CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002069
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carbamoyl-phosphate synthase arginine-specific large chain 
Protein Synonyms/Alias
 Arginine-specific carbamoyl-phosphate synthetase, ammonia chain 
Gene Name
 CPA2 
Gene Synonyms/Alias
 YJR109C; J2002 
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
135VLAKYNVKVLGTPIKacetylation[1]
184LEAAERVKYPVIVRSacetylation[1]
331RSSALASKATGYPLAubiquitination[2]
383IPKWDLSKFQYVDRSubiquitination[2]
473NELSKIDKWFLYKCMacetylation[1]
493YKELESVKSLSDLSKacetylation[1]
500KSLSDLSKDLLQRAKacetylation[1]
547LGIIPFVKRIDTLAAacetylation[1]
756NEEELKAKLTLASDVubiquitination[2]
851PFNMQIIKDGEHTLKacetylation[1]
897LGGDIVPKPVDLMLNacetylation[1]
1002YTTNETTKTYLQEHIacetylation[1]
1010TYLQEHIKEKNAKVSacetylation[1]
1020NAKVSLIKFPKNDKRacetylation[1]
1093AKIAEKIKILESHDVubiquitination[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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
  
Sequence Annotation
 DOMAIN 154 346 ATP-grasp 1.
 DOMAIN 698 890 ATP-grasp 2.
 NP_BIND 174 229 ATP (Potential).
 NP_BIND 321 371 ATP (Potential).
 METAL 303 303 Manganese 1 (By similarity).
 METAL 317 317 Manganese 1 (By similarity).
 METAL 317 317 Manganese 2 (By similarity).
 METAL 319 319 Manganese 2 (By similarity).
 METAL 848 848 Manganese 3 (By similarity).
 METAL 861 861 Manganese 3 (By similarity).  
Keyword
 Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Ligase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1118 AA 
Protein Sequence
MTSIYTSTEP TNSAFTTEDY KPQLVEGVNS VLVIGSGGLS IGQAGEFDYS GSQAIKALKE 60
DNKFTILVNP NIATNQTSHS LADKIYYLPV TPEYITYIIE LERPDAILLT FGGQTGLNCG 120
VALDESGVLA KYNVKVLGTP IKTLITSEDR DLFASALKDI NIPIAESFAC ETVDEALEAA 180
ERVKYPVIVR SAYALGGLGS GFANNASEMK ELAAQSLSLA PQILVEKSLK GWKEVEYEVV 240
RDRVGNCITV CNMENFDPLG VHTGDSMVFA PSQTLSDEEF HMLRSAAIKI IRHLGVIGEC 300
NVQYALQPDG LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIGLGYTL PELPNPITKT 360
TVANFEPSLD YIVAKIPKWD LSKFQYVDRS IGSSMKSVGE VMAIGRNYEE AFQKALRQVD 420
PSLLGFQGST EFGDQLDEAL RTPTDRRVLA IGQALIHENY TVERVNELSK IDKWFLYKCM 480
NIVNIYKELE SVKSLSDLSK DLLQRAKKLG FSDKQIAVTI NKHASTNINE LEIRSLRKTL 540
GIIPFVKRID TLAAEFPAQT NYLYTTYNAT KNDVEFNENG MLVLGSGVYR IGSSVEFDWC 600
AVNTAKTLRD QGKKTIMINY NPETVSTDFD EVDRLYFEEL SYERVMDIYE LEQSEGCIIS 660
VGGQLPQNIA LKLYDNGCNI MGTNPNDIDR AENRHKFSSI LDSIDVDQPE WSELTSVEEA 720
KLFASKVNYP VLIRPSYVLS GAAMSVVNNE EELKAKLTLA SDVSPDHPVV MSKFIEGAQE 780
IDVDAVAYNG NVLVHAISEH VENAGVHSGD ASLVLPPQHL SDDVKIALKD IADKVAKAWK 840
ITGPFNMQII KDGEHTLKVI ECNIRASRSF PFVSKVLGVN FIEIAVKAFL GGDIVPKPVD 900
LMLNKKYDYV ATKVPQFSFT RLAGADPFLG VEMASTGEVA SFGRDLIESY WTAIQSTMNF 960
HVPLPPSGIL FGGDTSREYL GQVASIVATI GYRIYTTNET TKTYLQEHIK EKNAKVSLIK 1020
FPKNDKRKLR ELFQEYDIKA VFNLASKRAE STDDVDYIMR RNAIDFAIPL FNEPQTALLF 1080
AKCLKAKIAE KIKILESHDV IVPPEVRSWD EFIGFKAY 1118 
Gene Ontology
 GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006526; P:arginine biosynthetic process; IMP:SGD. 
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.
 IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 IPR005483; CbamoylP_synth_lsu_CPSase_dom.
 IPR011607; MGS-like_dom.
 IPR016185; PreATP-grasp_dom. 
Pfam
 PF00289; CPSase_L_chain
 PF02786; CPSase_L_D2
 PF02787; CPSase_L_D3
 PF02142; MGS 
SMART
 SM01096; CPSase_L_D3 
PROSITE
 PS50975; ATP_GRASP
 PS00866; CPSASE_1
 PS00867; CPSASE_2 
PRINTS
 PR00098; CPSASE.