SSBP_HUMAN
ID SSBP_HUMAN Reviewed; 148 AA.
AC Q04837;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE Short=Mt-SSB;
DE Short=MtSSB;
DE AltName: Full=PWP1-interacting protein 17;
DE Flags: Precursor;
GN Name=SSBP1; Synonyms=SSBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8482537; DOI=10.1016/0378-1119(93)90370-i;
RA Tiranti V., Rocchi M., Didonato S., Zeviani M.;
RT "Cloning of human and rat cDNAs encoding the mitochondrial single-stranded
RT DNA-binding protein (SSB).";
RL Gene 126:219-225(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Honore B.;
RT "hPWP1-interacting protein 17 (ssDNA BP).";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 17-29.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP FUNCTION.
RX PubMed=12975372; DOI=10.1074/jbc.m306981200;
RA Korhonen J.A., Gaspari M., Falkenberg M.;
RT "TWINKLE has 5' -> 3' DNA helicase activity and is specifically stimulated
RT by mitochondrial single-stranded DNA-binding protein.";
RL J. Biol. Chem. 278:48627-48632(2003).
RN [6]
RP FUNCTION.
RX PubMed=15167897; DOI=10.1038/sj.emboj.7600257;
RA Korhonen J.A., Pham X.H., Pellegrini M., Falkenberg M.;
RT "Reconstitution of a minimal mtDNA replisome in vitro.";
RL EMBO J. 23:2423-2429(2004).
RN [7]
RP INTERACTION WITH POLDIP2.
RX PubMed=16428295; DOI=10.1093/jb/mvi169;
RA Cheng X., Kanki T., Fukuoh A., Ohgaki K., Takeya R., Aoki Y., Hamasaki N.,
RA Kang D.;
RT "PDIP38 associates with proteins constituting the mitochondrial DNA
RT nucleoid.";
RL J. Biochem. 138:673-678(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18063578; DOI=10.1074/jbc.m708444200;
RA Bogenhagen D.F., Rousseau D., Burke S.;
RT "The layered structure of human mitochondrial DNA nucleoids.";
RL J. Biol. Chem. 283:3665-3675(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF 49-GLU--LYS-51; 67-SER--LEU-75;
RP 99-TYR-GLN-100; 116-TYR--GLU-118 AND 122-LYS--ASN-124.
RX PubMed=21953457; DOI=10.1074/jbc.m111.289983;
RA Oliveira M.T., Kaguni L.S.;
RT "Reduced stimulation of recombinant DNA polymerase gamma and mitochondrial
RT DNA (mtDNA) helicase by variants of mitochondrial single-stranded DNA-
RT binding protein (mtSSB) correlates with defects in mtDNA replication in
RT animal cells.";
RL J. Biol. Chem. 286:40649-40658(2011).
RN [13]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MPG.
RX PubMed=23290262; DOI=10.1016/j.dnarep.2012.11.009;
RA van Loon B., Samson L.D.;
RT "Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts
RT with mitochondrial single-stranded binding protein (mtSSB).";
RL DNA Repair 12:177-187(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION.
RX PubMed=26446790; DOI=10.1074/jbc.m115.673707;
RA Ciesielski G.L., Bermek O., Rosado-Ruiz F.A., Hovde S.L., Neitzke O.J.,
RA Griffith J.D., Kaguni L.S.;
RT "Mitochondrial Single-stranded DNA-binding Proteins Stimulate the Activity
RT of DNA Polymerase gamma by Organization of the Template DNA.";
RL J. Biol. Chem. 290:28697-28707(2015).
RN [17]
RP INTERACTION WITH PRIMPOL.
RX PubMed=25550423; DOI=10.1093/nar/gku1321;
RA Guilliam T.A., Jozwiakowski S.K., Ehlinger A., Barnes R.P., Rudd S.G.,
RA Bailey L.J., Skehel J.M., Eckert K.A., Chazin W.J., Doherty A.J.;
RT "Human PrimPol is a highly error-prone polymerase regulated by single-
RT stranded DNA binding proteins.";
RL Nucleic Acids Res. 43:1056-1068(2015).
RN [18]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER HIS-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-141.
RX PubMed=9033597; DOI=10.1038/nsb0297-153;
RA Yang C., Curth U., Urbanke C., Kang C.;
RT "Crystal structure of human mitochondrial single-stranded DNA binding
RT protein at 2.4-A resolution.";
RL Nat. Struct. Biol. 4:153-157(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-148.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of human mitochondrial single-stranded DNA-binding
RT protein (HMTSSB).";
RL Submitted (JAN-2007) to the PDB data bank.
RN [21]
RP INVOLVEMENT IN OPA13, AND VARIANTS OPA13 GLN-38; GLN-107 AND ASN-141.
RX PubMed=31298765; DOI=10.1002/ana.25550;
RA Jurkute N., Leu C., Pogoda H.M., Arno G., Robson A.G., Nuernberg G.,
RA Altmueller J., Thiele H., Motameny S., Toliat M.R., Powell K., Hoehne W.,
RA Michaelides M., Webster A.R., Moore A.T., Hammerschmidt M., Nuernberg P.,
RA Yu-Wai-Man P., Votruba M.;
RT "SSBP1 mutations in dominant optic atrophy with variable retinal
RT degeneration.";
RL Ann. Neurol. 86:368-383(2019).
RN [22]
RP VARIANTS OPA13 VAL-40; ASP-62; GLN-107 AND GLN-111, VARIANT VAL-132,
RP CHARACTERIZATION OF VARIANTS OPA13 VAL-40; ASP-62; GLN-107 AND GLN-111,
RP CHARACTERIZATION OF VARIANT VAL-132, FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=31550240; DOI=10.1172/jci128514;
RA Del Dotto V., Ullah F., Di Meo I., Magini P., Gusic M., Maresca A.,
RA Caporali L., Palombo F., Tagliavini F., Baugh E.H., Macao B., Szilagyi Z.,
RA Peron C., Gustafson M.A., Khan K., La Morgia C., Barboni P., Carbonelli M.,
RA Valentino M.L., Liguori R., Shashi V., Sullivan J., Nagaraj S.,
RA El-Dairi M., Iannaccone A., Cutcutache I., Bertini E., Carrozzo R.,
RA Emma F., Diomedi-Camassei F., Zanna C., Armstrong M., Page M., Stong N.,
RA Boesch S., Kopajtich R., Wortmann S., Sperl W., Davis E.E., Copeland W.C.,
RA Seri M., Falkenberg M., Prokisch H., Katsanis N., Tiranti V., Pippucci T.,
RA Carelli V.;
RT "SSBP1 mutations cause mtDNA depletion underlying a complex optic atrophy
RT disorder.";
RL J. Clin. Invest. 130:108-125(2020).
RN [23] {ECO:0000312|PDB:6RUP}
RP VARIANTS OPA13 GLN-38 AND GLN-107, CHARACTERIZATION OF VARIANT OPA13
RP GLN-38, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND X-RAY CRYSTALLOGRAPHY
RP (2.10 ANGSTROMS) OF 16-148.
RX PubMed=31550237; DOI=10.1172/jci128513;
RA Piro-Megy C., Sarzi E., Tarres-Sole A., Pequignot M., Hensen F., Quiles M.,
RA Manes G., Chakraborty A., Senechal A., Bocquet B., Cazevieille C.,
RA Roubertie A., Mueller A., Charif M., Goudenege D., Lenaers G., Wilhelm H.,
RA Kellner U., Weisschuh N., Wissinger B., Zanlonghi X., Hamel C.,
RA Spelbrink J.N., Sola M., Delettre C.;
RT "Dominant mutations in mtDNA maintenance gene SSBP1 cause optic atrophy and
RT foveopathy.";
RL J. Clin. Invest. 130:143-156(2020).
CC -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC single-stranded DNA (ss-DNA) (PubMed:21953457, PubMed:23290262,
CC PubMed:31550240). In vitro, required to maintain the copy number of
CC mitochondrial DNA (mtDNA) and plays a crucial role during mtDNA
CC replication by stimulating the activity of the replisome components
CC POLG and TWNK at the replication fork (PubMed:21953457,
CC PubMed:12975372, PubMed:26446790, PubMed:15167897, PubMed:31550240).
CC Promotes the activity of the gamma complex polymerase POLG, largely by
CC organizing the template DNA and eliminating secondary structures to
CC favor ss-DNA conformations that facilitate POLG activity
CC (PubMed:26446790, PubMed:21953457, PubMed:31550240). In addition it is
CC able to promote the 5'-3' unwinding activity of the mtDNA helicase TWNK
CC (PubMed:12975372). May also function in mtDNA repair (PubMed:23290262).
CC {ECO:0000269|PubMed:12975372, ECO:0000269|PubMed:15167897,
CC ECO:0000269|PubMed:21953457, ECO:0000269|PubMed:23290262,
CC ECO:0000269|PubMed:26446790, ECO:0000269|PubMed:31550240}.
CC -!- SUBUNIT: Homotetramer (PubMed:23290262, PubMed:31550240). Interacts
CC with MPG/AAG, through inhibition of its glycosylase activity it
CC potentially prevents formation of DNA breaks in ssDNA, ensuring that
CC base removal primarily occurs in dsDNA (PubMed:23290262). Interacts
CC with POLDIP2 (PubMed:16428295). Interacts with PRIMPOL
CC (PubMed:25550423). {ECO:0000269|PubMed:16428295,
CC ECO:0000269|PubMed:23290262, ECO:0000269|PubMed:25550423,
CC ECO:0000269|PubMed:31550240}.
CC -!- INTERACTION:
CC Q04837; O75603: GCM2; NbExp=3; IntAct=EBI-353460, EBI-10188645;
CC Q04837; P47929: LGALS7B; NbExp=6; IntAct=EBI-353460, EBI-357504;
CC Q04837; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-353460, EBI-11960139;
CC Q04837; Q04837: SSBP1; NbExp=3; IntAct=EBI-353460, EBI-353460;
CC Q04837; P04618: rev; Xeno; NbExp=3; IntAct=EBI-353460, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18063578,
CC ECO:0000269|PubMed:31550237, ECO:0000269|PubMed:31550240}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:18063578, ECO:0000269|PubMed:31550240}.
CC -!- TISSUE SPECIFICITY: Expressed in retinal ganglion cells,
CC photoreceptors, pigmented epithelium and fibroblasts (at protein
CC level). {ECO:0000269|PubMed:31550237}.
CC -!- DISEASE: Optic atrophy 13 with retinal and foveal abnormalities (OPA13)
CC [MIM:165510]: An autosomal dominant disease characterized by visual
CC impairment in association with bilateral optic atrophy. Atrophy of the
CC optic disk indicates a deficiency in the number of nerve fibers which
CC arise in the retina and converge to form the optic disk, optic nerve,
CC optic chiasm and optic tracts. Many OPA13 patients also exhibit retinal
CC pigmentary defects, attenuated retinal vasculature, macular dystrophy,
CC and foveopathy. Some patients may develop additional systemic features,
CC including sensorineural deafness and progressive nephropathy resulting
CC in renal failure. {ECO:0000269|PubMed:31298765,
CC ECO:0000269|PubMed:31550237, ECO:0000269|PubMed:31550240}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; M94556; AAA36332.1; -; mRNA.
DR EMBL; AF277319; AAK69112.1; -; mRNA.
DR EMBL; BC000895; AAH00895.1; -; mRNA.
DR CCDS; CCDS5866.1; -.
DR PIR; JN0568; JN0568.
DR RefSeq; NP_001243439.1; NM_001256510.1.
DR RefSeq; NP_001243440.1; NM_001256511.1.
DR RefSeq; NP_001243441.1; NM_001256512.1.
DR RefSeq; NP_001243442.1; NM_001256513.1.
DR RefSeq; NP_003134.1; NM_003143.2.
DR PDB; 1S3O; X-ray; 2.47 A; A/B=17-148.
DR PDB; 2DUD; X-ray; 2.70 A; A/B=16-148.
DR PDB; 3ULL; X-ray; 2.40 A; A/B=17-148.
DR PDB; 6RUP; X-ray; 2.10 A; A/B=16-148.
DR PDBsum; 1S3O; -.
DR PDBsum; 2DUD; -.
DR PDBsum; 3ULL; -.
DR PDBsum; 6RUP; -.
DR AlphaFoldDB; Q04837; -.
DR SMR; Q04837; -.
DR BioGRID; 112620; 542.
DR IntAct; Q04837; 181.
DR MINT; Q04837; -.
DR STRING; 9606.ENSP00000419665; -.
DR GlyGen; Q04837; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q04837; -.
DR MetOSite; Q04837; -.
DR PhosphoSitePlus; Q04837; -.
DR BioMuta; SSBP1; -.
DR UCD-2DPAGE; Q04837; -.
DR CPTAC; CPTAC-1637; -.
DR EPD; Q04837; -.
DR jPOST; Q04837; -.
DR MassIVE; Q04837; -.
DR MaxQB; Q04837; -.
DR PaxDb; Q04837; -.
DR PeptideAtlas; Q04837; -.
DR PRIDE; Q04837; -.
DR ProteomicsDB; 58286; -.
DR TopDownProteomics; Q04837; -.
DR Antibodypedia; 1260; 179 antibodies from 30 providers.
DR DNASU; 6742; -.
DR Ensembl; ENST00000265304.11; ENSP00000265304.6; ENSG00000106028.11.
DR Ensembl; ENST00000465582.5; ENSP00000420485.1; ENSG00000106028.11.
DR Ensembl; ENST00000481508.1; ENSP00000419665.1; ENSG00000106028.11.
DR Ensembl; ENST00000484178.5; ENSP00000419388.1; ENSG00000106028.11.
DR Ensembl; ENST00000498107.5; ENSP00000419541.1; ENSG00000106028.11.
DR Ensembl; ENST00000570667.5; ENSP00000460028.2; ENSG00000262771.5.
DR Ensembl; ENST00000571430.5; ENSP00000459367.2; ENSG00000262771.5.
DR Ensembl; ENST00000574199.5; ENSP00000461884.2; ENSG00000262771.5.
DR Ensembl; ENST00000575059.5; ENSP00000458815.2; ENSG00000262771.5.
DR Ensembl; ENST00000576834.2; ENSP00000459208.2; ENSG00000262771.5.
DR Ensembl; ENST00000612337.4; ENSP00000480488.1; ENSG00000106028.11.
DR GeneID; 6742; -.
DR KEGG; hsa:6742; -.
DR MANE-Select; ENST00000265304.11; ENSP00000265304.6; NM_003143.3; NP_003134.1.
DR UCSC; uc003vwo.3; human.
DR CTD; 6742; -.
DR DisGeNET; 6742; -.
DR GeneCards; SSBP1; -.
DR HGNC; HGNC:11317; SSBP1.
DR HPA; ENSG00000106028; Low tissue specificity.
DR MalaCards; SSBP1; -.
DR MIM; 165510; phenotype.
DR MIM; 600439; gene.
DR neXtProt; NX_Q04837; -.
DR OpenTargets; ENSG00000106028; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA36141; -.
DR VEuPathDB; HostDB:ENSG00000106028; -.
DR eggNOG; KOG1653; Eukaryota.
DR GeneTree; ENSGT00390000002796; -.
DR InParanoid; Q04837; -.
DR OMA; GNCIGRF; -.
DR OrthoDB; 1304218at2759; -.
DR PhylomeDB; Q04837; -.
DR TreeFam; TF314629; -.
DR PathwayCommons; Q04837; -.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q04837; -.
DR BioGRID-ORCS; 6742; 274 hits in 1082 CRISPR screens.
DR ChiTaRS; SSBP1; human.
DR EvolutionaryTrace; Q04837; -.
DR GeneWiki; SSBP1; -.
DR GenomeRNAi; 6742; -.
DR Pharos; Q04837; Tbio.
DR PRO; PR:Q04837; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q04837; protein.
DR Bgee; ENSG00000106028; Expressed in calcaneal tendon and 116 other tissues.
DR ExpressionAtlas; Q04837; baseline and differential.
DR Genevisible; Q04837; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:FlyBase.
DR GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:1905776; P:positive regulation of DNA helicase activity; IDA:FlyBase.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR PIRSF; PIRSF002070; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW DNA replication; DNA-binding; Mitochondrion; Mitochondrion nucleoid;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19892738,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 17..148
FT /note="Single-stranded DNA-binding protein, mitochondrial"
FT /id="PRO_0000033263"
FT DOMAIN 30..141
FT /note="SSB"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYR0"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 122
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYR0"
FT VARIANT 38
FT /note="R -> Q (in OPA13; may impair dimerization and
FT tetramerization)"
FT /evidence="ECO:0000269|PubMed:31298765,
FT ECO:0000269|PubMed:31550237"
FT /id="VAR_084732"
FT VARIANT 40
FT /note="G -> V (in OPA13; reduced ability to stimulate POLG-
FT dependent DNA synthesis in vitro)"
FT /evidence="ECO:0000269|PubMed:31550240"
FT /id="VAR_084733"
FT VARIANT 62
FT /note="N -> D (in OPA13; reduced ability to stimulate POLG-
FT dependent DNA synthesis in vitro)"
FT /evidence="ECO:0000269|PubMed:31550240"
FT /id="VAR_084734"
FT VARIANT 107
FT /note="R -> Q (in OPA13; reduced ability to stimulate POLG-
FT dependent DNA synthesis in vitro)"
FT /evidence="ECO:0000269|PubMed:31298765,
FT ECO:0000269|PubMed:31550237, ECO:0000269|PubMed:31550240"
FT /id="VAR_084735"
FT VARIANT 111
FT /note="E -> Q (in OPA13; reduced ability to stimulate POLG-
FT dependent DNA synthesis in vitro)"
FT /evidence="ECO:0000269|PubMed:31550240"
FT /id="VAR_084736"
FT VARIANT 132
FT /note="I -> V (found in a patient with a systemic
FT mitochondrial disorder; unknown pathological significance;
FT impaired multimerization; reduced ability to stimulate
FT POLG-dependent DNA synthesis in vitro; mtDNA depletion
FT without any detectable energetic defects;
FT dbSNP:rs777794675)"
FT /evidence="ECO:0000269|PubMed:31550240"
FT /id="VAR_084737"
FT VARIANT 141
FT /note="S -> N (in OPA13)"
FT /evidence="ECO:0000269|PubMed:31298765"
FT /id="VAR_084738"
FT MUTAGEN 49..51
FT /note="EGK->AAA: In mtSSBloop12; decreased unwinding of
FT double-stranded DNA by the helicase TWNK and increased
FT binding to single-stranded DNA, in vitro."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 67..75
FT /note="Missing: In mtSSBloop23; reduced ability to open
FT template DNA and decreased POLG polymerase activity, in
FT vitro. Also displays decreased unwinding of double-stranded
FT DNA by the helicase TWNK and increased binding to single-
FT stranded DNA."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 99..100
FT /note="YQ->AA: In mtSSBalpha1; decreased POLG polymerase
FT activity, in vitro. No effect on unwinding of double-
FT stranded DNA by the helicase TWNK."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 116..118
FT /note="YGE->AAA: In mtSSB45-1; decreased POLG polymerase
FT activity and increased unwinding of double-stranded DNA by
FT the helicase TWNK, in vitro."
FT /evidence="ECO:0000269|PubMed:21953457"
FT MUTAGEN 122..124
FT /note="KNN->AAA: In mtSSB45-2; decreased unwinding of
FT double-stranded DNA by the helicase TWNK, in vitro."
FT /evidence="ECO:0000269|PubMed:21953457"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1S3O"
FT STRAND 54..66
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:6RUP"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6RUP"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:6RUP"
SQ SEQUENCE 148 AA; 17260 MW; 98EE9E396D5636C2 CRC64;
MFRRPVLQVL RQFVRHESET TTSLVLERSL NRVHLLGRVG QDPVLRQVEG KNPVTIFSLA
TNEMWRSGDS EVYQLGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYL EGKIDYGEYM
DKNNVRRQAT TIIADNIIFL SDQTKEKE
