CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043851
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein SON 
Protein Synonyms/Alias
  
Gene Name
 SON 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1050KRLTDLDKAQLLEIAacetylation[1, 2, 3]
1156NLNIAAAKPTPPKSQubiquitination[4]
1168KSQVTLTKEFPVSSGubiquitination[3, 5]
1339VDFKTDRKGLVAVGEubiquitination[3, 4]
1365AMKDLSGKHPVSALMubiquitination[4, 6]
1377ALMEICNKRRWQPPEubiquitination[4, 6, 7]
1397DSGPDHRKHFLFRVLubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1454 AA 
Protein Sequence
XRSMMSSYER SMMSYERSMM SPMAERSMMS AYERSMMSAY ERSMMSPMAE RSMMSAYERS 60
MMSAYERSMM SPMADRSMMS MGADRSMMSS YSAADRSMMS SYSAADRSMM SSYTADRSMM 120
SMAADSYTDS YTDTYTEAYM VPPLPPEEPP TMPPLPPEEP PMTPPLPPEE PPEGPALPTE 180
QSALTAENTW PTEVPSSPSE ESVSQPEPPV SQSEISEPSA VPTDYSVSAS DPSVLVSEAA 240
VTVPEPPPEP ESSITLTPVE SAVVAEEHEV VPERPVTCMV SETPAMSAEP TVLASEPPVM 300
SETAETFDSM RASGHVASEV STSLLVPAVT TPVLAESILE PPAMAAPESS AMAVLESSAV 360
TVLESSTVTV LESSTVTVLE PSVVTVPEPP VVAEPDYVTI PVPVVSALEP SVPVLEPAVS 420
VLQPSMIVSE PSVSVQESTV TVSEPAVTVS EQTQVIPTEV AIESTPMILE SSIMSSHVMK 480
GINLSSGDQN LAPEIGMQEI ALHSGEEPHA EEHLKGDFYE SEHGINIDLN INNHLIAKEM 540
EHNTVCAAGT SPVGEIGEEK ILPTSETKQR TVLDTYPGVS EADAGETLSS TGPFALEPDA 600
TGTSKGIEFT TASTLSLVNK YDVDLSLTTQ DTEHDMVIST SPSGGSEADI EGPLPAKDIH 660
LDLPSNNNLV SKDTEEPLPV KESDQTLAAL LSPKESSGGE KEVPPPPKET LPDSGFSANI 720
EDINEADLVR PLLPKDMERL TSLRAGIEGP LLASDVGRDR SAASPVVSSM PERASESSSE 780
EKDDYEIFVK VKDTHEKSKK NKNRDKGEKE KKRDSSLRSR SKRSKSSEHK SRKRTSESRS 840
RARKRSSKSK SHRSQTRSRS RSRRRRRSSR SRSKSRGRRS VSKEKRKRSP KHRSKSRERK 900
RKRSSSRDNR KTVRARSRTP SRRSRSHTPS RRRRSRSVGR RRSFSISPSR RSRTPSRRSR 960
TPSRRSRTPS RRSRTPSRRS RTPSRRSRTP SRRRRSRSVV RRRSFSISPV RLRRSRTPLR 1020
RRFSRSPIRR KRSRSSERGR SPKRLTDLDK AQLLEIAKAN AAAMCAKAGV PLPPNLKPAP 1080
PPTIEEKVAK KSGGATIEEL TEKCKQIAQS KEDDDVIVNK PHVSDEEEEE PPFYHHPFKL 1140
SEPKPIFFNL NIAAAKPTPP KSQVTLTKEF PVSSGSQHRK KEADSVYGEW VPVEKNGEEN 1200
KDDDNVFSSN LPSEPVDIST AMSERALAQK RLSENAFDLE AMSMLNRAQE RIDAWAQLNS 1260
IPGQFTGSTG VQVLTQEQLA NTGAQAWIKK DQFLRAAPVT GGMGAVLMRK MGWREGEGLG 1320
KNKEGNKEPI LVDFKTDRKG LVAVGERAQK RSGNFSAAMK DLSGKHPVSA LMEICNKRRW 1380
QPPEFLLVHD SGPDHRKHFL FRVLINGSAY QPSFASPNKK HAKATAATVV LQAMGLVPKD 1440
LMANATCFRS ASRR 1454 
Gene Ontology
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR000467; G_patch_dom. 
Pfam
 PF00035; dsrm
 PF01585; G-patch 
SMART
 SM00358; DSRM
 SM00443; G_patch 
PROSITE
 PS50137; DS_RBD
 PS50174; G_PATCH 
PRINTS