GPDM_HUMAN - dbPTM
GPDM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPDM_HUMAN
UniProt AC P43304
Protein Name Glycerol-3-phosphate dehydrogenase, mitochondrial
Gene Name GPD2
Organism Homo sapiens (Human).
Sequence Length 727
Subcellular Localization Mitochondrion.
Protein Description
Protein Sequence MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYGIKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLYYEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPVDRSCGGL
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
33AcetylationQFAHYRRKQMNLAYV
HHHHHHHHHCCHHHH		44.9230589025
41AcetylationQMNLAYVKAADCISE
HCCHHHHHHHHHCCC		25.7730589031
47PhosphorylationVKAADCISEPVNREP
HHHHHHCCCCCCCCC		42.02-
67O-linked_GlycosylationQLLTLQNTSEFDILV
HEEEECCCCCCCEEE		19.3723301498
80O-linked_GlycosylationLVIGGGATGSGCALD
EEECCCCCCCCHHHH		34.8423301498
83 (in isoform 2)Ubiquitination-11.32-
94UbiquitinationDAVTRGLKTALVERD
HHHHHCHHEEEEECC		34.28-
104PhosphorylationLVERDDFSSGTSSRS
EEECCCCCCCCCCCC		34.55-
105PhosphorylationVERDDFSSGTSSRST
EECCCCCCCCCCCCC		46.19-
113UbiquitinationGTSSRSTKLIHGGVR
CCCCCCCEEECCHHH		46.84-
121PhosphorylationLIHGGVRYLQKAIMK
EECCHHHHHHHHHHC		15.86-
128UbiquitinationYLQKAIMKLDIEQYR
HHHHHHHCCCHHHHH		36.57-
128 (in isoform 2)Ubiquitination-36.57-
138UbiquitinationIEQYRMVKEALHERA
HHHHHHHHHHHHHHH		28.11-
190MethylationVAGSNCLKSSYVLSK
HHCCCCCCHHHHCCC		39.29-
191PhosphorylationAGSNCLKSSYVLSKS
HCCCCCCHHHHCCCC		17.6020860994
196PhosphorylationLKSSYVLSKSRALEH
CCHHHHCCCCHHHHH		20.6720860994
197UbiquitinationKSSYVLSKSRALEHF
CHHHHCCCCHHHHHC		39.54-
1972-HydroxyisobutyrylationKSSYVLSKSRALEHF
CHHHHCCCCHHHHHC		39.54-
2092-HydroxyisobutyrylationEHFPMLQKDKLVGAI
HHCCCCCCCCEEEEE		53.52-
2112-HydroxyisobutyrylationFPMLQKDKLVGAIVY
CCCCCCCCEEEEEEE		52.70-
218PhosphorylationKLVGAIVYYDGQHND
CEEEEEEEECCCCCC		6.96-
246PhosphorylationYGAATANYMEVVSLL
HCHHHCCHHHHHHHH		7.68-
251PhosphorylationANYMEVVSLLKKTDP
CCHHHHHHHHHCCCC		32.9124719451
271UbiquitinationRVSGARCKDVLTGQE
EEECCEECCCCCCCC		45.37-
275PhosphorylationARCKDVLTGQEFDVR
CEECCCCCCCCEEEE		36.35-
284UbiquitinationQEFDVRAKCVINATG
CCEEEEEEEEEECCC		20.62-
290PhosphorylationAKCVINATGPFTDSV
EEEEEECCCCCCHHH		40.6820068231
294PhosphorylationINATGPFTDSVRKMD
EECCCCCCHHHCCCC		30.4220068231
296PhosphorylationATGPFTDSVRKMDDK
CCCCCCHHHCCCCHH		22.2920068231
347 (in isoform 2)Ubiquitination-24.57-
355PhosphorylationKMTIAGTTDTPTDVT
EEEEECCCCCCCCCC		36.64-
357PhosphorylationTIAGTTDTPTDVTHH
EEECCCCCCCCCCCC		26.46-
359PhosphorylationAGTTDTPTDVTHHPI
ECCCCCCCCCCCCCC		45.23-
362PhosphorylationTDTPTDVTHHPIPSE
CCCCCCCCCCCCCCH		19.78-
378 (in isoform 2)Ubiquitination-39.1321906983
382PhosphorylationILNEVRNYLSCDVEV
HHHHHHHHHCCCEEE		6.8820068231
384 (in isoform 2)Ubiquitination-9.64-
384PhosphorylationNEVRNYLSCDVEVRR
HHHHHHHCCCEEEEC		9.6420068231
409UbiquitinationRPLVTDPKSADTQSI
CCCCCCCCCCCCCCC		62.17-
413PhosphorylationTDPKSADTQSISRNH
CCCCCCCCCCCCCCC		24.7528102081
415PhosphorylationPKSADTQSISRNHVV
CCCCCCCCCCCCCEE		25.3228102081
417PhosphorylationSADTQSISRNHVVDI
CCCCCCCCCCCEEEE		32.0728102081
4532-HydroxyisobutyrylationDTINAAVKTHNLKAG
HHHHHHHHHCCCCCC		39.06-
453UbiquitinationDTINAAVKTHNLKAG
HHHHHHHHHCCCCCC		39.06-
4582-HydroxyisobutyrylationAVKTHNLKAGPSRTV
HHHHCCCCCCCCCEE		57.52-
458UbiquitinationAVKTHNLKAGPSRTV
HHHHCCCCCCCCCEE		57.52-
476PhosphorylationLQGGKDWSPTLYIRL
EECCCCCCCEEHEEH		20.38-
480PhosphorylationKDWSPTLYIRLVQDY
CCCCCEEHEEHHHHH		6.1022817900
487PhosphorylationYIRLVQDYGLESEVA
HEEHHHHHCCHHHHH		13.4028152594
504 (in isoform 1)Ubiquitination-51.0821906983
504UbiquitinationLAATYGDKAFEVAKM
HHHHHCHHHHHHHHH		51.082190698
510UbiquitinationDKAFEVAKMASVTGK
HHHHHHHHHHHCCCC		39.93-
5102-HydroxyisobutyrylationDKAFEVAKMASVTGK
HHHHHHHHHHHCCCC		39.93-
513PhosphorylationFEVAKMASVTGKRWP
HHHHHHHHCCCCCCC		19.4020068231
515PhosphorylationVAKMASVTGKRWPIV
HHHHHHCCCCCCCEE		34.1920068231
5172-HydroxyisobutyrylationKMASVTGKRWPIVGV
HHHHCCCCCCCEEEE		41.76-
532PhosphorylationRLVSEFPYIEAEVKY
EEEEECCEEEEEHHH		19.40-
544PhosphorylationVKYGIKEYACTAVDM
HHHCCHHHHHHHHHH		11.28-
547PhosphorylationGIKEYACTAVDMISR
CCHHHHHHHHHHHHH		22.88-
553PhosphorylationCTAVDMISRRTRLAF
HHHHHHHHHHHHHHH		14.74-
586PhosphorylationRELNWDDYKKQEQLE
CCCCHHHHHHHHHHH		20.01-
5872-HydroxyisobutyrylationELNWDDYKKQEQLET
CCCHHHHHHHHHHHH		55.78-
600PhosphorylationETARKFLYYEMGYKS
HHHHHHHHHHHCCCC		10.6629759185
601PhosphorylationTARKFLYYEMGYKSR
HHHHHHHHHHCCCCH		11.1129759185
605PhosphorylationFLYYEMGYKSRSEQL
HHHHHHCCCCHHHHC		12.4129759185
607PhosphorylationYYEMGYKSRSEQLTD
HHHHCCCCHHHHCCC		32.3327251275
609PhosphorylationEMGYKSRSEQLTDRS
HHCCCCHHHHCCCHH		36.4627251275
619PhosphorylationLTDRSEISLLPSDID
CCCHHHHHCCCHHHH		21.5723186163
623PhosphorylationSEISLLPSDIDRYKK
HHHHCCCHHHHHHHH		47.36-
634AcetylationRYKKRFHKFDADQKG
HHHHHHHCCCCCCCC		42.0819608861
634MalonylationRYKKRFHKFDADQKG
HHHHHHHCCCCCCCC		42.0826320211
634UbiquitinationRYKKRFHKFDADQKG
HHHHHHHCCCCCCCC		42.0819608861
6402-HydroxyisobutyrylationHKFDADQKGFITIVD
HCCCCCCCCCEEEEE		57.23-
723PhosphorylationVPIPVDRSCGGL---
CCCCCCCCCCCC---		16.7925159151
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 GPDM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPDM_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 GPDM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COX2_HUMANCOX2physical
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 GPDM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-634, AND MASS SPECTROMETRY.

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