RIDA_HUMAN - dbPTM
RIDA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIDA_HUMAN
UniProt AC P52758
Protein Name 2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000305|PubMed:22094463}
Gene Name RIDA {ECO:0000312|HGNC:HGNC:16897}
Organism Homo sapiens (Human).
Sequence Length 137
Subcellular Localization Cytoplasm . Nucleus . Peroxisome . Mitochondrion . Mostly cytoplasmic but, in less differentiated cells occasionally nuclear.
Protein Description Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.; May also function as an endoribonuclease, cleaving mRNA phosphodiester bonds of single-stranded RNA (By similarity). Thereby, may inhibit protein translation. [PubMed: 8973653]
Protein Sequence MSSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL
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------MSSLIRRVI
------CCHHHHHHH
20068231
2Phosphorylation------MSSLIRRVI
------CCHHHHHHH
20068231
3Phosphorylation-----MSSLIRRVIS
-----CCHHHHHHHH
20068231
10PhosphorylationSLIRRVISTAKAPGA
HHHHHHHHHCCCCCC
29759185
11PhosphorylationLIRRVISTAKAPGAI
HHHHHHHHCCCCCCC
29759185
13AcetylationRRVISTAKAPGAIGP
HHHHHHCCCCCCCCC
25953088
13UbiquitinationRRVISTAKAPGAIGP
HHHHHHCCCCCCCCC
2205393
13SuccinylationRRVISTAKAPGAIGP
HHHHHHCCCCCCCCC
22053931
13SuccinylationRRVISTAKAPGAIGP
HHHHHHCCCCCCCCC
-
21PhosphorylationAPGAIGPYSQAVLVD
CCCCCCCCCCEEEEE
24927040
22PhosphorylationPGAIGPYSQAVLVDR
CCCCCCCCCEEEEEC
28258704
42PhosphorylationGQIGMDPSSGQLVSG
EECCCCCCCCCCCCC
27732954
43PhosphorylationQIGMDPSSGQLVSGG
ECCCCCCCCCCCCCC
27732954
48PhosphorylationPSSGQLVSGGVAEEA
CCCCCCCCCCHHHHH
27732954
60SuccinylationEEAKQALKNMGEILK
HHHHHHHHHHHHHHH
23954790
60AcetylationEEAKQALKNMGEILK
HHHHHHHHHHHHHHH
25038526
60SuccinylationEEAKQALKNMGEILK
HHHHHHHHHHHHHHH
-
67SuccinylationKNMGEILKAAGCDFT
HHHHHHHHHCCCCCC
-
67SuccinylationKNMGEILKAAGCDFT
HHHHHHHHHCCCCCC
-
74PhosphorylationKAAGCDFTNVVKTTV
HHCCCCCCHHCEEEE
24275569
91PhosphorylationADINDFNTVNEIYKQ
ECCCCCCHHHHHHHH
24275569
97AcetylationNTVNEIYKQYFKSNF
CHHHHHHHHHHHCCC
25038526
101AcetylationEIYKQYFKSNFPARA
HHHHHHHHCCCCHHH
25825284
102PhosphorylationIYKQYFKSNFPARAA
HHHHHHHCCCCHHHH
26437602
110PhosphorylationNFPARAAYQVAALPK
CCCHHHHHHHEECCC
28152594
117MalonylationYQVAALPKGSRIEIE
HHHEECCCCCCEEEE
26320211
117SuccinylationYQVAALPKGSRIEIE
HHHEECCCCCCEEEE
27452117
133PhosphorylationVAIQGPLTTASL---
EEEECCCCCCCC---
20068231
134PhosphorylationAIQGPLTTASL----
EEECCCCCCCC----
28258704
136PhosphorylationQGPLTTASL------
ECCCCCCCC------
28258704

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 RIDA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIDA_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 RIDA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MINT_HUMANSPENphysical
21988832
MDM2_HUMANMDM2physical
21988832
IPSP_HUMANSERPINA5physical
21988832
T176A_HUMANTMEM176Aphysical
21988832
RIDA_HUMANHRSP12physical
25416956
BROX_HUMANBROXphysical
26344197
TPIS_HUMANTPI1physical
26344197
ACOX1_HUMANACOX1physical
28514442
CARM1_HUMANCARM1physical
28514442
UBB_HUMANUBBphysical
28514442
OGA_HUMANMGEA5physical
28514442

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

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Related Literatures of Post-Translational Modification

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