CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011777
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Something about silencing protein 10 
Protein Synonyms/Alias
 U three protein 3; U3 small nucleolar RNA-associated protein 3; U3 snoRNA-associated protein 11 
Gene Name
 SAS10 
Gene Synonyms/Alias
 UTP3; YDL153C; D1545 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
10RKGSNRTKTSEVGDEacetylation[1]
422TLRFYTSKIDQQENKacetylation[2]
524VIAAREGKLAELAENacetylation[2]
546AINYQILKNKGLTPKacetylation[2]
Reference
 [1] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Primarily required at the G2/M phase. Essential for viability: involved in nucleolar processing of pre-18S ribosomal RNA as part of the ribosomal small subunit (SSU) processome. 
Sequence Annotation
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 314 314 Phosphoserine.
 MOD_RES 316 316 Phosphoserine.
 MOD_RES 336 336 Phosphoserine.
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 477 477 Phosphoserine.  
Keyword
 Cell cycle; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 610 AA 
Protein Sequence
MVRKGSNRTK TSEVGDEINP YGLNEVDDFA SKREKVLLGQ STFGDSNKDD DHSLLEDEDE 60
EEVLAMDEDD ESIDEREDEE EEEEEELDGA AAYKKIFGRN LETDQLPEED EENGMLDNEN 120
AWGSTKGEYY GADDLDDDEA AKEIEKEALR QQKKHLEELN MNDYLDEEEE EEWVKSAKEF 180
DMGEFKNSTK QADTKTSITD ILNMDDEARD NYLRTMFPEF APLSKEFTEL APKFDELKKS 240
EENEFNKLKL IALGSYLGTI SCYYSILLHE LHNNEDFTSM KGHPVMEKIL TTKEIWRQAS 300
ELPSSFDVNE GDGSESEETA NIEAFNEKKL NELQNSEDSD AEDGGKQKQE IDEEERESDE 360
EEEEEDVDID DFEEYVAQSR LHSKPKTSSM PEADDFIESE IADVDAQDKK ARRRTLRFYT 420
SKIDQQENKK TDRFKGDDDI PYKERLFERQ QRLLDEARKR GMHDNNGADL DDKDYGSEDE 480
AVSRSINTQG ENDYYQQVQR GKQDKKISRK EAHKNAVIAA REGKLAELAE NVSGDGKRAI 540
NYQILKNKGL TPKRNKDNRN SRVKKRKKYQ KAQKKLKSVR AVYSGGQSGV YEGEKTGIKK 600
GLTRSVKFKN 610 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0032040; C:small-subunit processome; IDA:SGD.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
 GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. 
Interpro
 IPR007146; Sas10/Utp3/C1D.
 IPR018972; Sas10_C_dom. 
Pfam
 PF04000; Sas10_Utp3
 PF09368; Sas10_Utp3_C 
SMART
  
PROSITE
  
PRINTS