CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011987
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
276WQENDFSKRILNVPQubiquitination[1, 2, 3, 4]
288VPQELYEKGYVKDVDubiquitination[1, 3, 5]
311VGYPVMIKASEGGGGubiquitination[1]
386SVQRRHQKIIEEAPAubiquitination[2]
410HMEQCAVKLAKMVGYubiquitination[2]
520ENPDEGFKPSSGTVQubiquitination[1]
747NKTCVFEKENDPSVMubiquitination[2]
817DPGCVLAKMQLDNPSubiquitination[2]
825MQLDNPSKVQQAELHubiquitination[1, 2, 4]
1316REFTQQNKATLVDHGubiquitination[1, 2]
1334LTFLVAQKDFRKQVNacetylation[6]
1334LTFLVAQKDFRKQVNubiquitination[2]
1338VAQKDFRKQVNYEVDubiquitination[2]
1435RHSDLVTKEASFEYLubiquitination[1]
1524IRLTPTGKAIPIRLFubiquitination[2]
1580INTPYVTKDLLQSKRacetylation[6]
1759YLTPQDYKRVSALNSubiquitination[7]
1781DEGESRYKITDIIGKubiquitination[2, 4]
1788KITDIIGKEEGIGPEubiquitination[1, 2, 3]
1856TGAGALNKVLGREVYubiquitination[1]
1916SVPLLNSKDPIDRIIubiquitination[1]
1929IIEFVPTKTPYDPRWubiquitination[1]
2127PEGTVEIKFRRKDLVacetylation[8]
2209ISDILDWKTSRTFFYubiquitination[1]
2302ISRDYVLKQIRSLVQubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
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
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS 60
DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK 120
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 180
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL 240
GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 300
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 360
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA 420
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY 480
GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 540
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 600
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV 660
LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG 720
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA 780
EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ 840
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 900
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 960
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD 1020
MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR 1080
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 1140
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 1200
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP 1260
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV 1320
DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ 1380
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE 1440
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 1500
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA 1560
YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA 1620
FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI 1680
GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD 1740
PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 1800
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR 1860
EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID 1920
RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG 1980
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL 2040
MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 2100
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE 2160
RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR 2220
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE 2280
EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST 2340
MDSPST 2346 
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