CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023592
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RuvB-like 2 
Protein Synonyms/Alias
 48 kDa TATA box-binding protein-interacting protein; 48 kDa TBP-interacting protein; 51 kDa erythrocyte cytosolic protein; ECP-51; INO80 complex subunit J; Repressing pontin 52; Reptin 52; TIP49b; TIP60-associated protein 54-beta; TAP54-beta 
Gene Name
 RUVBL2 
Gene Synonyms/Alias
 INO80J; TIP48; TIP49B; CGI-46 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9ATVTATTKVPEIRDVubiquitination[1, 2, 3, 4, 5]
67LEMIREGKIAGRAVLmethylation[6]
160GTGSKVGKLTLKTTEubiquitination[4]
164KVGKLTLKTTEMETIubiquitination[2, 4, 7]
177TIYDLGTKMIESLTKubiquitination[4]
184KMIESLTKDKVQAGDubiquitination[4, 7]
186IESLTKDKVQAGDVIubiquitination[4, 7]
197GDVITIDKATGKISKubiquitination[1, 4, 5, 7]
223DAMGSQTKFVQCPDGubiquitination[2, 4, 8]
234CPDGELQKRKEVVHTubiquitination[2, 4, 7, 9]
236DGELQKRKEVVHTVSubiquitination[4]
269SGDTGEIKSEVREQIubiquitination[4, 7, 8, 9]
279VREQINAKVAEWREEubiquitination[4, 7, 8]
365STTPYSEKDTKQILRubiquitination[2, 4, 7, 8]
368PYSEKDTKQILRIRCubiquitination[2, 4, 7]
415AASLVCRKRKGTEVQmethylation[10]
417SLVCRKRKGTEVQVDubiquitination[4, 7]
427EVQVDDIKRVYSLFLubiquitination[1, 2, 4, 5, 7, 8, 9]
444SRSTQYMKEYQDAFLubiquitination[2, 4, 7, 8]
456AFLFNELKGETMDTSsumoylation[11]
456AFLFNELKGETMDTSubiquitination[2, 4, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Negative regulation of hypoxic responses via induced Reptin methylation.
 Lee JS, Kim Y, Kim IS, Kim B, Choi HJ, Lee JM, Shin HJ, Kim JH, Kim JY, Seo SB, Lee H, Binda O, Gozani O, Semenza GL, Kim M, Kim KI, Hwang D, Baek SH.
 Mol Cell. 2010 Jul 9;39(1):71-85. [PMID: 20603076]
 [7] 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]
 [8] 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]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications.
 Pang CN, Gasteiger E, Wilkins MR.
 BMC Genomics. 2010 Feb 5;11:92. [PMID: 20137074]
 [11] Roles of sumoylation of a reptin chromatin-remodelling complex in cancer metastasis.
 Kim JH, Choi HJ, Kim B, Kim MH, Lee JM, Kim IS, Lee MH, Choi SJ, Kim KI, Kim SI, Chung CH, Baek SH.
 Nat Cell Biol. 2006 Jun;8(6):631-9. [PMID: 16699503] 
Functional Description
 Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. 
Sequence Annotation
 NP_BIND 77 84 ATP.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Activator; ATP-binding; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; Growth regulation; Helicase; Hydrolase; Membrane; Nucleotide-binding; Nucleus; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL 60
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT 120
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE 180
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH 240
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 300
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT 360
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE 420
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS 463 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0031011; C:Ino80 complex; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
 GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0042802; F:identical protein binding; IDA:UniProtKB.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0034644; P:cellular response to UV; IMP:UniProtKB.
 GO:0006310; P:DNA recombination; TAS:ProtInc.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
 GO:0006457; P:protein folding; TAS:ProtInc.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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.