PMM2_HUMAN - dbPTM
PMM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMM2_HUMAN
UniProt AC O15305
Protein Name Phosphomannomutase 2
Gene Name PMM2
Organism Homo sapiens (Human).
Sequence Length 246
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 MAAPGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQEQLGNDVVEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISFDVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYSVTAPEDTRRICELLFS
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------MAAPGPALC
------CCCCCCEEE
23.5122223895
16PhosphorylationCLFDVDGTLTAPRQK
EEEEECCCCCCCHHH
19.2430243723
18PhosphorylationFDVDGTLTAPRQKIT
EEECCCCCCCHHHHH
34.1620068231
26UbiquitinationAPRQKITKEMDDFLQ
CCHHHHHHHHHHHHH
55.29-
34AcetylationEMDDFLQKLRQKIKI
HHHHHHHHHHHHHCE
48.0226822725
34UbiquitinationEMDDFLQKLRQKIKI
HHHHHHHHHHHHHCE
48.02-
34UbiquitinationEMDDFLQKLRQKIKI
HHHHHHHHHHHHHCE
48.02-
47PhosphorylationKIGVVGGSDFEKVQE
CEEEECCCCHHHHHH
32.9524275569
51UbiquitinationVGGSDFEKVQEQLGN
ECCCCHHHHHHHHCC
49.5721890473
51UbiquitinationVGGSDFEKVQEQLGN
ECCCCHHHHHHHHCC
49.57-
63UbiquitinationLGNDVVEKYDYVFPE
HCCCHHHHCCEECCC
31.63-
76PhosphorylationPENGLVAYKDGKLLC
CCCCEEEEECCEEEE
11.35-
77UbiquitinationENGLVAYKDGKLLCR
CCCEEEEECCEEEEH
50.7121890473
77UbiquitinationENGLVAYKDGKLLCR
CCCEEEEECCEEEEH
50.71-
80AcetylationLVAYKDGKLLCRQNI
EEEEECCEEEEHHHH
48.7125953088
126SulfoxidationFIEFRNGMLNVSPIG
EEEEECCCEEECCCC
2.5528183972
130PhosphorylationRNGMLNVSPIGRSCS
ECCCEEECCCCCCCC
15.1023911959
137PhosphorylationSPIGRSCSQEERIEF
CCCCCCCCHHHCEEE
41.7023911959
145PhosphorylationQEERIEFYELDKKEN
HHHCEEEEECCHHHC
11.6426356563
149AcetylationIEFYELDKKENIRQK
EEEEECCHHHCHHHH
74.7023954790
1492-HydroxyisobutyrylationIEFYELDKKENIRQK
EEEEECCHHHCHHHH
74.70-
156UbiquitinationKKENIRQKFVADLRK
HHHCHHHHHHHHHHH
31.77-
202UbiquitinationHVENDGYKTIYFFGD
EEECCCEEEEEEECC
33.6921890473
202UbiquitinationHVENDGYKTIYFFGD
EEECCCEEEEEEECC
33.6921890473
203PhosphorylationVENDGYKTIYFFGDK
EECCCEEEEEEECCC
16.6628152594
205PhosphorylationNDGYKTIYFFGDKTM
CCCEEEEEEECCCCC
9.7028152594
2102-HydroxyisobutyrylationTIYFFGDKTMPGGND
EEEEECCCCCCCCCC
47.29-
210AcetylationTIYFFGDKTMPGGND
EEEEECCCCCCCCCC
47.2925953088
227SulfoxidationIFTDPRTMGYSVTAP
CCCCCCCCCEECCCC
5.1121406390
229PhosphorylationTDPRTMGYSVTAPED
CCCCCCCEECCCCHH
6.8020068231
230PhosphorylationDPRTMGYSVTAPEDT
CCCCCCEECCCCHHH
13.7820068231
232PhosphorylationRTMGYSVTAPEDTRR
CCCCEECCCCHHHHH
30.4720068231
237PhosphorylationSVTAPEDTRRICELL
ECCCCHHHHHHHHHH
21.8620068231

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 PMM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMM2_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 PMM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAGL3_HUMANTAGLN3physical
22939629
ACY3_HUMANACY3physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
212065Congenital disorder of glycosylation 1A (CDG1A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMM2_HUMAN

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Related Literatures of Post-Translational Modification

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