CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002535
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
55IVLEDGTKMKGYSFGacetylation[1]
57LEDGTKMKGYSFGHPacetylation[1]
119RDELGLNKYMESDGIacetylation[1]
157GQWLQEEKVPAIYGVacetylation[1]
171VDTRMLTKIIRDKGTacetylation[1]
182DKGTMLGKIEFEGQSacetylation[1]
197VDFVDPNKQNLIAEVacetylation[1]
207LIAEVSTKDVKVFGKacetylation[1]
210EVSTKDVKVFGKGNPacetylation[1]
214KDVKVFGKGNPTKVVacetylation[1]
287KILESDRKEPLFGISacetylation[1]
307TGLAAGAKSYKMSMAacetylation[1]
350NTLPAGWKPLFVNVNacetylation[1]
412TITSVLPKPALVASRacetylation[1]
458AMKEENVKTVLMNPNacetylation[1]
527LFKRGVLKEYGVKVLacetylation[1]
553DRQLFSDKLNEINEKacetylation[1]
560KLNEINEKIAPSFAVacetylation[1]
751GIPLPEIKNVVSGKTacetylation[1]
793SRIGSSMKSVGEVMAacetylation[1]
831TPRLPMNKEWPANLDacetylation[1]
856TRIYAIAKALENNMSacetylation[1]
869MSLDEIVKLTSIDKWacetylation[1]
875VKLTSIDKWFLYKMRacetylation[1]
889RDILNMDKTLKGLNSacetylation[1]
892LNMDKTLKGLNSESVacetylation[1]
1074PLYKNGVKIMGTSPLacetylation[1]
1100SAVLDELKVAQAPWKacetylation[1]
1168EHPVVLTKFIEGAREacetylation[1]
1183VEMDAVGKEGRVISHacetylation[1]
1232DATRKIAKAFAISGPacetylation[1]
1269RSFPFVSKTLGVDFIacetylation[1]
1291IGESVDEKHLPTLEQacetylation[1]
1356AMLSTGFKIPQKGILacetylation[1]
1360TGFKIPQKGILIGIQacetylation[1]
1486KARTVDSKSLFHYRQacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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.
 BINDING 1394 1394 Allosteric activator.
 BINDING 1410 1410 Allosteric activator.
 BINDING 1437 1437 Allosteric activator.
 BINDING 1440 1440 Allosteric activator.
 BINDING 1449 1449 Allosteric activator.
 MOD_RES 55 55 N6-acetyllysine (By similarity).
 MOD_RES 119 119 N6-acetyllysine (By similarity).
 MOD_RES 287 287 N6-acetyllysine; alternate (By
 MOD_RES 287 287 N6-succinyllysine; alternate (By
 MOD_RES 527 527 N6-acetyllysine (By similarity).
 MOD_RES 603 603 N6-acetyllysine (By similarity).
 MOD_RES 841 841 N6-acetyllysine (By similarity).
 MOD_RES 892 892 N6-acetyllysine (By similarity).
 MOD_RES 898 898 Phosphoserine (By similarity).
 MOD_RES 1291 1291 N6-acetyllysine; alternate (By
 MOD_RES 1291 1291 N6-succinyllysine; alternate (By  
Keyword
 Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; 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
MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 60
FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY 120
MESDGIKVAG LLVLNYSHDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 180
GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA 240
EVHLVPWNHD FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 300
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 360
NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV 420
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 480
AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 540
IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 600
PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 660
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 720
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 780
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR 840
KELSEPSSTR IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT 900
EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 960
TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 1020
STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 1080
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN 1140
VVFSEDEMKR FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG 1200
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 1260
SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI IPSDYVAIKA PMFSWPRLRD 1320
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 1380
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 1440
NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA 1500 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0005524; F:ATP binding; IDA:RGD.
 GO:0005509; F:calcium ion binding; IPI:RGD.
 GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IDA:RGD.
 GO:0004175; F:endopeptidase activity; IMP:RGD.
 GO:0016595; F:glutamate binding; IPI:RGD.
 GO:0072341; F:modified amino acid binding; IEA:Compara.
 GO:0005543; F:phospholipid binding; IDA:RGD.
 GO:0032403; F:protein complex binding; IDA:RGD.
 GO:0055081; P:anion homeostasis; IDA:RGD.
 GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro.
 GO:0071320; P:cellular response to cAMP; IEP:RGD.
 GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
 GO:0071377; P:cellular response to glucagon stimulus; IEP:RGD.
 GO:0071400; P:cellular response to oleic acid; IEP:RGD.
 GO:0006543; P:glutamine catabolic process; IEA:InterPro.
 GO:0005980; P:glycogen catabolic process; IEA:Compara.
 GO:0070365; P:hepatocyte differentiation; IEP:RGD.
 GO:0050667; P:homocysteine metabolic process; IEA:Compara.
 GO:0007494; P:midgut development; IEP:RGD.
 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; IEP:RGD.
 GO:0043200; P:response to amino acid stimulus; IEP:RGD.
 GO:0071548; P:response to dexamethasone stimulus; IEP:RGD.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0032094; P:response to food; IEP:RGD.
 GO:0060416; P:response to growth hormone stimulus; IEP:RGD.
 GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
 GO:0042594; P:response to starvation; IEP:RGD.
 GO:0009636; P:response to toxic substance; IEP:RGD.
 GO:0010043; P:response to zinc ion; IEP:RGD.
 GO:0019433; P:triglyceride catabolic process; IEA:Compara.
 GO:0000050; P:urea cycle; IDA:RGD. 
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.