CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000126
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-CoA carboxylase 2 
Protein Synonyms/Alias
 ACC-beta; Biotin carboxylase 
Gene Name
 ACACB 
Gene Synonyms/Alias
 ACC2; ACCB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
262GGDRVIEKVLIANNGubiquitination[1]
274NNGIAAVKCMRSIRRubiquitination[1]
454IGFPLMIKASEGGGGacetylation[2]
663ENPDEGFKPSSGTVQubiquitination[1]
1413LYSEDDCKSLREEPIubiquitination[1]
1473AQEKEFPKFFTFRARubiquitination[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] 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
 ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. 
Sequence Annotation
 DOMAIN 259 761 Biotin carboxylation.
 DOMAIN 414 609 ATP-grasp.
 DOMAIN 895 961 Biotinyl-binding.
 DOMAIN 1809 2305 Carboxyltransferase.
 NP_BIND 458 463 ATP (Potential).
 ACT_SITE 584 584 By similarity.
 METAL 567 567 Manganese 1 (By similarity).
 METAL 580 580 Manganese 1 (By similarity).
 METAL 580 580 Manganese 2 (By similarity).
 METAL 582 582 Manganese 2 (By similarity).
 BINDING 1934 1934 Coenzyme A (By similarity).
 BINDING 2238 2238 Coenzyme A (By similarity).
 BINDING 2240 2240 Coenzyme A (By similarity).
 MOD_RES 222 222 Phosphoserine; by AMPK.
 MOD_RES 929 929 N6-biotinyllysine (By similarity).  
Keyword
 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; Manganese; Membrane; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2458 AA 
Protein Sequence
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 60
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 120
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 180
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 240
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 300
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 360
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 420
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 480
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 540
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 600
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 660
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 720
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 780
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 840
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 900
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 960
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 1020
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 1080
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV 1140
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 1200
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP 1260
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV 1320
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR 1380
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP 1440
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL 1500
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY 1560
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS 1620
RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF 1680
GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK 1740
DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG 1800
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK 1860
YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL 1920
AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL 1980
GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR 2040
APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE 2100
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF 2160
SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA 2220
DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK 2280
AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK 2340
QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR 2400
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST 2458 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IEA:Compara.
 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:0006853; P:carnitine shuttle; TAS:Reactome.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
 GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR013537; AcCoA_COase_cen.
 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 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