CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023167
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Beta-citryl-glutamate synthase B 
Protein Synonyms/Alias
 N-acetyl-aspartyl-glutamate synthetase B; NAAG synthetase B; NAAGS; Ribosomal protein S6 modification-like protein B 
Gene Name
 RIMKLB 
Gene Synonyms/Alias
 FAM80B; KIAA1238 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24IREDYPQKEILRALKubiquitination[1]
33ILRALKAKCCEEELDubiquitination[1]
158LEFPMVVKNTRGHRGubiquitination[2]
174AVFLARDKHHLADLSubiquitination[2]
194EAPYLFQKYVKESHGubiquitination[1, 2, 3]
197YLFQKYVKESHGRDVubiquitination[3]
365TERELLTKLPGGLFNubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 Catalyzes the synthesis of beta-citryl-glutamate and N- acetyl-aspartyl-glutamate. Beta-citryl-glutamate is synthesized more efficiently than N-acetyl-aspartyl-glutamate (By similarity). 
Sequence Annotation
 DOMAIN 119 304 ATP-grasp.
 NP_BIND 193 203 ATP (By similarity).
 METAL 264 264 Magnesium or manganese 1 (By similarity).
 METAL 277 277 Magnesium or manganese 1 (By similarity).
 METAL 277 277 Magnesium or manganese 2 (By similarity).
 METAL 279 279 Magnesium or manganese 2 (By similarity).
 BINDING 158 158 ATP (By similarity).
 BINDING 219 219 ATP (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEVV LTIEQGNLGL 60
RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ 120
ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL 180
SHLIRHEAPY LFQKYVKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS 240
LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA 300
DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPPASTA VDNMSASSSS VDSDPESTER 360
ELLTKLPGGL FNMNQLLANE IKLLVD 386 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0016881; F:acid-amino acid ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0072591; F:citrate-L-glutamate ligase activity; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; ISS:UniProtKB.
 GO:0006464; P:cellular protein modification process; IEA:InterPro. 
Interpro
 IPR011761; ATP-grasp.
 IPR013651; ATP-grasp_RimK-type.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR016185; PreATP-grasp_dom.
 IPR004666; RpS6_RimK/Lys_biosynth_LsyX. 
Pfam
 PF08443; RimK 
SMART
  
PROSITE
 PS50975; ATP_GRASP 
PRINTS