UniProt Accession

 CPSM_MOUSE; Q8C196; A0JNU4; Q6NX75 

Genbank Protein ID

 AC101854; AC133187; BC067211; BC126969; AK028683 

Genbank Nucleotide ID

 AAH67211.1; AAI26970.1; BAC26064.1 

Protein Name

 Carbamoyl-phosphate synthase [ammonia], mitochondrial 

Protein Synonyms/Alias

 Carbamoyl-phosphate synthetase I; CPSase I 

Gene Name

 Cps1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
15	CKVVKTLKSGFGFAN	ubiquitination	[1]
26	GFANVTTKRQWDFSR	ubiquitination	[1]
42	GIRLLSVKAKTAHIV	acetylation	[2]
44	RLLSVKAKTAHIVLE	acetylation	[2, 3, 4, 5, 6, 7]
44	RLLSVKAKTAHIVLE	succinylation	[6]
44	RLLSVKAKTAHIVLE	ubiquitination	[1]
55	IVLEDGTKMKGYSFG	acetylation	[2, 3, 4, 5, 6, 7, 8]
55	IVLEDGTKMKGYSFG	succinylation	[6]
55	IVLEDGTKMKGYSFG	ubiquitination	[1]
57	LEDGTKMKGYSFGHP	acetylation	[2, 6, 7]
57	LEDGTKMKGYSFGHP	succinylation	[6]
57	LEDGTKMKGYSFGHP	ubiquitination	[1]
119	RDELGLNKYMESDGI	acetylation	[2, 3, 4, 5, 6, 7, 8, 9]
119	RDELGLNKYMESDGI	succinylation	[6]
119	RDELGLNKYMESDGI	ubiquitination	[1]
127	YMESDGIKVAGLLVL	acetylation	[7]
157	GQWLQEEKVPAIYGV	acetylation	[2, 3, 4, 5, 6, 7, 9]
157	GQWLQEEKVPAIYGV	succinylation	[6]
157	GQWLQEEKVPAIYGV	ubiquitination	[1]
171	VDTRMLTKIIRDKGT	acetylation	[2]
171	VDTRMLTKIIRDKGT	ubiquitination	[1]
176	LTKIIRDKGTMLGKI	acetylation	[2, 4, 6, 7]
176	LTKIIRDKGTMLGKI	succinylation	[6]
176	LTKIIRDKGTMLGKI	ubiquitination	[1]
182	DKGTMLGKIEFEGQS	acetylation	[2, 3, 4, 7]
182	DKGTMLGKIEFEGQS	ubiquitination	[1]
197	VDFVDPNKQNLIAEV	acetylation	[2, 3, 5, 7, 9]
197	VDFVDPNKQNLIAEV	ubiquitination	[1]
207	LIAEVSTKDVKVFGK	acetylation	[2, 3, 4, 6, 7]
207	LIAEVSTKDVKVFGK	succinylation	[6]
207	LIAEVSTKDVKVFGK	ubiquitination	[1]
210	EVSTKDVKVFGKGNP	acetylation	[2, 3, 4, 7]
210	EVSTKDVKVFGKGNP	ubiquitination	[1]
214	KDVKVFGKGNPTKVV	acetylation	[2, 3, 4, 6, 7]
214	KDVKVFGKGNPTKVV	phosphoglycerylation	[10]
214	KDVKVFGKGNPTKVV	succinylation	[6]
214	KDVKVFGKGNPTKVV	ubiquitination	[1]
219	FGKGNPTKVVAVDCG	acetylation	[2, 3, 4, 7]
219	FGKGNPTKVVAVDCG	ubiquitination	[1]
228	VAVDCGIKNNVIRLL	acetylation	[2]
228	VAVDCGIKNNVIRLL	phosphoglycerylation	[10]
228	VAVDCGIKNNVIRLL	ubiquitination	[1]
279	QPLIQNVKKILESDR	acetylation	[2, 4]
280	PLIQNVKKILESDRK	acetylation	[2]
287	KILESDRKEPLFGIS	acetylation	[2, 3, 5, 6, 8]
287	KILESDRKEPLFGIS	succinylation	[6]
287	KILESDRKEPLFGIS	ubiquitination	[1]
307	TGLAAGAKSYKMSMA	acetylation	[2, 3, 4, 6, 7]
307	TGLAAGAKSYKMSMA	succinylation	[6]
307	TGLAAGAKSYKMSMA	ubiquitination	[1]
310	AAGAKSYKMSMANRG	acetylation	[2, 4]
310	AAGAKSYKMSMANRG	ubiquitination	[1]
400	SFFSLIKKGKGTTIT	acetylation	[4, 6]
400	SFFSLIKKGKGTTIT	succinylation	[6]
402	FSLIKKGKGTTITSV	acetylation	[2, 4, 6, 7]
402	FSLIKKGKGTTITSV	succinylation	[6]
402	FSLIKKGKGTTITSV	ubiquitination	[1]
412	TITSVLPKPALVASR	acetylation	[2, 3, 4, 5, 6, 7]
412	TITSVLPKPALVASR	succinylation	[6]
412	TITSVLPKPALVASR	ubiquitination	[1]
453	SQAVKAMKEENVKTV	acetylation	[2, 3, 4, 7]
458	AMKEENVKTVLMNPN	acetylation	[2, 3, 4, 5, 6, 7]
458	AMKEENVKTVLMNPN	succinylation	[6]
458	AMKEENVKTVLMNPN	ubiquitination	[1]
477	QTNEVGLKQADAVYF	acetylation	[7]
522	NCGVELFKRGVLKEY	acetylation	[2, 3, 4, 5, 6, 7]
522	NCGVELFKRGVLKEY	succinylation	[6]
522	NCGVELFKRGVLKEY	ubiquitination	[1]
527	LFKRGVLKEYGVKVL	acetylation	[2, 3, 4, 6, 7, 8]
527	LFKRGVLKEYGVKVL	succinylation	[6]
527	LFKRGVLKEYGVKVL	ubiquitination	[1]
532	VLKEYGVKVLGTSVE	acetylation	[2, 3, 4, 7]
532	VLKEYGVKVLGTSVE	ubiquitination	[1]
553	DRQLFSDKLNEINEK	acetylation	[2, 3, 4, 6, 7, 9]
553	DRQLFSDKLNEINEK	succinylation	[6]
553	DRQLFSDKLNEINEK	ubiquitination	[1]
560	KLNEINEKIAPSFAV	acetylation	[2, 3, 5, 6, 7, 9]
560	KLNEINEKIAPSFAV	succinylation	[6]
560	KLNEINEKIAPSFAV	ubiquitination	[1]
575	ESMEDALKAADTIGY	acetylation	[2, 3, 5, 6, 7, 9]
575	ESMEDALKAADTIGY	succinylation	[6]
603	GSGICPNKETLIDLG	acetylation	[2, 3, 4, 6, 7, 8]
603	GSGICPNKETLIDLG	succinylation	[6]
603	GSGICPNKETLIDLG	ubiquitination	[1]
612	TLIDLGTKAFAMTNQ	acetylation	[2, 3, 6, 7]
612	TLIDLGTKAFAMTNQ	succinylation	[6]
612	TLIDLGTKAFAMTNQ	ubiquitination	[1]
630	ERSVTGWKEIEYEVV	acetylation	[2]
630	ERSVTGWKEIEYEVV	ubiquitination	[1]
728	RSSALASKATGYPLA	ubiquitination	[1]
740	PLAFIAAKIALGIPL	acetylation	[7]
751	GIPLPEIKNVVSGKT	acetylation	[2, 3, 4, 6, 7, 9]
751	GIPLPEIKNVVSGKT	succinylation	[6]
751	GIPLPEIKNVVSGKT	ubiquitination	[1]
757	IKNVVSGKTSACFEP	acetylation	[2, 3, 4, 6, 7]
757	IKNVVSGKTSACFEP	succinylation	[6]
757	IKNVVSGKTSACFEP	ubiquitination	[1]
772	SLDYMVTKIPRWDLD	acetylation	[2, 7]
772	SLDYMVTKIPRWDLD	ubiquitination	[1]
793	SRIGSSMKSVGEVMA	acetylation	[2, 3, 4, 6, 7]
793	SRIGSSMKSVGEVMA	succinylation	[6]
793	SRIGSSMKSVGEVMA	ubiquitination	[1]
811	TFEESFQKALRMCHP	acetylation	[2, 4, 7]
811	TFEESFQKALRMCHP	phosphoglycerylation	[10]
811	TFEESFQKALRMCHP	ubiquitination	[1]
831	TPRLPMNKEWPANLD	acetylation	[2, 3, 4, 6]
831	TPRLPMNKEWPANLD	succinylation	[6]
831	TPRLPMNKEWPANLD	ubiquitination	[1]
840	WPANLDLKKELSEPS	acetylation	[2, 3, 4, 5, 6, 7, 8]
840	WPANLDLKKELSEPS	succinylation	[6]
840	WPANLDLKKELSEPS	ubiquitination	[1]
841	PANLDLKKELSEPSS	acetylation	[2, 3, 4, 6, 8]
841	PANLDLKKELSEPSS	succinylation	[6]
841	PANLDLKKELSEPSS	ubiquitination	[1]
856	TRIYAIAKALENNMS	acetylation	[2, 3, 4, 5, 7, 9]
856	TRIYAIAKALENNMS	ubiquitination	[1]
875	VRLTSIDKWFLYKMR	acetylation	[2, 3, 4, 6, 7, 9]
875	VRLTSIDKWFLYKMR	succinylation	[6]
875	VRLTSIDKWFLYKMR	ubiquitination	[1]
880	IDKWFLYKMRDILNM	acetylation	[2, 7]
880	IDKWFLYKMRDILNM	ubiquitination	[1]
889	RDILNMDKTLKGLNS	acetylation	[2, 3, 4, 5, 6, 7, 9]
889	RDILNMDKTLKGLNS	succinylation	[6]
889	RDILNMDKTLKGLNS	ubiquitination	[1]
892	LNMDKTLKGLNSDSV	acetylation	[2, 3, 4, 5, 6, 7, 8]
892	LNMDKTLKGLNSDSV	succinylation	[6]
892	LNMDKTLKGLNSDSV	ubiquitination	[1]
908	EETLRKAKEIGFSDK	acetylation	[2, 4]
908	EETLRKAKEIGFSDK	ubiquitination	[1]
915	KEIGFSDKQISKCLG	acetylation	[2, 3, 4, 5, 6, 7, 9]
915	KEIGFSDKQISKCLG	succinylation	[6]
915	KEIGFSDKQISKCLG	ubiquitination	[1]
919	FSDKQISKCLGLTEA	acetylation	[2, 3, 4, 5, 6, 7]
919	FSDKQISKCLGLTEA	succinylation	[6]
919	FSDKQISKCLGLTEA	ubiquitination	[1]
935	TRELRLKKNIHPWVK	acetylation	[2]
935	TRELRLKKNIHPWVK	ubiquitination	[1]
1009	TLRQLGKKTVVVNCN	acetylation	[2]
1009	TLRQLGKKTVVVNCN	ubiquitination	[1]
1029	TDFDECDKLYFEELS	acetylation	[7]
1070	NLAVPLYKNGVKIMG	acetylation	[2, 3, 4, 7]
1074	PLYKNGVKIMGTSPL	acetylation	[2, 3, 4, 5, 6, 7]
1074	PLYKNGVKIMGTSPL	succinylation	[6]
1074	PLYKNGVKIMGTSPL	ubiquitination	[1]
1100	SAVLDELKVAQAPWK	acetylation	[2, 3, 5, 6, 7]
1100	SAVLDELKVAQAPWK	succinylation	[6]
1107	KVAQAPWKAVNTLNE	acetylation	[6]
1107	KVAQAPWKAVNTLNE	succinylation	[6]
1149	VFSEDEMKRFLEEAT	acetylation	[2, 3, 6]
1149	VFSEDEMKRFLEEAT	succinylation	[6]
1168	EHPVVLTKFVEGARE	acetylation	[2, 3, 4, 5, 6, 7, 9]
1168	EHPVVLTKFVEGARE	succinylation	[6]
1168	EHPVVLTKFVEGARE	ubiquitination	[1]
1183	VEMDAVGKEGRVISH	acetylation	[2, 3, 4, 5, 6, 7]
1183	VEMDAVGKEGRVISH	succinylation	[6]
1183	VEMDAVGKEGRVISH	ubiquitination	[1]
1222	ISQGAIEKVKDATRK	acetylation	[2, 7]
1222	ISQGAIEKVKDATRK	ubiquitination	[1]
1232	DATRKIAKAFAISGP	acetylation	[2, 6]
1232	DATRKIAKAFAISGP	succinylation	[6]
1247	FNVQFLVKGNDVLVI	acetylation	[2]
1269	RSFPFVSKTLGVDFI	acetylation	[2, 3, 6, 7]
1269	RSFPFVSKTLGVDFI	succinylation	[6]
1269	RSFPFVSKTLGVDFI	ubiquitination	[1]
1281	DFIDVATKVMIGESI	acetylation	[7]
1291	IGESIDEKRLPTLEQ	acetylation	[2, 3, 4, 5, 6, 7, 8, 9]
1291	IGESIDEKRLPTLEQ	succinylation	[6]
1291	IGESIDEKRLPTLEQ	ubiquitination	[1]
1309	PSDYVAIKAPMFSWP	acetylation	[7]
1309	PSDYVAIKAPMFSWP	ubiquitination	[1]
1348	GIHTAFLKAMLSTGF	acetylation	[7]
1356	AMLSTGFKIPQKGIL	acetylation	[2, 3, 4, 6, 7]
1356	AMLSTGFKIPQKGIL	succinylation	[6]
1356	AMLSTGFKIPQKGIL	ubiquitination	[1]
1360	TGFKIPQKGILIGIQ	acetylation	[2, 4, 6]
1360	TGFKIPQKGILIGIQ	succinylation	[6]
1387	QLHNEGFKLFATEAT	acetylation	[2, 7]
1444	NLPNNNTKFVHDNYV	acetylation	[2, 3, 4, 6, 7]
1444	NLPNNNTKFVHDNYV	succinylation	[6]
1444	NLPNNNTKFVHDNYV	ubiquitination	[1]
1471	LTNFQVTKLFAEAVQ	acetylation	[2, 3, 6, 7]
1471	LTNFQVTKLFAEAVQ	succinylation	[6]
1479	LFAEAVQKSRTVDSK	acetylation	[2, 4, 6, 7]
1479	LFAEAVQKSRTVDSK	phosphoglycerylation	[10]
1479	LFAEAVQKSRTVDSK	succinylation	[6]
1479	LFAEAVQKSRTVDSK	ubiquitination	[1]
1486	KSRTVDSKSLFHYRQ	acetylation	[2, 3, 4, 5, 6, 7, 9]
1486	KSRTVDSKSLFHYRQ	succinylation	[6]
1486	KSRTVDSKSLFHYRQ	ubiquitination	[1]
1498	YRQYSAGKAA*****	acetylation	[2, 7]

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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 

Functional Description

 Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell. 

Sequence Annotation

 DOMAIN 219 404 Glutamine amidotransferase type-1.
 DOMAIN 551 743 ATP-grasp 1.
 DOMAIN 1093 1284 ATP-grasp 2.
 REGION 39 218 Anthranilate phosphoribosyltransferase
 BINDING 1391 1391 Allosteric activator (By similarity).
 BINDING 1394 1394 Allosteric activator (By similarity).
 BINDING 1410 1410 Allosteric activator (By similarity).
 BINDING 1437 1437 Allosteric activator (By similarity).
 BINDING 1440 1440 Allosteric activator (By similarity).
 BINDING 1449 1449 Allosteric activator (By similarity).
 MOD_RES 44 44 N6-acetyllysine; alternate.
 MOD_RES 44 44 N6-succinyllysine; alternate.
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 119 119 N6-acetyllysine.
 MOD_RES 287 287 N6-acetyllysine; alternate.
 MOD_RES 287 287 N6-succinyllysine; alternate.
 MOD_RES 527 527 N6-acetyllysine.
 MOD_RES 603 603 N6-acetyllysine.
 MOD_RES 840 840 N6-acetyllysine.
 MOD_RES 841 841 N6-acetyllysine.
 MOD_RES 892 892 N6-acetyllysine.
 MOD_RES 898 898 Phosphoserine.
 MOD_RES 1291 1291 N6-acetyllysine; alternate.
 MOD_RES 1291 1291 N6-succinyllysine; alternate.  

Keyword

 Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transit peptide; Urea cycle. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1500 AA 

Protein Sequence

Gene Ontology

 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; IEA:Compara.
 GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:MGI.
 GO:0004175; F:endopeptidase activity; IEA:Compara.
 GO:0016595; F:glutamate binding; IEA:Compara.
 GO:0072341; F:modified amino acid binding; IEA:Compara.
 GO:0005543; F:phospholipid binding; IEA:Compara.
 GO:0055081; P:anion homeostasis; IEA:Compara.
 GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro.
 GO:0071320; P:cellular response to cAMP; IEA:Compara.
 GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Compara.
 GO:0071377; P:cellular response to glucagon stimulus; IEA:Compara.
 GO:0071400; P:cellular response to oleic acid; IEA:Compara.
 GO:0006543; P:glutamine catabolic process; IEA:InterPro.
 GO:0005980; P:glycogen catabolic process; IEA:Compara.
 GO:0070365; P:hepatocyte differentiation; IEA:Compara.
 GO:0050667; P:homocysteine metabolic process; IEA:Compara.
 GO:0007494; P:midgut development; IEA:Compara.
 GO:0046209; P:nitric oxide metabolic process; IEA:Compara.
 GO:0045909; P:positive regulation of vasodilation; IEA:Compara.
 GO:0014075; P:response to amine stimulus; IEA:Compara.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0071548; P:response to dexamethasone stimulus; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032094; P:response to food; IEA:Compara.
 GO:0060416; P:response to growth hormone stimulus; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0042594; P:response to starvation; IEA:Compara.
 GO:0009636; P:response to toxic substance; IEA:Compara.
 GO:0010043; P:response to zinc ion; IEA:Compara.
 GO:0019433; P:triglyceride catabolic process; IEA:Compara.
 GO:0000050; P:urea cycle; IC:MGI. 

Interpro

 IPR011761; ATP-grasp.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR006275; CarbamoylP_synth_lsu.
 IPR005481; CarbamoylP_synth_lsu_N.
 IPR005480; CarbamoylP_synth_lsu_oligo.
 IPR006274; CarbamoylP_synth_ssu.
 IPR002474; CarbamoylP_synth_ssu_N.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR005483; CbamoylP_synth_lsu_CPSase_dom.
 IPR017926; GATASE.
 IPR011607; MGS-like_dom.
 IPR016185; PreATP-grasp_dom. 

Pfam

 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2
 PF02787; CPSase_L_D3
 PF00988; CPSase_sm_chain
 PF00117; GATase
 PF02142; MGS 

SMART

 SM01096; CPSase_L_D3
 SM01097; CPSase_sm_chain
 SM00851; MGS 

PROSITE

 PS50975; ATP_GRASP
 PS00866; CPSASE_1
 PS00867; CPSASE_2
 PS51273; GATASE_TYPE_1 

PRINTS

 PR00098; CPSASE.