CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015687
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Staphylococcal nuclease domain-containing protein 1 
Protein Synonyms/Alias
 100 kDa coactivator; p100 co-activator 
Gene Name
 Snd1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
339PTANLDQKDKQFVAKacetylation[1]
641AERSAYYKPLLSAEEacetylation[1, 2, 3, 4]
641AERSAYYKPLLSAEEubiquitination[5]
752WYRARVEKVESPAKVacetylation[1, 3]
873RKEKQFQKVITEYLNubiquitination[5]
886LNAQESAKSARLNLWubiquitination[5]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Plays a role in cell viability (By similarity). Functions as a transcriptional coactivator for STAT5. 
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 (By similarity).
 MOD_RES 193 193 N6-acetyllysine (By similarity).
 MOD_RES 641 641 N6-acetyllysine (By similarity).
 MOD_RES 909 909 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 910 AA 
Protein Sequence
MASSAQSSGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA 60
RRAAATQPDG KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG 120
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKASK KGMWSEGNGS HTIRDLKYTI 180
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPGHHLVT VMLSGIKCPT FRRETDGSET 240
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNLLGTILHP NGNITELLLK EGFARCVDWS 300
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV PPTANLDQKD KQFVAKVMQV LNADAIVVKL 360
NSGDYKTIHL SSIRPPRLEG DNIQDKNKKL 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 LHMDGANLSV LLVEQALSKV HFTAERSAYY KPLLSAEEAA KQRKEKVWAH 660
YEERPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDISS 720
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKVH VFYIDYGNRE ILPSTRLGTL 780
PPAFSTRVLP AQATEYAFAF IQVPQDEDAR TDAVDSVVRD IQNTQCLLNV EHLSASCPHV 840
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA 900
DDADEFGYSR 910 
Gene Ontology
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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: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. 
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