CPT1A_MOUSE - dbPTM
CPT1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPT1A_MOUSE
UniProt AC P97742
Protein Name Carnitine O-palmitoyltransferase 1, liver isoform
Gene Name Cpt1a
Organism Mus musculus (Mouse).
Sequence Length 773
Subcellular Localization Mitochondrion outer membrane
Multi-pass membrane protein.
Protein Description Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Plays an important role in triglyceride metabolism..
Protein Sequence MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGIITGVFPASPSSWLIVVVGVISSMHTKVDPSLGMIAKINRTLDTTGRMSSQTKNIVSGVLFGTGLWVAIIMTMRYSLKVLLSYHGWMFAEHGKMSRSTRIWMAMVKVFSGRKPMLYSFQTSLPRLPVPAVKDTVSRYLESVRPLMKEGDFQRMTALAQDFAVNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPIMVNSNYYAMEMLYITPTHIQAARAGNTIHAILLYRRTVDREELKPIRLLGSTIPLCSAQWERLFNTSRIPGEETDTIQHVKDSRHIVVYHRGRYFKVWLYHDGRLLRPRELEQQMQQILDDTSEPQPGEAKLAALTAADRVPWAKCRQTYFARGKNKQSLDAVEKAAFFVTLDESEQGYREEDPEASIDSYAKSLLHGRCFDRWFDKSITFVVFKNSKIGINAEHSWADAPIVGHLWEYVMATDVFQLGYSEDGHCKGDKNPNIPKPTRLQWDIPGECQEVIETSLSSASFLANDVDLHSFPFDTFGKGLIKKCRTSPDAFIQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTTESCNFVLAMMDPTTTAEQRFKLFKIACEKHQHLYRLAMTGAGIDRHLFCLYVVSKYLAVDSPFLKEVLSEPWRLSTSQTPQQQVELFDFEKYPDYVSCGGGFGPVADDGYGVSYIIVGENFIHFHISSKFSSPETDSHRFGKHLRQAMMDIITLFGLTANSKK
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------MAEAHQAVA
------CCCCCCEEE		23.76-
29UbiquitinationRLSHEALKQICLSGL
ECCHHHHHHHHHHCH		44.6722790023
32S-palmitoylationHEALKQICLSGLHSW
HHHHHHHHHHCHHHH		1.9828526873
125PhosphorylationIIMTMRYSLKVLLSY
HHHHHHHHHHHHHHH		16.0224719451
161UbiquitinationVKVFSGRKPMLYSFQ
HHHHCCCCCEEEEEE		38.0022790023
180UbiquitinationRLPVPAVKDTVSRYL
CCCCCCHHHHHHHHH		50.19-
180SuccinylationRLPVPAVKDTVSRYL
CCCCCCHHHHHHHHH		50.1923954790
195AcetylationESVRPLMKEGDFQRM
HHHHHHHHHCCHHHH		67.2523201123
195UbiquitinationESVRPLMKEGDFQRM
HHHHHHHHHCCHHHH		67.2522790023
282Nitrated tyrosineTIHAILLYRRTVDRE
CEEEEEEEECCCCHH		8.46-
282NitrationTIHAILLYRRTVDRE
CEEEEEEEECCCCHH		8.46-
285PhosphorylationAILLYRRTVDREELK
EEEEEECCCCHHHHC		20.1224719451
292AcetylationTVDREELKPIRLLGS
CCCHHHHCCCEECCC		41.5023864654
292UbiquitinationTVDREELKPIRLLGS
CCCHHHHCCCEECCC		41.5022790023
304S-palmitoylationLGSTIPLCSAQWERL
CCCCHHCCHHHHHHH		2.3828526873
329UbiquitinationTDTIQHVKDSRHIVV
CCCCCHHCCCCEEEE		48.1122790023
344MalonylationYHRGRYFKVWLYHDG
EECCCEEEEEEEECC		24.4626073543
348PhosphorylationRYFKVWLYHDGRLLR
CEEEEEEEECCCCCC		5.1125195567
379AcetylationEPQPGEAKLAALTAA
CCCCCHHHHHHHHHH		34.0623954790
393UbiquitinationADRVPWAKCRQTYFA
HHCCCHHHHHHHHHH		26.5322790023
441UbiquitinationASIDSYAKSLLHGRC
CCHHHHHHHHHCCCH		33.1422790023
463UbiquitinationSITFVVFKNSKIGIN
CEEEEEECCCEEEEC		49.0222790023
508MalonylationDGHCKGDKNPNIPKP
CCCCCCCCCCCCCCC		80.9126320211
508AcetylationDGHCKGDKNPNIPKP
CCCCCCCCCCCCCCC		80.9123864654
514UbiquitinationDKNPNIPKPTRLQWD
CCCCCCCCCCEEECC		56.0522790023
580AcetylationALQLAHYKDMGKFCL
HHHHHHHCCHHHHHH		31.2223954790
586S-palmitoylationYKDMGKFCLTYEASM
HCCHHHHHHEHHHHH		2.9428526873
588PhosphorylationDMGKFCLTYEASMTR
CHHHHHHEHHHHHHH		22.09-
589Nitrated tyrosineMGKFCLTYEASMTRL
HHHHHHEHHHHHHHH		9.13-
589NitrationMGKFCLTYEASMTRL
HHHHHHEHHHHHHHH		9.13-
604PhosphorylationFREGRTETVRSCTTE
HHCCCCCCHHHCCCC		22.17-
608S-palmitoylationRTETVRSCTTESCNF
CCCCHHHCCCCCCCE		3.7028526873
613S-palmitoylationRSCTTESCNFVLAMM
HHCCCCCCCEEEEEC		3.5928526873
634AcetylationEQRFKLFKIACEKHQ
HHHHHHHHHHHHHCH		39.5723864654
671PhosphorylationSKYLAVDSPFLKEVL
HHHHCCCCHHHHHHH		15.7929514104
675UbiquitinationAVDSPFLKEVLSEPW
CCCCHHHHHHHCCCC		46.27-
675AcetylationAVDSPFLKEVLSEPW
CCCCHHHHHHHCCCC		46.2723954790
689PhosphorylationWRLSTSQTPQQQVEL
CCCCCCCCCHHHEEE		23.8825338131
741PhosphorylationFHISSKFSSPETDSH
EEEECCCCCCCCCHH		49.04-
747PhosphorylationFSSPETDSHRFGKHL
CCCCCCCHHHHHHHH		24.79-
752AcetylationTDSHRFGKHLRQAMM
CCHHHHHHHHHHHHH		36.4323864654
768PhosphorylationIITLFGLTANSKK--
HHHHHHHHHCCCC--		24.9523140645
771PhosphorylationLFGLTANSKK-----
HHHHHHCCCC-----		39.0823140645
772UbiquitinationFGLTANSKK------
HHHHHCCCC------		63.4122790023
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 CPT1A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPT1A_MOUSE !!
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 CPT1A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL2_MOUSEBcl2physical
9070836
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPT1A_MOUSE

loading...

Related Literatures of Post-Translational Modification

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