LONP2_HUMAN - dbPTM
LONP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LONP2_HUMAN
UniProt AC Q86WA8
Protein Name Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121}
Gene Name LONP2 {ECO:0000255|HAMAP-Rule:MF_03121}
Organism Homo sapiens (Human).
Sequence Length 852
Subcellular Localization Peroxisome matrix .
Protein Description ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import (By similarity). May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1..
Protein Sequence MSSVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGTSLQSTILGVIPNTPDPASDAQDLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDRLEEFPNTCKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTRKPKQDDDKRVIAIRPIRRITHISGTLEDEDEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDVTEREGCREHILEDEKPESISDTTDLALPPEMPILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNAFGSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDGGFTVKTRPGLLNSKL
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
2Acetylation------MSSVSPIQI
------CCCCCCCCC		39.1722814378
11PhosphorylationVSPIQIPSRLPLLLT
CCCCCCCCCCCEEEE		48.3430243723
68PhosphorylationPNTPDPASDAQDLPP
CCCCCCCCCCCCCCC		38.58-
117UbiquitinationIVQVLKEKPYPIAEV
EEHHHHCCCCCEEEH		48.54-
151PhosphorylationGELSEQFYKYAVQLV
HHHHHHHHHHHHHHH		11.6424719451
153PhosphorylationLSEQFYKYAVQLVEM
HHHHHHHHHHHHHHH		10.7123090842
164PhosphorylationLVEMLDMSVPAVAKL
HHHHHCCCHHHHHHH		25.3123090842
226AcetylationVRQIEGLKLLQKTRK
HHHHHHHHHHHHCCC		58.9925953088
252PhosphorylationIRPIRRITHISGTLE
EEEEEEEEEEECCCC		16.0226434776
255PhosphorylationIRRITHISGTLEDED
EEEEEEEECCCCCCC		20.3726434776
257PhosphorylationRITHISGTLEDEDED
EEEEEECCCCCCCCC		21.8626434776
275AcetylationDDIVMLEKKIRTSSM
CCEEEEEHHHHCCCC		49.9226051181
304AcetylationLKKMPQSMPEYALTR
HHCCCCCCHHHHHHH		2.17-
307PhosphorylationMPQSMPEYALTRNYL
CCCCCHHHHHHHHHH		10.8822817900
323UbiquitinationLMVELPWNKSTTDRL
HHHHCCCCCCCCCCH		26.85-
344PhosphorylationILLDNDHYAMEKLKK
HHHHCCHHHHHHHHH		15.54-
348UbiquitinationNDHYAMEKLKKRVLE
CCHHHHHHHHHHHHH		53.15-
348AcetylationNDHYAMEKLKKRVLE
CCHHHHHHHHHHHHH		53.1523236377
356PhosphorylationLKKRVLEYLAVRQLK
HHHHHHHHHHHHHHH		8.87-
367UbiquitinationRQLKNNLKGPILCFV
HHHHHCCCCCEEEEE		65.84-
387PhosphorylationGKTSVGRSVAKTLGR
CHHHHHHHHHHHHCH		22.09-
416PhosphorylationDIRGHRRTYVGSMPG
HCCCCCCEECCCCCC		23.63-
446AcetylationFLLDEVDKLGKSLQG
EEHHHHHHHCHHCCC		65.4026051181
446UbiquitinationFLLDEVDKLGKSLQG
EEHHHHHHHCHHCCC		65.40-
567UbiquitinationGVRSLDRKLGAICRA
CCCHHHHHHHHHHHH		51.44-
592PhosphorylationKEAKLDRSDVTEREG
CCCCCCHHHCCCCCH		35.7825159151
709AcetylationSWLRSNAKKYQLTNA
HHHHHHCHHCCCCCC		57.1519822255
711PhosphorylationLRSNAKKYQLTNAFG
HHHHCHHCCCCCCCC		14.1918452278
743PhosphorylationAVTKDGPSAGVTIVT
CCCCCCCCCCHHHHH		43.0918767875
754PhosphorylationTIVTCLASLFSGRLV
HHHHHHHHHHCCCCC		19.5918767875
757PhosphorylationTCLASLFSGRLVRSD
HHHHHHHCCCCCCCC		28.4424719451
762AcetylationLFSGRLVRSDVAMTG
HHCCCCCCCCCCCCC		31.56-
806AcetylationIIPRRNEKDLEGIPG
EECCCCCCCCCCCCC		71.7723236377
851AcetylationRPGLLNSKL------
CCCCCCCCC------		58.0825953088
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 LONP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LONP2_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 LONP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LONP2_HUMAN !!
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 LONP2_HUMAN

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Related Literatures of Post-Translational Modification

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