CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010801
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acetyl-CoA carboxylase 
Protein Synonyms/Alias
 ACC; Fatty acid synthetase 3; mRNA transport-defective protein 7; Biotin carboxylase 
Gene Name
 ACC1 
Gene Synonyms/Alias
 ABP2; FAS3; MTR7; YNR016C; N3175 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
51SPLRDFVKSHGGHTVacetylation[1]
73NNGIAAVKEIRSVRKubiquitination[2]
197TIVAQSAKVPCIPWSubiquitination[2]
216DTVHVDEKTGLVSVDubiquitination[2]
229VDDDIYQKGCCTSPEubiquitination[2]
241SPEDGLQKAKRIGFPubiquitination[2]
327SVQRRHQKIIEEAPVubiquitination[2]
338EAPVTIAKAETFHEMacetylation[1]
347ETFHEMEKAAVRLGKacetylation[1]
469EDPNDGFKPSGGTLHacetylation[1]
469EDPNDGFKPSGGTLHubiquitination[2]
574THKMTAEKPDPTLAVubiquitination[2]
599ASEEARHKYIESLQKacetylation[1]
606KYIESLQKGQVLSKDubiquitination[2]
713PSPGKLVKFLVENGEacetylation[1]
837IEVLRNPKLPYSEWKubiquitination[2]
857LHSRLPAKLDEQMEEacetylation[1]
883FPARQLSKLIDMAVKacetylation[1]
890KLIDMAVKNPEYNPDubiquitination[2]
898NPEYNPDKLLGAVVEubiquitination[2]
1038QGALPSVKERTEQIEubiquitination[2]
1054ILKSSVVKVAYGSSNacetylation[1]
1063AYGSSNPKRSEPDLNubiquitination[2]
1274FKDGSYPKYYTFNGPubiquitination[2]
1311RLSNFNIKPIFTDNRacetylation[1]
1461TEMYTEVKNAKGEWVubiquitination[2]
1470AKGEWVFKSLGKPGSacetylation[1]
1474WVFKSLGKPGSMHLRubiquitination[2]
1524QASSSQWKNFSADVKubiquitination[2]
1572VAFKITVKTPEYPRGubiquitination[2]
1606QEDEFFNKVTEYARKubiquitination[2]
1671ETLKKFDKENSVLTEacetylation[1]
1671ETLKKFDKENSVLTEubiquitination[2]
1764TGAPAINKMLGREVYacetylation[1]
1764TGAPAINKMLGREVYubiquitination[2]
1813WMSYVPAKRNMPVPIubiquitination[2]
2034PQGMVGIKFRREKLLacetylation[1]
2034PQGMVGIKFRREKLLubiquitination[2]
2039GIKFRREKLLDTMNRubiquitination[2]
2061LRSQLSNKSLAPEVHubiquitination[2]
2073EVHQQISKQLADRERacetylation[1]
2106RSSRMVAKGVISKELubiquitination[2]
2137LNEEYLIKRLSHQVGacetylation[1]
2137LNEEYLIKRLSHQVGubiquitination[2]
2185NYKTLDDKLKGLKLEubiquitination[2]
2190DDKLKGLKLESFAQDacetylation[1]
2200SFAQDLAKKIRSDHDubiquitination[2]
2225KMLSTDDKEKLLKTLubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole. 
Sequence Annotation
 DOMAIN 58 567 Biotin carboxylation.
 DOMAIN 216 408 ATP-grasp.
 DOMAIN 701 767 Biotinyl-binding.
 DOMAIN 1603 2101 Carboxyltransferase.
 NP_BIND 256 261 ATP (By similarity).
 REGION 1627 1629 Acetyl-CoA binding.
 ACT_SITE 383 383 By similarity.
 METAL 365 365 Manganese 1 (By similarity).
 METAL 379 379 Manganese 1 (By similarity).
 METAL 379 379 Manganese 2 (By similarity).
 METAL 381 381 Manganese 2 (By similarity).
 BINDING 1731 1731 Coenzyme A.
 BINDING 1998 1998 Acetyl-CoA; via amide nitrogen.
 BINDING 2034 2034 Coenzyme A.
 BINDING 2036 2036 Coenzyme A.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 735 735 N6-biotinyllysine (By similarity).
 MOD_RES 790 790 Phosphoserine.
 MOD_RES 1148 1148 Phosphoserine.
 MOD_RES 1157 1157 Phosphoserine.
 MOD_RES 1162 1162 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Biotin; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; Manganese; Membrane; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2233 AA 
Protein Sequence
MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS 60
KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP 120
GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM 180
RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ 240
KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE 300
VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS 360
AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT 420
LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF 480
RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV 540
EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY 600
IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD 660
GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE 720
HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP 780
FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY 840
SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL 900
GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK 960
DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK 1020
VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY 1080
VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF 1140
STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH 1200
QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR 1260
ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI 1320
HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS 1380
DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL 1440
RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA 1500
HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN 1560
AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY 1620
LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT 1680
VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV 1740
RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV 1800
EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL 1860
FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP 1920
GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD 1980
YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL 2040
LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS 2100
SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP 2160
ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML 2220
STDDKEKLLK TLK 2233 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0003989; F:acetyl-CoA carboxylase activity; IMP:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004075; F:biotin carboxylase activity; IMP:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
 GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006998; P:nuclear envelope organization; TAS:SGD.
 GO:0006606; P:protein import into nucleus; IMP:SGD. 
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