CLPB_HUMAN - dbPTM
CLPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLPB_HUMAN
UniProt AC Q9H078
Protein Name Caseinolytic peptidase B protein homolog
Gene Name CLPB
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Mitochondrion .
Protein Description May function as a regulatory ATPase and be related to secretion/protein trafficking process..
Protein Sequence MLGSLVLRRKALAPRLLLRLLRSPTLRGHGGASGRNVTTGSLGEPQWLRVATGGRPGTSPALFSGRGAATGGRQGGRFDTKCLAAATWGRLPGPEETLPGQDSWNGVPSRAGLGMCALAAALVVHCYSKSPSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEDGGQDGASRHITNQWTSALEFRRWLGLPAGVLITREDDFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREGEVMKLLRTSEAKYQEKQRKREAEERRRFPLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDAKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALQLRQEALEMSRNRIAENLGDVQISDKITISKNFKENVIRPILKAHFRRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVEDSDKQLLKSPELPSPQAEKRLPKLRLEIIDKDSKTRRLDIRAPLHPEKVCNTI
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
23PhosphorylationLLLRLLRSPTLRGHG
HHHHHHCCCCCCCCC		23.3922167270
25PhosphorylationLRLLRSPTLRGHGGA
HHHHCCCCCCCCCCC		30.2722167270
38PhosphorylationGASGRNVTTGSLGEP
CCCCCCCCCCCCCCC		29.05-
41PhosphorylationGRNVTTGSLGEPQWL
CCCCCCCCCCCCEEE		30.98-
58PhosphorylationATGGRPGTSPALFSG
ECCCCCCCCCCHHCC		33.9325394399
64PhosphorylationGTSPALFSGRGAATG
CCCCCHHCCCCCCCC		28.5624719451
112UbiquitinationNGVPSRAGLGMCALA
CCCCCCHHHHHHHHH		22.96-
134UbiquitinationYSKSPSNKDAALLEA
HCCCCCCHHHHHHHH		53.75-
163 (in isoform 2)Ubiquitination-24.85-
163UbiquitinationEGADVNAKHRLGWTA
CCCCCCHHHHHHHHH		24.85-
240UbiquitinationALEFRRWLGLPAGVL
HHHHHHHHCCCCEEE		4.85-
263PhosphorylationNRLNNRASFKGCTAL
CCCCCCCCCCCCCHH		25.0124719451
283 (in isoform 2)Ubiquitination-41.87-
298SulfoxidationNPLQRNEMGHTPLDY
CCCCCCCCCCCCCCH		5.6428183972
313UbiquitinationAREGEVMKLLRTSEA
HHHHHHHHHHHHHHH		49.93-
313AcetylationAREGEVMKLLRTSEA
HHHHHHHHHHHHHHH		49.9325953088
321AcetylationLLRTSEAKYQEKQRK
HHHHHHHHHHHHHHH		43.3326051181
322PhosphorylationLRTSEAKYQEKQRKR
HHHHHHHHHHHHHHH		29.0224275569
388UbiquitinationGSSGIGKTELAKQTA
CCCCCCHHHHHHHHH		30.90-
392AcetylationIGKTELAKQTAKYMH
CCHHHHHHHHHHHHC		61.8925953088
411 (in isoform 2)Ubiquitination-4.97-
412 (in isoform 2)Ubiquitination-34.62-
426PhosphorylationEVAKFIGSPPGYVGH
HHHHHHCCCCCCCCC		24.0925159151
4412-HydroxyisobutyrylationEEGGQLTKKLKQCPN
CHHCHHHHHHHHCCC		65.78-
441MalonylationEEGGQLTKKLKQCPN
CHHCHHHHHHHHCCC		65.7826320211
441UbiquitinationEEGGQLTKKLKQCPN
CHHCHHHHHHHHCCC		65.78-
530AcetylationENLGDVQISDKITIS
HHHCCCCCCCCEEEC		6.0519608861
538AcetylationSDKITISKNFKENVI
CCCEEECCCHHHHCH		63.6525953088
538UbiquitinationSDKITISKNFKENVI
CCCEEECCCHHHHCH		63.65-
541AcetylationITISKNFKENVIRPI
EEECCCHHHHCHHHH		58.7425953088
544AcetylationSKNFKENVIRPILKA
CCCHHHHCHHHHHHH		4.0519608861
559AcetylationHFRRDEFLGRINEIV
HHCHHHHHHHHHHHH		4.1919608861
559 (in isoform 2)Ubiquitination-4.19-
589AcetylationKELNFWAKRAKQRHN
HHHHHHHHHHHHHCC		43.4119608861
589UbiquitinationKELNFWAKRAKQRHN
HHHHHHHHHHHHHCC		43.4119608861
652PhosphorylationGGCTLRITVEDSDKQ
CCCEEEEEEECHHHH		16.0620068231
656PhosphorylationLRITVEDSDKQLLKS
EEEEEECHHHHHHCC		32.9520068231
658AcetylationITVEDSDKQLLKSPE
EEEECHHHHHHCCCC		46.9627452117
663PhosphorylationSDKQLLKSPELPSPQ
HHHHHHCCCCCCCHH		24.4725159151
668PhosphorylationLKSPELPSPQAEKRL
HCCCCCCCHHHHHHC		42.1221815630
6732-HydroxyisobutyrylationLPSPQAEKRLPKLRL
CCCHHHHHHCCCCCE		63.35-
673UbiquitinationLPSPQAEKRLPKLRL
CCCHHHHHHCCCCCE		63.35-
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 CLPB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLPB_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 CLPB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDFI_HUMANMDFIphysical
19060904
ERC6L_HUMANERCC6Lphysical
26186194
SEN2_HUMANTSEN2physical
26186194
OGA_HUMANMGEA5physical
26186194
TTF2_HUMANTTF2physical
26186194
CLU_HUMANCLUHphysical
28514442
P33MX_HUMANKIAA1191physical
28514442
PHAG1_HUMANPAG1physical
28514442
ARFP1_HUMANARFIP1physical
28514442
SETB1_HUMANSETDB1physical
28514442
TRI11_HUMANTRIM11physical
28514442
IF2M_HUMANMTIF2physical
28514442
MDM2_HUMANMDM2physical
28514442
GTPBA_HUMANGTPBP10physical
28514442
EXOG_HUMANEXOGphysical
28514442
IF5_HUMANEIF5physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
6162713-methylglutaconic aciduria with cataracts, neurologic involvement and neutropenia (MEGCANN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CLPB_HUMAN

loading...

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-589, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory