Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Branched-chain-amino-acid aminotransferase, mitochondrial  

UniProtKB / Swiss-Prot ID :  BCAT2_HUMAN

Gene Name (Synonyms) : 
BCAT2, BCATM, BCT2, ECA40  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform A: Mitochondrion. Isoform B: Cytoplasm. 

Protein Function :  Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids. 

Protein Sequence MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEW...
Predicted Secondary Structure CCHHHHHHHHCCHHCCEEEEEECCCCCCCCCEEEEEEEEEECCCCCCCCCCCCCCCCCEEECEEEEEEEE...
Protein Variant
LocationDescription
186T -> R (in dbSNP:rs11548193). VAR_048234
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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
44N6-acetyllysineEMTQKPHKK
EECCCCCCC
39.67HPRD
Link
44N6-acetyllysineEMTQKPHKK
EECCCCCCC
39.67Phosphositeplus
Link
186PhosphothreonineVSQPTRALL
CCCCCCCEE
22.42HPRD
Link
229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VGNYKLGGN
CCCCHHHHH
44.66Phosphositeplus
Link
229N6-(pyridoxal phosphate)lysine.VGNYKLGGN
CCCCHHHHH
44.66UniProtKB
Link
246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEALKRGCE
HHHHHCCCE
54.51Phosphositeplus
Link
321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TITMKQLLR
EEEHHHHHH
29.19Phosphositeplus
Link
321N6-acetyllysineTITMKQLLR
EEEHHHHHH
29.19HPRD
Link
321N6-acetyllysineTITMKQLLR
EEEHHHHHH
29.19Phosphositeplus
Link
321N6-acetyllysine.TITMKQLLR
EEEHHHHHH
29.19UniProtKB
Link
342S-nitrosocysteineSGTACQVCP
ECCEEEEEE
2.90dbSNO
Link
345S-nitrosocysteineACQVCPVHR
EEEEEEEEE
0.89dbSNO
Link
377N6-acetyllysineQKELKEIQY
HHHHHHHEE
54.59HPRD
Link
377N6-acetyllysineQKELKEIQY
HHHHHHHEE
54.59Phosphositeplus
Link
377N6-acetyllysine.QKELKEIQY
HHHHHHHEE
54.59UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
BCAT2_HUMANin vitroHPRD:00217HPRD11264579
12269802
SYV_HUMANENSP00000322991STRING
SYLM_HUMANENSP00000322991STRING
ODBA_HUMANENSP00000322991STRING
ODBB_HUMANENSP00000322991STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00167L-Isoleucine
DB00149L-Leucine
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-321 AND LYS-377, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures