CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011247
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Single-stranded DNA-binding protein, mitochondrial 
Protein Synonyms/Alias
 Mt-SSB; MtSSB; PWP1-interacting protein 17 
Gene Name
 SSBP1 
Gene Synonyms/Alias
 SSBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51VLRQVEGKNPVTIFSubiquitination[1, 2, 3]
81QLGDVSQKTTWHRISubiquitination[1, 2, 3, 4, 5]
103DVAYQYVKKGSRIYLacetylation[6]
103DVAYQYVKKGSRIYLubiquitination[3]
104VAYQYVKKGSRIYLEubiquitination[2]
113SRIYLEGKIDYGEYMacetylation[6, 7]
122DYGEYMDKNNVRRQAubiquitination[1, 2, 3, 5]
145IFLSDQTKEKE****ubiquitination[2]
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] 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]
 [3] 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]
 [4] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [5] 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]
 [6] 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]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA. 
Sequence Annotation
 DOMAIN 30 141 SSB.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 113 113 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; DNA replication; DNA-binding; Mitochondrion; Mitochondrion nucleoid; Phosphoprotein; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 148 AA 
Protein Sequence
MFRRPVLQVL RQFVRHESET TTSLVLERSL NRVHLLGRVG QDPVLRQVEG KNPVTIFSLA 60
TNEMWRSGDS EVYQLGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYL EGKIDYGEYM 120
DKNNVRRQAT TIIADNIIFL SDQTKEKE 148 
Gene Ontology
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0070584; P:mitochondrion morphogenesis; IEA:Compara.
 GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR000424; Primosome_PriB/ssb.
 IPR011344; ssDNA-bd. 
Pfam
 PF00436; SSB 
SMART
  
PROSITE
 PS50935; SSB 
PRINTS