CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011989
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-CoA carboxylase 1 
Protein Synonyms/Alias
 ACC1; ACC-alpha; Biotin carboxylase 
Gene Name
 ACACA 
Gene Synonyms/Alias
 ACAC; ACC1; ACCA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
313WQENDFSKRILNVPQubiquitination[1]
423SVQRRHQKIIEEAPAubiquitination[1]
447HMEQCAVKLAKMVGYubiquitination[1]
784NKTCVFEKENDPSVMubiquitination[1]
854DPGCVLAKMQLDNPSubiquitination[1]
862MQLDNPSKVQQAELHubiquitination[1]
1353REFTQQNKATLVDHGubiquitination[1]
1371LTFLVAQKDFRKQVNubiquitination[1]
1375VAQKDFRKQVNYEVDubiquitination[1]
1561IRLTPTGKAIPIRLFubiquitination[1]
1796YLTPQDYKRVSALNSubiquitination[1, 2]
1818DEGESRYKITDIIGKubiquitination[1]
1825KITDIIGKEEGIGPEubiquitination[1]
1966IIEFVPTKTPYDPRWubiquitination[1]
2068FKTYQAIKDFNREGLubiquitination[1]
2164PEGTVEIKFRRKDLVubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional 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. 
Sequence Annotation
 DOMAIN 117 618 Biotin carboxylation.
 DOMAIN 275 466 ATP-grasp.
 DOMAIN 752 818 Biotinyl-binding.
 DOMAIN 1698 2194 Carboxyltransferase.
 NP_BIND 315 320 ATP (Potential).
 ACT_SITE 441 441 By similarity.
 METAL 424 424 Manganese 1 (By similarity).
 METAL 437 437 Manganese 1 (By similarity).
 METAL 437 437 Manganese 2 (By similarity).
 METAL 439 439 Manganese 2 (By similarity).
 BINDING 1823 1823 Coenzyme A (By similarity).
 BINDING 2127 2127 Coenzyme A (By similarity).
 BINDING 2129 2129 Coenzyme A (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 48 48 Phosphoserine.
 MOD_RES 53 53 Phosphoserine.
 MOD_RES 78 78 Phosphoserine (By similarity).
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 786 786 N6-biotinyllysine (By similarity).
 MOD_RES 1201 1201 Phosphoserine (By similarity).
 MOD_RES 1216 1216 Phosphoserine (By similarity).
 MOD_RES 1263 1263 Phosphoserine.
 MOD_RES 1334 1334 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; Alternative promoter usage; ATP-binding; Biotin; Complete proteome; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2346 AA 
Protein Sequence
MWWSTLMSIL RARSFWKWIS TQTVRIIRAV RAHFGGIMDE PSPLAQPLEL NQHSRFIIGS 60
VSEDNSEDEI SNLVKLDLLE EKEGSLSPAS VGSDTLSDLG ISSLQDGLAL HIRSSMSGLH 120
LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE 180
MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ 240
AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS 300
GLRVDWQEND FSKRILNVPQ ELYEKGYVKD VDDGLQAAEE VGYPVMIKAS EGGGGKGIRK 360
VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR 420
HQKIIEEAPA TIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ 480
VEHPCTEMVA DVNLPAAQLQ IAMGIPLYRI KDIRMMYGVS PWGDSPIDFE DSAHVPCPRG 540
HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW 600
GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QMNRIDTGWL DRLIAEKVQA 660
ERPDTMLGVV CGALHVADVS LRNSVSNFLH SLERGQVLPA HTLLNTVDVE LIYEGVKYVL 720
KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC 780
VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA VESGCIHYVK 840
RPGAALDPGC VLAKMQLDNP SKVQQAELHT GSLPRIQSTA LRGEKLHRVF HYVLDNLVNV 900
MNGYCLPDPF FSSKVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPPN VEKSIKKEMA 960
QYASNITSVL CQFPSQQIAN ILDSHAATLN RKSEREVFFM NTQSIVQLVQ RYRSGIRGHM 1020
KAVVMDLLRQ YLRVETQFQN GHYDKCVFAL REENKSDMNT VLNYIFSHAQ VTKKNLLVTM 1080
LIDQLCGRDP TLTDELLNIL TELTQLSKTT NAKVALRARQ VLIASHLPSY ELRHNQVESI 1140
FLSAIDMYGH QFCIENLQKL ILSETSIFDV LPNFFYHSNQ VVRMAALEVY VRRAYIAYEL 1200
NSVQHRQLKD NTCVVEFQFM LPTSHPNRGN IPTLNRMSFS SNLNHYGMTH VASVSDVLLD 1260
NSFTPPCQRM GGMVSFRTFE DFVRIFDEVM GCFSDSPPQS PTFPEAGHTS LYDEDKVPRD 1320
EPIHILNVAI KTDCDIEDDR LAAMFREFTQ QNKATLVDHG IRRLTFLVAQ KDFRKQVNYE 1380
VDRRFHREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL 1440
YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN 1500
TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG 1560
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT AQIMFQAYGD KQGPLHGMLI NTPYVTKDLL 1620
QSKRFQAQSL GTTYIYDIPE MFRQSLIKLW ESMSTQAFLP SPPLPSDMLT YTELVLDDQG 1680
QLVHMNRLPG GNEIGMVAWK MTFKSPEYPE GRDIIVIGND ITYRIGSFGP QEDLLFLRAS 1740
ELARAEGIPR IYVSANSGAR IGLAEEIRHM FHVAWVDPED PYKGYRYLYL TPQDYKRVSA 1800
LNSVHCEHVE DEGESRYKIT DIIGKEEGIG PENLRGSGMI AGESSLAYNE IITISLVTCR 1860
AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHC 1920
TVCDDFEGVF TVLHWLSYMP KSVHSSVPLL NSKDPIDRII EFVPTKTPYD PRWMLAGRPH 1980
PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN 2040
LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF 2100
GAYIVDGLRE CCQPVLVYIP PQAELRGGSW VVIDSSINPR HMEMYADRES RGSVLEPEGT 2160
VEIKFRRKDL VKTMRRVDPV YIHLAERLGT PELSTAERKE LENKLKEREE FLIPIYHQVA 2220
VQFADLHDTP GRMQEKGVIS DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ 2280
IQAMLRRWFV EVEGTVKAYV WDNNKDLAEW LEKQLTEEDG VHSVIEENIK CISRDYVLKQ 2340
IRSLVQANPE VAMDSIIHMT QHISPTQRAE VIRILSTMDS PST 2383 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004075; F:biotin carboxylase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB.
 GO:0006853; P:carnitine shuttle; TAS:Reactome.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
 GO:0055088; P:lipid homeostasis; IEA:Compara.
 GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
 GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0044268; P:multicellular organismal protein metabolic process; IEA:Compara.
 GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
 GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
 GO:0001894; P:tissue homeostasis; IEA:Compara.
 GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome. 
Interpro
 IPR013537; AcCoA_COase_cen.
 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR001882; Biotin_BS.
 IPR011764; Biotin_carboxylation_dom.
 IPR005482; Biotin_COase_C.
 IPR000089; Biotin_lipoyl.
 IPR005481; CarbamoylP_synth_lsu_N.
 IPR000022; Carboxyl_trans.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR011763; COA_CT_C.
 IPR011762; COA_CT_N.
 IPR016185; PreATP-grasp_dom.
 IPR011054; Rudment_hybrid_motif.
 IPR011053; Single_hybrid_motif. 
Pfam
 PF08326; ACC_central
 PF02785; Biotin_carb_C
 PF00364; Biotin_lipoyl
 PF01039; Carboxyl_trans
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2 
SMART
 SM00878; Biotin_carb_C 
PROSITE
 PS50975; ATP_GRASP
 PS50979; BC
 PS00188; BIOTIN
 PS50968; BIOTINYL_LIPOYL
 PS50989; COA_CT_CTER
 PS50980; COA_CT_NTER
 PS00866; CPSASE_1
 PS00867; CPSASE_2 
PRINTS