BCAT2_HUMAN - dbPTM
BCAT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAT2_HUMAN
UniProt AC O15382
Protein Name Branched-chain-amino-acid aminotransferase, mitochondrial
Gene Name BCAT2
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Isoform A: Mitochondrion.
Isoform B: Cytoplasm.
Protein Description 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 MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
14 (in isoform 2)Ubiquitination-3.43-
41SulfoxidationAADLQLEMTQKPHKK
HHHHHHECCCCCCCC		6.9921406390
44TrimethylationLQLEMTQKPHKKPGP
HHHECCCCCCCCCCC		39.67-
44SuccinylationLQLEMTQKPHKKPGP
HHHECCCCCCCCCCC		39.6727452117
44MalonylationLQLEMTQKPHKKPGP
HHHECCCCCCCCCCC		39.6726320211
44AcetylationLQLEMTQKPHKKPGP
HHHECCCCCCCCCCC		39.6723954790
44MethylationLQLEMTQKPHKKPGP
HHHECCCCCCCCCCC		39.6723644510
73AcetylationLMVEWNDKGWGQPRI
EEEEECCCCCCCCCE		54.0423954790
130PhosphorylationNMDRMLRSAMRLCLP
CHHHHHHHHHHHHCC		23.5822210691
135S-nitrosylationLRSAMRLCLPSFDKL
HHHHHHHHCCCCCHH		3.5625040305
137 (in isoform 2)Ubiquitination-31.77-
141AcetylationLCLPSFDKLELLECI
HHCCCCCHHHHHHHH		41.6825825284
154 (in isoform 2)Ubiquitination-9.81-
166PhosphorylationVPDAAGTSLYVRPVL
CCCCCCCEEEEEEEE		19.4524719451
179PhosphorylationVLIGNEPSLGVSQPT
EEECCCCCCCCCCCH		31.4120068231
183PhosphorylationNEPSLGVSQPTRALL
CCCCCCCCCCHHHHH		28.7520068231
186PhosphorylationSLGVSQPTRALLFVI
CCCCCCCHHHHHEEE		22.4220068231
189 (in isoform 2)Ubiquitination-3.2521890473
206 (in isoform 2)Ubiquitination-8.7421890473
228PhosphorylationWVGGVGNYKLGGNYG
HHCCCCCCCCCCCCC		11.14-
229N6-(pyridoxal phosphate)lysineVGGVGNYKLGGNYGP
HCCCCCCCCCCCCCC		44.66-
229OtherVGGVGNYKLGGNYGP
HCCCCCCCCCCCCCC		44.66-
229 (in isoform 1)Ubiquitination-44.6621890473
229AcetylationVGGVGNYKLGGNYGP
HCCCCCCCCCCCCCC		44.6623236377
229UbiquitinationVGGVGNYKLGGNYGP
HCCCCCCCCCCCCCC		44.6621906983
246UbiquitinationLVQQEALKRGCEQVL
HHCHHHHHCCCCEEE		54.5121906983
246AcetylationLVQQEALKRGCEQVL
HHCHHHHHCCCCEEE		54.5125953088
246 (in isoform 1)Ubiquitination-54.5121890473
281 (in isoform 2)Ubiquitination-5.2821890473
285AcetylationDGVLELVTPPLNGVI
CCEEEEECCCCCCCC		31.6419608861
285 (in isoform 2)Ubiquitination-31.64-
3212-HydroxyisobutyrylationVERTITMKQLLRALE
EECCCCHHHHHHHHH		29.19-
321 (in isoform 1)Ubiquitination-29.1921890473
321MalonylationVERTITMKQLLRALE
EECCCCHHHHHHHHH		29.1926320211
321AcetylationVERTITMKQLLRALE
EECCCCHHHHHHHHH		29.1925825284
321UbiquitinationVERTITMKQLLRALE
EECCCCHHHHHHHHH		29.1919608861
342S-nitrosylationVFGSGTACQVCPVHR
EECCCCCCEECCCEE		2.9019483679
342S-nitrosocysteineVFGSGTACQVCPVHR
EECCCCCCEECCCEE		2.90-
345S-nitrosocysteineSGTACQVCPVHRILY
CCCCCEECCCEEEEE		0.89-
345S-nitrosylationSGTACQVCPVHRILY
CCCCCEECCCEEEEE		0.8919483679
353UbiquitinationPVHRILYKDRNLHIP
CCEEEEECCCCCCCC		46.93-
353AcetylationPVHRILYKDRNLHIP
CCEEEEECCCCCCCC		46.937691943
374UbiquitinationELILRFQKELKEIQY
HHHHHHHHHHHHHHH		63.40-
377MalonylationLRFQKELKEIQYGIR
HHHHHHHHHHHHCHH		54.5926320211
377SuccinylationLRFQKELKEIQYGIR
HHHHHHHHHHHHCHH		54.5927452117
377UbiquitinationLRFQKELKEIQYGIR
HHHHHHHHHHHHCHH		54.5919608861
377AcetylationLRFQKELKEIQYGIR
HHHHHHHHHHHHCHH		54.5923954790
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BCAT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAT2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BCAT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCAT2_HUMANBCAT2physical
11264579
A4_HUMANAPPphysical
21832049
PTGDS_HUMANPTGDSphysical
21988832
CREB3_HUMANCREB3physical
21988832
CATA_HUMANCATphysical
26344197
UFM1_HUMANUFM1physical
26344197
CH60_HUMANHSPD1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00167L-Isoleucine
DB00149L-Leucine
Regulatory Network of BCAT2_HUMAN

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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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