CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004687
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein SON 
Protein Synonyms/Alias
 Bax antagonist selected in saccharomyces 1; BASS1; Negative regulatory element-binding protein; NRE-binding protein; Protein DBP-5; SON3 
Gene Name
 SON 
Gene Synonyms/Alias
 C21orf50; DBP5; KIAA1019; NREBP; HSPC310; HSPC312 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16FRSFVVSKFREIQQEacetylation[1]
16FRSFVVSKFREIQQEubiquitination[2]
80LDTELRYKPDLKEGSubiquitination[3, 4]
84LRYKPDLKEGSRKSRubiquitination[3, 4]
117KHKKHKNKKKKKKKEacetylation[5]
206PHILETLKPATKTAEacetylation[5]
277YQMKSVLKSVESTSPubiquitination[4]
288STSPEPSKIMLVEPPacetylation[1, 4, 6, 7]
2055KRLTDLDKAQLLEIAacetylation[1, 8]
2173KSQVTLTKEFPVSSGubiquitination[2]
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] 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]
 [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] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [6] 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]
 [7] 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]
 [8] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 
Functional Description
 RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'- GA[GT]AN[CG][AG]CC-3'. May indirectly repress hepatitis B virus (HBV) core promoter activity and transcription of HBV genes and production of HBV virions. 
Sequence Annotation
 REPEAT 1006 1011 1-1.
 REPEAT 1014 1019 1-2.
 REPEAT 1021 1026 1-3.
 REPEAT 1030 1035 1-4.
 REPEAT 1038 1043 1-5.
 REPEAT 1046 1051 1-6.
 REPEAT 1055 1060 1-7.
 REPEAT 1063 1068 1-8.
 REPEAT 1071 1076 1-9.
 REPEAT 1080 1085 1-10.
 REPEAT 1089 1094 1-11.
 REPEAT 1100 1105 1-12.
 REPEAT 1111 1116 1-13.
 REPEAT 1121 1126 1-14.
 REPEAT 1925 1931 2-1.
 REPEAT 1934 1952 3-1.
 REPEAT 1953 1959 2-2.
 REPEAT 1960 1966 2-3.
 REPEAT 1967 1973 2-4.
 REPEAT 1974 1980 2-5.
 REPEAT 1981 1987 2-6.
 REPEAT 1988 1994 2-7.
 REPEAT 1995 2013 3-2.
 DOMAIN 2305 2351 G-patch.
 DOMAIN 2371 2426 DRBM.
 REGION 726 895 17 X 10 AA tandem repeats of L-A-[ST]-
 REGION 912 988 11 X 7 AA tandem repeats of [DR]-P-Y-R-
 REGION 1006 1126 14 X 6 AA repeats of [ED]-R-S-M-M-S.
 REGION 1147 1179 3 X 11 AA tandem repats of P-P-L-P-P-E-E-
 REGION 1359 1390 4 X 8 AA tandem repeats of V-L-E-SS-
 REGION 1925 1994 7 X 7 AA repeats of P-S-R-R-S-R-[TS].
 REGION 1934 2013 2 X 19 AA repeats of P-S-R-R-R-R-S-R-S-V-
 REGION 2013 2039 3 X tandem repeats of [ST]-P-[VLI]-R-
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 16 16 N6-acetyllysine.
 MOD_RES 94 94 Phosphoserine.
 MOD_RES 142 142 Phosphoserine.
 MOD_RES 152 152 Phosphoserine.
 MOD_RES 154 154 Phosphoserine.
 MOD_RES 160 160 Phosphoserine.
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 288 288 N6-acetyllysine.
 MOD_RES 1556 1556 Phosphoserine.
 MOD_RES 1688 1688 Phosphoserine (By similarity).
 MOD_RES 1697 1697 Phosphoserine.
 MOD_RES 1769 1769 Phosphoserine.
 MOD_RES 1783 1783 Phosphoserine.
 MOD_RES 1784 1784 Phosphoserine (By similarity).
 MOD_RES 1820 1820 Phosphoserine (By similarity).
 MOD_RES 1821 1821 Phosphoserine (By similarity).
 MOD_RES 1824 1824 Phosphoserine (By similarity).
 MOD_RES 1948 1948 Phosphoserine.
 MOD_RES 1950 1950 Phosphoserine.
 MOD_RES 1961 1961 Phosphoserine (By similarity).
 MOD_RES 2009 2009 Phosphoserine.
 MOD_RES 2011 2011 Phosphoserine.
 MOD_RES 2013 2013 Phosphoserine.
 MOD_RES 2055 2055 N6-acetyllysine.
 MOD_RES 2163 2163 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Complete proteome; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2426 AA 
Protein Sequence
MATNIEQIFR SFVVSKFREI QQELSSGRNE GQLNGETNTP IEGNQAGDAA ASARSLPNEE 60
IVQKIEEVLS GVLDTELRYK PDLKEGSRKS RCVSVQTDPT DEIPTKKSKK HKKHKNKKKK 120
KKKEKEKKYK RQPEESESKT KSHDDGNIDL ESDSFLKFDS EPSAVALELP TRAFGPSETN 180
ESPAVVLEPP VVSMEVSEPH ILETLKPATK TAELSVVSTS VISEQSEQSV AVMPEPSMTK 240
ILDSFAAAPV PTTTLVLKSS EPVVTMSVEY QMKSVLKSVE STSPEPSKIM LVEPPVAKVL 300
EPSETLVVSS ETPTEVYPEP STSTTMDFPE SSAIEALRLP EQPVDVPSEI ADSSMTRPQE 360
LPELPKTTAL ELQESSVASA MELPGPPATS MPELQGPPVT PVLELPGPSA TPVPELPGPL 420
STPVPELPGP PATAVPELPG PSVTPVPQLS QELPGLPAPS MGLEPPQEVP EPPVMAQELP 480
GLPLVTAAVE LPEQPAVTVA MELTEQPVTT TELEQPVGMT TVEHPGHPEV TTATGLLGQP 540
EATMVLELPG QPVATTALEL PGQPSVTGVP ELPGLPSATR ALELSGQPVA TGALELPGPL 600
MAAGALEFSG QSGAAGALEL LGQPLATGVL ELPGQPGAPE LPGQPVATVA LEISVQSVVT 660
TSELSTMTVS QSLEVPSTTA LESYNTVAQE LPTTLVGETS VTVGVDPLMA PESHILASNT 720
METHILASNT MDSQMLASNT MDSQMLASNT MDSQMLASST MDSQMLATSS MDSQMLATSS 780
MDSQMLATST MDSQMLATSS MDSQMLATSS MDSQMLATSS MDSQMLATSS MDSQMLATST 840
MDSQMLATST MDSQMLATSS MDSQMLASGT MDSQMLASGT MDAQMLASGT MDAQMLASST 900
QDSAMLGSKS PDPYRLAQDP YRLAQDPYRL GHDPYRLGHD AYRLGQDPYR LGHDPYRLTP 960
DPYRMSPRPY RIAPRSYRIA PRPYRLAPRP LMLASRRSMM MSYAAERSMM SSYERSMMSY 1020
ERSMMSPMAE RSMMSAYERS MMSAYERSMM SPMAERSMMS AYERSMMSAY ERSMMSPMAD 1080
RSMMSMGADR SMMSSYSAAD RSMMSSYSAA DRSMMSSYTA DRSMMSMAAD SYTDSYTDTY 1140
TEAYMVPPLP PEEPPTMPPL PPEEPPMTPP LPPEEPPEGP ALPTEQSALT AENTWPTEVP 1200
SSPSEESVSQ PEPPVSQSEI SEPSAVPTDY SVSASDPSVL VSEAAVTVPE PPPEPESSIT 1260
LTPVESAVVA EEHEVVPERP VTCMVSETPA MSAEPTVLAS EPPVMSETAE TFDSMRASGH 1320
VASEVSTSLL VPAVTTPVLA ESILEPPAMA APESSAMAVL ESSAVTVLES STVTVLESST 1380
VTVLEPSVVT VPEPPVVAEP DYVTIPVPVV SALEPSVPVL EPAVSVLQPS MIVSEPSVSV 1440
QESTVTVSEP AVTVSEQTQV IPTEVAIEST PMILESSIMS SHVMKGINLS SGDQNLAPEI 1500
GMQEIALHSG EEPHAEEHLK GDFYESEHGI NIDLNINNHL IAKEMEHNTV CAAGTSPVGE 1560
IGEEKILPTS ETKQRTVLDT YPGVSEADAG ETLSSTGPFA LEPDATGTSK GIEFTTASTL 1620
SLVNKYDVDL SLTTQDTEHD MVISTSPSGG SEADIEGPLP AKDIHLDLPS NNNLVSKDTE 1680
EPLPVKESDQ TLAALLSPKE SSGGEKEVPP PPKETLPDSG FSANIEDINE ADLVRPLLPK 1740
DMERLTSLRA GIEGPLLASD VGRDRSAASP VVSSMPERAS ESSSEEKDDY EIFVKVKDTH 1800
EKSKKNKNRD KGEKEKKRDS SLRSRSKRSK SSEHKSRKRT SESRSRARKR SSKSKSHRSQ 1860
TRSRSRSRRR RRSSRSRSKS RGRRSVSKEK RKRSPKHRSK SRERKRKRSS SRDNRKTVRA 1920
RSRTPSRRSR SHTPSRRRRS RSVGRRRSFS ISPSRRSRTP SRRSRTPSRR SRTPSRRSRT 1980
PSRRSRTPSR RSRTPSRRRR SRSVVRRRSF SISPVRLRRS RTPLRRRFSR SPIRRKRSRS 2040
SERGRSPKRL TDLDKAQLLE IAKANAAAMC AKAGVPLPPN LKPAPPPTIE EKVAKKSGGA 2100
TIEELTEKCK QIAQSKEDDD VIVNKPHVSD EEEEEPPFYH HPFKLSEPKP IFFNLNIAAA 2160
KPTPPKSQVT LTKEFPVSSG SQHRKKEADS VYGEWVPVEK NGEENKDDDN VFSSNLPSEP 2220
VDISTAMSER ALAQKRLSEN AFDLEAMSML NRAQERIDAW AQLNSIPGQF TGSTGVQVLT 2280
QEQLANTGAQ AWIKKDQFLR AAPVTGGMGA VLMRKMGWRE GEGLGKNKEG NKEPILVDFK 2340
TDRKGLVAVG ERAQKRSGNF SAAMKDLSGK HPVSALMEIC NKRRWQPPEF LLVHDSGPDH 2400
RKHFLFRVLR NGALTRPNCM FFLNRY 2426 
Gene Ontology
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
 GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR000467; G_patch_dom. 
Pfam
 PF01585; G-patch 
SMART
 SM00443; G_patch 
PROSITE
 PS50137; DS_RBD
 PS50174; G_PATCH 
PRINTS