CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020251
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein-like 3 
Protein Synonyms/Alias
 E2-induced gene 3 protein; Novel nucleolar protein 47; NNP47; Nucleolar GTP-binding protein 3; Nucleostemin 
Gene Name
 GNL3 
Gene Synonyms/Alias
 E2IG3; NS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57VPNSAPFKEALLREAubiquitination[1, 2]
79EELKQQQKLDRQKELacetylation[3]
136LYCQELKKVIEASDVubiquitination[2]
171AIVQSGQKKLVLILNubiquitination[4]
179KLVLILNKSDLVPKEacetylation[5]
179KLVLILNKSDLVPKEubiquitination[2]
196ESWLNYLKKELPTVVubiquitination[6]
237RSEVCFGKEGLWKLLubiquitination[2, 6]
253GFQETCSKAIRVGVIubiquitination[2, 7]
332PASIEVVKPMEAASAubiquitination[6]
352DARQVVLKYTVPGYRubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity). 
Sequence Annotation
 DOMAIN 266 347 G.
 NP_BIND 178 181 GTP (Potential).
 NP_BIND 261 268 GTP (Potential).
 NP_BIND 305 308 GTP (Potential).
 REGION 2 46 Basic (By similarity).
 REGION 282 456 Intermediate (By similarity).
 REGION 465 543 Acidic (By similarity).
 MOD_RES 79 79 N6-acetyllysine.
 MOD_RES 529 529 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 549 AA 
Protein Sequence
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV PNSAPFKEAL 60
LREAELRKQR LEELKQQQKL DRQKELEKKR KLETNPDIKP SNVEPMEKEF GLCKTENKAK 120
SGKQNSKKLY CQELKKVIEA SDVVLEVLDA RDPLGCRCPQ VEEAIVQSGQ KKLVLILNKS 180
DLVPKENLES WLNYLKKELP TVVFRASTKP KDKGKITKRV KAKKNAAPFR SEVCFGKEGL 240
WKLLGGFQET CSKAIRVGVI GFPNVGKSSI INSLKQEQMC NVGVSMGLTR SMQVVPLDKQ 300
ITIIDSPSFI VSPLNSSSAL ALRSPASIEV VKPMEAASAI LSQADARQVV LKYTVPGYRN 360
SLEFFTVLAQ RRGMHQKGGI PNVEGAAKLL WSEWTGASLA YYCHPPTSWT PPPYFNESIV 420
VDMKSGFNLE ELEKNNAQSI RAIKGPHLAN SILFQSSGLT NGIIEEKDIH EELPKRKERK 480
QEEREDDKDS DQETVDEEVD ENSSGMFAAE ETGEALSEET TAGEQSTRSF ILDKIIEEDD 540
AYDFSTDYV 549 
Gene Ontology
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:Compara.
 GO:0005525; F:GTP binding; ISS:UniProtKB.
 GO:0003924; F:GTPase activity; IBA:RefGenome.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
 GO:0042254; P:ribosome biogenesis; IBA:RefGenome. 
Interpro
 IPR014813; Gnl3_N_dom.
 IPR006073; GTP_binding_domain.
 IPR027417; P-loop_NTPase. 
Pfam
 PF08701; GN3L_Grn1
 PF01926; MMR_HSR1 
SMART
  
PROSITE
  
PRINTS