEES
HHHHCCCCCCCCCCC		26.8315054810
129PhosphorylationTPPPIEESHPYYQEI
CCCCCCCCCCCHHHH		19.5722673903
143UbiquitinationIYNDRRYKVCDVPLD
HHCCCCCEECCCCHH		34.28-
155PhosphorylationPLDQLPRSESLKDVL
CHHHCCCCHHHHHHH		29.6028857561
157PhosphorylationDQLPRSESLKDVLER
HHCCCCHHHHHHHHH		41.8028857561
159N-linked_GlycosylationLPRSESLKDVLERLL
CCCCHHHHHHHHHHH		55.889832630
159GlycationLPRSESLKDVLERLL
CCCCHHHHHHHHHHH		55.88-
159UbiquitinationLPRSESLKDVLERLL
CCCCHHHHHHHHHHH		55.88-
179MethylationRIAPEVLRGKTILIS
CCCHHHHCCCEEEEE		50.14-
182PhosphorylationPEVLRGKTILISAHG
HHHHCCCEEEEECCC		24.6829083192
186PhosphorylationRGKTILISAHGNSSR
CCCEEEEECCCHHHH		15.6929083192
191PhosphorylationLISAHGNSSRALLKH
EEECCCHHHHHHHHH		26.2929083192
192PhosphorylationISAHGNSSRALLKHL
EECCCHHHHHHHHHH		26.1029083192
197N-linked_GlycosylationNSSRALLKHLEGISD
HHHHHHHHHHCCCCH		47.179832630
197GlycationNSSRALLKHLEGISD
HHHHHHHHHHCCCCH		47.17-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PMGE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMGE_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PMGE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEK3_HUMANNEK3physical
21988832
EGR2_HUMANEGR2physical
21988832
EHD2_HUMANEHD2physical
21988832
FWCH2_HUMANFLYWCH2physical
26186194
VIGLN_HUMANHDLBPphysical
26186194
IF1AX_HUMANEIF1AXphysical
26186194
NRBP_HUMANNRBP1physical
26186194
MRGBP_HUMANMRGBPphysical
26186194
KLF16_HUMANKLF16physical
26186194
KLF16_HUMANKLF16physical
28514442
NRBP_HUMANNRBP1physical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
222800Bisphosphoglycerate mutase deficiency (BPGMD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMGE_HUMAN

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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.

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