Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Acetyl-coenzyme A synthetase 2-like, mitochondrial  

UniProtKB / Swiss-Prot ID :  ACS2L_HUMAN

Gene Name (Synonyms) : 
ACSS1, ACAS2L, KIAA1846  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion matrix. 

Protein Function :  Important for maintaining normal body temperature during fasting and for energy homeostasis. Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2). 

Protein Sequence MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPALSAQAAREPA...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHCCHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
488V -> M (in dbSNP:rs6050249). VAR_048184
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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
Protein Variant
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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
396N6-acetyllysineRLLLKYGDA
HHHHHCCCC
47.35HPRD
Link-
396N6-acetyllysineRLLLKYGDA
HHHHHCCCC
47.35Phosphositeplus
Link-
396N6-acetyllysine.RLLLKYGDA
HHHHHCCCC
47.35UniProtKB
Link-
642N6-acetyllysineTRSGKVMRR
CCCCCCCHH
33.82Phosphositeplus
Link
642N6-acetyllysine.TRSGKVMRR
CCCCCCCHH
33.82UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
AL3B1_HUMANENSP00000316924STRING
DLDH_HUMANENSP00000316924STRING
ODPX_HUMANENSP00000316924STRING
ACADL_HUMANENSP00000316924STRING
ACYP1_HUMANENSP00000316924STRING
PCCB_HUMANENSP00000316924STRING
ACLY_HUMANENSP00000316924STRING
AL3B2_HUMANENSP00000316924STRING
THIL_HUMANENSP00000316924STRING
ODP2_HUMANENSP00000316924STRING
ODPAT_HUMANENSP00000316924STRING
ODPAT_HUMANENSP00000316924STRING
ODPAT_HUMANENSP00000316924STRING
ACO12_HUMANENSP00000316924STRING
ACYP2_HUMANENSP00000316924STRING
ODPB_HUMANENSP00000316924STRING
ACD10_HUMANENSP00000316924STRING
AL1A3_HUMANENSP00000316924STRING
MMSA_HUMANENSP00000316924STRING
ACACA_HUMANENSP00000316924STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00131Adenosine monophosphate
DB00171Adenosine triphosphate
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Reversible lysine acetylation controls the activity of themitochondrial enzyme acetyl-CoA synthetase 2.";
Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.;
Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006).
Cited for: ACETYLATION AT LYS-642, MUTAGENESIS OF LYS-642, FUNCTION, ENZYMEREGULATION, PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY, ANDSUBCELLULAR LOCATION.
"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-396, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures