CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015733
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Staphylococcal nuclease domain-containing protein 1 
Protein Synonyms/Alias
 100 kDa coactivator; EBNA2 coactivator p100; Tudor domain-containing protein 11; p100 co-activator 
Gene Name
 SND1 
Gene Synonyms/Alias
 TDRD11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71AATQPDAKDTPDEPWubiquitination[1, 2, 3, 4, 5]
93LRKKLIGKEVCFTIEubiquitination[3]
102VCFTIENKTPQGREYubiquitination[2, 3, 5, 6]
116YGMIYLGKDTNGENIubiquitination[2]
157SECEEQAKAAKKGMWubiquitination[3]
161EQAKAAKKGMWSEGNubiquitination[3]
177SHTIRDLKYTIENPRubiquitination[1, 2, 3, 5, 6, 7, 8]
193FVDSHHQKPVNAIIEacetylation[5, 9, 10]
193FVDSHHQKPVNAIIEubiquitination[2, 3, 7, 8]
249EPFAAEAKFFTESRLubiquitination[1, 2, 3, 4, 5, 7, 8, 11]
339PTANLDQKDKQFVAKacetylation[10]
339PTANLDQKDKQFVAKubiquitination[1]
341ANLDQKDKQFVAKVMubiquitination[3]
366KLNSGDYKTIHLSSIubiquitination[2, 7, 8]
389NTQDKNKKLRPLYDIubiquitination[3]
414RKKLIGKKVNVTVDYubiquitination[3]
497GKGLHSKKEVPIHRVubiquitination[3]
513DISGDTQKAKQFLPFubiquitination[1, 3, 6]
515SGDTQKAKQFLPFLQubiquitination[3, 7, 8]
641AERSSYYKSLLSAEEacetylation[9]
641AERSSYYKSLLSAEEubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 11]
676VMPVLEEKERSASYKubiquitination[2, 3, 4]
739RGEFCIAKFVDGEWYubiquitination[1, 3]
752WYRARVEKVESPAKIacetylation[9]
848TLQFADSKGDVGLGLubiquitination[1, 2]
857DVGLGLVKEGLVMVEubiquitination[1]
873RKEKQFQKVITEYLNubiquitination[1, 3]
886LNAQESAKSARLNLWubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 11, 12]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
 Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2). 
Sequence Annotation
 DOMAIN 18 166 TNase-like 1.
 DOMAIN 193 328 TNase-like 2.
 DOMAIN 341 496 TNase-like 3.
 DOMAIN 525 660 TNase-like 4.
 DOMAIN 729 787 Tudor.
 MOTIF 321 325 Nuclear localization signal (Potential).
 MOTIF 388 392 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 193 193 N6-acetyllysine.
 MOD_RES 641 641 N6-acetyllysine.
 MOD_RES 781 781 Phosphoserine.
 MOD_RES 909 909 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 910 AA 
Protein Sequence
MASSAQSGGS SGGPAVPTVQ RGIIKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA 60
RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG 120
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI 180
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET 240
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS 300
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV LNADAIVVKL 360
NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD 420
YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL 480
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL 540
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES 600
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSSYY KSLLSAEEAA KQKKEKVWAH 660
YEEQPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDIAS 720
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKIH VFYIDYGNRE VLPSTRLGTL 780
SPAFSTRVLP AQATEYAFAF IQVPQDDDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV 840
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA 900
DDADEFGYSR 910 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0016442; C:RNA-induced silencing complex; IEA:InterPro.
 GO:0004518; F:nuclease activity; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
 GO:0031047; P:gene silencing by RNA; IEA:InterPro.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016685; Silence_cplx_Nase-comp_TudorSN.
 IPR016071; Staphylococal_nuclease_OB-fold.
 IPR006021; Staphylococcal_nuclease.
 IPR002071; Thermonucl_AS.
 IPR002999; Tudor. 
Pfam
 PF00565; SNase
 PF00567; TUDOR 
SMART
 SM00318; SNc
 SM00333; TUDOR 
PROSITE
 PS01123; TNASE_1
 PS01284; TNASE_2
 PS50830; TNASE_3
 PS50304; TUDOR 
PRINTS