PGM5_HUMAN - dbPTM
PGM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGM5_HUMAN
UniProt AC Q15124
Protein Name Phosphoglucomutase-like protein 5
Gene Name PGM5
Organism Homo sapiens (Human).
Sequence Length 567
Subcellular Localization Cell junction, adherens junction . Cytoplasm, cytoskeleton . Adherens-type cellular junctions. Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments.
Protein Description Component of adherens-type cell-cell and cell-matrix junctions. Lacks phosphoglucomutase activity..
Protein Sequence MEGSPIPVLTVPTAPYEDQRPAGGGGLRRPTGLFEGQRNYLPNFIQSVLSSIDLRDRQGCTMVVGSDGRYFSRTAIEIVVQMAAANGIGRLIIGQNGILSTPAVSCIIRKIKAAGGIILTASHCPGGPGGEFGVKFNVANGGPAPDVVSDKIYQISKTIEEYAICPDLRIDLSRLGRQEFDLENKFKPFRVEIVDPVDIYLNLLRTIFDFHAIKGLLTGPSQLKIRIDAMHGVMGPYVRKVLCDELGAPANSAINCVPLEDFGGQHPDPNLTYATTLLEAMKGGEYGFGAAFDADGDRYMILGQNGFFVSPSDSLAIIAANLSCIPYFRQMGVRGFGRSMPTSMALDRVAKSMKVPVYETPAGWRFFSNLMDSGRCNLCGEESFGTGSDHLREKDGLWAVLVWLSIIAARKQSVEEIVRDHWAKFGRHYYCRFDYEGLDPKTTYYIMRDLEALVTDKSFIGQQFAVGSHVYSVAKTDSFEYVDPVDGTVTKKQGLRIIFSDASRLIFRLSSSSGVRATLRLYAESYERDPSGHDQEPQAVLSPLIAIALKISQIHERTGRRGPTVIT
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
4Phosphorylation----MEGSPIPVLTV
----CCCCCCCEEEC		13.3228355574
13PhosphorylationIPVLTVPTAPYEDQR
CCEEECCCCCCCCCC		35.6128634298
16PhosphorylationLTVPTAPYEDQRPAG
EECCCCCCCCCCCCC		29.6728634298
31PhosphorylationGGGLRRPTGLFEGQR
CCCCCCCCCCCCCHH		44.7123312004
66PhosphorylationGCTMVVGSDGRYFSR
CCEEEECCCCCEECH		25.8620068231
120PhosphorylationAAGGIILTASHCPGG
HCCCEEEEECCCCCC		18.7323401153
122PhosphorylationGGIILTASHCPGGPG
CCEEEEECCCCCCCC		22.0123401153
149PhosphorylationGPAPDVVSDKIYQIS
CCCCCHHHHHHHHHC		32.7928442448
153PhosphorylationDVVSDKIYQISKTIE
CHHHHHHHHHCHHHH		12.9222817900
156PhosphorylationSDKIYQISKTIEEYA
HHHHHHHCHHHHHHC		14.2819060867
173PhosphorylationPDLRIDLSRLGRQEF
CCCEEEHHHHCCCCC		23.0130387612
221PhosphorylationKGLLTGPSQLKIRID
HCCCCCHHHCCEEHH		49.8725159151
286PhosphorylationEAMKGGEYGFGAAFD
HHHCCCCCCCCEEEC		22.4924248375
299PhosphorylationFDADGDRYMILGQNG
ECCCCCEEEEECCCC		8.01-
352PhosphorylationALDRVAKSMKVPVYE
HHHHHHHHCCCCEEE		17.69-
358PhosphorylationKSMKVPVYETPAGWR
HHCCCCEEECCCCHH		14.1721253578
360PhosphorylationMKVPVYETPAGWRFF
CCCCEEECCCCHHHH		10.7623312004
368PhosphorylationPAGWRFFSNLMDSGR
CCCHHHHHHHHCCCC		26.75-
444PhosphorylationGLDPKTTYYIMRDLE
CCCHHHEEEEHHCHH		9.02-
491AcetylationPVDGTVTKKQGLRII
CCCCCEEEECCEEEE		38.477668627
510PhosphorylationSRLIFRLSSSSGVRA
CHHHHHHHCCCCHHH		24.7428857561
511PhosphorylationRLIFRLSSSSGVRAT
HHHHHHHCCCCHHHE		32.87-
512PhosphorylationLIFRLSSSSGVRATL
HHHHHHCCCCHHHEE		27.9528857561
513PhosphorylationIFRLSSSSGVRATLR
HHHHHCCCCHHHEEH		43.1622817900
522PhosphorylationVRATLRLYAESYERD
HHHEEHHHHHHHCCC		11.24-
525PhosphorylationTLRLYAESYERDPSG
EEHHHHHHHCCCCCC		24.91-
526PhosphorylationLRLYAESYERDPSGH
EHHHHHHHCCCCCCC		13.39-
531PhosphorylationESYERDPSGHDQEPQ
HHHCCCCCCCCCCCH		53.72-
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 PGM5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGM5_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 PGM5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UTRO_HUMANUTRNphysical
7589238
VINC_HUMANVCLphysical
22939629
G6PI_HUMANGPIphysical
26344197
GLYG_HUMANGYG1physical
26344197
CH10_HUMANHSPE1physical
26344197
AGM1_HUMANPGM3physical
26344197
TALDO_HUMANTALDO1physical
26344197
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 PGM5_HUMAN

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Related Literatures of Post-Translational Modification

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