LACB2_HUMAN - dbPTM
LACB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LACB2_HUMAN
UniProt AC Q53H82
Protein Name Endoribonuclease LACTB2 {ECO:0000303|PubMed:26826708}
Gene Name LACTB2
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Mitochondrion matrix .
Protein Description Endoribonuclease; cleaves preferentially 3' to purine-pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage product contains a free 3' -OH group. Has no activity with double-stranded RNA or DNA. Required for normal mitochondrial function and cell viability..
Protein Sequence MAAVLQRVERLSNRVVRVLGCNPGPMTLQGTNTYLVGTGPRRILIDTGEPAIPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKLPRNPQREEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTVFEDLYDYMNSLKELLKIKADIIYPGHGPVIHNAEAKIQQYISHRNIREQQILTLFRENFEKSFTVMELVKIIYKNTPENLHEMAKHNLLLHLKKLEKEGKIFSNTDPDKKWKAHL
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
12PhosphorylationLQRVERLSNRVVRVL
HHHHHHHHHCEEEEC		28.8922210691
912-HydroxyisobutyrylationGGIGDICKSINNDTT
CCHHHHHHHCCCCCC		55.49-
91UbiquitinationGGIGDICKSINNDTT
CCHHHHHHHCCCCCC		55.49-
97PhosphorylationCKSINNDTTYCIKKL
HHHCCCCCCEEEEEC		23.0728152594
98PhosphorylationKSINNDTTYCIKKLP
HHCCCCCCEEEEECC		21.1828152594
99PhosphorylationSINNDTTYCIKKLPR
HCCCCCCEEEEECCC		8.3528152594
1022-HydroxyisobutyrylationNDTTYCIKKLPRNPQ
CCCCEEEEECCCCCC		44.70-
102AcetylationNDTTYCIKKLPRNPQ
CCCCEEEEECCCCCC		44.7023954790
102UbiquitinationNDTTYCIKKLPRNPQ
CCCCEEEEECCCCCC		44.7019608861
103UbiquitinationDTTYCIKKLPRNPQR
CCCEEEEECCCCCCC		43.76-
121PhosphorylationIGNGEQQYVYLKDGD
CCCCCEEEEEECCCC		7.2527642862
125UbiquitinationEQQYVYLKDGDVIKT
CEEEEEECCCCEEEE		41.8121906983
131UbiquitinationLKDGDVIKTEGATLR
ECCCCEEEECCCEEE		40.1321906983
141PhosphorylationGATLRVLYTPGHTDD
CCEEEEEECCCCCCC		14.1821406692
142PhosphorylationATLRVLYTPGHTDDH
CEEEEEECCCCCCCC		20.7321406692
146PhosphorylationVLYTPGHTDDHMALL
EEECCCCCCCCHHHH		49.3821406692
162PhosphorylationEEENAIFSGDCILGE
HHHCCEEECCCCCCC		27.8421406692
171PhosphorylationDCILGEGTTVFEDLY
CCCCCCCCCHHHHHH		18.5821406692
172PhosphorylationCILGEGTTVFEDLYD
CCCCCCCCHHHHHHH		33.7721406692
178PhosphorylationTTVFEDLYDYMNSLK
CCHHHHHHHHHHHHH		19.8321406692
180PhosphorylationVFEDLYDYMNSLKEL
HHHHHHHHHHHHHHH		5.6621406692
183PhosphorylationDLYDYMNSLKELLKI
HHHHHHHHHHHHHHH		25.0421406692
191AcetylationLKELLKIKADIIYPG
HHHHHHHCCCEECCC		38.1230589807
191UbiquitinationLKELLKIKADIIYPG
HHHHHHHCCCEECCC		38.12-
1912-HydroxyisobutyrylationLKELLKIKADIIYPG
HHHHHHHCCCEECCC		38.12-
209AcetylationVIHNAEAKIQQYISH
CCCCHHHHHHHHHHC		32.3326051181
213PhosphorylationAEAKIQQYISHRNIR
HHHHHHHHHHCCCCC		6.5028152594
215PhosphorylationAKIQQYISHRNIREQ
HHHHHHHHCCCCCHH		16.0928152594
235PhosphorylationFRENFEKSFTVMELV
HHHCHHHCCCHHHHH		20.96-
247UbiquitinationELVKIIYKNTPENLH
HHHHHHHHCCCCHHH		43.8919608861
247AcetylationELVKIIYKNTPENLH
HHHHHHHHCCCCHHH		43.8923236377
247MalonylationELVKIIYKNTPENLH
HHHHHHHHCCCCHHH		43.8926320211
249PhosphorylationVKIIYKNTPENLHEM
HHHHHHCCCCHHHHH		28.03-
258AcetylationENLHEMAKHNLLLHL
CHHHHHHHHHHHHHH		31.5425825284
266UbiquitinationHNLLLHLKKLEKEGK
HHHHHHHHHHHHCCC		44.56-
2662-HydroxyisobutyrylationHNLLLHLKKLEKEGK
HHHHHHHHHHHHCCC		44.56-
267AcetylationNLLLHLKKLEKEGKI
HHHHHHHHHHHCCCC		69.1420167786
273AcetylationKKLEKEGKIFSNTDP
HHHHHCCCCCCCCCC		41.49130447
273SuccinylationKKLEKEGKIFSNTDP
HHHHHCCCCCCCCCC		41.49-
273SuccinylationKKLEKEGKIFSNTDP
HHHHHCCCCCCCCCC		41.49-
2822-HydroxyisobutyrylationFSNTDPDKKWKAHL-
CCCCCCCCCCHHCC-		66.96-
282AcetylationFSNTDPDKKWKAHL-
CCCCCCCCCCHHCC-		66.96-
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 LACB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LACB2_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 LACB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDRG3_HUMANNDRG3physical
22939629
PALM2_HUMANPALM2physical
22939629
P4R3B_HUMANSMEK2physical
22939629
COIL_HUMANCOILphysical
22939629
PO210_HUMANNUP210physical
22939629
SPSY_HUMANSMSphysical
22939629
SSU72_HUMANSSU72physical
22939629
UBE2H_HUMANUBE2Hphysical
22939629
TXNL1_HUMANTXNL1physical
22939629
NAGK_HUMANNAGKphysical
21988832
OGA_HUMANMGEA5physical
26186194
G6PI_HUMANGPIphysical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
OGA_HUMANMGEA5physical
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 LACB2_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-247, AND MASS SPECTROMETRY.

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