PCCA_HUMAN - dbPTM
PCCA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCCA_HUMAN
UniProt AC P05165
Protein Name Propionyl-CoA carboxylase alpha chain, mitochondrial
Gene Name PCCA
Organism Homo sapiens (Human).
Sequence Length 728
Subcellular Localization Mitochondrion matrix .
Protein Description
Protein Sequence MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE
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
8PhosphorylationMAGFWVGTAPLVAAG
CCCCEEECCCHHHCC		18.58-
28PhosphorylationPPQQLMLSAALRTLK
CHHHHHHHHHHHHHH		9.4928122231
33PhosphorylationMLSAALRTLKHVLYY
HHHHHHHHHHHHHHH		40.8029853039
41PhosphorylationLKHVLYYSRQCLMVS
HHHHHHHHHHHHHHC		11.4329853039
48PhosphorylationSRQCLMVSRNLGSVG
HHHHHHHCCCCCCCC		11.0729853039
65AcetylationPNEKTFDKILVANRG
CCCCCCCEEEEECCH		33.48-
65SuccinylationPNEKTFDKILVANRG
CCCCCCCEEEEECCH		33.48-
65SuccinylationPNEKTFDKILVANRG
CCCCCCCEEEEECCH		33.48-
88AcetylationTCKKMGIKTVAIHSD
HHHHCCCEEEEEECC		31.087306835
89PhosphorylationCKKMGIKTVAIHSDV
HHHCCCEEEEEECCC		17.1623401153
94PhosphorylationIKTVAIHSDVDASSV
CEEEEEECCCCCCCC		32.96-
117PhosphorylationVCVGPAPTSKSYLNM
EEECCCCCCHHHCCH		51.3923401153
119SuccinylationVGPAPTSKSYLNMDA
ECCCCCCHHHCCHHH		45.67-
119SuccinylationVGPAPTSKSYLNMDA
ECCCCCCHHHCCHHH		45.67-
124UbiquitinationTSKSYLNMDAIMEAI
CCHHHCCHHHHHHHH		3.2129967540
143PhosphorylationAQAVHPGYGFLSENK
HHHCCCCCCCCCCCH		14.7828857561
147PhosphorylationHPGYGFLSENKEFAR
CCCCCCCCCCHHHHH		36.5428442448
150AcetylationYGFLSENKEFARCLA
CCCCCCCHHHHHHHH		50.59-
150SuccinylationYGFLSENKEFARCLA
CCCCCCCHHHHHHHH		50.59-
150SuccinylationYGFLSENKEFARCLA
CCCCCCCHHHHHHHH		50.59-
150UbiquitinationYGFLSENKEFARCLA
CCCCCCCHHHHHHHH		50.5929967540
191PhosphorylationAKKAEVNTIPGFDGV
HHHCCCCCCCCCCCC		33.4521406692
200SuccinylationPGFDGVVKDAEEAVR
CCCCCCCCCHHHHHH		49.14-
200AcetylationPGFDGVVKDAEEAVR
CCCCCCCCCHHHHHH		49.14-
200SuccinylationPGFDGVVKDAEEAVR
CCCCCCCCCHHHHHH		49.14-
245PhosphorylationTRDGFRLSSQEAASS
CCCCEEECHHHHHHH		26.2223312004
246PhosphorylationRDGFRLSSQEAASSF
CCCEEECHHHHHHHH		36.3123312004
251PhosphorylationLSSQEAASSFGDDRL
ECHHHHHHHHCCCCC		32.9930108239
252PhosphorylationSSQEAASSFGDDRLL
CHHHHHHHHCCCCCH		28.6430108239
262SuccinylationDDRLLIEKFIDNPRH
CCCCHHHHHCCCCCE		40.40-
262SuccinylationDDRLLIEKFIDNPRH
CCCCHHHHHCCCCCE		40.40-
272UbiquitinationDNPRHIEIQVLGDKH
CCCCEEEEEEEECCC		3.2029967540
273UbiquitinationNPRHIEIQVLGDKHG
CCCEEEEEEEECCCC		16.1621139048
295UbiquitinationRECSIQRRNQKVVEE
HHHHHHHHCHHHHHH		33.2921139048
298UbiquitinationSIQRRNQKVVEEAPS
HHHHHCHHHHHHCCC		52.3729967540
302UbiquitinationRNQKVVEEAPSIFLD
HCHHHHHHCCCEEEC		55.0321139048
328UbiquitinationVALARAVKYSSAGTV
HHHHHHHHHCCCCEE		38.1321139048
328SuccinylationVALARAVKYSSAGTV
HHHHHHHHHCCCCEE		38.1321139048
328SuccinylationVALARAVKYSSAGTV
HHHHHHHHHCCCCEE		38.13-
328AcetylationVALARAVKYSSAGTV
HHHHHHHHHCCCCEE		38.13-
341PhosphorylationTVEFLVDSKKNFYFL
EEEEEEECCCCEEEE		37.74-
342AcetylationVEFLVDSKKNFYFLE
EEEEEECCCCEEEEE		47.4724885163
343AcetylationEFLVDSKKNFYFLEM
EEEEECCCCEEEEEE		57.1330585223
346PhosphorylationVDSKKNFYFLEMNTR
EECCCCEEEEEECCE		19.3521712546
385SuccinylationKGYPLRHKQADIRIN
CCCCCCCCCCEEEEC		40.52-
385SuccinylationKGYPLRHKQADIRIN
CCCCCCCCCCEEEEC		40.52-
401PhosphorylationWAVECRVYAEDPYKS
EEEEEEEEECCCCHH		5.7320736484
406PhosphorylationRVYAEDPYKSFGLPS
EEEECCCCHHCCCCC		31.4220736484
407SuccinylationVYAEDPYKSFGLPSI
EEECCCCHHCCCCCC		44.70-
407SuccinylationVYAEDPYKSFGLPSI
EEECCCCHHCCCCCC		44.70-
464AcetylationSDRTEALKRMADALD
CCHHHHHHHHHHHHH		47.372380475
473PhosphorylationMADALDNYVIRGVTH
HHHHHHHHHHHHHCH		9.27-
492PhosphorylationLREVIINSRFVKGDI
HHHHHHHCCCCCCCC		19.3818187866
496AcetylationIINSRFVKGDISTKF
HHHCCCCCCCCCHHH		48.42-
502SuccinylationVKGDISTKFLSDVYP
CCCCCCHHHHHCCCC		37.20-
502SuccinylationVKGDISTKFLSDVYP
CCCCCCHHHHHCCCC		37.20-
513AcetylationDVYPDGFKGHMLTKS
CCCCCCCCCCCCCHH		54.132380477
513SuccinylationDVYPDGFKGHMLTKS
CCCCCCCCCCCCCHH		54.13-
513SuccinylationDVYPDGFKGHMLTKS
CCCCCCCCCCCCCHH		54.13-
519AcetylationFKGHMLTKSEKNQLL
CCCCCCCHHHHHHHH		53.297672093
520PhosphorylationKGHMLTKSEKNQLLA
CCCCCCHHHHHHHHH		48.87-
547PhosphorylationAQHFQENSRMPVIKP
HHHHHHCCCCCCCCC		29.24-
553AcetylationNSRMPVIKPDIANWE
CCCCCCCCCCCCCEE		36.5520167786
562PhosphorylationDIANWELSVKLHDKV
CCCCEEEEEEEECCE		12.99-
626PhosphorylationREAGGNMSIQFLGTV
HCCCCCCEEEECCCC		19.7620068231
632PhosphorylationMSIQFLGTVYKVNIL
CEEEECCCCHHHHHH		23.8620068231
634PhosphorylationIQFLGTVYKVNILTR
EEECCCCHHHHHHHH		14.7320068231
640PhosphorylationVYKVNILTRLAAELN
CHHHHHHHHHHHHHH		21.6020068231
648SuccinylationRLAAELNKFMLEKVT
HHHHHHHHHHHHHCC		44.79-
648SuccinylationRLAAELNKFMLEKVT
HHHHHHHHHHHHHCC		44.79-
655O-linked_GlycosylationKFMLEKVTEDTSSVL
HHHHHHCCCCCHHHH		38.9331492838
659O-linked_GlycosylationEKVTEDTSSVLRSPM
HHCCCCCHHHHCCCC		30.6731492838
694BiotinylationICVIEAMKMQNSMTA
EEEEEEEEHHCCCCC		44.3620443544
694N6-biotinyllysineICVIEAMKMQNSMTA
EEEEEEEEHHCCCCC		44.36-
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 PCCA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCCA_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 PCCA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCCB_HUMANPCCBphysical
26344197
PCCB_HUMANPCCBphysical
28514442
TTC1_HUMANTTC1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606054Propionic acidemia type I (PA-1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121Biotin
Regulatory Network of PCCA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASSSPECTROMETRY.

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