CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015960
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RBBP6 
Protein Synonyms/Alias
 Proliferation potential-related protein; Protein P2P-R; Retinoblastoma-binding Q protein 1; RBQ-1; Retinoblastoma-binding protein 6; p53-associated cellular protein of testis 
Gene Name
 RBBP6 
Gene Synonyms/Alias
 P2PR; PACT; RBQ1; My038 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MSCVHYKFSSKLNYacetylation[1]
130ANASEEDKIKAMMSQacetylation[2]
843EWYEKYYKGYAAGAQubiquitination[3]
901IGSNYPEKLSARDGHubiquitination[4, 5, 6]
1571NPCKDREKHVLEARNacetylation[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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [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] 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]
 [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] 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
Functional Description
 E3 ubiquitin-protein ligase which promotes ubiquitination of YBX1, leading to its degradation by the proteasome. May play a role as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in increase of MDM2-mediated ubiquitination and degradation of p53/TP53; may function as negative regulator of p53/TP53, leading to both apoptosis and cell growth. 
Sequence Annotation
 DOMAIN 4 76 DWNN.
 ZN_FING 159 176 CCHC-type.
 ZN_FING 259 300 RING-type; degenerate.
 REGION 982 1139 Interaction with RB1 (By similarity).
 REGION 1433 1544 Interaction with p53 (By similarity).
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 245 245 Phosphoserine.
 MOD_RES 246 246 Phosphoserine.
 MOD_RES 247 247 Phosphoserine.
 MOD_RES 360 360 Phosphoserine.
 MOD_RES 516 516 Phosphoserine.
 MOD_RES 770 770 Phosphoserine.
 MOD_RES 772 772 Phosphoserine.
 MOD_RES 780 780 Phosphoserine.
 MOD_RES 861 861 Phosphoserine.
 MOD_RES 1179 1179 Phosphoserine.
 MOD_RES 1271 1271 Phosphothreonine (By similarity).
 MOD_RES 1277 1277 Phosphoserine.
 MOD_RES 1328 1328 Phosphoserine.
 MOD_RES 1468 1468 Phosphothreonine.
 MOD_RES 1646 1646 Phosphoserine.
 MOD_RES 1648 1648 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1792 AA 
Protein Sequence
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADCDLQITN AQTKEEYTDD 60
NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPAMATTK AIDDSSASIS LAQLTKTANL 120
AEANASEEDK IKAMMSQSGH EYDPINYMKK PLGPPPPSYT CFRCGKPGHY IKNCPTNGDK 180
NFESGPRIKK STGIPRSFMM EVKDPNMKGA MLTNTGKYAI PTIDAEAYAI GKKEKPPFLP 240
EEPSSSSEED DPIPDELLCL ICKDIMTDAV VIPCCGNSYC DECIRTALLE SDEHTCPTCH 300
QNDVSPDALI ANKFLRQAVN NFKNETGYTK RLRKQLPPPP PPIPPPRPLI QRNLQPLMRS 360
PISRQQDPLM IPVTSSSTHP APSISSLTSN QSSLAPPVSG NPSSAPAPVP DITATVSISV 420
HSEKSDGPFR DSDNKILPAA ALASEHSKGT SSIAITALME EKGYQVPVLG TPSLLGQSLL 480
HGQLIPTTGP VRINTARPGG GRPGWEHSNK LGYLVSPPQQ IRRGERSCYR SINRGRHHSE 540
RSQRTQGPSL PATPVFVPVP PPPLYPPPPH TLPLPPGVPP PQFSPQFPPG QPPPAGYSVP 600
PPGFPPAPAN LSTPWVSSGV QTAHSNTIPT TQAPPLSREE FYREQRRLKE EEKKKSKLDE 660
FTNDFAKELM EYKKIQKERR RSFSRSKSPY SGSSYSRSSY TYSKSRSGST RSRSYSRSFS 720
RSHSRSYSRS PPYPRRGRGK SRNYRSRSRS HGYHRSRSRS PPYRRYHSRS RSPQAFRGQS 780
PNKRNVPQGE TEREYFNRYR EVPPPYDMKA YYGRSVDFRD PFEKERYREW ERKYREWYEK 840
YYKGYAAGAQ PRPSANRENF SPERFLPLNI RNSPFTRGRR EDYVGGQSHR SRNIGSNYPE 900
KLSARDGHNQ KDNTKSKEKE SENAPGDGKG NKHKKHRKRR KGEESEGFLN PELLETSRKS 960
REPTGVEENK TDSLFVLPSR DDATPVRDEP MDAESITFKS VSEKDKRERD KPKAKGDKTK 1020
RKNDGSAVSK KENIVKPAKG PQEKVDGERE RSPRSEPPIK KAKEETPKTD NTKSSSSSQK 1080
DEKITGTPRK AHSKSAKEHQ ETKPVKEEKV KKDYSKDVKS EKLTTKEEKA KKPNEKNKPL 1140
DNKGEKRKRK TEEKGVDKDF ESSSMKISKL EVTEIVKPSP KRKMEPDTEK MDRTPEKDKI 1200
SLSAPAKKIK LNRETGKKIG STENISNTKE PSEKLESTSS KVKQEKVKGK VRRKVTGTEG 1260
SSSTLVDYTS TSSTGGSPVR KSEEKTDTKR TVIKTMEEYN NDNTAPAEDV IIMIQVPQSK 1320
WDKDDFESEE EDVKSTQPIS SVGKPASVIK NVSTKPSNIV KYPEKESEPS EKIQKFTKDV 1380
SHEIIQHEVK SSKNSASSEK GKTKDRDYSV LEKENPEKRK NSTQPEKESN LDRLNEQGNF 1440
KSLSQSSKEA RTSDKHDSTR ASSNKDFTPN RDKKTDYDTR EYSSSKRRDE KNELTRRKDS 1500
PSRNKDSASG QKNKPREERD LPKKGTGDSK KSNSSPSRDR KPHDHKATYD TKRPNEETKS 1560
VDKNPCKDRE KHVLEARNNK ESSGNKLLYI LNPPETQVEK EQITGQIDKS TVKPKPQLSH 1620
SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEESSGN ISKDLKDKIV EKAKESLDTA 1680
AVVQVGISRN QSHSSPSVSP SRSHSPSGSQ TRSHSSSASS AESQDSKKKK KKKEKKKHKK 1740
HKKHKKHKKH AGTEVELEKS QKHKHKKKKS KKNKDKEKEK EKDDQKVKSV TV 1792 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB. 
Interpro
 IPR014891; DWNN_domain.
 IPR001878; Znf_CCHC.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF08783; DWNN
 PF00098; zf-CCHC 
SMART
 SM00184; RING
 SM00343; ZnF_C2HC 
PROSITE
 PS51282; DWNN
 PS50158; ZF_CCHC
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS