PMM1_HUMAN - dbPTM
PMM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMM1_HUMAN
UniProt AC Q92871
Protein Name Phosphomannomutase 1
Gene Name PMM1
Organism Homo sapiens (Human).
Sequence Length 262
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. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain..
Protein Sequence MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPETAHEA
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------MAVTAQAAR
------CCHHHHHHH
13.8422814378
19PhosphorylationERVLCLFDVDGTLTP
CCEEEEEECCCCCCC
25.349603909
30UbiquitinationTLTPARQKIDPEVAA
CCCCHHHHCCHHHHH
43.4521890473
30UbiquitinationTLTPARQKIDPEVAA
CCCCHHHHCCHHHHH
43.4521890473
41UbiquitinationEVAAFLQKLRSRVQI
HHHHHHHHHHHCCEE
48.2721890473
41UbiquitinationEVAAFLQKLRSRVQI
HHHHHHHHHHHCCEE
48.2721890473
58UbiquitinationVGGSDYCKIAEQLGD
CCCCHHHHHHHHHCC
38.43-
114PhosphorylationDLINFCLSYMALLRL
HHHHHHHHHHHHHCC
17.6522210691
115PhosphorylationLINFCLSYMALLRLP
HHHHHHHHHHHHCCC
3.5722210691
158UbiquitinationIEFSELDKKEKIREK
CCHHHHCHHHHHHHH
75.38-
165UbiquitinationKKEKIREKFVEALKT
HHHHHHHHHHHHHHH
44.88-
171UbiquitinationEKFVEALKTEFAGKG
HHHHHHHHHHHCCCC
53.72-
177UbiquitinationLKTEFAGKGLRFSRG
HHHHHCCCCCCCCCC
51.87-
183MethylationGKGLRFSRGGMISFD
CCCCCCCCCCCEEEE
42.86115487977
198UbiquitinationVFPEGWDKRYCLDSL
CCCCCCCCCEEHHHC
38.46-
235PhosphorylationEIFADPRTVGHSVVS
EEEECCCCCCCCCCC
35.9123312004
239PhosphorylationDPRTVGHSVVSPQDT
CCCCCCCCCCCHHHH
20.4823312004
242PhosphorylationTVGHSVVSPQDTVQR
CCCCCCCCHHHHHHH
18.0623312004
246PhosphorylationSVVSPQDTVQRCREI
CCCCHHHHHHHHHHH
17.1923312004

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 PMM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMM1_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 PMM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB6A_HUMANRAB6Aphysical
16189514
ZN363_HUMANRCHY1physical
21988832
RAB6A_HUMANRAB6Aphysical
25416956
POTEE_HUMANPOTEEphysical
26186194
HPHL1_HUMANHEPHL1physical
26186194
PMM2_HUMANPMM2physical
26186194
QRIC1_HUMANQRICH1physical
26186194
DSG4_HUMANDSG4physical
26186194
GBB2_HUMANGNB2physical
26186194
DUS14_HUMANDUSP14physical
26186194
LRC15_HUMANLRRC15physical
26186194
PMM2_HUMANPMM2physical
28514442
POTEE_HUMANPOTEEphysical
28514442
QRIC1_HUMANQRICH1physical
28514442
DSG4_HUMANDSG4physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
DUS14_HUMANDUSP14physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMM1_HUMAN

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Related Literatures of Post-Translational Modification

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