ACACA_HUMAN - dbPTM
ACACA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACACA_HUMAN
UniProt AC Q13085
Protein Name Acetyl-CoA carboxylase 1
Gene Name ACACA
Organism Homo sapiens (Human).
Sequence Length 2346
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase..
Protein Sequence MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQVLPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSINPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAERKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLRRLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTEEDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILSTMDSPST
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
1Acetylation-------MDEPSPLA
-------CCCCCCCC		51.9019369195
4 (in isoform 4)Phosphorylation-54.2919845377
5Phosphorylation---MDEPSPLAQPLE
---CCCCCCCCCCCC		30.4223401153
5 (in isoform 4)Phosphorylation-30.42-
8 (in isoform 4)Phosphorylation-16.60-
17PhosphorylationPLELNQHSRFIIGSV
CCCCCCCCCEEEECC		21.0822199227
20 (in isoform 2)Phosphorylation-3.207907095
21 (in isoform 4)Phosphorylation-2.8622817900
22 (in isoform 2)Phosphorylation-19.7220166139
23PhosphorylationHSRFIIGSVSEDNSE
CCCEEEECCCCCCCH		16.4422167270
25PhosphorylationRFIIGSVSEDNSEDE
CEEEECCCCCCCHHH		40.7122167270
29PhosphorylationGSVSEDNSEDEISNL
ECCCCCCCHHHHHHH		59.7619664994
34PhosphorylationDNSEDEISNLVKLDL
CCCHHHHHHHHHHHH		23.2830266825
42 (in isoform 4)Phosphorylation-8.7918691976
45UbiquitinationKLDLLEEKEGSLSPA
HHHHHHHCCCCCCCC		58.98-
48PhosphorylationLLEEKEGSLSPASVG
HHHHCCCCCCCCCCC		27.1130278072
50PhosphorylationEEKEGSLSPASVGSD
HHCCCCCCCCCCCCC		21.8130278072
53PhosphorylationEGSLSPASVGSDTLS
CCCCCCCCCCCCCHH		30.3225159151
56PhosphorylationLSPASVGSDTLSDLG
CCCCCCCCCCHHHCC		25.8525159151
58PhosphorylationPASVGSDTLSDLGIS
CCCCCCCCHHHCCCC		29.8322115753
60PhosphorylationSVGSDTLSDLGISSL
CCCCCCHHHCCCCCC		32.6422115753
65PhosphorylationTLSDLGISSLQDGLA
CHHHCCCCCCCCCEE		24.1720873877
66PhosphorylationLSDLGISSLQDGLAL
HHHCCCCCCCCCEEH		28.2919664994
77PhosphorylationGLALHIRSSMSGLHL
CEEHHHHHHHCHHCH		29.7722167270
78PhosphorylationLALHIRSSMSGLHLV
EEHHHHHHHCHHCHH		13.717907095
80PhosphorylationLHIRSSMSGLHLVKQ
HHHHHHHCHHCHHHC		39.9022167270
86UbiquitinationMSGLHLVKQGRDRKK
HCHHCHHHCCCCCCC		54.09-
96PhosphorylationRDRKKIDSQRDFTVA
CCCCCCCCCCCCEEC		30.509453269
101PhosphorylationIDSQRDFTVASPAEF
CCCCCCCEECCHHHH		21.3229759185
104PhosphorylationQRDFTVASPAEFVTR
CCCCEECCHHHHHHH		21.9525850435
110PhosphorylationASPAEFVTRFGGNKV
CCHHHHHHHCCCCCE		26.1229759185
116UbiquitinationVTRFGGNKVIEKVLI
HHHCCCCCEEEEEEE		48.11-
120UbiquitinationGGNKVIEKVLIANNG
CCCCEEEEEEEECCC		31.08-
132UbiquitinationNNGIAAVKCMRSIRR
CCCCHHHHHHHHHHH		20.00-
141PhosphorylationMRSIRRWSYEMFRNE
HHHHHHHCHHHHCCC		14.9227499020
142PhosphorylationRSIRRWSYEMFRNER
HHHHHHCHHHHCCCC		12.4027499020
198 (in isoform 3)Ubiquitination-51.7121890473
210 (in isoform 3)Ubiquitination-12.9321890473
218 (in isoform 2)Ubiquitination-4.1421890473
230 (in isoform 2)Ubiquitination-6.1021890473
233 (in isoform 3)Ubiquitination-33.0921890473
234PhosphorylationIAFMGPPSQAMWALG
CCEECCHHHHHHHHH		33.4368727001
253 (in isoform 2)Ubiquitination-11.2221890473
2762-HydroxyisobutyrylationWQENDFSKRILNVPQ
CCCCCHHHHHHCCCH		43.37-
276UbiquitinationWQENDFSKRILNVPQ
CCCCCHHHHHHCCCH		43.3721906983
276 (in isoform 1)Ubiquitination-43.3721890473
286PhosphorylationLNVPQELYEKGYVKD
HCCCHHHHHCCCCCC		18.1618083107
288UbiquitinationVPQELYEKGYVKDVD
CCHHHHHCCCCCCCH		41.82-
288UbiquitinationVPQELYEKGYVKDVD
CCHHHHHCCCCCCCH		41.8221139048
288 (in isoform 1)Ubiquitination-41.8221890473
290PhosphorylationQELYEKGYVKDVDDG
HHHHHCCCCCCCHHH		18.52119453
292UbiquitinationLYEKGYVKDVDDGLQ
HHHCCCCCCCHHHHH		43.48-
311UbiquitinationVGYPVMIKASEGGGG
HCCCEEEEECCCCCC		27.9721906983
311 (in isoform 1)Ubiquitination-27.9721890473
313 (in isoform 4)Ubiquitination-31.6021890473
323MalonylationGGGKGIRKVNNADDF
CCCCCCEECCCCCCC		47.6026320211
325 (in isoform 4)Ubiquitination-40.7921890473
344PhosphorylationVQAEVPGSPIFVMRL
HHCCCCCCCEEHHHH		14.5772255733
348 (in isoform 4)Ubiquitination-1.9521890473
386UbiquitinationSVQRRHQKIIEEAPA
HHHHHHHHHHHHCCC		39.25-
410UbiquitinationHMEQCAVKLAKMVGY
HHHHHHHHHHHHHCC		24.97-
417PhosphorylationKLAKMVGYVSAGTVE
HHHHHHCCEECCEEE		4.657601369
423 (in isoform 4)Ubiquitination-4.44-
434PhosphorylationYSQDGSFYFLELNPR
EECCCCEEEEEECCC		14.677601381
442 (in isoform 3)Ubiquitination-7.6421890473
447 (in isoform 4)Ubiquitination-17.14-
462 (in isoform 2)Ubiquitination-3.2221890473
488PhosphorylationGVSPWGDSPIDFEDS
CCCCCCCCCCCCCCC		21.5919060867
520UbiquitinationENPDEGFKPSSGTVQ
CCCCCCCCCCCCCEE		55.64-
520 (in isoform 1)Ubiquitination-55.6421890473
557 (in isoform 4)Ubiquitination-9.2721890473
579UbiquitinationSNMVVALKELSIRGD
HHHHHHHHHHCCCCC		47.04-
582PhosphorylationVVALKELSIRGDFRT
HHHHHHHCCCCCHHH		16.0124719451
610PhosphorylationFQMNRIDTGWLDRLI
CCCCCCCCCHHHHHH		28.0823917254
676PhosphorylationTVDVELIYEGVKYVL
CCCHHHHHCCCEEEE		21.1846157461
734PhosphorylationMKEEVDRYRITIGNK
EHHHCCEEEEEECCE		11.2546157467
737PhosphorylationEVDRYRITIGNKTCV
HCCEEEEEECCEEEE		17.5228258704
747UbiquitinationNKTCVFEKENDPSVM
CEEEEEEECCCCCHH		50.80-
747 (in isoform 3)Ubiquitination-50.8021890473
752PhosphorylationFEKENDPSVMRSPSA
EEECCCCCHHCCCCC		31.2625159151
756PhosphorylationNDPSVMRSPSAGKLI
CCCCHHCCCCCCCEE		12.7125159151
758PhosphorylationPSVMRSPSAGKLIQY
CCHHCCCCCCCEEEE		51.4026270265
767 (in isoform 2)Ubiquitination-4.7021890473
784 (in isoform 4)Ubiquitination-5.70-
786N6-biotinyllysineYAEIEVMKMVMTLTA
EEHHHHHCHHHHHHH		33.25-
786BiotinylationYAEIEVMKMVMTLTA
EEHHHHHCHHHHHHH		33.25-
790PhosphorylationEVMKMVMTLTAVESG
HHHCHHHHHHHHHHC		15.0023663014
792PhosphorylationMKMVMTLTAVESGCI
HCHHHHHHHHHHCCE		21.3523663014
796PhosphorylationMTLTAVESGCIHYVK
HHHHHHHHCCEEEEC		32.1623663014
801PhosphorylationVESGCIHYVKRPGAA
HHHCCEEEECCCCCC		6.4323663014
813S-palmitoylationGAALDPGCVLAKMQL
CCCCCCCCEEEEEEC		2.4929575903
817AcetylationDPGCVLAKMQLDNPS
CCCCEEEEEECCCHH		24.0225953088
817UbiquitinationDPGCVLAKMQLDNPS
CCCCEEEEEECCCHH		24.02-
825UbiquitinationMQLDNPSKVQQAELH
EECCCHHHCCCHHHH		45.3721906983
825 (in isoform 1)Ubiquitination-45.3721890473
833PhosphorylationVQQAELHTGSLPRIQ
CCCHHHHCCCCCCHH		40.8823312004
835PhosphorylationQAELHTGSLPRIQST
CHHHHCCCCCCHHCC		36.0325159151
841PhosphorylationGSLPRIQSTALRGEK
CCCCCHHCCCCCCCH		17.1828857561
854 (in isoform 4)Ubiquitination-14.66-
855PhosphorylationKLHRVFHYVLDNLVN
HHHHHHHHHHHHHHH		7.407332677
862 (in isoform 4)Ubiquitination-30.4121890473
867PhosphorylationLVNVMNGYCLPDPFF
HHHHHCCCCCCCHHH		5.947332689
875PhosphorylationCLPDPFFSSKVKDWV
CCCCHHHCHHHHHHH		29.6324719451
876PhosphorylationLPDPFFSSKVKDWVE
CCCHHHCHHHHHHHH		35.9928060719
879UbiquitinationPFFSSKVKDWVERLM
HHHCHHHHHHHHHHH		50.00-
893PhosphorylationMKTLRDPSLPLLELQ
HHHHCCCCCCHHHHH		47.0863737025
907PhosphorylationQDIMTSVSGRIPPNV
HHHHHHHCCCCCCCH		23.3221712546
916UbiquitinationRIPPNVEKSIKKEMA
CCCCCHHHHHHHHHH		53.88-
977PhosphorylationQLVQRYRSGIRGHMK
HHHHHHHHCCCHHHH		29.6368718317
994PhosphorylationVMDLLRQYLRVETQF
HHHHHHHHHHHHHHC		7.0523312004
1023PhosphorylationENKSDMNTVLNYIFS
CCCHHHHHHHHHHHH		21.5222468782
1042PhosphorylationTKKNLLVTMLIDQLC
CCHHHHHHHHHHHHC		13.2620068231
1073PhosphorylationLTQLSKTTNAKVALR
HHHHCCCCCHHHHHH		36.5946157455
1076UbiquitinationLSKTTNAKVALRARQ
HCCCCCHHHHHHHHH		30.06-
1196PhosphorylationPNRGNIPTLNRMSFS
CCCCCCCCCCCEECC		32.6330576142
1201PhosphorylationIPTLNRMSFSSNLNH
CCCCCCEECCCCCCC		20.817907095
1203PhosphorylationTLNRMSFSSNLNHYG
CCCCEECCCCCCCCC		15.8323898821
1204PhosphorylationLNRMSFSSNLNHYGM
CCCEECCCCCCCCCC		43.2423898821
1209PhosphorylationFSSNLNHYGMTHVAS
CCCCCCCCCCEEEEE		13.9119276368
1212PhosphorylationNLNHYGMTHVASVSD
CCCCCCCEEEEEHHH		14.6126074081
1216PhosphorylationYGMTHVASVSDVLLD
CCCEEEEEHHHHHHC		22.5127422710
1218PhosphorylationMTHVASVSDVLLDNS
CEEEEEHHHHHHCCC		21.3626074081
1225PhosphorylationSDVLLDNSFTPPCQR
HHHHHCCCCCCCCHH		30.1126074081
1227PhosphorylationVLLDNSFTPPCQRMG
HHHCCCCCCCCHHCC		26.589453341
1238PhosphorylationQRMGGMVSFRTFEDF
HHCCCEEEEECHHHH		10.507907095
1238 (in isoform 3)Ubiquitination-10.5021890473
1257PhosphorylationDEVMGCFSDSPPQSP
HHHHCCCCCCCCCCC		41.0522167270
1258 (in isoform 2)Ubiquitination-44.9321890473
1259PhosphorylationVMGCFSDSPPQSPTF
HHCCCCCCCCCCCCC		36.9626503892
1263PhosphorylationFSDSPPQSPTFPEAG
CCCCCCCCCCCCCCC		31.5122167270
1265PhosphorylationDSPPQSPTFPEAGHT
CCCCCCCCCCCCCCC		58.0023927012
1272PhosphorylationTFPEAGHTSLYDEDK
CCCCCCCCCCCCCCC		21.3623927012
1273PhosphorylationFPEAGHTSLYDEDKV
CCCCCCCCCCCCCCC		21.1823927012
1275PhosphorylationEAGHTSLYDEDKVPR
CCCCCCCCCCCCCCC		19.6323927012
1316UbiquitinationREFTQQNKATLVDHG
HHHHHHCHHHHHHHH		38.1121906983
1316 (in isoform 1)Ubiquitination-38.1121890473
1334AcetylationLTFLVAQKDFRKQVN
HEEEEECHHHHHHCC		49.4419608861
1334MalonylationLTFLVAQKDFRKQVN
HEEEEECHHHHHHCC		49.4426320211
1334UbiquitinationLTFLVAQKDFRKQVN
HEEEEECHHHHHHCC		49.4419608861
1338UbiquitinationVAQKDFRKQVNYEVD
EECHHHHHHCCHHHH		59.60-
1342PhosphorylationDFRKQVNYEVDRRFH
HHHHHCCHHHHHHHH		20.6245553623
1353 (in isoform 4)Ubiquitination-28.0021890473
1354UbiquitinationRFHREFPKFFTFRAR
HHHHHCCCCEEEECC		59.43-
1357 (in isoform 3)Ubiquitination-18.4921890473
1370PhosphorylationKFEEDRIYRHLEPAL
CCCHHHHHHHHHHHH		7.9023917254
1371 (in isoform 4)Ubiquitination-26.08-
1375 (in isoform 4)Ubiquitination-38.64-
1377 (in isoform 2)Ubiquitination-7.7921890473
1414PhosphorylationAAKVEVGTEVTDYRF
CEEEECCCCCCCHHH		32.2420860994
1417PhosphorylationVEVGTEVTDYRFFVR
EECCCCCCCHHHHHH		22.5320860994
1435UbiquitinationRHSDLVTKEASFEYL
HCCCCCCHHHHHHHH		43.7521906983
1435 (in isoform 1)Ubiquitination-43.7521890473
1438PhosphorylationDLVTKEASFEYLQNE
CCCCHHHHHHHHHHH		21.5020068231
1441PhosphorylationTKEASFEYLQNEGER
CHHHHHHHHHHHHHH		16.1620068231
1468PhosphorylationFNNTNVRTDCNHIFL
HCCCCCCCCCCCCCC		40.3929255136
1472 (in isoform 4)Ubiquitination-20.6421890473
1480PhosphorylationIFLNFVPTVIMDPSK
CCCCCCCEEECCHHH		19.8429255136
1486PhosphorylationPTVIMDPSKIEESVR
CEEECCHHHHHHHHH		41.8429255136
1494PhosphorylationKIEESVRSMVMRYGS
HHHHHHHHHHHHHHH		17.3626074081
1499PhosphorylationVRSMVMRYGSRLWKL
HHHHHHHHHHHHHHH		11.0126074081
1501PhosphorylationSMVMRYGSRLWKLRV
HHHHHHHHHHHHHEE		18.4426074081
1524UbiquitinationIRLTPTGKAIPIRLF
EEECCCCCEEEEEEE		45.69-
1545PhosphorylationYYLDISLYKEVTDSR
EEEEEEEEEECCCCC		9.79-
1561 (in isoform 4)Ubiquitination-18.31-
1580AcetylationINTPYVTKDLLQSKR
ECCCCCCHHHHHCCC		36.0119608861
1586UbiquitinationTKDLLQSKRFQAQSL
CHHHHHCCCCCCHHC		44.25-
1608PhosphorylationIPEMFRQSLIKLWES
CHHHHHHHHHHHHHH		28.0124719451
1681 (in isoform 3)Ubiquitination-18.1821890473
1701 (in isoform 2)Ubiquitination-28.8221890473
1703PhosphorylationDLLFLRASELARAEG
HHHHHCHHHHHHHCC		27.0625002506
1710 (in isoform 3)Ubiquitination-33.9321890473
1720PhosphorylationRIYVSANSGARIGLA
EEEEECCCCCCCCHH		33.2869213931
1730 (in isoform 2)Ubiquitination-2.4921890473
1745PhosphorylationWVDPEDPYKGYRYLY
ECCCCCCCCCEEEEE		29.3925278378
1759AcetylationYLTPQDYKRVSALNS
EECHHHHHHHHHCCC		55.3919865879
1759UbiquitinationYLTPQDYKRVSALNS
EECHHHHHHHHHCCC		55.3921890473
1759 (in isoform 1)Ubiquitination-55.3921890473
1762PhosphorylationPQDYKRVSALNSVHC
HHHHHHHHHCCCEEC		30.9529116813
1769GlutathionylationSALNSVHCEHVEDEG
HHCCCEECEECCCCC		3.4722555962
1778PhosphorylationHVEDEGESRYKITDI
ECCCCCCCCEEEEEC		52.3329116813
1778 (in isoform 3)Ubiquitination-52.3321890473
1781UbiquitinationDEGESRYKITDIIGK
CCCCCCEEEEECCCC		37.71-
1788AcetylationKITDIIGKEEGIGPE
EEEECCCCCCCCCCC		42.0326051181
1788UbiquitinationKITDIIGKEEGIGPE
EEEECCCCCCCCCCC		42.0321906983
1788 (in isoform 1)Ubiquitination-42.0321890473
1796 (in isoform 4)Ubiquitination-37.8721890473
1798 (in isoform 2)Ubiquitination-49.1421890473
1818 (in isoform 4)Ubiquitination-14.24-
1825 (in isoform 4)Ubiquitination-1.8221890473
1838 (in isoform 3)Ubiquitination-14.1021890473
1844PhosphorylationRTIQVENSHLILTGA
CEEEEECCEEEEECH		13.2319060867
1849PhosphorylationENSHLILTGAGALNK
ECCEEEEECHHHHHH		20.2818187866
1851 (in isoform 3)Ubiquitination-8.5421890473
1856AcetylationTGAGALNKVLGREVY
ECHHHHHHHHCCEEE		39.4223954790
1856UbiquitinationTGAGALNKVLGREVY
ECHHHHHHHHCCEEE		39.4221906983
1856 (in isoform 1)Ubiquitination-39.4221890473
1858 (in isoform 2)Ubiquitination-5.9721890473
1871 (in isoform 2)Ubiquitination-19.7421890473
1893 (in isoform 4)Ubiquitination-6.0121890473
1908PhosphorylationYMPKSVHSSVPLLNS
CCCCCHHHCCCCCCC		30.7646157449
1916UbiquitinationSVPLLNSKDPIDRII
CCCCCCCCCCCHHHH		67.4621906983
1916 (in isoform 1)Ubiquitination-67.4621890473
1929UbiquitinationIIEFVPTKTPYDPRW
HHHCCCCCCCCCCCC		41.2421906983
1929 (in isoform 1)Ubiquitination-41.2421890473
1953 (in isoform 4)Ubiquitination-25.6821890473
1966 (in isoform 4)Ubiquitination-15.8121890473
2031AcetylationFKTYQAIKDFNREGL
HHHHHHHHHCCCCCC		60.32132707
2031UbiquitinationFKTYQAIKDFNREGL
HHHHHHHHHCCCCCC		60.32-
2047DimethylationLMVFANWRGFSGGMK
EEEEECCCCCCCCHH		35.77-
2050PhosphorylationFANWRGFSGGMKDMY
EECCCCCCCCHHHHH		36.9428258704
2068 (in isoform 4)Ubiquitination-2.88-
2081PhosphorylationCCQPVLVYIPPQAEL
HCCCEEEEECCCCCC		11.9824248375
2092PhosphorylationQAELRGGSWVVIDSS
CCCCCCCCEEEECCC		21.3727499020
2098PhosphorylationGSWVVIDSSINPRHM
CCEEEECCCCCHHHH		23.2224248375
2099PhosphorylationSWVVIDSSINPRHME
CEEEECCCCCHHHHH		23.7224248375
2108PhosphorylationNPRHMEMYADRESRG
CHHHHHEECCCHHCC		7.6419060867
2116PhosphorylationADRESRGSVLEPEGT
CCCHHCCCCCCCCCE		23.5527499020
2123PhosphorylationSVLEPEGTVEIKFRR
CCCCCCCEEEEEEEH		17.1927499020
2127AcetylationPEGTVEIKFRRKDLV
CCCEEEEEEEHHHHH		21.2220167786
2127UbiquitinationPEGTVEIKFRRKDLV
CCCEEEEEEEHHHHH		21.22-
2131 (in isoform 3)Ubiquitination-51.6721890473
2135UbiquitinationFRRKDLVKTMRRVDP
EEHHHHHHHHHHCCH		43.85-
2144PhosphorylationMRRVDPVYIHLAERL
HHHCCHHHHHHHHHH		6.496824431
2151 (in isoform 2)Ubiquitination-7.2521890473
2153PhosphorylationHLAERLGTPELSTAE
HHHHHHCCCCCCHHH		20.4121815630
2157PhosphorylationRLGTPELSTAERKEL
HHCCCCCCHHHHHHH		24.7424719451
2164 (in isoform 4)Ubiquitination-11.16-
2209UbiquitinationISDILDWKTSRTFFY
CCCCCCCCHHHHHHH		35.972190698
2209 (in isoform 1)Ubiquitination-35.9721890473
2231UbiquitinationLEDLVKKKIHNANPE
HHHHHHHHHHCCCCC		43.40-
2235 (in isoform 2)Ubiquitination-20.84-
2246 (in isoform 4)Ubiquitination-10.7021890473
2268UbiquitinationAYVWDNNKDLAEWLE
EEEEECCHHHHHHHH		61.44-
2293UbiquitinationSVIEENIKCISRDYV
HHHHHHHHEECHHHH		36.78-
2302UbiquitinationISRDYVLKQIRSLVQ
ECHHHHHHHHHHHHH		33.37-
2318PhosphorylationNPEVAMDSIIHMTQH
CHHHHHHHHHHHHCC		15.45101544951
2323PhosphorylationMDSIIHMTQHISPTQ
HHHHHHHHCCCCHHH		11.6628348404
2327PhosphorylationIHMTQHISPTQRAEV
HHHHCCCCHHHHHHH		21.5525627689
2339PhosphorylationAEVIRILSTMDSPST
HHHHHHHHCCCCCCC		21.2223186163
2340PhosphorylationEVIRILSTMDSPST-
HHHHHHHCCCCCCC-		22.8829396449
2343PhosphorylationRILSTMDSPST----
HHHHCCCCCCC----		15.2125159151
2345PhosphorylationLSTMDSPST------
HHCCCCCCC------		51.1820068231
2346PhosphorylationSTMDSPST-------
HCCCCCCC-------		46.1123186163
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
25SPhosphorylationKinaseCAMK1-FAMILY-GPS
25SPhosphorylationKinaseCAM-KI_GROUP-PhosphoELM
29SPhosphorylationKinaseCK2-FAMILY-GPS
29SPhosphorylationKinaseCK2_GROUP-PhosphoELM
78SPhosphorylationKinaseKAPCAP17612
PhosphoELM
78SPhosphorylationKinasePRKACAP17252
GPS
80SPhosphorylationKinasePRKAA1Q13131
GPS
80SPhosphorylationKinasePRKAA2P54646
GPS
80SPhosphorylationKinaseAMPK-FAMILY-GPS
80SPhosphorylationKinaseAMPK_GROUP-PhosphoELM
1201SPhosphorylationKinaseKAPCAP17612
PhosphoELM
1201SPhosphorylationKinasePRKACAP17252
GPS
1201SPhosphorylationKinaseAMPK-FAMILY-GPS
1201SPhosphorylationKinaseAMPK_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseDET1Q7L5Y6
PMID:16794074
-KUbiquitinationE3 ubiquitin ligaseCOP1Q8NHY2
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseDET1#COP1Q7L5Y6#Q8NHY2
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
80SPhosphorylation


1263SPhosphorylation

16698035
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 ACACA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCG1_HUMANCHGBphysical
16169070
BRCA1_HUMANBRCA1physical
16326698
BRCA1_HUMANBRCA1physical
18452305
BRCA1_HUMANBRCA1physical
16698035
ERC6L_HUMANERCC6Lphysical
22939629
PSB7_HUMANPSMB7physical
22863883
P4R3A_HUMANSMEK1physical
22863883
PSMD2_HUMANPSMD2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613933Acetyl-CoA carboxylase 1 deficiency (ACACAD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121Biotin
Regulatory Network of ACACA_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-1334 AND LYS-1580, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29,AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-23; SER-29 ANDSER-80, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 ANDSER-80, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-29 ANDSER-48, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-488, AND MASSSPECTROMETRY.
"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-1844, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1042; SER-2099 ANDTYR-2108, AND MASS SPECTROMETRY.
"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
J. Mol. Biol. 359:973-982(2006).
Cited for: PHOSPHORYLATION AT SER-1263, AND MUTAGENESIS OF SER-78; SER-344;SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29;SER-48; SER-50; SER-53; SER-56; THR-58 AND SER-60, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

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