CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003965
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ornithine carbamoyltransferase, mitochondrial 
Protein Synonyms/Alias
 Ornithine transcarbamylase; OTCase 
Gene Name
 Otc 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
38VQSQVQLKGRDLLTLacetylation[1]
70LKFRIKQKGEYLPLLacetylation[1, 2, 3, 4, 5]
70LKFRIKQKGEYLPLLsuccinylation[4]
80YLPLLQGKSLGMIFEacetylation[4]
80YLPLLQGKSLGMIFEsuccinylation[4]
88SLGMIFEKRSTRTRLacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9]
88SLGMIFEKRSTRTRLsuccinylation[4]
144AVLARVYKQSDLDTLacetylation[1, 2, 3, 4, 5]
144AVLARVYKQSDLDTLsuccinylation[4]
144AVLARVYKQSDLDTLubiquitination[10]
221HLQAATPKGYEPDPNacetylation[1, 2, 3, 4, 5]
221HLQAATPKGYEPDPNsuccinylation[4]
221HLQAATPKGYEPDPNubiquitination[10]
231EPDPNIVKLAEQYAKacetylation[1, 2, 3, 4, 5, 6, 8, 9]
231EPDPNIVKLAEQYAKsuccinylation[4]
231EPDPNIVKLAEQYAKubiquitination[10]
238KLAEQYAKENGTKLSacetylation[1, 2, 3, 4, 5, 6, 7, 9]
238KLAEQYAKENGTKLSsuccinylation[4]
238KLAEQYAKENGTKLSubiquitination[10]
243YAKENGTKLSMTNDPacetylation[1, 2, 3, 5, 9]
243YAKENGTKLSMTNDPubiquitination[10]
274SMGQEDEKKKRLQAFacetylation[1, 3, 4, 5]
274SMGQEDEKKKRLQAFsuccinylation[4]
275MGQEDEKKKRLQAFQacetylation[3]
289QGYQVTMKTAKVAASacetylation[1, 3, 4]
289QGYQVTMKTAKVAASsuccinylation[4]
289QGYQVTMKTAKVAASubiquitination[10]
292QVTMKTAKVAASDWTacetylation[1, 3, 4]
292QVTMKTAKVAASDWTsuccinylation[4]
292QVTMKTAKVAASDWTubiquitination[10]
307FLHCLPRKPEEVDDEacetylation[1, 2, 4]
307FLHCLPRKPEEVDDEsuccinylation[4]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [8] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [10] 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
  
Sequence Annotation
 REGION 90 94 Carbamoyl phosphate binding (By
 REGION 263 267 Ornithine binding (By similarity).
 REGION 302 305 Ornithine binding (By similarity).
 ACT_SITE 303 303 By similarity.
 BINDING 141 141 Carbamoyl phosphate (By similarity).
 BINDING 141 141 Ornithine (By similarity).
 BINDING 168 168 Carbamoyl phosphate (By similarity).
 BINDING 199 199 Ornithine (By similarity).
 BINDING 330 330 Carbamoyl phosphate (By similarity).
 BINDING 330 330 Ornithine (By similarity).
 MOD_RES 88 88 N6-acetyllysine.
 MOD_RES 231 231 N6-acetyllysine.
 MOD_RES 238 238 N6-acetyllysine.  
Keyword
 Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Disease mutation; Mitochondrion; Reference proteome; Transferase; Transit peptide; Urea cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 354 AA 
Protein Sequence
MLSNLRILLN NAALRKGHTS VVRHFWCGKP VQSQVQLKGR DLLTLKNFTG EEIQYMLWLS 60
ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPSF LTTQDIHLGV 120
NESLTDTARV LSSMTDAVLA RVYKQSDLDT LAKEASIPIV NGLSDLYHPI QILADYLTLQ 180
EHYGSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQAATP KGYEPDPNIV KLAEQYAKEN 240
GTKLSMTNDP LEAARGGNVL ITDTWISMGQ EDEKKKRLQA FQGYQVTMKT AKVAASDWTF 300
LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPVLQ KPKF 354 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0004585; F:ornithine carbamoyltransferase activity; IEA:EC.
 GO:0042301; F:phosphate ion binding; IEA:Compara.
 GO:0005543; F:phospholipid binding; IEA:Compara.
 GO:0055081; P:anion homeostasis; IEA:Compara.
 GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
 GO:0019240; P:citrulline biosynthetic process; IEA:Compara.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0007494; P:midgut development; IEA:Compara.
 GO:0070207; P:protein homotrimerization; IEA:Compara.
 GO:0070781; P:response to biotin; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032868; P:response to insulin stimulus; IEA:Compara.
 GO:0010043; P:response to zinc ion; IEA:Compara.
 GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006132; Asp/Orn_carbamoyltranf_P-bd.
 IPR006130; Asp/Orn_carbamoylTrfase.
 IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
 IPR002292; Orn/put_carbamltrans. 
Pfam
 PF00185; OTCace
 PF02729; OTCace_N 
SMART
  
PROSITE
 PS00097; CARBAMOYLTRANSFERASE 
PRINTS
 PR00100; AOTCASE.
 PR00102; OTCASE.