Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial  

UniProtKB / Swiss-Prot ID :  AL4A1_MOUSE

Gene Name (Synonyms) : 
Aldh4a1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Mitochondrion matrix (By similarity). 

Protein Function :  Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). 

Protein Sequence MLPLPSLRRSLLSHAWRGAGLRWKHTSSLKVTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDE...
Predicted Secondary Structure CCCCHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCEEECCE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
43PhosphoserineFSQGSPERD
CCCCCHHHH
18.89Phosphositeplus
Link
92N6-acetyllysineHKVAKFCYA
CEEEEEECC
38.67Phosphositeplus
Link
98N6-acetyllysineCYADKALLN
ECCCHHHHH
32.53Phosphositeplus
Link
98N6-acetyllysineCYADKALLN
ECCCHHHHH
32.53SysPTM
Link
98N6-acetyllysine.CYADKALLN
ECCCHHHHH
32.53UniProtKB
Link
113N6-acetyllysineLAARKEWDL
HHHHHHHHC
59.43Phosphositeplus
Link
113N6-acetyllysineLAARKEWDL
HHHHHHHHC
59.43SysPTM
Link
113N6-acetyllysine.LAARKEWDL
HHHHHHHHC
59.43UniProtKB
Link
279S-nitrosocysteineSEHLCGINF
CCCCCEEEE
5.77dbSNO
Link
357N6-acetyllysineLYVPKSLWP
EEECHHHHH
48.41Phosphositeplus
Link
401N6-acetyllysineARIKKWLEH
HHHHHHHHH
55.42Phosphositeplus
Link
401N6-acetyllysineARIKKWLEH
HHHHHHHHH
55.42SysPTM
Link
401N6-acetyllysine.ARIKKWLEH
HHHHHHHHH
55.42UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98; LYS-113 AND LYS-401, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures