CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013934
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-CoA carboxylase 1 
Protein Synonyms/Alias
 ACC1; ACC-alpha; Acetyl-CoA carboxylase 265; Biotin carboxylase 
Gene Name
 Acaca 
Gene Synonyms/Alias
 Acac; Gm738 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
47DEPSPLAKTLELNQHubiquitination[1]
157GGNKVIEKVLIANNGubiquitination[1]
313WQENDFSKRILNVPQubiquitination[1]
325VPQDLYEKGYVKDVDubiquitination[1]
557ENPDEGFKPSSGTVQubiquitination[1]
862MQLDNPSKVQQAELHubiquitination[1]
953RIPLNVEKSIKKEMAubiquitination[1]
1353REFTQQNKATLVEHGubiquitination[1]
1375VAQKDFRKQVNCEVDubiquitination[1]
1700EIGMVAWKMSLKSPEubiquitination[1]
1704VAWKMSLKSPEYPDGubiquitination[1]
1786EDPYKGYKYLYLTPQubiquitination[1]
1796YLTPQDYKRVSALNSubiquitination[1]
1818DEGESRYKITDIIGKubiquitination[1]
1825KITDIIGKEEGLGAEubiquitination[1]
1966IIEFVPTKAPYDPRWubiquitination[1]
2068FKTYQAIKDFNREGLubiquitination[1]
2091RGFSGGMKDMYDQVLubiquitination[1]
2164PEGTVEIKFRKKDLVubiquitination[1]
2268LEDLVKKKIHNANPEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity). 
Sequence Annotation
 DOMAIN 116 617 Biotin carboxylation.
 DOMAIN 274 465 ATP-grasp.
 DOMAIN 751 817 Biotinyl-binding.
 DOMAIN 1697 2193 Carboxyltransferase.
 NP_BIND 300 357 ATP (Potential).
 ACT_SITE 440 440 By similarity.
 METAL 423 423 Manganese 1 (By similarity).
 METAL 436 436 Manganese 1 (By similarity).
 METAL 436 436 Manganese 2 (By similarity).
 METAL 438 438 Manganese 2 (By similarity).
 BINDING 1822 1822 Coenzyme A (By similarity).
 BINDING 2126 2126 Coenzyme A (By similarity).
 BINDING 2128 2128 Coenzyme A (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 5 5 Phosphoserine (By similarity).
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 47 47 Phosphoserine (By similarity).
 MOD_RES 52 52 Phosphoserine (By similarity).
 MOD_RES 77 77 Phosphoserine (By similarity).
 MOD_RES 79 79 Phosphoserine; by AMPK (Probable).
 MOD_RES 785 785 N6-biotinyllysine (By similarity).
 MOD_RES 1200 1200 Phosphoserine (By similarity).
 MOD_RES 1215 1215 Phosphoserine (By similarity).
 MOD_RES 1262 1262 Phosphoserine (By similarity).
 MOD_RES 1333 1333 N6-acetyllysine (By similarity).  
Keyword
 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; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2345 AA 
Protein Sequence
MMWWSTLMSL LRASSFWRRI SAETIRIIRA LRAYFERIMD EPSPLAKTLE LNQHSRFIIG 60
SVSEDNSEDE ISNLVKLDLE EKEGSLSPAS VSSDTLSDLG ISGLQDGLAF HMRSSMSGLH 120
LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE 180
MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ 240
AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS 300
GLRVDWQEND FSKRILNVPQ DLYEKGYVKD VDDGLKAAEE VGYPVMIKAS EGGGGKGIRK 360
VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR 420
HQKIIEEAPA AIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ 480
VEHPCTEMVA DVNLPAAQLQ IAMGIPLFRI KDIRMMYGVS PWGDAPIDFE NSAHVPCPRG 540
HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW 600
GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QLNRIDTGWL DRLIAEKVQA 660
ERPDTMLGVV CGALHVADVS LRNSISNFLH SLERGQVLPA HTLLNTVDVE LIYEGIKYVL 720
KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC 780
VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA VESGCIHYVK 840
RPGAALDPGC VIAKMQLDNP SKVQQAELHT GSLPQIQSTA LRGEKLHRVF HYVLDNLVNV 900
MNGYCLPDPF FSSRVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPLN 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 IPTLNRMSFA SNLNHYGMTH VASVSDVLLD 1260
NAFTPPCQRM GGMVSFRTFE DFVRIFDEIM GCFCDSPPQS PTFPESGHTS LYDEDKVPRD 1320
EPIHILNVAI KTDGDIEDDR LAAMFREFTQ QNKATLVEHG IRRLTFLVAQ KDFRKQVNCE 1380
VDQRFHREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL 1440
YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN 1500
TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTTTG 1560
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT AQIMFQAYGD KQGPLHGMLI NTPYVTKDLL 1620
QSKRFQAQSL GTTYIYDIPE MFRQSLIKLW ESMSTQAFLP SPPLPSDILT YTELVLDDQG 1680
QLVHMNRLPG GNEIGMVAWK MSLKSPEYPD GRDIIVIGND ITYRIGSFGP QEDLLFLRAS 1740
ELARAEGIPR IYVAANSGAR IGLAEEIRHM FHVAWVDPED PYKGYKYLYL TPQDYKRVSA 1800
LNSVHCEHVE DEGESRYKIT DIIGKEEGLG AENLRGSGMI AGESSLAYDE VITISLVTCR 1860
AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHS 1920
TVCDDFEGVF TVLHWLSYMP KSVHSSVPLL NSKDPIDRII EFVPTKAPYD PRWMLAGRPH 1980
PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN 2040
LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF 2100
GAYIVDGLRE CSQPVMVYIP PQAELRGGSW VVIDPTINPR HMEMYADRES RGSVLEPEGT 2160
VEIKFRKKDL VKTMRRVDPV YIRLAERLGT PELSPTERKE LESKLKEREE FLIPIYHQVA 2220
VQFADLHDTP GRMQEKGVIN DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ 2280
IQAMLRRWFV EVEGTVKAYV WDNNKDLVEW LEKQLTEEDG VRSVIEENIK YISRDYVLKQ 2340
IRSLVQANPE VAMDSIVHMT QHISPTQRAE VVRILSTMDS PST 2383 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0003989; F:acetyl-CoA carboxylase activity; IDA: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; IDA:UniProtKB.
 GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
 GO:0055088; P:lipid homeostasis; IMP:MGI.
 GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0044268; P:multicellular organismal protein metabolic process; IMP:MGI.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0001894; P:tissue homeostasis; IMP:MGI. 
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