G3P_BOVIN - dbPTM
G3P_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3P_BOVIN
UniProt AC P10096
Protein Name Glyceraldehyde-3-phosphate dehydrogenase
Gene Name GAPDH
Organism Bos taurus (Bovine).
Sequence Length 333
Subcellular Localization Cytoplasm, cytosol. Nucleus. Cytoplasm, cytoskeleton. Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal..
Protein Description Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity)..
Protein Sequence MVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLHYMVYMFQYDSTHGKFNGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYNNTLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDEIKKVVKQASEGPLKGILGYTEDQVVSCDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVHMASKE
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
3"N6,N6-dimethyllysine"-----MVKVGVNGFG
-----CCEEECCCCC		31.79-
3Methylation-----MVKVGVNGFG
-----CCEEECCCCC		31.79-
7Deamidated asparagine-MVKVGVNGFGRIGR
-CCEEECCCCCHHHH		33.86-
7Deamidation-MVKVGVNGFGRIGR
-CCEEECCCCCHHHH		33.86-
40PhosphorylationDPFIDLHYMVYMFQY
CCCEEEEEEEEEEEE		8.79-
59AcetylationGKFNGTVKAENGKLV
CEECEEEEEECCEEE		50.23-
62DeamidationNGTVKAENGKLVING
CEEEEEECCEEEECC		58.73-
62Deamidated asparagineNGTVKAENGKLVING
CEEEEEECCEEEECC		58.73-
64"N6,N6-dimethyllysine"TVKAENGKLVINGKA
EEEEECCEEEECCEE		51.68-
64MethylationTVKAENGKLVINGKA
EEEEECCEEEECCEE		51.68-
68DeamidationENGKLVINGKAITIF
ECCEEEECCEEEEEE		38.13-
68Deamidated asparagineENGKLVINGKAITIF
ECCEEEECCEEEEEE		38.13-
73PhosphorylationVINGKAITIFQERDP
EECCEEEEEEEECCC		22.1629541418
120PhosphorylationGAKRVIISAPSADAP
CCEEEEEECCCCCCC		24.01-
146PhosphorylationNNTLKIVSNASCTTN
CCEEEEECCCCHHHC		30.10-
147Deamidated asparagineNTLKIVSNASCTTNC
CEEEEECCCCHHHCC		25.61-
147DeamidationNTLKIVSNASCTTNC
CEEEEECCCCHHHCC		25.61-
149PhosphorylationLKIVSNASCTTNCLA
EEEECCCCHHHCCHH		19.08-
150ADP-ribosylationKIVSNASCTTNCLAP
EEECCCCHHHCCHHH		5.17-
150ADP-ribosylationKIVSNASCTTNCLAP
EEECCCCHHHCCHHH		5.17-
150SulfhydrationKIVSNASCTTNCLAP
EEECCCCHHHCCHHH		5.17-
150S-nitrosylationKIVSNASCTTNCLAP
EEECCCCHHHCCHHH		5.17-
150SuccinylationKIVSNASCTTNCLAP
EEECCCCHHHCCHHH		5.17-
151PhosphorylationIVSNASCTTNCLAPL
EECCCCHHHCCHHHH		20.67-
153DeamidationSNASCTTNCLAPLAK
CCCCHHHCCHHHHHH		10.72-
153Deamidated asparagineSNASCTTNCLAPLAK
CCCCHHHCCHHHHHH		10.72-
174PhosphorylationGIVEGLMTTVHAITA
CHHHHHHHHHHHHHE		30.6129541418
175PhosphorylationIVEGLMTTVHAITAT
HHHHHHHHHHHHHEE		9.0629541418
180PhosphorylationMTTVHAITATQKTVD
HHHHHHHHEEECCCC		25.1629541418
182PhosphorylationTVHAITATQKTVDGP
HHHHHHEEECCCCCC		23.1929541418
185PhosphorylationAITATQKTVDGPSGK
HHHEEECCCCCCCCC		17.6329541418
190PhosphorylationQKTVDGPSGKLWRDG
ECCCCCCCCCCCCCC		54.8329541418
192"N6,N6-dimethyllysine"TVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC		49.57-
192UbiquitinationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC		49.5721890473
192MethylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC		49.57-
192MalonylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC		49.57-
192AcetylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC		49.57-
208PhosphorylationAQNIIPASTGAAKAV
HHHCCCCCCCHHHHH		23.2429541418
209PhosphorylationQNIIPASTGAAKAVG
HHCCCCCCCHHHHHH		32.7129541418
213MethylationPASTGAAKAVGKVIP
CCCCCHHHHHHHHHH		42.97-
213"N6,N6-dimethyllysine"PASTGAAKAVGKVIP
CCCCCHHHHHHHHHH		42.97-
213MalonylationPASTGAAKAVGKVIP
CCCCCHHHHHHHHHH		42.97-
217UbiquitinationGAAKAVGKVIPELNG
CHHHHHHHHHHHHCC		30.3221890473
217AcetylationGAAKAVGKVIPELNG
CHHHHHHHHHHHHCC		30.32-
223Deamidated asparagineGKVIPELNGKLTGMA
HHHHHHHCCEEEEEE		43.84-
223DeamidationGKVIPELNGKLTGMA
HHHHHHHCCEEEEEE		43.84-
225MethylationVIPELNGKLTGMAFR
HHHHHCCEEEEEEEE		41.63-
225UbiquitinationVIPELNGKLTGMAFR
HHHHHCCEEEEEEEE		41.6321890473
225"N6,N6-dimethyllysine"VIPELNGKLTGMAFR
HHHHHCCEEEEEEEE		41.63-
225AcetylationVIPELNGKLTGMAFR
HHHHHCCEEEEEEEE		41.63-
227PhosphorylationPELNGKLTGMAFRVP
HHHCCEEEEEEEECC		28.53-
235PhosphorylationGMAFRVPTPNVSVVD
EEEEECCCCCEEEEE		25.33-
239PhosphorylationRVPTPNVSVVDLTCR
ECCCCCEEEEEEEEE		24.06-
245S-nitrosocysteineVSVVDLTCRLEKPAK
EEEEEEEEEECCCCC		6.42-
245SuccinylationVSVVDLTCRLEKPAK
EEEEEEEEEECCCCC		6.42-
245S-nitrosylationVSVVDLTCRLEKPAK
EEEEEEEEEECCCCC		6.42-
252AcetylationCRLEKPAKYDEIKKV
EEECCCCCHHHHHHH		62.86-
258"N6,N6-dimethyllysine"AKYDEIKKVVKQASE
CCHHHHHHHHHHHHC		58.90-
258MethylationAKYDEIKKVVKQASE
CCHHHHHHHHHHHHC		58.90-
261UbiquitinationDEIKKVVKQASEGPL
HHHHHHHHHHHCCCC		43.0421890473
261"N6,N6-dimethyllysine"DEIKKVVKQASEGPL
HHHHHHHHHHHCCCC		43.04-
261MethylationDEIKKVVKQASEGPL
HHHHHHHHHHHCCCC		43.04-
310PhosphorylationDHFVKLISWYDNEFG
HHHHHHHHHCCCCCC		29.98-
314Deamidated asparagineKLISWYDNEFGYSNR
HHHHHCCCCCCCHHH		30.69-
314DeamidationKLISWYDNEFGYSNR
HHHHHCCCCCCCHHH		30.69-
318PhosphorylationWYDNEFGYSNRVVDL
HCCCCCCCHHHHHHH		14.2129541418
319PhosphorylationYDNEFGYSNRVVDLM
CCCCCCCHHHHHHHH		20.6629541418
331PhosphorylationDLMVHMASKE-----
HHHHHHHCCC-----		29.7329541418
332"N6,N6-dimethyllysine"LMVHMASKE------
HHHHHHCCC------		58.88-
332MethylationLMVHMASKE------
HHHHHHCCC------		58.88-
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 G3P_BOVIN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of G3P_BOVIN !!
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 G3P_BOVIN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPPP_BOVINTPPPphysical
17027006
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of G3P_BOVIN

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Related Literatures of Post-Translational Modification

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