CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005975
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157GQWLQEEKVPAIYGVubiquitination[1]
207LIAEVSTKDVKVYGKubiquitination[1]
453SQAVKAMKEENVKTVubiquitination[1]
458AMKEENVKTVLMNPNubiquitination[1, 2]
522NCGVELFKRGVLKEYubiquitination[1]
527LFKRGVLKEYGVKVLubiquitination[2]
553DRQLFSDKLNEINEKubiquitination[1]
560KLNEINEKIAPSFAVubiquitination[1, 2]
728RSSALASKATGYPLAubiquitination[1, 3]
751GIPLPEIKNVVSGKTubiquitination[1, 2]
772SLDYMVTKIPRWDLDmethylation[4]
772SLDYMVTKIPRWDLDubiquitination[1, 3]
793SRIGSSMKSVGEVMAubiquitination[1, 2]
811TFEESFQKALRMCHPubiquitination[1, 2]
831TPRLPMNKEWPSNLDubiquitination[1, 2]
856TRIYAIAKAIDDNMSubiquitination[2]
869MSLDEIEKLTYIDKWacetylation[5]
892LNMEKTLKGLNSESMubiquitination[2, 3]
1074PLYKNGVKIMGTSPLubiquitination[1]
1100SAVLDELKVAQAPWKubiquitination[3]
1107KVAQAPWKAVNTLNEubiquitination[1, 2, 3]
1168EHPVVLTKFVEGAREubiquitination[1, 2]
1183VEMDAVGKDGRVISHubiquitination[1, 2]
1222ISQGAIEKVKDATRKubiquitination[1]
1269RSFPFVSKTLGVDFIubiquitination[1, 2, 3]
1309PADYVAIKAPMFSWPubiquitination[1]
1356AMLSTGFKIPQKGILubiquitination[2]
1360TGFKIPQKGILIGIQubiquitination[1]
1444NLPNNNTKFVHDNYVubiquitination[1]
1471LTNFQVTKLFAEAVQubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [5] 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
 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 (Probable).
 BINDING 1394 1394 Allosteric activator (Probable).
 BINDING 1410 1410 Allosteric activator (Probable).
 BINDING 1437 1437 Allosteric activator (Probable).
 BINDING 1440 1440 Allosteric activator (Probable).
 BINDING 1449 1449 Allosteric activator (Probable).
 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 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
 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Ligase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transit peptide; Urea cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1500 AA 
Protein Sequence
MTRILTAFKV VRTLKTGFGF TNVTAHQKWK FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 60
FGHPSSVAGE VVFNTGLGGY PEAITDPAYK GQILTMANPI IGNGGAPDTT ALDELGLSKY 120
LESNGIKVSG LLVLDYSKDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 180
GKIEFEGQPV DFVDPNKQNL IAEVSTKDVK VYGKGNPTKV VAVDCGIKNN VIRLLVKRGA 240
EVHLVPWNHD FTKMEYDGIL IAGGPGNPAL AEPLIQNVRK ILESDRKEPL FGISTGNLIT 300
GLAAGAKTYK MSMANRGQNQ PVLNITNKQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 360
NEGIMHESKP FFAVQFHPEV TPGPIDTEYL FDSFFSLIKK GKATTITSVL PKPALVASRV 420
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 480
TVYFLPITPQ FVTEVIKAEQ PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 540
IMATEDRQLF SDKLNEINEK IAPSFAVESI EDALKAADTI GYPVMIRSAY ALGGLGSGIC 600
PNRETLMDLS TKAFAMTNQI LVEKSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 660
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 720
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 780
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSI EGFTPRLPMN KEWPSNLDLR 840
KELSEPSSTR IYAIAKAIDD NMSLDEIEKL TYIDKWFLYK MRDILNMEKT LKGLNSESMT 900
EETLKRAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 960
TYNGQEHDVN FDDHGMMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 1020
STDFDECDKL YFEELSLERI LDIYHQEACG GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 1080
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAK SVDYPCLLRP SYVLSGSAMN 1140
VVFSEDEMKK FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKDGRVISH AISEHVEDAG 1200
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 1260
SRSFPFVSKT LGVDFIDVAT KVMIGENVDE KHLPTLDHPI IPADYVAIKA PMFSWPRLRD 1320
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 1380
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 1440
NNTKFVHDNY VIRRTAVDSG IPLLTNFQVT KLFAEAVQKS RKVDSKSLFH YRQYSAGKAA 1500 
Gene Ontology
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IMP:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
 GO:0070409; P:carbamoyl phosphate biosynthetic process; IMP:UniProtKB.
 GO:0019240; P:citrulline biosynthetic process; NAS:BHF-UCL.
 GO:0006543; P:glutamine catabolic process; IEA:InterPro.
 GO:0005980; P:glycogen catabolic process; IMP:BHF-UCL.
 GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
 GO:0046209; P:nitric oxide metabolic process; IMP:BHF-UCL.
 GO:0045909; P:positive regulation of vasodilation; IMP:BHF-UCL.
 GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
 GO:0019433; P:triglyceride catabolic process; IMP:BHF-UCL.
 GO:0000050; P:urea cycle; NAS:BHF-UCL. 
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.