CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013933
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
9DEPSPLAKTLELNQHubiquitination[1]
275WQENDFSKRILNVPQubiquitination[1]
287VPQDLYEKGYVKDVDubiquitination[1]
746NKTCVFEKENDPSVMacetylation[2]
824MQLDNPSKVQQAELHubiquitination[1]
915RIPLNVEKSIKKEMAubiquitination[1]
1315REFTQQNKATLVEHGubiquitination[1]
1337VAQKDFRKQVNCEVDubiquitination[1]
1579INTPYVTKDLLQSKRacetylation[2, 3]
1662EIGMVAWKMSLKSPEubiquitination[1]
1666VAWKMSLKSPEYPDGubiquitination[1]
1748EDPYKGYKYLYLTPQubiquitination[1]
1758YLTPQDYKRVSALNSubiquitination[1]
1780DEGESRYKITDIIGKubiquitination[1]
1787KITDIIGKEEGLGAEubiquitination[1]
1928IIEFVPTKAPYDPRWubiquitination[1]
2030FKTYQAIKDFNREGLubiquitination[1]
2053RGFSGGMKDMYDQVLubiquitination[1]
2126PEGTVEIKFRKKDLVubiquitination[1]
2230LEDLVKKKIHNANPEubiquitination[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]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
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
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD 60
LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV 120
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG 180
PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG 240
DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 300
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ 360
ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG 420
TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG 480
VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF 540
SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 600
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL 660
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS 720
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE 780
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS 840
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD 900
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF 960
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM 1020
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA 1080
RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS 1140
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1200
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP 1260
QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE 1320
HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL 1380
ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY 1440
LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1500
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY 1560
GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF 1620
LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG 1680
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP 1740
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1800
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE 1860
VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR 1920
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI 1980
PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM 2040
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2100
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER 2160
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR 2220
LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE 2280
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM 2340
DSPST 2345 
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