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Protein Page:
BCAT1 (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
BCAT1 Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.6.1.42; Transferase; Cofactor and Vitamin Metabolism - pantothenate and CoA biosynthesis; Amino Acid Metabolism - valine, leucine and isoleucine degradation; Amino Acid Metabolism - valine, leucine and isoleucine biosynthesis
Cellular Component: mitochondrion; cytosol
Molecular Function: identical protein binding; branched-chain-amino-acid transaminase activity
Biological Process: cell proliferation; branched chain family amino acid catabolic process; G1/S transition of mitotic cell cycle; branched chain family amino acid biosynthetic process
Reference #:  P54687 (UniProtKB)
Alt. Names/Synonyms: BCAT(c); BCAT1; BCT1; branched chain aminotransferase 1, cytosolic; Branched-chain-amino-acid aminotransferase, cytosolic; DKFZp686E12175; ECA39; MECA39; placental protein 18; PNAS-121; PP18; Protein ECA39
Gene Symbols: BCAT1
Molecular weight: 42,966 Da
Basal Isoelectric point: 5.17  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BCAT1

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

► Hide Isoforms
 
0 1 S5 ___MKDCSNGCsAEC
0 3 S9-p KDCSNGCsAECtGEG
0 2 T13-p NGCsAECtGEGGskE
0 2 S18-p ECtGEGGskEVVGTF
0 4 K19-ub CtGEGGskEVVGTFK
0 4 K28-ub VVGTFKAkDLIVTPA
0 1 Y90-p PGSSALHyAVELFEG
0 2 D118 FQPNLNMDRMYRSAV
0 1 K134-ac ATLPVFDkEELLECI
0 1 K134-ub ATLPVFDkEELLECI
0 1 K215 PKYVRAWKGGTGDCK
0 1 S331-p RVREMFGsGtACVVC
0 1 T333-p REMFGsGtACVVCPV
0 1 S341-p ACVVCPVsDILyKGE
0 1 Y345-p CPVsDILyKGETIHI
0 1 K360 PTMENGPKLASRILS
0 1 K368 LASRILSKLTDIQYG
  BCAT1 iso5  
S17-p ALARQDCsNGCsAEC
S21-p QDCsNGCsAECtGEG
T25-p NGCsAECtGEGGsKE
S30-p ECtGEGGsKEVVGTF
K31 CtGEGGsKEVVGTFK
K40 VVGTFKAKDLIVTPA
Y102 PGSSALHYAVELFEG
D130 FQPNLNMDRMYRSAV
K146 ATLPVFDKEELLECI
K146 ATLPVFDKEELLECI
K227 PKYVRAWKGGTGDCK
S343 RVREMFGSGTACVVC
T345 REMFGSGTACVVCPV
S353 ACVVCPVSDILYKGE
Y357 CPVSDILYKGETIHI
K372 PTMENGPKLASRILS
K380 LASRILSKLTDIQYG
  mouse

 
S5 ___MKDCSNGCsAPF
S9-p KDCSNGCsAPFAGER
A13 NGCsAPFAGERGSEE
S18 PFAGERGSEEVAETF
E19 FAGERGSEEVAETFR
K28-ub VAETFRAkDLIITPA
Y90 PAASVLHYAVELFEG
D118 FRPDLNMDRMCRSAV
K134 TTLPMFDKEELLKCI
K134 TTLPMFDKEELLKCI
K215 PKYIRAWKGGTGDCK
S331 RVKEMFGSGTACVVC
T333 KEMFGSGTACVVCPV
S341 ACVVCPVSDILYKGQ
Y345 CPVSDILYKGQMLHI
K360-ub PTMENGPkLASRILG
K368-ub LASRILGkLTDIQYG
  rat

 
S17 TLARQDCSNGCSASY
S21 QDCSNGCSASYAEEE
A25 NGCSASYAEEEELEA
S43 SYDEEGGSEASTQTF
E44 YDEEGGSEASTQTFR
K53 STQTFRAKDLIITKA
Y115 PAASVLHYAVELFEG
K143-ub FRPDLNMkRMCRSAV
K159 TTLPEFDKEELLQCV
K159 TTLPEFDKEELLQCV
K240-ub PKFVRSWkGGTGDFK
S356 RVKEMFGSGTACVVC
T358 KEMFGSGTACVVCPV
A366 ACVVCPVASILYKGQ
Y370 CPVASILYKGQMLHI
K385 PTMENGHKLSSRIMA
K393 LSSRIMAKLTDIQYG
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