CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044649
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MCG15755 
Protein Synonyms/Alias
 Uncharacterized protein 
Gene Name
 Gm5424 
Gene Synonyms/Alias
 mCG_15755 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
41YLANIGQKEDFEEARacetylation[1]
41YLANIGQKEDFEEARubiquitination[2]
53EARKKALKLGAKKVFacetylation[3]
58ALKLGAKKVFIEDVSacetylation[4]
58ALKLGAKKVFIEDVSubiquitination[2]
112IAQREGAKYVSHGATacetylation[1, 3, 4, 5]
112IAQREGAKYVSHGATubiquitination[2]
121VSHGATGKGNDQVRFacetylation[1, 3]
121VSHGATGKGNDQVRFubiquitination[2]
140YSLAPQIKVIAPWRMubiquitination[2]
155PEFYNRFKGRNDLMEubiquitination[2]
165NDLMEYAKQHGIPIPacetylation[1, 5, 6]
199AGILENPKNQAPPGLubiquitination[2]
228DVLEIEFKKGVPVKVacetylation[1, 5]
234FKKGVPVKVTNIKDGubiquitination[2]
239PVKVTNIKDGTTRTTacetylation[1]
239PVKVTNIKDGTTRTTubiquitination[2]
260YLNEVAGKHGVGRIDacetylation[3]
260YLNEVAGKHGVGRIDubiquitination[2]
277ENRFIGMKSRGIYETubiquitination[2]
310DREVRKIKQGLGLKFubiquitination[2]
340FVRHCIQKSQERVEGacetylation[1, 3, 4]
340FVRHCIQKSQERVEGphosphoglycerylation[7]
340FVRHCIQKSQERVEGubiquitination[2]
355KVQVSVFKGQVYILGacetylation[3]
408EYHRLQSKVTAK***ubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF 60
IEDVSKEFVE EFIWPAVQSS ALYEDRYLLG TSLARPCIAR RQVEIAQREG AKYVSHGATG 120
KGNDQVRFEL TCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVSPKSPWS 180
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DVLEIEFKKG VPVKVTNIKD 240
GTTRTTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 300
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIQK SQERVEGKVQ VSVFKGQVYI 360
LGRESPLSLY NEELVSMNVQ GDYEPIDATG FININSLRLK EYHRLQSKVT AK 412 
Gene Ontology
 GO:0004055; F:argininosuccinate synthase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0006526; P:arginine biosynthetic process; IEA:InterPro. 
Interpro
 IPR001518; Arginosuc_synth.
 IPR018223; Arginosuc_synth_CS.
 IPR023434; Arginosuc_synth_type_1_subfam.
 IPR024074; AS_cat/multimer_dom_body.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00764; Arginosuc_synth 
SMART
  
PROSITE
 PS00564; ARGININOSUCCIN_SYN_1
 PS00565; ARGININOSUCCIN_SYN_2 
PRINTS