CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020397
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar GTP-binding protein 1 
Protein Synonyms/Alias
 Chronic renal failure gene protein; GTP-binding protein NGB 
Gene Name
 GTPBP4 
Gene Synonyms/Alias
 CRFG; NOG1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MAHYNFKKITVVPSubiquitination[1]
8MAHYNFKKITVVPSAubiquitination[1]
16ITVVPSAKDFIDLTLubiquitination[1]
25FIDLTLSKTQRKTPTubiquitination[1, 2, 3]
103LGQINIAKNLVDNVAacetylation[4]
103LGQINIAKNLVDNVAubiquitination[1, 2, 5]
111NLVDNVAKDYVRLMKubiquitination[1, 2]
118KDYVRLMKYGDSLYRubiquitination[1, 5]
142GRMCTVIKRQKQSLEubiquitination[1]
145CTVIKRQKQSLEYLEubiquitination[1, 5]
181CGYPNVGKSSFINKVubiquitination[1, 2, 6]
187GKSSFINKVTRADVDubiquitination[1]
203QPYAFTTKSLFVGHMubiquitination[1, 5]
213FVGHMDYKYLRWQVVubiquitination[1]
282IRPLFINKPLIVVANubiquitination[1]
371IPTRRDDKERPPFIPubiquitination[1]
449IDPAIMKKLEELEKEubiquitination[1]
494IREKKKLKILESKEKubiquitination[1]
522VQRTVLEKEMRSLGVacetylation[4]
522VQRTVLEKEMRSLGVubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] 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] 
Functional Description
 Involved in the biogenesis of the 60S ribosomal subunit (By similarity). 
Sequence Annotation
 NP_BIND 175 182 GTP (Potential).
 NP_BIND 221 225 GTP (Potential).
 NP_BIND 289 292 GTP (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 103 103 N6-acetyllysine.
 MOD_RES 468 468 Phosphoserine.
 MOD_RES 470 470 Phosphoserine.
 MOD_RES 472 472 Phosphoserine.
 MOD_RES 522 522 N6-acetyllysine.
 MOD_RES 558 558 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 634 AA 
Protein Sequence
MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK VKFTQQNYHD 60
RLSQILTDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN IAKNLVDNVA KDYVRLMKYG 120
DSLYRCKQLK RAALGRMCTV IKRQKQSLEY LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG 180
KSSFINKVTR ADVDVQPYAF TTKSLFVGHM DYKYLRWQVV DTPGILDHPL EDRNTIEMQA 240
ITALAHLRAA VLYVMDLSEQ CGHGLREQLE LFQNIRPLFI NKPLIVVANK CDVKRIAELS 300
EDDQKIFTDL QSEGFPVIET STLTEEGVIK VKTEACDRLL AHRVETKMKG NKVNEVLNRL 360
HLAIPTRRDD KERPPFIPEG VVARRKRMET EESRKKRERD LELEMGDDYI LDLQKYWDLM 420
NLSEKHDKIP EIWEGHNIAD YIDPAIMKKL EELEKEEELR TAAGEYDSVS ESEDEEMLEI 480
RQLAKQIREK KKLKILESKE KNTQGPRMPR TAKKVQRTVL EKEMRSLGVD MDDKDDAHYA 540
VQARRSRSIT RKRKREDSAP PSSVARSGSC SRTPRDVSGL RDVKMVKKAK TMMKNAQKKM 600
NRLGKKGEAD RHVFDMKPKH LLSGKRKAGK KDRR 634 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
 GO:0005525; F:GTP binding; IDA:HGNC.
 GO:0003924; F:GTPase activity; IDA:HGNC.
 GO:0030336; P:negative regulation of cell migration; IDA:HGNC.
 GO:0008285; P:negative regulation of cell proliferation; IMP:HGNC.
 GO:0022408; P:negative regulation of cell-cell adhesion; IDA:HGNC.
 GO:0033342; P:negative regulation of collagen binding; IMP:HGNC.
 GO:0008156; P:negative regulation of DNA replication; IMP:HGNC.
 GO:0031397; P:negative regulation of protein ubiquitination; IDA:HGNC.
 GO:0050821; P:protein stabilization; IDA:HGNC.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:HGNC.
 GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. 
Interpro
 IPR006073; GTP_binding_domain.
 IPR024926; NOG1.
 IPR010674; NOG1_Rossman_fold_dom.
 IPR012973; NOG_C.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom. 
Pfam
 PF06858; NOG1
 PF08155; NOGCT 
SMART
  
PROSITE
  
PRINTS
 PR00326; GTP1OBG.