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Protein Page:
BCAT2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BCAT2 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. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. Homodimer. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transferase; Amino Acid Metabolism - valine, leucine and isoleucine biosynthesis; EC 2.6.1.42; Cofactor and Vitamin Metabolism - pantothenate and CoA biosynthesis; Amino Acid Metabolism - valine, leucine and isoleucine degradation; Mitochondrial
Cellular Component: mitochondrion; mitochondrial matrix
Molecular Function: branched-chain-amino-acid transaminase activity
Biological Process: valine metabolic process; branched chain family amino acid catabolic process; leucine metabolic process; branched chain family amino acid biosynthetic process; isoleucine catabolic process
Reference #:  O15382 (UniProtKB)
Alt. Names/Synonyms: BCAM; BCAT(m); BCAT2; BCATM; BCT2; branched chain aminotransferase 2, mitochondrial; branched-chain amino acid aminotransferase; Branched-chain-amino-acid aminotransferase, mitochondrial; ECA40; Placental protein 18; PP18
Gene Symbols: BCAT2
Molecular weight: 44,288 Da
Basal Isoelectric point: 8.88  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BCAT2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 K44-ac LQLEMTQkPHKKPGP
0 1 K44-m3 LQLEMTQkPHKKPGP
0 1 K73-ac LMVEWNDkGWGQPRI
0 1 K141 LCLPSFDKLELLECI
0 8 Y228-p WVGGVGNykLGGNYG
0 2 K229-ac VGGVGNykLGGNYGP
0 1 K229-ub VGGVGNykLGGNYGP
0 50 K246-ac LVQQEALkRGCEQVL
0 1 K246-ub LVQQEALkRGCEQVL
0 1 K246-sc LVQQEALkRGCEQVL
0 1 K321-ac VERTITMkQLLRALE
0 1 K321-ub VERTITMkQLLRALE
0 1 K321-sc VERTITMkQLLRALE
0 1 K353-ac PVHRILYkDRNLHIP
0 6 K377-ac LRFQKELkEIQYGIR
0 1 K377-sc LRFQKELkEIQYGIR
  mouse

 
K43 DLQIQMTKEPQKKPA
K43 DLQIQMTKEPQKKPA
K73 LMVEWNNKAGWGPPR
K142-ac LCLPDFDkQELLECI
C229 WIGGVGDCKLGGNYG
K230 IGGVGDCKLGGNYGP
K230 IGGVGDCKLGGNYGP
K247 AVQREAQKRGCEQVL
K247 AVQREAQKRGCEQVL
K247 AVQREAQKRGCEQVL
K322 AERKVTMKELKRALE
K322 AERKVTMKELKRALE
K322 AERKVTMKELKRALE
E354 PVHQILYEGKQLHIP
K378 LRFQKELKAIQYGAS
K378 LRFQKELKAIQYGAS
  rat

 
R43 DLQVQVTREPQKKPA
R43 DLQVQVTREPQKKPA
K73 LMVEWNSKTGWGPPR
K142 LCLPDFDKQELLECI
C229 WIGGVGDCKLGGNYG
K230 IGGVGDCKLGGNYGP
K230 IGGVGDCKLGGNYGP
K247 AVQQEAQKKGCEQVL
K247 AVQQEAQKKGCEQVL
K247 AVQQEAQKKGCEQVL
K322 AERKVTMKELKRALE
K322 AERKVTMKELKRALE
K322 AERKVTMKELKRALE
E354 PVHQILYEGKQLHIP
K378 LRFQKELKAIQYGTS
K378 LRFQKELKAIQYGTS
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