CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein-like 3-like protein 
Protein Synonyms/Alias
  
Gene Name
 GNL3L 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61NREAELKKKWVEEMRubiquitination[1]
122LDDEATRKAYYKEFRubiquitination[1]
174KLVLVLNKIDLVPKEubiquitination[1]
185VPKEVVEKWLDYLRNubiquitination[1]
200ELPTVAFKASTQHQVubiquitination[1]
208ASTQHQVKNLNRCSVubiquitination[1]
226QASESLLKSKACFGAubiquitination[1]
228SESLLKSKACFGAENubiquitination[1, 2, 3, 4]
265VGLPNVGKSSLINSLubiquitination[1, 5]
273SSLINSLKRSRACSVubiquitination[1, 2, 3]
288GAVPGITKFMQEVYLubiquitination[1, 2]
297MQEVYLDKFIRLLDAubiquitination[1, 2, 3, 5]
327RNCVHVQKLADPVTPubiquitination[1, 2, 3]
375HRLGKKKKGGLYSQEubiquitination[1]
386YSQEQAAKAVLADWVubiquitination[1, 2, 5]
469LLHSPMTKIADAIENubiquitination[1]
477IADAIENKTTVYKIGubiquitination[1, 3, 4, 5]
482ENKTTVYKIGDLTGYubiquitination[1, 4, 6]
502RHQMGWAKRNVDHRPacetylation[7]
502RHQMGWAKRNVDHRPubiquitination[1]
546QALASALKNKKKMQKubiquitination[1]
548LASALKNKKKMQKRAubiquitination[1]
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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
Functional Description
 Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP. 
Sequence Annotation
 DOMAIN 264 320 G.
 NP_BIND 173 176 GTP (Potential).
 NP_BIND 259 266 GTP (Potential).
 NP_BIND 303 306 GTP (Potential).
 REGION 9 35 Required for nucleolar localization.  
Keyword
 Coiled coil; Complete proteome; GTP-binding; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 582 AA 
Protein Sequence
MMKLRHKNKK PGEGSKGHKK ISWPYPQPAK QNGKKATSKV PSAPHFVHPN DHANREAELK 60
KKWVEEMREK QQAAREQERQ KRRTIESYCQ DVLRRQEEFE HKEEVLQELN MFPQLDDEAT 120
RKAYYKEFRK VVEYSDVILE VLDARDPLGC RCFQMEEAVL RAQGNKKLVL VLNKIDLVPK 180
EVVEKWLDYL RNELPTVAFK ASTQHQVKNL NRCSVPVDQA SESLLKSKAC FGAENLMRVL 240
GNYCRLGEVR THIRVGVVGL PNVGKSSLIN SLKRSRACSV GAVPGITKFM QEVYLDKFIR 300
LLDAPGIVPG PNSEVGTILR NCVHVQKLAD PVTPVETILQ RCNLEEISNY YGVSGFQTTE 360
HFLTAVAHRL GKKKKGGLYS QEQAAKAVLA DWVSGKISFY IPPPATHTLP THLSAEIVKE 420
MTEVFDIEDT EQANEDTMEC LATGESDELL GDTDPLEMEI KLLHSPMTKI ADAIENKTTV 480
YKIGDLTGYC TNPNRHQMGW AKRNVDHRPK SNSMVDVCSV DRRSVLQRIM ETDPLQQGQA 540
LASALKNKKK MQKRADKIAS KLSDSMMSAL DLSGNADDGV GD 582 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IBA:RefGenome.
 GO:0042254; P:ribosome biogenesis; IBA:RefGenome. 
Interpro
 IPR006073; GTP_binding_domain.
 IPR027417; P-loop_NTPase. 
Pfam
 PF01926; MMR_HSR1 
SMART
  
PROSITE
  
PRINTS
 PR00326; GTP1OBG.