CPT2_HUMAN - dbPTM
CPT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPT2_HUMAN
UniProt AC P23786
Protein Name Carnitine O-palmitoyltransferase 2, mitochondrial
Gene Name CPT2
Organism Homo sapiens (Human).
Sequence Length 658
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side.
Protein Description
Protein Sequence MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLIIAKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELTDALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHGQLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLGGFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
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
38PhosphorylationPGQYLQRSIVPTMHY
CCHHHHHHCCCCCCC		18.2520068231
42PhosphorylationLQRSIVPTMHYQDSL
HHHHCCCCCCCCCCC		12.9920068231
45PhosphorylationSIVPTMHYQDSLPRL
HCCCCCCCCCCCCCC		11.8220068231
48PhosphorylationPTMHYQDSLPRLPIP
CCCCCCCCCCCCCCC		25.4220068231
51MethylationHYQDSLPRLPIPKLE
CCCCCCCCCCCCCHH		59.39-
60PhosphorylationPIPKLEDTIRRYLSA
CCCCHHHHHHHHHHH		13.6520068231
69AcetylationRRYLSAQKPLLNDGQ
HHHHHHCCCCCCCCC		37.0320167786
69SuccinylationRRYLSAQKPLLNDGQ
HHHHHHCCCCCCCCC		37.03-
69UbiquitinationRRYLSAQKPLLNDGQ
HHHHHHCCCCCCCCC		37.03-
69SuccinylationRRYLSAQKPLLNDGQ
HHHHHHCCCCCCCCC		37.0323954790
79AcetylationLNDGQFRKTEQFCKS
CCCCCCHHHHHHHHH		58.67-
79SuccinylationLNDGQFRKTEQFCKS
CCCCCCHHHHHHHHH		58.6727452117
85SuccinylationRKTEQFCKSFENGIG
HHHHHHHHHHHCCCC		60.51-
85SuccinylationRKTEQFCKSFENGIG
HHHHHHHHHHHCCCC		60.51-
85AcetylationRKTEQFCKSFENGIG
HHHHHHHHHHHCCCC		60.5125038526
104MalonylationEQLVALDKQNKHTSY
HHHHHHHHCCCCCCC		57.5326320211
126PhosphorylationMYLSARDSVVLNFNP
EEEECCCEEEEECCC		14.4720068231
153PhosphorylationNDQLTRATNMTVSAI
HHHHHHHHHCHHHHH		23.4120860994
156PhosphorylationLTRATNMTVSAIRFL
HHHHHHCHHHHHHHH		17.2424400094
158PhosphorylationRATNMTVSAIRFLKT
HHHHCHHHHHHHHHH		14.6020860994
165PhosphorylationSAIRFLKTLRAGLLE
HHHHHHHHHHHCCCC		24.5122210691
182UbiquitinationVFHLNPAKSDTITFK
EEECCCCCCCCEEHH		50.55-
187PhosphorylationPAKSDTITFKRLIRF
CCCCCCEEHHHHHHH		25.7922210691
1892-HydroxyisobutyrylationKSDTITFKRLIRFVP
CCCCEEHHHHHHHCC		37.33-
197PhosphorylationRLIRFVPSSLSWYGA
HHHHHCCCCCCHHHH		38.3120068231
198PhosphorylationLIRFVPSSLSWYGAY
HHHHCCCCCCHHHHH		21.9820068231
200PhosphorylationRFVPSSLSWYGAYLV
HHCCCCCCHHHHHHH		21.8720068231
202PhosphorylationVPSSLSWYGAYLVNA
CCCCCCHHHHHHHHC		6.6220068231
205PhosphorylationSLSWYGAYLVNAYPL
CCCHHHHHHHHCEEC		13.5620068231
210PhosphorylationGAYLVNAYPLDMSQY
HHHHHHCEECCHHHH		10.1020068231
215PhosphorylationNAYPLDMSQYFRLFN
HCEECCHHHHHHHHC		22.7720068231
217PhosphorylationYPLDMSQYFRLFNST
EECCHHHHHHHHCCC		5.3720068231
223PhosphorylationQYFRLFNSTRLPKPS
HHHHHHCCCCCCCCC		13.9420068231
224PhosphorylationYFRLFNSTRLPKPSR
HHHHHCCCCCCCCCH		37.0120068231
239SuccinylationDELFTDDKARHLLVL
HHCCCCHHHHEEEEE		50.56-
239AcetylationDELFTDDKARHLLVL
HHCCCCHHHHEEEEE		50.5625038526
239SuccinylationDELFTDDKARHLLVL
HHCCCCHHHHEEEEE		50.56-
290PhosphorylationAPEFPLAYLTSENRD
CCCCCHHHHCCCCHH		20.42-
305MalonylationIWAELRQKLMSSGNE
HHHHHHHHHHHCCCH		39.4626320211
305AcetylationIWAELRQKLMSSGNE
HHHHHHHHHHHCCCH		39.4625953088
307SulfoxidationAELRQKLMSSGNEES
HHHHHHHHHCCCHHH		3.7421406390
308PhosphorylationELRQKLMSSGNEESL
HHHHHHHHCCCHHHH		45.5923403867
309PhosphorylationLRQKLMSSGNEESLR
HHHHHHHCCCHHHHH		31.5023403867
320PhosphorylationESLRKVDSAVFCLCL
HHHHHHCHHHHHEEC		29.3526074081
339PhosphorylationIKDLVHLSHNMLHGD
HHHHHHHCCCCCCCC		9.6526074081
348PhosphorylationNMLHGDGTNRWFDKS
CCCCCCCCCCCCCCC		26.7626074081
389AcetylationRFFNEVFKDSTQTPA
HHHHHHHCCCCCCCC		56.8125038526
424AcetylationFELTDALKTGITAAK
EEHHHHHHHCCHHHH		46.5625038526
424SuccinylationFELTDALKTGITAAK
EEHHHHHHHCCHHHH		46.56-
424SuccinylationFELTDALKTGITAAK
EEHHHHHHHCCHHHH		46.56-
439SuccinylationEKFDATMKTLTIDCV
HHHCCCCCEEEEEEE		35.71-
439SuccinylationEKFDATMKTLTIDCV
HHHCCCCCEEEEEEE		35.71-
453SuccinylationVQFQRGGKEFLKKQK
EEECCCCHHHHHHCC		48.3823954790
453AcetylationVQFQRGGKEFLKKQK
EEECCCCHHHHHHCC		48.3826822725
453MalonylationVQFQRGGKEFLKKQK
EEECCCCHHHHHHCC		48.3826320211
490PhosphorylationVATYESCSTAAFKHG
EEEHHHHCCCHHHCC		30.29-
491PhosphorylationATYESCSTAAFKHGR
EEHHHHCCCHHHCCC		26.74-
495AcetylationSCSTAAFKHGRTETI
HHCCCHHHCCCCCCC		40.1826051181
508PhosphorylationTIRPASVYTKRCSEA
CCCCCCCEECCCHHH		12.21-
510SuccinylationRPASVYTKRCSEAFV
CCCCCEECCCHHHHC		33.45-
510SuccinylationRPASVYTKRCSEAFV
CCCCCEECCCHHHHC		33.45-
510AcetylationRPASVYTKRCSEAFV
CCCCCEECCCHHHHC		33.4519608861
510MethylationRPASVYTKRCSEAFV
CCCCCEECCCHHHHC		33.4519608861
513PhosphorylationSVYTKRCSEAFVREP
CCEECCCHHHHCCCC		35.6723312004
537MalonylationQMMVECSKYHGQLTK
HHHHHHHHHHCCCHH		53.5826320211
537AcetylationQMMVECSKYHGQLTK
HHHHHHHHHHCCCHH		53.5819608861
544MalonylationKYHGQLTKEAAMGQG
HHHCCCHHHHHCCCC		54.6826320211
544SuccinylationKYHGQLTKEAAMGQG
HHHCCCHHHHHCCCC		54.6823954790
544SuccinylationKYHGQLTKEAAMGQG
HHHCCCHHHHHCCCC		54.68-
544AcetylationKYHGQLTKEAAMGQG
HHHCCCHHHHHCCCC		54.6823954790
554MethylationAMGQGFDRHLFALRH
HCCCCHHHHHHHHHH		26.58-
655PhosphorylationFDALEGKSIKS----
HHHHCCCCCCC----		46.2128857561
658PhosphorylationLEGKSIKS-------
HCCCCCCC-------		43.7328857561
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 CPT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPT2_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 CPT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G6PI_YEASTPGI1physical
22493507
3HAO_YEASTBNA1physical
22493507
CCHL_HUMANHCCSphysical
26344197
Drug and Disease Associations
Kegg Disease
H00525 Disorders of fatty-acid oxidation, including: Medium-chain (MC) acyl-CoA dehydrogenase (AD) deficien
OMIM Disease
255110Carnitine palmitoyltransferase 2 deficiency late-onset (CPT2D)
600649Carnitine palmitoyltransferase 2 deficiency infantile (CPT2DI)
608836Carnitine palmitoyltransferase 2 deficiency lethal neonatal (CPT2D-LN)
614212Encephalopathy, acute, infection-induced, 4 (IIAE4)
Kegg Drug
D05442 Perhexiline maleate (USAN)
D08340 Perhexiline (INN)
DrugBank
DB00583L-Carnitine
DB01074Perhexiline
Regulatory Network of CPT2_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-510 AND LYS-544, AND MASSSPECTROMETRY.

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