PGM2_HUMAN - dbPTM
PGM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGM2_HUMAN
UniProt AC Q96G03
Protein Name Phosphoglucomutase-2
Gene Name PGM2
Organism Homo sapiens (Human).
Sequence Length 612
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity..
Protein Sequence MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRFARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKASYFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFFQPQKYNLQPKAD
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------MAAPEGSGL
------CCCCCCCCC		31.5519413330
19PhosphorylationDARLDQETAQWLRWD
CCCCCHHHHHHHHCC		20.6520068231
27UbiquitinationAQWLRWDKNSLTLEA
HHHHHCCCCCCHHHH		41.2921890473
27UbiquitinationAQWLRWDKNSLTLEA
HHHHHCCCCCCHHHH		41.2922817900
27AcetylationAQWLRWDKNSLTLEA
HHHHHCCCCCCHHHH		41.2926822725
29PhosphorylationWLRWDKNSLTLEAVK
HHHCCCCCCHHHHHH		28.5925159151
36UbiquitinationSLTLEAVKRLIAEGN
CCHHHHHHHHHHCCC		48.8432015554
44UbiquitinationRLIAEGNKEELRKCF
HHHHCCCHHHHHHHH		64.5224816145
59PhosphorylationGARMEFGTAGLRAAM
CCCCCHHHHHHHHHH		23.9123684312
66SulfoxidationTAGLRAAMGPGISRM
HHHHHHHHCCCCCCC		6.9430846556
91UbiquitinationGFCRYLEKQFSDLKQ
HHHHHHHHHHHHHHH		54.7921890473
91UbiquitinationGFCRYLEKQFSDLKQ
HHHHHHHHHHHHHHH		54.7921890473
91AcetylationGFCRYLEKQFSDLKQ
HHHHHHHHHHHHHHH		54.7926822725
153UbiquitinationFVPFTVSHLKLCAGI
CCCCCHHHHHHEEEE		23.73-
153UbiquitinationFVPFTVSHLKLCAGI
CCCCCHHHHHHEEEE		23.7321890473
153AcetylationFVPFTVSHLKLCAGI
CCCCCHHHHHHEEEE		23.73-
163PhosphorylationLCAGIMITASHNPKQ
HEEEEEEEECCCCCC		12.5322167270
165PhosphorylationAGIMITASHNPKQDN
EEEEEEECCCCCCCC		18.3629255136
174PhosphorylationNPKQDNGYKVYWDNG
CCCCCCCCEEEECCC		11.9723403867
186PhosphorylationDNGAQIISPHDKGIS
CCCCEEECCCHHHHH		20.1528857561
194UbiquitinationPHDKGISQAIEENLE
CCHHHHHHHHHHCCC		44.42-
231UbiquitinationSINNDYFEDLKKYCF
CCCCCHHHHHHHHHH		57.0923000965
253PhosphorylationTKVKFVHTSVHGVGH
CCEEEEEECCCCCCH		27.4325850435
254PhosphorylationKVKFVHTSVHGVGHS
CEEEEEECCCCCCHH		9.3825850435
261PhosphorylationSVHGVGHSFVQSAFK
CCCCCCHHHHHHHHH		22.6025850435
265PhosphorylationVGHSFVQSAFKAFDL
CCHHHHHHHHHHHCC		30.3025850435
268MethylationSFVQSAFKAFDLVPP
HHHHHHHHHHCCCCC		48.11-
268"N6,N6-dimethyllysine"SFVQSAFKAFDLVPP
HHHHHHHHHHCCCCC		48.11-
292AcetylationDPEFPTVKYPNPEEG
CCCCCCCCCCCHHCC		58.4226822725
292UbiquitinationDPEFPTVKYPNPEEG
CCCCCCCCCCCHHCC		58.4221890473
292UbiquitinationDPEFPTVKYPNPEEG
CCCCCCCCCCCHHCC		58.4222817900
293PhosphorylationPEFPTVKYPNPEEGK
CCCCCCCCCCHHCCC		12.1428102081
304PhosphorylationEEGKGVLTLSFALAD
HCCCCEEEEEEEECC		20.2529255136
306PhosphorylationGKGVLTLSFALADKT
CCCEEEEEEEECCCC		11.8423403867
313PhosphorylationSFALADKTKARIVLA
EEEECCCCCCEEEEC		30.4023403867
327MethylationANDPDADRLAVAEKQ
CCCCCHHHEEEEEEC		26.68115487289
333UbiquitinationDRLAVAEKQDSGEWR
HHEEEEEECCCCCEE		50.06-
367PhosphorylationKEKNQDRSALKDTYM
HHHCCCHHHHHHHHH		46.3620068231
370UbiquitinationNQDRSALKDTYMLSS
CCCHHHHHHHHHHHH		47.9823000965
372PhosphorylationDRSALKDTYMLSSTV
CHHHHHHHHHHHHHH		14.8320068231
373PhosphorylationRSALKDTYMLSSTVS
HHHHHHHHHHHHHHH		13.2420068231
376PhosphorylationLKDTYMLSSTVSSKI
HHHHHHHHHHHHHHH		13.8720068231
377PhosphorylationKDTYMLSSTVSSKIL
HHHHHHHHHHHHHHH		28.9420068231
378PhosphorylationDTYMLSSTVSSKILR
HHHHHHHHHHHHHHH		22.4920068231
380PhosphorylationYMLSSTVSSKILRAI
HHHHHHHHHHHHHHH		26.4620068231
381PhosphorylationMLSSTVSSKILRAIA
HHHHHHHHHHHHHHH		21.2720068231
410UbiquitinationKWMGNRAKQLIDQGK
CCCHHHHHHHHHCCC		42.2629967540
447PhosphorylationGVSAAVISAELASFL
CCCHHHHHHHHHHHH		14.75-
469PhosphorylationSQQLKAIYVEYGYHI
HHHHHHHHHHHCCCC		7.6522817900
472PhosphorylationLKAIYVEYGYHITKA
HHHHHHHHCCCCEEE		16.9722817900
481PhosphorylationYHITKASYFICHDQE
CCCEEECEEEECCHH		11.2121253578
489PhosphorylationFICHDQETIKKLFEN
EEECCHHHHHHHHHH		32.25-
492UbiquitinationHDQETIKKLFENLRN
CCHHHHHHHHHHHHC		55.3319608861
492AcetylationHDQETIKKLFENLRN
CCHHHHHHHHHHHHC		55.3319608861
503UbiquitinationNLRNYDGKNNYPKAC
HHHCCCCCCCCCCCC		38.84-
512AcetylationNYPKACGKFEISAIR
CCCCCCCCEEEEHHH		39.4425953088
512UbiquitinationNYPKACGKFEISAIR
CCCCCCCCEEEEHHH		39.4432015554
525PhosphorylationIRDLTTGYDDSQPDK
HHHCCCCCCCCCCCC		17.9332142685
528PhosphorylationLTTGYDDSQPDKKAV
CCCCCCCCCCCCCCC		40.4932142685
532AcetylationYDDSQPDKKAVLPTS
CCCCCCCCCCCCCCC		49.6825953088
533UbiquitinationDDSQPDKKAVLPTSK
CCCCCCCCCCCCCCC		51.6229967540
538PhosphorylationDKKAVLPTSKSSQMI
CCCCCCCCCCCCCEE		44.6327251275
539PhosphorylationKKAVLPTSKSSQMIT
CCCCCCCCCCCCEEE		28.7124719451
541PhosphorylationAVLPTSKSSQMITFT
CCCCCCCCCCEEEEE		26.1020068231
542PhosphorylationVLPTSKSSQMITFTF
CCCCCCCCCEEEEEE		27.7520068231
546PhosphorylationSKSSQMITFTFANGG
CCCCCEEEEEEECCC		15.9824719451
548PhosphorylationSSQMITFTFANGGVA
CCCEEEEEEECCCEE		17.1220068231
556PhosphorylationFANGGVATMRTSGTE
EECCCEEEEECCCCC		12.5520068231
567AcetylationSGTEPKIKYYAELCA
CCCCCCEEEEEECCC		38.0325953088
568PhosphorylationGTEPKIKYYAELCAP
CCCCCEEEEEECCCC		16.0422817900
569PhosphorylationTEPKIKYYAELCAPP
CCCCEEEEEECCCCC		6.65-
585AcetylationNSDPEQLKKELNELV
CCCHHHHHHHHHHHH		43.8525953088
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 PGM2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGM2_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 PGM2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CK054_HUMANC11orf54physical
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 PGM2_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.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-14, AND ACETYLATION AT ALA-2.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-492, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.

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