CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023755
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome maturation protein SBDS 
Protein Synonyms/Alias
 Shwachman-Bodian-Diamond syndrome protein 
Gene Name
 SBDS 
Gene Synonyms/Alias
 CGI-97 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
62SVFVNVSKGQVAKKEubiquitination[1, 2]
90ICKQILTKGEVQVSDubiquitination[1, 2, 3]
98GEVQVSDKERHTQLEacetylation[4]
98GEVQVSDKERHTQLEubiquitination[1, 2, 3]
118IATIVADKCVNPETKubiquitination[3]
125KCVNPETKRPYTVILubiquitination[3]
151VKTNKSTKQQALEVIubiquitination[3]
159QQALEVIKQLKEKMKubiquitination[1, 2, 3]
225REIDELIKKETKGKGacetylation[4]
225REIDELIKKETKGKGubiquitination[5]
248DVEEGDEKFE*****ubiquitination[6]
Reference
 [1] 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]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFTUD1, triggers the GTP- dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Nucleus; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 250 AA 
Protein Sequence
MSIFTPTNQI RLTNVAVVRM KRAGKRFEIA CYKNKVVGWR SGVEKDLDEV LQTHSVFVNV 60
SKGQVAKKED LISAFGTDDQ TEICKQILTK GEVQVSDKER HTQLEQMFRD IATIVADKCV 120
NPETKRPYTV ILIERAMKDI HYSVKTNKST KQQALEVIKQ LKEKMKIERA HMRLRFILPV 180
NEGKKLKEKL KPLIKVIESE DYGQQLEIVC LIDPGCFREI DELIKKETKG KGSLEVLNLK 240
DVEEGDEKFE 250 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0043022; F:ribosome binding; IDA:UniProtKB.
 GO:0019843; F:rRNA binding; IDA:UniProtKB.
 GO:0048539; P:bone marrow development; IMP:UniProtKB.
 GO:0030282; P:bone mineralization; IMP:UniProtKB.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0001833; P:inner cell mass cell proliferation; IEA:Compara.
 GO:0030595; P:leukocyte chemotaxis; IDA:UniProtKB.
 GO:0042256; P:mature ribosome assembly; IDA:UniProtKB.
 GO:0043148; P:mitotic spindle stabilization; IDA:UniProtKB.
 GO:0042273; P:ribosomal large subunit biogenesis; IBA:RefGenome.
 GO:0006364; P:rRNA processing; IMP:UniProtKB. 
Interpro
 IPR018978; Ribosome_mat_SBDS_C.
 IPR018023; Ribosome_mat_SBDS_CS.
 IPR019783; Ribosome_mat_SBDS_N.
 IPR002140; Ribosome_maturation_pr_SBDS. 
Pfam
 PF01172; SBDS
 PF09377; SBDS_C 
SMART
  
PROSITE
 PS01267; UPF0023 
PRINTS