CACP_HUMAN - dbPTM
CACP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACP_HUMAN
UniProt AC P43155
Protein Name Carnitine O-acetyltransferase
Gene Name CRAT
Organism Homo sapiens (Human).
Sequence Length 626
Subcellular Localization Endoplasmic reticulum . Peroxisome . Mitochondrion inner membrane
Peripheral membrane protein
Matrix side .
Isoform 1: Mitochondrion .
Isoform 2: Peroxisome .
Protein Description Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria..
Protein Sequence MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIEYTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNAARLAHYLEKALLDMRALLQSHPRAKL
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
25PhosphorylationPFSLMKASSRFKAHQ
HHHHCHHHHHHHHCC		19.2722496350
29MethylationMKASSRFKAHQDALP
CHHHHHHHHCCCCCC		43.80-
52AcetylationQSLDHYLKALQPIVS
HHHHHHHHHHHHCCC		39.6325038526
59PhosphorylationKALQPIVSEEEWAHT
HHHHHCCCHHHHHHH		39.76-
93SuccinylationGLERRARKTENWLSE
HHHHHHHHCHHHHHH		60.24-
93SuccinylationGLERRARKTENWLSE
HHHHHHHHCHHHHHH		60.24-
107PhosphorylationEWWLKTAYLQYRQPV
HHHHHHHHHHCCCCE		10.2822817900
110PhosphorylationLKTAYLQYRQPVVIY
HHHHHHHCCCCEEEE		14.5022817900
117PhosphorylationYRQPVVIYSSPGVML
CCCCEEEEECCCEEC		7.4722817900
166AcetylationPVEYLGGKPLCMNQY
CCEECCCEEEHHHHH		32.7725038526
186AcetylationSCRVPGPKQDTVSNF
CCCCCCCCCCCCCCC		67.7223954790
186SuccinylationSCRVPGPKQDTVSNF
CCCCCCCCCCCCCCC		67.7227452117
186MalonylationSCRVPGPKQDTVSNF
CCCCCCCCCCCCCCC		67.7226320211
195AcetylationDTVSNFSKTKKPPTH
CCCCCCCCCCCCCCE		61.2930585313
201PhosphorylationSKTKKPPTHITVVHN
CCCCCCCCEEEEEEE		34.14-
245AcetylationNSSLQTNKEPVGILT
HHCCCCCCCCCEEEC		67.7825038526
245MalonylationNSSLQTNKEPVGILT
HHCCCCCCCCCEEEC		67.7826320211
252PhosphorylationKEPVGILTSNHRNSW
CCCCEEECCCCHHHH		26.0927251275
253PhosphorylationEPVGILTSNHRNSWA
CCCEEECCCCHHHHH		27.4827251275
258PhosphorylationLTSNHRNSWAKAYNT
ECCCCHHHHHHHHHH		28.5027251275
261AcetylationNHRNSWAKAYNTLIK
CCHHHHHHHHHHHHH		45.1819608861
261SuccinylationNHRNSWAKAYNTLIK
CCHHHHHHHHHHHHH		45.1823954790
261SuccinylationNHRNSWAKAYNTLIK
CCHHHHHHHHHHHHH		45.18-
261MalonylationNHRNSWAKAYNTLIK
CCHHHHHHHHHHHHH		45.1826320211
268AcetylationKAYNTLIKDKVNRDS
HHHHHHHHHCCCHHH		55.3919608861
268SuccinylationKAYNTLIKDKVNRDS
HHHHHHHHHCCCHHH		55.3923954790
270AcetylationYNTLIKDKVNRDSVR
HHHHHHHCCCHHHHH		36.0925038526
281AcetylationDSVRSIQKSIFTVCL
HHHHHHHHHHHHHHH		43.8025038526
370PhosphorylationKKPELVRSPLVPLPM
CCCHHCCCCCCCCCC		18.3327251275
379AcetylationLVPLPMPKKLRFNIT
CCCCCCCCCCCCCCC		59.182418805
380UbiquitinationVPLPMPKKLRFNITP
CCCCCCCCCCCCCCH		38.74-
390MalonylationFNITPEIKSDIEKAK
CCCCHHHHHHHHHHH		40.1726320211
390AcetylationFNITPEIKSDIEKAK
CCCCHHHHHHHHHHH		40.1725038526
428PhosphorylationFPKSEKLSPDAFIQM
CCCHHCCCHHHHHHH		31.6224043423
441PhosphorylationQMALQLAYYRIYGQA
HHHHHHHHHHHHCHH		11.2324043423
442PhosphorylationMALQLAYYRIYGQAC
HHHHHHHHHHHCHHH		5.7324043423
454PhosphorylationQACATYESASLRMFH
HHHHCHHHCEEEEHH		16.8524905233
456PhosphorylationCATYESASLRMFHLG
HHCHHHCEEEEHHCC		26.2824905233
467PhosphorylationFHLGRTDTIRSASMD
HHCCCCHHHHHCCCC		20.06-
472PhosphorylationTDTIRSASMDSLTFV
CHHHHHCCCCCEEEE		25.11-
485PhosphorylationFVKAMDDSSVTEHQK
EEEECCCCCCCHHHH		23.5720833797
606PhosphorylationNAARLAHYLEKALLD
HHHHHHHHHHHHHHH		15.79-
609AcetylationRLAHYLEKALLDMRA
HHHHHHHHHHHHHHH		41.5623954790
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 CACP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of CACP_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
DB00583L-Carnitine
Regulatory Network of CACP_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-261 AND LYS-268, AND MASSSPECTROMETRY.

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