LACTB_HUMAN - dbPTM
LACTB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LACTB_HUMAN
UniProt AC P83111
Protein Name Serine beta-lactamase-like protein LACTB, mitochondrial {ECO:0000305}
Gene Name LACTB {ECO:0000312|HGNC:HGNC:16468}
Organism Homo sapiens (Human).
Sequence Length 547
Subcellular Localization Mitochondrion .
Protein Description Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism. [PubMed: 28329758 Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism]
Protein Sequence MYRLMSAVTARAAAPGGLASSCGRRGVHQRAGLPPLGHGWVGGLGLGLGLALGVKLAGGLRGAAPAQSPAAPDPEASPLAEPPQEQSLAPWSPQTPAPPCSRCFARAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDIPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMMKENVAFEQEKEGKSNEKNDFTKFKTEQENEAKCRNSKPGKKKNDFEQGELYLREKFENSIESLRLFKNDPLFFKPGSQFLYSTFGYTLLAAIVERASGCKYLDYMQKIFHDLDMLTTVQEENEPVIYNRARFYVYNKKKRLVNTPYVDNSYKWAGGGFLSTVGDLLKFGNAMLYGYQVGLFKNSNENLLPGYLKPETMVMMWTPVPNTEMSWDKEGKYAMAWGVVERKQTYGSCRKQRHYASHTGGAVGASSVLLVLPEELDTETINNKVPPRGIIVSIICNMQSVGLNSTALKIALEFDKDRSD
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
2Phosphorylation------MYRLMSAVT
------CCHHHHHHH		16.6824043423
6Phosphorylation--MYRLMSAVTARAA
--CCHHHHHHHHHHC		24.9520068231
9PhosphorylationYRLMSAVTARAAAPG
CHHHHHHHHHHCCCC		15.3328258704
20PhosphorylationAAPGGLASSCGRRGV
CCCCCCHHHCCCCCH		31.0724670416
21PhosphorylationAPGGLASSCGRRGVH
CCCCCHHHCCCCCHH		18.2524670416
140PhosphorylationVDGKEVWSEGLGYAD
ECCHHHHCCCCCCCC		27.28-
164PhosphorylationETVMRIASISKSLTM
HHHHHHHHHCHHHHH		25.6419764811
166PhosphorylationVMRIASISKSLTMVA
HHHHHHHCHHHHHHH		17.4424641631
168PhosphorylationRIASISKSLTMVALA
HHHHHCHHHHHHHHH		23.4520860994
170PhosphorylationASISKSLTMVALAKL
HHHCHHHHHHHHHHH		19.3820860994
182UbiquitinationAKLWEAGKLDLDIPV
HHHHHCCCCCCCCCH		45.9729967540
199UbiquitinationYVPEFPEKEYEGEKV
HCCCCCCHHCCCCEE		66.8729967540
201PhosphorylationPEFPEKEYEGEKVSV
CCCCCHHCCCCEEEH		40.06-
2052-HydroxyisobutyrylationEKEYEGEKVSVTTRL
CHHCCCCEEEHHHHH		51.14-
205UbiquitinationEKEYEGEKVSVTTRL
CHHCCCCEEEHHHHH		51.1433845483
207PhosphorylationEYEGEKVSVTTRLLI
HCCCCEEEHHHHHHH		25.4726437602
215PhosphorylationVTTRLLISHLSGIRH
HHHHHHHHHHHCCCH		20.5320068231
218PhosphorylationRLLISHLSGIRHYEK
HHHHHHHHCCCHHHH		27.1024719451
2252-HydroxyisobutyrylationSGIRHYEKDIKKVKE
HCCCHHHHHHHHHHH		58.55-
228AcetylationRHYEKDIKKVKEEKA
CHHHHHHHHHHHHHH		62.742380299
2342-HydroxyisobutyrylationIKKVKEEKAYKALKM
HHHHHHHHHHHHHHH		59.10-
236PhosphorylationKVKEEKAYKALKMMK
HHHHHHHHHHHHHHH		14.0930631047
237TrimethylationVKEEKAYKALKMMKE
HHHHHHHHHHHHHHH		52.69-
237AcetylationVKEEKAYKALKMMKE
HHHHHHHHHHHHHHH		52.697970937
237MethylationVKEEKAYKALKMMKE
HHHHHHHHHHHHHHH		52.69-
2432-HydroxyisobutyrylationYKALKMMKENVAFEQ
HHHHHHHHHHCCCHH		42.51-
243MalonylationYKALKMMKENVAFEQ
HHHHHHHHHHCCCHH		42.5126320211
243SuccinylationYKALKMMKENVAFEQ
HHHHHHHHHHCCCHH		42.5127452117
243AcetylationYKALKMMKENVAFEQ
HHHHHHHHHHCCCHH		42.5125825284
252MalonylationNVAFEQEKEGKSNEK
HCCCHHHHCCCCCCC		72.0326320211
252SuccinylationNVAFEQEKEGKSNEK
HCCCHHHHCCCCCCC		72.0327452117
252AcetylationNVAFEQEKEGKSNEK
HCCCHHHHCCCCCCC		72.0325953088
259SuccinylationKEGKSNEKNDFTKFK
HCCCCCCCCCCCCHH		67.1023954790
259AcetylationKEGKSNEKNDFTKFK
HCCCCCCCCCCCCHH		67.1023749302
264MalonylationNEKNDFTKFKTEQEN
CCCCCCCCHHHHHHH		44.8726320211
264AcetylationNEKNDFTKFKTEQEN
CCCCCCCCHHHHHHH		44.8719608861
266SuccinylationKNDFTKFKTEQENEA
CCCCCCHHHHHHHHH		53.3527452117
266AcetylationKNDFTKFKTEQENEA
CCCCCCHHHHHHHHH		53.3526051181
266MalonylationKNDFTKFKTEQENEA
CCCCCCHHHHHHHHH		53.3526320211
274SuccinylationTEQENEAKCRNSKPG
HHHHHHHHHCCCCCC		27.7827452117
279UbiquitinationEAKCRNSKPGKKKND
HHHHCCCCCCCCCCC		62.4324816145
283MalonylationRNSKPGKKKNDFEQG
CCCCCCCCCCCHHHC		63.8226320211
283SuccinylationRNSKPGKKKNDFEQG
CCCCCCCCCCCHHHC		63.82-
283SuccinylationRNSKPGKKKNDFEQG
CCCCCCCCCCCHHHC		63.8227452117
284SuccinylationNSKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.30-
284SuccinylationNSKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3027452117
284UbiquitinationNSKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3029967540
284MalonylationNSKPGKKKNDFEQGE
CCCCCCCCCCHHHCC		66.3026320211
2972-HydroxyisobutyrylationGELYLREKFENSIES
CCCHHHHHHHCHHHH		52.09-
297AcetylationGELYLREKFENSIES
CCCHHHHHHHCHHHH		52.0923236377
297UbiquitinationGELYLREKFENSIES
CCCHHHHHHHCHHHH		52.0924816145
297MalonylationGELYLREKFENSIES
CCCHHHHHHHCHHHH		52.0926320211
342AcetylationVERASGCKYLDYMQK
HHHHCCCCHHHHHHH		52.9919608861
342MalonylationVERASGCKYLDYMQK
HHHHCCCCHHHHHHH		52.9926320211
343PhosphorylationERASGCKYLDYMQKI
HHHCCCCHHHHHHHH		14.64-
346PhosphorylationSGCKYLDYMQKIFHD
CCCCHHHHHHHHHHC		10.00-
377PhosphorylationNRARFYVYNKKKRLV
ECCEEEEEECCCCCC		15.19-
379MalonylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.8226320211
3792-HydroxyisobutyrylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.82-
379AcetylationARFYVYNKKKRLVNT
CEEEEEECCCCCCCC		41.8219608861
380AcetylationRFYVYNKKKRLVNTP
EEEEEECCCCCCCCC		39.226570433
388PhosphorylationKRLVNTPYVDNSYKW
CCCCCCCCCCCCCCC		20.5620068231
392PhosphorylationNTPYVDNSYKWAGGG
CCCCCCCCCCCCCCC		24.5120068231
392O-linked_GlycosylationNTPYVDNSYKWAGGG
CCCCCCCCCCCCCCC		24.5128510447
393PhosphorylationTPYVDNSYKWAGGGF
CCCCCCCCCCCCCCH		19.4620068231
418PhosphorylationGNAMLYGYQVGLFKN
CCEEECCEEEEEECC		6.1020860994
473PhosphorylationVVERKQTYGSCRKQR
EEECCCCCCCHHCCH		12.44-
475PhosphorylationERKQTYGSCRKQRHY
ECCCCCCCHHCCHHH		10.59-
532PhosphorylationMQSVGLNSTALKIAL
CCCCCCCHHHHHHHH		21.7920833797
543UbiquitinationKIALEFDKDRSD---
HHHHHCCCCCCC---		61.4329967540
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LACTB_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 LACTB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LACTB_HUMANLACTBphysical
27499296
NDKM_HUMANNME4physical
27499296
ECH1_HUMANECH1physical
27499296
PDIP2_HUMANPOLDIP2physical
27499296
PREP_HUMANPITRM1physical
27499296
C1QBP_HUMANC1QBPphysical
27499296
C102A_HUMANCCDC102Aphysical
28514442
COPRS_HUMANCOPRSphysical
28514442
RIOK1_HUMANRIOK1physical
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
There are no disease associations of PTM sites.
Regulatory Network of LACTB_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-264 AND LYS-342, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.

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