ECHB_MOUSE - dbPTM
ECHB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECHB_MOUSE
UniProt AC Q99JY0
Protein Name Trifunctional enzyme subunit beta, mitochondrial
Gene Name Hadhb
Organism Mus musculus (Mouse).
Sequence Length 475
Subcellular Localization Mitochondrion. Mitochondrion inner membrane. Mitochondrion outer membrane. Endoplasmic reticulum.
Protein Description
Protein Sequence MTTILTSTFRNLSTTSKWALRSSIRPLSCSSQLHSAPAVQTKSKKTLAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYPK
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
49AcetylationKSKKTLAKPNMKNIV
CCCCCCCCCCCCCEE		39.7823864654
53AcetylationTLAKPNMKNIVVVEG
CCCCCCCCCEEEEEC		50.6023806337
53SuccinylationTLAKPNMKNIVVVEG
CCCCCCCCCEEEEEC		50.6023806337
53SuccinylationTLAKPNMKNIVVVEG
CCCCCCCCCEEEEEC		50.60-
68PhosphorylationVRIPFLLSGTSYKDL
CEECEECCCCCHHHC		42.0230352176
70PhosphorylationIPFLLSGTSYKDLMP
ECEECCCCCHHHCCH		26.0523737553
71PhosphorylationPFLLSGTSYKDLMPH
CEECCCCCHHHCCHH		33.4423737553
72PhosphorylationFLLSGTSYKDLMPHD
EECCCCCHHHCCHHH		14.3621183079
73SuccinylationLLSGTSYKDLMPHDL
ECCCCCHHHCCHHHH		44.12-
73UbiquitinationLLSGTSYKDLMPHDL
ECCCCCHHHCCHHHH		44.12-
73SuccinylationLLSGTSYKDLMPHDL
ECCCCCHHHCCHHHH		44.1223806337
73AcetylationLLSGTSYKDLMPHDL
ECCCCCHHHCCHHHH		44.1223576753
73GlutarylationLLSGTSYKDLMPHDL
ECCCCCHHHCCHHHH		44.1224703693
86PhosphorylationDLARAALSGLLHRTN
HHHHHHHHHHHHHCC		23.7522817900
96SuccinylationLHRTNIPKDVVDYII
HHHCCCCHHHHHHHH		60.4026388266
96AcetylationLHRTNIPKDVVDYII
HHHCCCCHHHHHHHH		60.4023954790
127PhosphorylationAALGAGFSDKTPAHT
HHHCCCCCCCCCCCE		36.9626525534
129AcetylationLGAGFSDKTPAHTVT
HCCCCCCCCCCCEEE		56.0323864654
182AcetylationRHSRNMRKMMLDLNK
CCCHHHHHHHHHHHH		20.2124062335
189GlutarylationKMMLDLNKAKTLGQR
HHHHHHHHHHHHHHH		59.5624703693
189SuccinylationKMMLDLNKAKTLGQR
HHHHHHHHHHHHHHH		59.56-
189SuccinylationKMMLDLNKAKTLGQR
HHHHHHHHHHHHHHH		59.5623806337
189AcetylationKMMLDLNKAKTLGQR
HHHHHHHHHHHHHHH		59.5623576753
189MalonylationKMMLDLNKAKTLGQR
HHHHHHHHHHHHHHH		59.5626320211
191GlutarylationMLDLNKAKTLGQRLS
HHHHHHHHHHHHHHH		45.9824703693
191SuccinylationMLDLNKAKTLGQRLS
HHHHHHHHHHHHHHH		45.9823806337
191MalonylationMLDLNKAKTLGQRLS
HHHHHHHHHHHHHHH		45.9826320211
191AcetylationMLDLNKAKTLGQRLS
HHHHHHHHHHHHHHH		45.9823864654
191SuccinylationMLDLNKAKTLGQRLS
HHHHHHHHHHHHHHH		45.98-
198PhosphorylationKTLGQRLSLLSKFRL
HHHHHHHHHHHHHCH		29.4722817900
201PhosphorylationGQRLSLLSKFRLNFL
HHHHHHHHHHCHHCC		34.7321183079
202SuccinylationQRLSLLSKFRLNFLS
HHHHHHHHHCHHCCC		34.18-
202MalonylationQRLSLLSKFRLNFLS
HHHHHHHHHCHHCCC		34.1826320211
202UbiquitinationQRLSLLSKFRLNFLS
HHHHHHHHHCHHCCC		34.18-
202AcetylationQRLSLLSKFRLNFLS
HHHHHHHHHCHHCCC		34.1823864654
251PhosphorylationEYALRSHSLAKKAQD
HHHHHHHHHHHHHCC		31.1327149854
254AcetylationLRSHSLAKKAQDEGH
HHHHHHHHHHCCCCC		54.6723864654
263PhosphorylationAQDEGHLSDIVPFKV
HCCCCCHHHCCCEEC		21.4426525534
269AcetylationLSDIVPFKVPGKDTV
HHHCCCEECCCCCCC		41.2624062335
269SuccinylationLSDIVPFKVPGKDTV
HHHCCCEECCCCCCC		41.2623954790
273MalonylationVPFKVPGKDTVTKDN
CCEECCCCCCCCCCC		44.1226320211
273AcetylationVPFKVPGKDTVTKDN
CCEECCCCCCCCCCC		44.1223864654
273SuccinylationVPFKVPGKDTVTKDN
CCEECCCCCCCCCCC		44.1223806337
273SuccinylationVPFKVPGKDTVTKDN
CCEECCCCCCCCCCC		44.12-
273GlutarylationVPFKVPGKDTVTKDN
CCEECCCCCCCCCCC		44.1224703693
278MalonylationPGKDTVTKDNGIRPS
CCCCCCCCCCCCCCC		44.8826320211
278GlutarylationPGKDTVTKDNGIRPS
CCCCCCCCCCCCCCC		44.8824703693
278SuccinylationPGKDTVTKDNGIRPS
CCCCCCCCCCCCCCC		44.8823806337
278AcetylationPGKDTVTKDNGIRPS
CCCCCCCCCCCCCCC		44.8823864654
285PhosphorylationKDNGIRPSSLEQMAK
CCCCCCCCHHHHHHH		37.3928066266
286PhosphorylationDNGIRPSSLEQMAKL
CCCCCCCHHHHHHHH		38.3128066266
292AcetylationSSLEQMAKLKPAFIK
CHHHHHHHHCCCCCC		52.2623806337
292SuccinylationSSLEQMAKLKPAFIK
CHHHHHHHHCCCCCC		52.2623806337
292SuccinylationSSLEQMAKLKPAFIK
CHHHHHHHHCCCCCC		52.26-
294SuccinylationLEQMAKLKPAFIKPY
HHHHHHHCCCCCCCC		33.3323806337
294AcetylationLEQMAKLKPAFIKPY
HHHHHHHCCCCCCCC		33.3323576753
294SuccinylationLEQMAKLKPAFIKPY
HHHHHHHCCCCCCCC		33.33-
299AcetylationKLKPAFIKPYGTVTA
HHCCCCCCCCCEEEE		26.2323576753
299SuccinylationKLKPAFIKPYGTVTA
HHCCCCCCCCCEEEE		26.2323806337
333SuccinylationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.0223806337
333UbiquitinationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.0227667366
333SuccinylationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.02-
333MalonylationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.0226320211
333GlutarylationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.0224703693
333AcetylationRALAMGYKPKAYLRD
HHHHCCCCCCHHHCC		34.0223576753
335AcetylationLAMGYKPKAYLRDFI
HHCCCCCCHHHCCEE		45.5723864654
335SuccinylationLAMGYKPKAYLRDFI
HHCCCCCCHHHCCEE		45.5723954790
349SuccinylationIYVSQDPKDQLLLGP
EEECCCCCCCEECCC		67.4126388266
349AcetylationIYVSQDPKDQLLLGP
EEECCCCCCCEECCC		67.4123576753
362UbiquitinationGPTYATPKVLEKAGL
CCCCCCHHHHHHCCC		55.91-
362GlutarylationGPTYATPKVLEKAGL
CCCCCCHHHHHHCCC		55.9124703693
362AcetylationGPTYATPKVLEKAGL
CCCCCCHHHHHHCCC		55.9123576753
412PhosphorylationGRKTKVGSPPLEKFN
CCCCCCCCCCHHHCC		26.7427180971
417AcetylationVGSPPLEKFNIWGGS
CCCCCHHHCCCCCCC		51.9323864654
436S-palmitoylationHPFGATGCRLVMAAA
CCCCHHHHHHHHHHH		2.3628526873
436S-nitrosocysteineHPFGATGCRLVMAAA
CCCCHHHHHHHHHHH		2.36-
436S-nitrosylationHPFGATGCRLVMAAA
CCCCHHHHHHHHHHH		2.3621278135
448AcetylationAAANRLRKDGGQYAL
HHHHHHHHCCCCEEH		66.3724062335
448SuccinylationAAANRLRKDGGQYAL
HHHHHHHHCCCCEEH		66.3726388266
459S-nitrosocysteineQYALVAACAAGGQGH
CEEHHHHHHCCCCCE		1.60-
459S-nitrosylationQYALVAACAAGGQGH
CEEHHHHHHCCCCCE		1.6021278135
475AcetylationMIVEAYPK-------
EEEEECCC-------		61.3623864654
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 ECHB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
202KAcetylation

-
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 ECHB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ECHB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECHB_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202 AND LYS-349, AND MASSSPECTROMETRY.

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