BCAT1_HUMAN - dbPTM
BCAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCAT1_HUMAN
UniProt AC P54687
Protein Name Branched-chain-amino-acid aminotransferase, cytosolic
Gene Name BCAT1
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine..
Protein Sequence MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS
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
1Acetylation-------MKDCSNGC
-------CCCCCCCC		8.1319413330
2Acetylation------MKDCSNGCS
------CCCCCCCCC		68.4025953088
2Ubiquitination------MKDCSNGCS
------CCCCCCCCC		68.40-
3Phosphorylation-----MKDCSNGCSA
-----CCCCCCCCCC		39.5224719451
3 (in isoform 5)Phosphorylation-39.5228355574
9PhosphorylationKDCSNGCSAECTGEG
CCCCCCCCCCCCCCC		28.62-
13PhosphorylationNGCSAECTGEGGSKE
CCCCCCCCCCCCCEE		29.76-
17PhosphorylationAECTGEGGSKEVVGT
CCCCCCCCCEEEEEE		31.10-
17 (in isoform 5)Phosphorylation-31.10-
17 (in isoform 4)Phosphorylation-31.1024719451
18PhosphorylationECTGEGGSKEVVGTF
CCCCCCCCEEEEEEE		36.18-
19UbiquitinationCTGEGGSKEVVGTFK
CCCCCCCEEEEEEEE		58.78-
21PhosphorylationGEGGSKEVVGTFKAK
CCCCCEEEEEEEEEC		5.75-
21 (in isoform 5)Phosphorylation-5.75-
25PhosphorylationSKEVVGTFKAKDLIV
CEEEEEEEEECCEEE		6.27-
26UbiquitinationKEVVGTFKAKDLIVT
EEEEEEEEECCEEEE		55.13-
28UbiquitinationVVGTFKAKDLIVTPA
EEEEEEECCEEEECH		54.37-
30PhosphorylationGTFKAKDLIVTPATI
EEEEECCEEEECHHH		3.15-
90PhosphorylationPGSSALHYAVELFEG
CCCHHHHHHHHHHHH		17.13-
107UbiquitinationAFRGVDNKIRLFQPN
HHCCCCCCCEEECCC		25.41-
117SulfoxidationLFQPNLNMDRMYRSA
EECCCCCHHHHHHHH		3.7821406390
119MethylationQPNLNMDRMYRSAVR
CCCCCHHHHHHHHHH		17.17-
134UbiquitinationATLPVFDKEELLECI
HHCCCCCHHHHHHHH		41.44-
134AcetylationATLPVFDKEELLECI
HHCCCCCHHHHHHHH		41.4424431205
215UbiquitinationPKYVRAWKGGTGDCK
HHHEEECCCCCCCCC		46.61-
222OtherKGGTGDCKMGGNYGS
CCCCCCCCCCCCHHC		45.37-
222N6-(pyridoxal phosphate)lysineKGGTGDCKMGGNYGS
CCCCCCCCCCCCHHC		45.37-
305UbiquitinationAHQWGEFKVSERYLT
HHHHCCCEECEEEEC		40.32-
313SulfoxidationVSERYLTMDDLTTAL
ECEEEECHHHHHHHH		3.3130846556
331PhosphorylationRVREMFGSGTACVVC
HHHHHHCCCCEEEEE		23.00-
333PhosphorylationREMFGSGTACVVCPV
HHHHCCCCEEEEEEH		20.69-
341PhosphorylationACVVCPVSDILYKGE
EEEEEEHHHHEECCC		12.22-
345PhosphorylationCPVSDILYKGETIHI
EEHHHHEECCCEEEC		19.79-
346UbiquitinationPVSDILYKGETIHIP
EHHHHEECCCEEECC		46.99-
360UbiquitinationPTMENGPKLASRILS
CCCCCCHHHHHHHHH		59.07-
368UbiquitinationLASRILSKLTDIQYG
HHHHHHHHHHCCCCC		52.54-
370PhosphorylationSRILSKLTDIQYGRE
HHHHHHHHCCCCCCC		34.49-
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 BCAT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCAT1_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 BCAT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
GDE_HUMANAGLphysical
22863883
T2FA_HUMANGTF2F1physical
22863883
SAP_HUMANPSAPphysical
22863883
GDN_HUMANSERPINE2physical
22863883
SNF8_HUMANSNF8physical
22863883
YETS2_HUMANYEATS2physical
26186194
UBP15_HUMANUSP15physical
26186194
PR14L_HUMANPRR14Lphysical
26186194
FWCH2_HUMANFLYWCH2physical
26186194
IF4G3_HUMANEIF4G3physical
26186194
LRIF1_HUMANLRIF1physical
26186194
2A5D_HUMANPPP2R5Dphysical
26186194
ZNHI2_HUMANZNHIT2physical
26186194
RB3GP_HUMANRAB3GAP1physical
26186194
PER1_HUMANPER1physical
26186194
PJA1_HUMANPJA1physical
26186194
ATX2_HUMANATXN2physical
26186194
TRM44_HUMANTRMT44physical
26186194
ARNT_HUMANARNTphysical
26186194
FBX7_HUMANFBXO7physical
26186194
ARI3B_HUMANARID3Bphysical
26186194
TRIPC_HUMANTRIP12physical
26186194
TRIPC_HUMANTRIP12physical
28514442
ARNT_HUMANARNTphysical
28514442
ATX2_HUMANATXN2physical
28514442
2A5D_HUMANPPP2R5Dphysical
28514442
YETS2_HUMANYEATS2physical
28514442
RB3GP_HUMANRAB3GAP1physical
28514442
FBX7_HUMANFBXO7physical
28514442
ZZZ3_HUMANZZZ3physical
28514442
DMWD_HUMANDMWDphysical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
LRIF1_HUMANLRIF1physical
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
DB00996Gabapentin
DB00167L-Isoleucine
DB00149L-Leucine
DB00161L-Valine
Regulatory Network of BCAT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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