CLPX_HUMAN - dbPTM
CLPX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLPX_HUMAN
UniProt AC O76031
Protein Name ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
Gene Name CLPX
Organism Homo sapiens (Human).
Sequence Length 633
Subcellular Localization Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid.
Protein Description ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. [PubMed: 11923310]
Protein Sequence MPSCGACTCGAAAVRLITSSLASAQRGISGGRIHMSVLGRLGTFETQILQRAPLRSFTETPAYFASKDGISKDGSGDGNKKSASEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQIPQEKRGGEVLDSSHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPTKESSEEEYDSGVEEEGWPRQADAANS
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
29PhosphorylationASAQRGISGGRIHMS
HHHHHCCCCCCCCHH		37.7124719451
36PhosphorylationSGGRIHMSVLGRLGT
CCCCCCHHHHCCCCC		10.4624719451
43PhosphorylationSVLGRLGTFETQILQ
HHHCCCCCHHHHHHH		23.9224719451
66PhosphorylationETPAYFASKDGISKD
CCCCEECCCCCCCCC		22.75-
67UbiquitinationTPAYFASKDGISKDG
CCCEECCCCCCCCCC		57.45-
71PhosphorylationFASKDGISKDGSGDG
ECCCCCCCCCCCCCC		30.17-
80UbiquitinationDGSGDGNKKSASEGS
CCCCCCCCCCCCCCC		54.34-
81UbiquitinationGSGDGNKKSASEGSS
CCCCCCCCCCCCCCC		56.08-
89UbiquitinationSASEGSSKKSGSGNS
CCCCCCCCCCCCCCC		53.29-
90UbiquitinationASEGSSKKSGSGNSG
CCCCCCCCCCCCCCC		63.10-
98AcetylationSGSGNSGKGGNQLRC
CCCCCCCCCCCCEEC		64.5620167786
145PhosphorylationSEADSKKSIIKEPES
EHHHHCCCCCCCHHH		33.0324719451
152O-linked_GlycosylationSIIKEPESAAEAVKL
CCCCCHHHHHHHHHH		43.4230379171
178AcetylationKIYNYLDKYVVGQSF
HHHHHHHHHHHCHHH		37.0319608861
179PhosphorylationIYNYLDKYVVGQSFA
HHHHHHHHHHCHHHH		10.4728258704
187MethylationVVGQSFAKKVLSVAV
HHCHHHHHHHHHHHH		41.21-
1872-HydroxyisobutyrylationVVGQSFAKKVLSVAV
HHCHHHHHHHHHHHH		41.21-
217UbiquitinationRQQAEVEKQTSLTPR
HHHHHHHHHCCCCHH		65.14-
220PhosphorylationAEVEKQTSLTPRELE
HHHHHHCCCCHHHHH		27.9623403867
222PhosphorylationVEKQTSLTPRELEIR
HHHHCCCCHHHHHHH		21.77-
239UbiquitinationEDEYRFTKLLQIAGI
HHHHHHHHHHHHCCC		44.48-
269UbiquitinationNQQIPQEKRGGEVLD
HHHCCHHHCCCCCCC		51.61-
270MethylationQQIPQEKRGGEVLDS
HHCCHHHCCCCCCCC		58.56-
277PhosphorylationRGGEVLDSSHDDIKL
CCCCCCCCCCCCCEE		25.9726471730
278PhosphorylationGGEVLDSSHDDIKLE
CCCCCCCCCCCCEEC		30.5126471730
286UbiquitinationHDDIKLEKSNILLLG
CCCCEECCCCEEEEC		60.27-
2862-HydroxyisobutyrylationHDDIKLEKSNILLLG
CCCCEECCCCEEEEC		60.27-
287PhosphorylationDDIKLEKSNILLLGP
CCCEECCCCEEEECC		21.5220068231
295PhosphorylationNILLLGPTGSGKTLL
CEEEECCCCCCHHHH		42.0320068231
297PhosphorylationLLLGPTGSGKTLLAQ
EEECCCCCCHHHHHH		39.3320068231
299UbiquitinationLGPTGSGKTLLAQTL
ECCCCCCHHHHHHHH		37.38-
300PhosphorylationGPTGSGKTLLAQTLA
CCCCCCHHHHHHHHH		30.45-
349UbiquitinationDANYNVEKAQQGIVF
HCCCCHHHHHCCEEE		47.41-
362UbiquitinationVFLDEVDKIGSVPGI
EEEECCCCCCCCCCC		54.89-
373MethylationVPGIHQLRDVGGEGV
CCCCEECCCCCCHHH		29.96-
386UbiquitinationGVQQGLLKLLEGTIV
HHHHHHHHHHCCCEE		56.95-
398UbiquitinationTIVNVPEKNSRKLRG
CEEECCCCCCCHHCC		54.90-
398AcetylationTIVNVPEKNSRKLRG
CEEECCCCCCCHHCC		54.9025953088
407PhosphorylationSRKLRGETVQVDTTN
CCHHCCCEEEECCCC		21.0429978859
412PhosphorylationGETVQVDTTNILFVA
CCEEEECCCCEEEEE		23.9228258704
413PhosphorylationETVQVDTTNILFVAS
CEEEECCCCEEEEEC		18.7928258704
420PhosphorylationTNILFVASGAFNGLD
CCEEEEECCHHCCHH		25.9229978859
437AcetylationISRRKNEKYLGFGTP
HHHCCCCCCCCCCCC		55.9919608861
437UbiquitinationISRRKNEKYLGFGTP
HHHCCCCCCCCCCCC		55.9919608861
438PhosphorylationSRRKNEKYLGFGTPS
HHCCCCCCCCCCCCC		13.0923684312
443PhosphorylationEKYLGFGTPSNLGKG
CCCCCCCCCCCCCCH		22.6816964243
445PhosphorylationYLGFGTPSNLGKGRR
CCCCCCCCCCCCHHH		44.5229396449
449MalonylationGTPSNLGKGRRAAAA
CCCCCCCCHHHHHHH		53.0326320211
449UbiquitinationGTPSNLGKGRRAAAA
CCCCCCCCHHHHHHH		53.03-
475AcetylationTHQDIEEKDRLLRHV
CCCCHHHHHHHHHHH		35.0423749302
512UbiquitinationPLHSLDEKTLVQILT
ECCCCCCCHHHHHHH		46.99-
529PhosphorylationRNAVIPQYQALFSMD
CCCCCHHHHHHHCCC		7.1522817900
548UbiquitinationNVTEDALKAIARLAL
CCCHHHHHHHHHHHH		39.19-
591AcetylationIVCVEVDKEVVEGKK
EEEEEECHHHHCCCC		58.5519828841
597AcetylationDKEVVEGKKEPGYIR
CHHHHCCCCCCCCCC		40.2219828849
607PhosphorylationPGYIRAPTKESSEEE
CCCCCCCCCCCCHHH		46.5928450419
610PhosphorylationIRAPTKESSEEEYDS
CCCCCCCCCHHHHHC		44.6023927012
611PhosphorylationRAPTKESSEEEYDSG
CCCCCCCCHHHHHCC		50.5525159151
615PhosphorylationKESSEEEYDSGVEEE
CCCCHHHHHCCCCCC		20.7730576142
617PhosphorylationSSEEEYDSGVEEEGW
CCHHHHHCCCCCCCC		43.7828355574
633PhosphorylationRQADAANS-------
CCHHHCCC-------		36.5521406692
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 CLPX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLPX_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 CLPX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLPP_HUMANCLPPphysical
11923310
CH10_HUMANHSPE1physical
26344197
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 CLPX_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-178 AND LYS-437, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.

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