CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023611
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RuvB-like 1 
Protein Synonyms/Alias
 49 kDa TATA box-binding protein-interacting protein; 49 kDa TBP-interacting protein; 54 kDa erythrocyte cytosolic protein; ECP-54; INO80 complex subunit H; Nuclear matrix protein 238; NMP 238; Pontin 52; TIP49a; TIP60-associated protein 54-alpha; TAP54-alpha 
Gene Name
 RUVBL1 
Gene Synonyms/Alias
 INO80H; NMP238; TIP49; TIP49A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2******MKIEEVKSTacetylation[1, 2]
2******MKIEEVKSTubiquitination[3, 4]
7*MKIEEVKSTTKTQRubiquitination[5]
22IASHSHVKGLGLDESubiquitination[6, 7]
33LDESGLAKQAASGLVubiquitination[3, 5, 7, 8]
57GVIVELIKSKKMAGRubiquitination[3, 4]
76AGPPGTGKTALALAIubiquitination[3, 7]
171AKGTKQLKLDPSIFEubiquitination[3, 6, 7]
182SIFESLQKERVEAGDubiquitination[3, 7]
201EANSGAVKRQGRCDTubiquitination[7]
225EEYVPLPKGDVHKKKsumoylation[9]
274KKTEITDKLRGEINKubiquitination[3]
281KLRGEINKVVNKYIDubiquitination[7]
372LYTPQEMKQIIKIRAubiquitination[3]
400HLGEIGTKTTLRYSVubiquitination[3, 6, 7]
418TPANLLAKINGKDSIubiquitination[3]
445YDAKSSAKILADQQDubiquitination[7]
453ILADQQDKYMK****acetylation[1]
Reference
 [1] 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]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] 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]
 [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] 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]
 [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] 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] 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]
 [9] SUMOylation of pontin chromatin-remodeling complex reveals a signal integration code in prostate cancer cells.
 Kim JH, Lee JM, Nam HJ, Choi HJ, Yang JW, Lee JS, Kim MH, Kim SI, Chung CH, Kim KI, Baek SH.
 Proc Natl Acad Sci U S A. 2007 Dec 26;104(52):20793-8. [PMID: 18087039] 
Functional Description
 Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (3' to 5') 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 70 77 ATP (By similarity).
 MOD_RES 453 453 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding; Cell cycle; Cell division; Chromatin regulator; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; Growth regulation; Helicase; Hydrolase; Membrane; Mitosis; Nucleotide-binding; Nucleus; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK 60
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI 120
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL 180
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL 240
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF 300
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI 360
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN 420
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK 456 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0031011; C:Ino80 complex; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005815; C:microtubule organizing center; 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:0003678; F:DNA helicase activity; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0007283; P:spermatogenesis; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase.
 IPR027238; RuvB-like.
 IPR010339; TIP49_C. 
Pfam
 PF06068; TIP49 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS