LACTB_MOUSE - dbPTM
LACTB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LACTB_MOUSE
UniProt AC Q9EP89
Protein Name Serine beta-lactamase-like protein LACTB, mitochondrial {ECO:0000305}
Gene Name Lactb {ECO:0000312|MGI:MGI:1933395}
Organism Mus musculus (Mouse).
Sequence Length 551
Subcellular Localization Mitochondrion .
Protein Description Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (By similarity). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (By similarity). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (By similarity). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism. [PubMed: 28329758]
Protein Sequence MYRLLSSVTARAAATAGPAWDGGRRGAHRRPGLPVLGLGWAGGLGLGLGLALGAKLVVGLRGAVPIQSPADPEASGTTELSHEQALSPGSPHTPAPPAARGFSRAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDLPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMVKGTPPPSDQEKELKEKGGKNNEKSDAPKAKVEQDSEARCRSAKPGKKKNDFEQGELYLKEKFENSIESLRLFKNDPLFFKPGSQFLYSTFGYTLLAAIVERASGYKYLDYMQKIFHDLDMLTTVQEENEPVIYNRARFYVYNKKKRLVNTPYVDNSYKWAGGGFLSTVGDLLKFGNAMLYGYQVGQFKNSNENLLPGYLKPETMVMMWTPVPNTEMSWDKEGKYAMAWGVVEKKQTYGSCRKQRHYASHTGGAVGASSVLLVLPEELDSEAVNNKVPPRGIIVSIICNMQSVGLNSTALKIALEFDKDRAD
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
162PhosphorylationETVMRIASISKSLTM
HHHHHHHHHCHHHHH		25.6417208939
164PhosphorylationVMRIASISKSLTMVA
HHHHHHHCHHHHHHH		17.4423140645
165MalonylationMRIASISKSLTMVAL
HHHHHHCHHHHHHHH		48.0626320211
180AcetylationAKLWEAGKLDLDLPV
HHHHHCCCCCCCCCC		45.9723864654
203AcetylationEKEYEGEKVSVTTRL
CHHCCCCEEEHHHHH		51.1423954790
213PhosphorylationVTTRLLISHLSGIRH
HHHHHHHHHHHCCCH		20.5327180971
216PhosphorylationRLLISHLSGIRHYEK
HHHHHHHHCCCHHHH		27.1027180971
223AcetylationSGIRHYEKDIKKVKE
HCCCHHHHHHHHHHH		58.5523864654
226AcetylationRHYEKDIKKVKEEKA
CHHHHHHHHHHHHHH		62.742374471
227AcetylationHYEKDIKKVKEEKAY
HHHHHHHHHHHHHHH		59.892392021
232AcetylationIKKVKEEKAYKALKM
HHHHHHHHHHHHHHH		59.1023864654
238MalonylationEKAYKALKMVKGTPP
HHHHHHHHHHCCCCC		46.6526320211
241SuccinylationYKALKMVKGTPPPSD
HHHHHHHCCCCCCCH		54.2726388266
241MalonylationYKALKMVKGTPPPSD
HHHHHHHCCCCCCCH		54.2726320211
247PhosphorylationVKGTPPPSDQEKELK
HCCCCCCCHHHHHHH		58.6729176673
251MalonylationPPPSDQEKELKEKGG
CCCCHHHHHHHHHCC		63.8126073543
251AcetylationPPPSDQEKELKEKGG
CCCCHHHHHHHHHCC		63.8123201123
263SuccinylationKGGKNNEKSDAPKAK
HCCCCCCCCCCCCHH		56.6223954790
264PhosphorylationGGKNNEKSDAPKAKV
CCCCCCCCCCCCHHH		32.5917208939
270GlutarylationKSDAPKAKVEQDSEA
CCCCCCHHHHHCHHH		53.0524703693
270AcetylationKSDAPKAKVEQDSEA
CCCCCCHHHHHCHHH		53.0523864654
270SuccinylationKSDAPKAKVEQDSEA
CCCCCCHHHHHCHHH		53.0523954790
275PhosphorylationKAKVEQDSEARCRSA
CHHHHHCHHHHHHCC		32.61-
286MalonylationCRSAKPGKKKNDFEQ
HHCCCCCCCCCCHHH		69.9326073543
287AcetylationRSAKPGKKKNDFEQG
HCCCCCCCCCCHHHC		63.8223806337
287SuccinylationRSAKPGKKKNDFEQG
HCCCCCCCCCCHHHC		63.82-
287SuccinylationRSAKPGKKKNDFEQG
HCCCCCCCCCCHHHC		63.8223806337
287MalonylationRSAKPGKKKNDFEQG
HCCCCCCCCCCHHHC		63.8226320211
288SuccinylationSAKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.30-
288SuccinylationSAKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3023806337
288MalonylationSAKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3026320211
288AcetylationSAKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3023806337
288GlutarylationSAKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3024703693
299SuccinylationEQGELYLKEKFENSI
HHCCCHHHHHHHCCH		45.3523954790
301AcetylationGELYLKEKFENSIES
CCCHHHHHHHCCHHH		57.2923576753
301MalonylationGELYLKEKFENSIES
CCCHHHHHHHCCHHH		57.2926320211
305PhosphorylationLKEKFENSIESLRLF
HHHHHHCCHHHHHHH		22.1229176673
308PhosphorylationKFENSIESLRLFKND
HHHCCHHHHHHHCCC		19.6729176673
313SuccinylationIESLRLFKNDPLFFK
HHHHHHHCCCCCCCC		66.1023806337
313AcetylationIESLRLFKNDPLFFK
HHHHHHHCCCCCCCC		66.1023806337
346MalonylationVERASGYKYLDYMQK
HHHHCCCHHHHHHHH		42.7526320211
346AcetylationVERASGYKYLDYMQK
HHHHCCCHHHHHHHH		42.7523864654
383MalonylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.8226320211
383SuccinylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.8223954790
383AcetylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.8223864654
383PhosphoglycerylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.82-
384AcetylationRFYVYNKKKRLVNTP
EEEEEECCCCCCCCC		39.226569467
398AcetylationPYVDNSYKWAGGGFL
CCCCCCCCCCCCCHH		30.3223954790
460AcetylationNTEMSWDKEGKYAMA
CCCCCCCCCCCEEEE		63.2123954790
463AcetylationMSWDKEGKYAMAWGV
CCCCCCCCEEEEEEE		30.8123864654
463MalonylationMSWDKEGKYAMAWGV
CCCCCCCCEEEEEEE		30.8126320211
473MalonylationMAWGVVEKKQTYGSC
EEEEEEECEECCCCH		38.2726320211
547AcetylationKIALEFDKDRAD---
HHHHHHCHHCCC---		55.2023954790
547SuccinylationKIALEFDKDRAD---
HHHHHHCHHCCC---		55.2023954790
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 LACTB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LACTB_MOUSE !!
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 LACTB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LACTB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LACTB_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-463, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-264, ANDMASS SPECTROMETRY.

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