CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-025137
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Staphylococcal nuclease domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 Snd1 
Gene Synonyms/Alias
 AL033314 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
177SHTIRDLKYTIENPRacetylation[1]
177SHTIRDLKYTIENPRubiquitination[2]
193FVDSHHQKPVNAIIEacetylation[1, 3]
249EPFAAEAKFFTESRLubiquitination[2]
346KDKQFVAKVMQVLNAacetylation[1]
389NIQDKNKKLRPLYDIubiquitination[2]
414RKKLIGKKVNVTVDYubiquitination[2]
491ARAIKNGKGLHSKKEacetylation[3]
513DISGDTQKAKQFLPFubiquitination[2]
515SGDTQKAKQFLPFLQacetylation[1]
515SGDTQKAKQFLPFLQubiquitination[2]
541VFSGSRLKLYLPKETacetylation[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 608 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 QRELLEINHG 600
PKISNGKF 608 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004518; F:nuclease activity; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. 
Interpro
 IPR016071; Staphylococal_nuclease_OB-fold.
 IPR006021; Staphylococcal_nuclease.
 IPR002071; Thermonucl_AS. 
Pfam
 PF00565; SNase 
SMART
 SM00318; SNc 
PROSITE
 PS01284; TNASE_2
 PS50830; TNASE_3 
PRINTS