CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030488
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RuvB-like 2 
Protein Synonyms/Alias
 RuvB-like 2 (E. coli), isoform CRA_a; cDNA FLJ32936 fis, clone TESTI2007533, highly similar to RuvB-like 2 (EC 3.6.1.-) 
Gene Name
 RUVBL2 
Gene Synonyms/Alias
 hCG_16214 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
115GTGSKVGKLTLKTTEubiquitination[1]
119KVGKLTLKTTEMETIubiquitination[1, 2, 3, 4]
132TIYDLGTKMIESLTKubiquitination[1]
139KMIESLTKDKVQAGDubiquitination[1, 2]
141IESLTKDKVQAGDVIubiquitination[1, 2, 5]
152GDVITIDKATGKISKubiquitination[1, 2, 5, 6]
178DAMGSQTKFVQCPDGubiquitination[1, 3, 4, 5, 7]
189CPDGELQKRKEVVHTubiquitination[1, 2, 3, 4, 5]
191DGELQKRKEVVHTVSubiquitination[1]
224SGDTGEIKSEVREQIubiquitination[1, 2, 3, 7]
234VREQINAKVAEWREEubiquitination[1, 2, 3, 5, 7]
320STTPYSEKDTKQILRacetylation[5, 8]
320STTPYSEKDTKQILRubiquitination[1, 2, 3, 4, 5, 7]
323PYSEKDTKQILRIRCubiquitination[1, 2, 5]
372SLVCRKRKGTEVQVDubiquitination[1, 2, 5]
382EVQVDDIKRVYSLFLacetylation[8]
382EVQVDDIKRVYSLFLubiquitination[1, 2, 3, 4, 5, 6, 7, 9]
399SRSTQYMKEYQDAFLubiquitination[1, 2, 3, 4, 7]
411AFLFNELKGETMDTSubiquitination[1, 2, 3, 4, 7]
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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 418 AA 
Protein Sequence
MVGQLAARRA AGVVLEMIRE GKIAGRAVLI AGQPGTGKTA IAMGMAQALG PDTPFTAIAG 60
SEIFSLEMSK TEALTQAFRR SIGVRIKEET EIIEGEVVEI QIDRPATGTG SKVGKLTLKT 120
TEMETIYDLG TKMIESLTKD KVQAGDVITI DKATGKISKL GRSFTRARDY DAMGSQTKFV 180
QCPDGELQKR KEVVHTVSLH EIDVINSRTQ GFLALFSGDT GEIKSEVREQ INAKVAEWRE 240
EGKAEIIPGV LFIDEVHMLD IESFSFLNRA LESDMAPVLI MATNRGITRI RGTSYQSPHG 300
IPIDLLDRLL IVSTTPYSEK DTKQILRIRC EEEDVEMSED AYTVLTRIGL ETSLRYAIQL 360
ITAASLVCRK RKGTEVQVDD IKRVYSLFLD ESRSTQYMKE YQDAFLFNEL KGETMDTS 418 
Gene Ontology
 GO:0031011; C:Ino80 complex; IEA:InterPro.
 GO:0030529; C:ribonucleoprotein complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006281; P:DNA repair; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR004504; DNA_repair_RadA.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase.
 IPR027238; RuvB-like.
 IPR010339; TIP49_C. 
Pfam
 PF06068; TIP49 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS
 PR01874; DNAREPAIRADA.