MPI_HUMAN - dbPTM
MPI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPI_HUMAN
UniProt AC P34949
Protein Name Mannose-6-phosphate isomerase
Gene Name MPI
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Cytoplasm .
Protein Description Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions..
Protein Sequence MAAPRVFPLSCAVQQYAWGKMGSNSEVARLLASSDPLAQIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQFLIGDEAATHLKQTMSHDSQAVASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDIFGELLLQLHQQYPGDIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLSYTPSSSKDRLFLPTRSQEDPYLSIYDPPVPDFTIMKTEVPGSVTEYKVLALDSASILLMVQGTVIASTPTTQTPIPLQRGGVLFIGANESVSLKLTEPKDLLIFRACCLL
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------MAAPRVFPL
------CCCCCEEEC
26.6019413330
23PhosphorylationYAWGKMGSNSEVARL
HHCCCCCCHHHHHHH
33.4130622161
25PhosphorylationWGKMGSNSEVARLLA
CCCCCCHHHHHHHHH
34.8330622161
44UbiquitinationLAQIAEDKPYAELWM
HHHHHCCCCCCEEEC
31.28-
46PhosphorylationQIAEDKPYAELWMGT
HHHCCCCCCEEECCC
20.6027642862
60UbiquitinationTHPRGDAKILDNRIS
CCCCCCHHHHCCHHC
48.84-
65MethylationDAKILDNRISQKTLS
CHHHHCCHHCHHHHH
29.60115483641
67PhosphorylationKILDNRISQKTLSQW
HHHCCHHCHHHHHHH
23.5330622161
69 (in isoform 2)Ubiquitination-44.6421890473
69 (in isoform 1)Ubiquitination-44.6421890473
69UbiquitinationLDNRISQKTLSQWIA
HCCHHCHHHHHHHHH
44.6421890473
70PhosphorylationDNRISQKTLSQWIAE
CCHHCHHHHHHHHHH
24.8130622161
72PhosphorylationRISQKTLSQWIAENQ
HHCHHHHHHHHHHCC
28.8030622161
85UbiquitinationNQDSLGSKVKDTFNG
CCCCCCCCCHHHHCC
52.05-
87UbiquitinationDSLGSKVKDTFNGNL
CCCCCCCHHHHCCCC
55.58-
99UbiquitinationGNLPFLFKVLSVETP
CCCCEEEEEEEECCC
44.40-
102PhosphorylationPFLFKVLSVETPLSI
CEEEEEEEECCCCEE
22.3923312004
105PhosphorylationFKVLSVETPLSIQAH
EEEEEECCCCEECCC
27.6330622161
108PhosphorylationLSVETPLSIQAHPNK
EEECCCCEECCCCCH
17.549525984
115UbiquitinationSIQAHPNKELAEKLH
EECCCCCHHHHHHHH
59.56-
163SumoylationEIVTFLKKVPEFQFL
HHHHHHHCCCCCEEE
66.23-
163UbiquitinationEIVTFLKKVPEFQFL
HHHHHHHCCCCCEEE
66.23-
2182-HydroxyisobutyrylationEQLNLLVKRISQQAA
HHHHHHHHHHHHHHH
43.94-
218UbiquitinationEQLNLLVKRISQQAA
HHHHHHHHHHHHHHH
43.94-
287SulfoxidationKGDCVECMACSDNTV
CCCEEEEEEECCCCC
2.3921406390
320UbiquitinationSYTPSSSKDRLFLPT
CCCCCCCCCCEECCC
49.14-
322MethylationTPSSSKDRLFLPTRS
CCCCCCCCEECCCCC
30.95115483633
338PhosphorylationEDPYLSIYDPPVPDF
CCCCCEECCCCCCCC
21.0127642862
349UbiquitinationVPDFTIMKTEVPGSV
CCCCEEEEEECCCCC
37.37-
366PhosphorylationYKVLALDSASILLMV
EEEEEECCCCEEEEE
25.43-
376PhosphorylationILLMVQGTVIASTPT
EEEEEECEEEEECCC
7.52-

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 MPI_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPI_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 MPI_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TGM1_HUMANTGM1physical
26186194
INVO_HUMANIVLphysical
26186194
S10AE_HUMANS100A14physical
26186194
MIF_HUMANMIFphysical
26344197
NECP1_HUMANNECAP1physical
26344197
NECP2_HUMANNECAP2physical
26344197
PCBP1_HUMANPCBP1physical
26344197
PIPNB_HUMANPITPNBphysical
26344197
AACT_HUMANSERPINA3physical
28514442
SPB4_HUMANSERPINB4physical
28514442
TGM1_HUMANTGM1physical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
602579Congenital disorder of glycosylation 1B (CDG1B)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPI_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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