CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028842
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Ribosome-binding protein 1 
Protein Synonyms/Alias
  
Gene Name
 Rrbp1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
97PNVTIILKEPVRVSAubiquitination[1]
131VPAMPQEKLASSPKDubiquitination[1]
148KKEKKVAKVEPAVSSubiquitination[1]
166SIQVLASKSAILEATubiquitination[1]
175AILEATPKEVPMVAVubiquitination[1]
188AVPPVGSKASSPATSubiquitination[1]
199PATSSQGKKGQGAQNacetylation[2]
219EGAQNQGKKGEGAQNacetylation[2]
229EGAQNQAKKGEGAQNubiquitination[1]
349EGGQNQAKKGEGAQNubiquitination[1]
530EGPQNQAKKGEGAQNubiquitination[1]
611TVANQGTKQEGVSNQubiquitination[1]
671MAPAQGQKASMVQSQubiquitination[1]
682VQSQEAPKQDAPAKKubiquitination[1]
696KKSGSRKKGEPGPPDubiquitination[1]
739LIEILSEKTGVIQDTubiquitination[1]
753TWHKATQKGDPVAILubiquitination[1]
761GDPVAILKRQLEEKEacetylation[3]
761GDPVAILKRQLEEKEubiquitination[1]
769RQLEEKEKLLATEQEubiquitination[1]
782QEDAAVAKSKLRELNubiquitination[1]
833ASYRDHVKEVQQLQGubiquitination[1]
841EVQQLQGKIRTLQEQubiquitination[1]
881ATSQVESKQNTELAKubiquitination[1]
888KQNTELAKLRQELSKubiquitination[1]
920QRKALEAKAATFEKQubiquitination[1]
926AKAATFEKQVLQLQAacetylation[3, 4]
983RVAELHSKLQSSEVEubiquitination[1]
992QSSEVEVKSKCEELSacetylation[2]
994SEVEVKSKCEELSSLacetylation[3, 5, 6]
1006SSLHGQLKEARAENSubiquitination[1]
1049NQQQTRLKELESQVSacetylation[3]
1085DLREKNWKAMEALALubiquitination[1]
1158KGSELLKKPPTLEPSubiquitination[1]
1201AETEGMLKDLQKSVEubiquitination[1]
1205GMLKDLQKSVEEEERubiquitination[1]
1217EERVWKAKVGAAEEEubiquitination[1]
1227AAEEELHKSRVTVKHubiquitination[1]
1233HKSRVTVKHLEDIVEubiquitination[1]
1241HLEDIVEKLKGELESubiquitination[1]
1243EDIVEKLKGELESSDubiquitination[1]
1299QSQLDEAKSEAQKQSubiquitination[1]
1304EAKSEAQKQSDELALubiquitination[1]
1345EQDPMKLKTQLERTEubiquitination[1]
1364AEQTRRQKLTAEFEEubiquitination[1]
1423DLGRAAIKLQELLKTacetylation[3]
1423DLGRAAIKLQELLKTubiquitination[1]
1429IKLQELLKTTQEQLTubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1464 AA 
Protein Sequence
MDIYDTQTLG VVVFGGFMVV SAIGIFLVST FSMKETSYEE ALANQRKEMA KTHHQKGEKK 60
KKEKTVEKKG KTKKKEEKPN GKIPEHDLDP NVTIILKEPV RVSAVAVAPT SVHSSVGHTP 120
IATVPAMPQE KLASSPKDRK KKEKKVAKVE PAVSSIVNSI QVLASKSAIL EATPKEVPMV 180
AVPPVGSKAS SPATSSQGKK GQGAQNQAKK GEGAQNQGKK GEGAQNQAKK GEGAQNQAKK 240
GEGAQNQGKK GEGAQNQAKK GEGGQNQAKK GEGAQNQGKK GEGAQNQGKK GEGAQNQAKK 300
GEGAQNQAKK GEGAQNQGKK GEGAQNQSKK GEGAQNQAKK GEGGQNQAKK GEGAQNQAKK 360
GEGAQNQAKK GEGVQNQAKK GVEGAQNQGK KGEANQNQAK KGEGGQNQTK KGEGPQNQGK 420
KGEAAQKQDK KIEGAQNQGK KPEGTSNQGK KGEGAQNQGK KGEGAQNQGK KGEGAQNQGK 480
KGEGAQNQGK KGEGAQNQGK KGEGAQNQGK KGEGAQNQGK KGEGPQNQAK KGEGAQNQGK 540
KGEGAQNQGK KGEGAQNQGK KAEGVQSQSK KGEGTQNQGK KGDGNPNQGK KGEGASNQNR 600
KTDTVANQGT KQEGVSNQVK KSEGSPNQGK KAEGAPNQGK KKDGSPSQAK KVDAAANQGK 660
KSEMAPAQGQ KASMVQSQEA PKQDAPAKKK SGSRKKGEPG PPDCDGPLFL PYKTLVSTVG 720
SMVFSEGEAQ RLIEILSEKT GVIQDTWHKA TQKGDPVAIL KRQLEEKEKL LATEQEDAAV 780
AKSKLRELNK EMASEKAKAA AGEAKVKKQL VAREQEIAAV QARMQASYRD HVKEVQQLQG 840
KIRTLQEQLE NGPNTQLARL QQENSILRDA LNQATSQVES KQNTELAKLR QELSKVNKEL 900
VEKSEASRQE EQQRKALEAK AATFEKQVLQ LQASHKESEE ALQKRLEEVT RELCRAQTSH 960
ANLRADAEKA QEQQQRVAEL HSKLQSSEVE VKSKCEELSS LHGQLKEARA ENSQLTERIR 1020
SIEALLEAGQ AQDTQASHAE ANQQQTRLKE LESQVSCLEK ETSELKEAME QQKGKNNDLR 1080
EKNWKAMEAL ALAERACEEK LRSLTQAKEE SEKQLHLAEA QTKETLLALL PGLSISAHQN 1140
YAEWLQEFKE KGSELLKKPP TLEPSMDIVL KLREAEETQN SLQAECDQYR TILAETEGML 1200
KDLQKSVEEE ERVWKAKVGA AEEELHKSRV TVKHLEDIVE KLKGELESSD QVREHTSHLE 1260
AELEKHMAAA SAECQNYAKE VAGLRQLLLE SQSQLDEAKS EAQKQSDELA LVRQQLSDMR 1320
SHVEDGDVAG SPAVPPAEQD PMKLKTQLER TEATLEAEQT RRQKLTAEFE EAQRTACRIQ 1380
EELEKLRAAG PLESSGKEEI TQLKERLEKE KRLTSDLGRA AIKLQELLKT TQEQLTKEKD 1440
TVKKLQEQLG KAEDGSSSKE GTSV 1464 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:InterPro.
 GO:0015031; P:protein transport; IEA:InterPro. 
Interpro
 IPR007794; Rib_rcpt_KP. 
Pfam
 PF05104; Rib_recp_KP_reg 
SMART
  
PROSITE
  
PRINTS