G3P_RABIT - dbPTM
G3P_RABIT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3P_RABIT
UniProt AC P46406
Protein Name Glyceraldehyde-3-phosphate dehydrogenase
Gene Name GAPDH
Organism Oryctolagus cuniculus (Rabbit).
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 MVKVGVNGFGRIGRLVTRAAFNSGKVDVVAINDPFIDLHYMVYMFQYDSTHGKFHGTVKAENGKLVINGKAITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDHFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKAAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSATHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMVHMASKE
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-
7Deamidation-MVKVGVNGFGRIGR
-CCEEECCCCCHHHH
33.86-
7Deamidated asparagine-MVKVGVNGFGRIGR
-CCEEECCCCCHHHH
33.86-
40PhosphorylationDPFIDLHYMVYMFQY
CCCEEEEEEEEEEEE
8.79-
47NitrationYMVYMFQYDSTHGKF
EEEEEEEEECCCCEE
10.70-
59AcetylationGKFHGTVKAENGKLV
CEEEEEEEEECCEEE
50.23-
62DeamidationHGTVKAENGKLVING
EEEEEEECCEEEECC
58.73-
62Deamidated asparagineHGTVKAENGKLVING
EEEEEEECCEEEECC
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
22.16-
92NitrationWGDAGAEYVVESTGV
CCCCCCEEEEEECCC
14.84-
120PhosphorylationGAKRVIISAPSADAP
CCEEEEEECCCCCCC
24.01-
146PhosphorylationDNSLKIVSNASCTTN
CCCEEEEECCCHHHC
30.10-
147Deamidated asparagineNSLKIVSNASCTTNC
CCEEEEECCCHHHCC
25.61-
147DeamidationNSLKIVSNASCTTNC
CCEEEEECCCHHHCC
25.61-
149PhosphorylationLKIVSNASCTTNCLA
EEEEECCCHHHCCHH
19.08-
150GlutathionylationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.1710092623
150S-nitrosylationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.17-
150SuccinylationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.1717934141
150SulfhydrationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.17-
150ADP-ribosylationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.17-
150ADP-ribosylationKIVSNASCTTNCLAP
EEEECCCHHHCCHHH
5.17-
151PhosphorylationIVSNASCTTNCLAPL
EEECCCHHHCCHHHH
20.67-
153Deamidated asparagineSNASCTTNCLAPLAK
ECCCHHHCCHHHHHH
10.72-
153DeamidationSNASCTTNCLAPLAK
ECCCHHHCCHHHHHH
10.72-
154GlutathionylationNASCTTNCLAPLAKV
CCCHHHCCHHHHHHH
3.0110092623
175PhosphorylationIVEGLMTTVHAITAT
HHHHHHHHHHHHHEE
9.06-
180PhosphorylationMTTVHAITATQKTVD
HHHHHHHHEEECCCC
25.16-
182PhosphorylationTVHAITATQKTVDGP
HHHHHHEEECCCCCC
23.19-
184AcetylationHAITATQKTVDGPSG
HHHHEEECCCCCCCC
46.274316369
192MalonylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC
49.57-
192MethylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC
49.57-
192AcetylationTVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC
49.57-
192"N6,N6-dimethyllysine"TVDGPSGKLWRDGRG
CCCCCCCCCCCCCCC
49.57-
209PhosphorylationQNIIPASTGAAKAVG
HHCCCCCCCHHHHHH
32.71-
213MalonylationPASTGAAKAVGKVIP
CCCCCHHHHHHHHHH
42.97-
213MethylationPASTGAAKAVGKVIP
CCCCCHHHHHHHHHH
42.97-
213"N6,N6-dimethyllysine"PASTGAAKAVGKVIP
CCCCCHHHHHHHHHH
42.97-
217AcetylationGAAKAVGKVIPELNG
CHHHHHHHHHHHHCC
30.32-
223Deamidated asparagineGKVIPELNGKLTGMA
HHHHHHHCCEEEEEE
43.84-
223DeamidationGKVIPELNGKLTGMA
HHHHHHHCCEEEEEE
43.84-
225"N6,N6-dimethyllysine"VIPELNGKLTGMAFR
HHHHHCCEEEEEEEE
41.63-
225MethylationVIPELNGKLTGMAFR
HHHHHCCEEEEEEEE
41.63-
225AcetylationVIPELNGKLTGMAFR
HHHHHCCEEEEEEEE
41.63-
227PhosphorylationPELNGKLTGMAFRVP
HHHCCEEEEEEEECC
28.53-
235PhosphorylationGMAFRVPTPNVSVVD
EEEEECCCCCEEEEE
25.33-
239PhosphorylationRVPTPNVSVVDLTCR
ECCCCCEEEEEEEEE
24.06-
245S-nitrosocysteineVSVVDLTCRLEKAAK
EEEEEEEEEHHHHHC
6.42-
245SuccinylationVSVVDLTCRLEKAAK
EEEEEEEEEHHHHHC
6.4217934141
245S-palmitoylationVSVVDLTCRLEKAAK
EEEEEEEEEHHHHHC
6.4216128592
245S-nitrosylationVSVVDLTCRLEKAAK
EEEEEEEEEHHHHHC
6.42-
252AcetylationCRLEKAAKYDDIKKV
EEHHHHHCHHHHHHH
54.81-
258"N6,N6-dimethyllysine"AKYDDIKKVVKQASE
HCHHHHHHHHHHHCC
53.23-
258MethylationAKYDDIKKVVKQASE
HCHHHHHHHHHHHCC
53.23-
261MethylationDDIKKVVKQASEGPL
HHHHHHHHHHCCCCC
43.04-
261"N6,N6-dimethyllysine"DDIKKVVKQASEGPL
HHHHHHHHHHCCCCC
43.04-
310PhosphorylationDHFVKLISWYDNEFG
HHHHHHHHHCCCCCC
29.98-
312NitrationFVKLISWYDNEFGYS
HHHHHHHCCCCCCCH
11.33-
314DeamidationKLISWYDNEFGYSNR
HHHHHCCCCCCCHHH
30.69-
314Deamidated asparagineKLISWYDNEFGYSNR
HHHHHCCCCCCCHHH
30.69-
318NitrationWYDNEFGYSNRVVDL
HCCCCCCCHHHHHHH
14.21-
331PhosphorylationDLMVHMASKE-----
HHHHHHHCCC-----
29.73-
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_RABIT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of G3P_RABIT !!

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_RABIT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of G3P_RABIT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of G3P_RABIT

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Related Literatures of Post-Translational Modification

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