CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040795
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Uncharacterized protein 
Protein Synonyms/Alias
  
Gene Name
  
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27LTTLDVTKLTPLSHEacetylation[1]
27LTTLDVTKLTPLSHEubiquitination[2, 3, 4, 5, 6, 7]
54IGHVAHGKSTVVKAIubiquitination[4]
59HGKSTVVKAISGVHTubiquitination[2, 4, 5, 7]
70GVHTVRFKNELERNIubiquitination[2, 4, 5, 7]
80LERNITIKLGYANAKubiquitination[4]
183AIEIMKLKHILILQNubiquitination[4]
191HILILQNKIDLVKERubiquitination[3, 4, 5]
241VVCEYIVKKIPVPPRubiquitination[4]
242VCEYIVKKIPVPPRDubiquitination[5]
266IRSFDVNKPGCEVDDubiquitination[4, 5, 7, 8]
275GCEVDDLKGGVAGGSubiquitination[4, 5, 7, 8]
285VAGGSILKGVLKVGQubiquitination[3, 4, 6, 7]
303VRPGIVSKDSEGKLMubiquitination[6]
342GLIGVGTKIDPTLCRubiquitination[4, 5]
400AKVQKLSKNEVLMVNubiquitination[4]
421GGRVSAVKADLGKIVubiquitination[2, 3, 4, 5, 7]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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]
 [8] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 466 AA 
Protein Sequence
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 60
ISGVHTVRFK NELERNITIK LGYANAKIYQ LDDPSCPRPE CYRSCGSSMP DEFPTDIPGT 120
KGNFRLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 180
KLKHILILQN KIDLVKERQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 240
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQETEVRPGI 300
VSKDSEGKLM CKSIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQILGA 360
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 420
KADLGKIVLT NPVCTEIHLI HLDLIKELEW GPVLTNETQR KSAANF 466 
Gene Ontology
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR015256; TIF2_gsu_C.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF09173; eIF2_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
  
PROSITE
  
PRINTS
 PR00315; ELONGATNFCT.