Full text data of SSBP1
SSBP1
(SSBP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Single-stranded DNA-binding protein, mitochondrial; Mt-SSB; MtSSB (PWP1-interacting protein 17; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Single-stranded DNA-binding protein, mitochondrial; Mt-SSB; MtSSB (PWP1-interacting protein 17; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q04837
ID SSBP_HUMAN Reviewed; 148 AA.
AC Q04837;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 139.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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-
RT stranded 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
RT project: 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
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Buerckstuemmer T., 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 [9]
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 [10]
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.
CC -!- FUNCTION: This protein binds preferentially and cooperatively to
CC ss-DNA. Probably involved in mitochondrial DNA replication.
CC Associates with mitochondrial DNA.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- INTERACTION:
CC P04618:rev (xeno); NbExp=3; IntAct=EBI-353460, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix,
CC mitochondrion nucleoid.
CC -!- SIMILARITY: Contains 1 SSB domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M94556; AAA36332.1; -; mRNA.
DR EMBL; AF277319; AAK69112.1; -; mRNA.
DR EMBL; BC000895; AAH00895.1; -; mRNA.
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 UniGene; Hs.490394; -.
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 PDBsum; 1S3O; -.
DR PDBsum; 2DUD; -.
DR PDBsum; 3ULL; -.
DR ProteinModelPortal; Q04837; -.
DR SMR; Q04837; 26-140.
DR IntAct; Q04837; 25.
DR MINT; MINT-3025472; -.
DR STRING; 9606.ENSP00000265304; -.
DR PhosphoSite; Q04837; -.
DR DMDM; 417811; -.
DR UCD-2DPAGE; Q04837; -.
DR PaxDb; Q04837; -.
DR PeptideAtlas; Q04837; -.
DR PRIDE; Q04837; -.
DR DNASU; 6742; -.
DR Ensembl; ENST00000265304; ENSP00000265304; ENSG00000106028.
DR Ensembl; ENST00000465582; ENSP00000420485; ENSG00000106028.
DR Ensembl; ENST00000481508; ENSP00000419665; ENSG00000106028.
DR Ensembl; ENST00000484178; ENSP00000419388; ENSG00000106028.
DR Ensembl; ENST00000498107; ENSP00000419541; ENSG00000106028.
DR Ensembl; ENST00000570667; ENSP00000460028; ENSG00000262771.
DR Ensembl; ENST00000571430; ENSP00000459367; ENSG00000262771.
DR Ensembl; ENST00000574199; ENSP00000461884; ENSG00000262771.
DR Ensembl; ENST00000575059; ENSP00000458815; ENSG00000262771.
DR Ensembl; ENST00000576834; ENSP00000459208; ENSG00000262771.
DR GeneID; 6742; -.
DR KEGG; hsa:6742; -.
DR UCSC; uc003vwo.2; human.
DR CTD; 6742; -.
DR GeneCards; GC07P141442; -.
DR HGNC; HGNC:11317; SSBP1.
DR HPA; HPA002866; -.
DR MIM; 600439; gene.
DR neXtProt; NX_Q04837; -.
DR PharmGKB; PA36141; -.
DR eggNOG; COG0629; -.
DR HOVERGEN; HBG001181; -.
DR InParanoid; Q04837; -.
DR KO; K03111; -.
DR OMA; ITYGEIT; -.
DR PhylomeDB; Q04837; -.
DR ChiTaRS; SSBP1; human.
DR EvolutionaryTrace; Q04837; -.
DR GeneWiki; SSBP1; -.
DR GenomeRNAi; 6742; -.
DR NextBio; 26300; -.
DR PRO; PR:Q04837; -.
DR ArrayExpress; Q04837; -.
DR Bgee; Q04837; -.
DR CleanEx; HS_SSBP1; -.
DR Genevestigator; Q04837; -.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 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; Complete proteome;
KW Direct protein sequencing; DNA replication; DNA-binding;
KW Mitochondrion; Mitochondrion nucleoid; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1 16 Mitochondrion.
FT CHAIN 17 148 Single-stranded DNA-binding protein,
FT mitochondrial.
FT /FTId=PRO_0000033263.
FT DOMAIN 30 141 SSB.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 113 113 N6-acetyllysine.
FT STRAND 30 39
FT STRAND 44 46
FT STRAND 48 51
FT STRAND 54 65
FT STRAND 79 89
FT HELIX 94 101
FT STRAND 107 115
FT STRAND 119 126
FT STRAND 130 138
SQ SEQUENCE 148 AA; 17260 MW; 98EE9E396D5636C2 CRC64;
MFRRPVLQVL RQFVRHESET TTSLVLERSL NRVHLLGRVG QDPVLRQVEG KNPVTIFSLA
TNEMWRSGDS EVYQLGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYL EGKIDYGEYM
DKNNVRRQAT TIIADNIIFL SDQTKEKE
//
ID SSBP_HUMAN Reviewed; 148 AA.
AC Q04837;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 139.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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-
RT stranded 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
RT project: 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
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [8]
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.,
RA Buerckstuemmer T., 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 [9]
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 [10]
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.
CC -!- FUNCTION: This protein binds preferentially and cooperatively to
CC ss-DNA. Probably involved in mitochondrial DNA replication.
CC Associates with mitochondrial DNA.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- INTERACTION:
CC P04618:rev (xeno); NbExp=3; IntAct=EBI-353460, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix,
CC mitochondrion nucleoid.
CC -!- SIMILARITY: Contains 1 SSB domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M94556; AAA36332.1; -; mRNA.
DR EMBL; AF277319; AAK69112.1; -; mRNA.
DR EMBL; BC000895; AAH00895.1; -; mRNA.
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 UniGene; Hs.490394; -.
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 PDBsum; 1S3O; -.
DR PDBsum; 2DUD; -.
DR PDBsum; 3ULL; -.
DR ProteinModelPortal; Q04837; -.
DR SMR; Q04837; 26-140.
DR IntAct; Q04837; 25.
DR MINT; MINT-3025472; -.
DR STRING; 9606.ENSP00000265304; -.
DR PhosphoSite; Q04837; -.
DR DMDM; 417811; -.
DR UCD-2DPAGE; Q04837; -.
DR PaxDb; Q04837; -.
DR PeptideAtlas; Q04837; -.
DR PRIDE; Q04837; -.
DR DNASU; 6742; -.
DR Ensembl; ENST00000265304; ENSP00000265304; ENSG00000106028.
DR Ensembl; ENST00000465582; ENSP00000420485; ENSG00000106028.
DR Ensembl; ENST00000481508; ENSP00000419665; ENSG00000106028.
DR Ensembl; ENST00000484178; ENSP00000419388; ENSG00000106028.
DR Ensembl; ENST00000498107; ENSP00000419541; ENSG00000106028.
DR Ensembl; ENST00000570667; ENSP00000460028; ENSG00000262771.
DR Ensembl; ENST00000571430; ENSP00000459367; ENSG00000262771.
DR Ensembl; ENST00000574199; ENSP00000461884; ENSG00000262771.
DR Ensembl; ENST00000575059; ENSP00000458815; ENSG00000262771.
DR Ensembl; ENST00000576834; ENSP00000459208; ENSG00000262771.
DR GeneID; 6742; -.
DR KEGG; hsa:6742; -.
DR UCSC; uc003vwo.2; human.
DR CTD; 6742; -.
DR GeneCards; GC07P141442; -.
DR HGNC; HGNC:11317; SSBP1.
DR HPA; HPA002866; -.
DR MIM; 600439; gene.
DR neXtProt; NX_Q04837; -.
DR PharmGKB; PA36141; -.
DR eggNOG; COG0629; -.
DR HOVERGEN; HBG001181; -.
DR InParanoid; Q04837; -.
DR KO; K03111; -.
DR OMA; ITYGEIT; -.
DR PhylomeDB; Q04837; -.
DR ChiTaRS; SSBP1; human.
DR EvolutionaryTrace; Q04837; -.
DR GeneWiki; SSBP1; -.
DR GenomeRNAi; 6742; -.
DR NextBio; 26300; -.
DR PRO; PR:Q04837; -.
DR ArrayExpress; Q04837; -.
DR Bgee; Q04837; -.
DR CleanEx; HS_SSBP1; -.
DR Genevestigator; Q04837; -.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
DR Gene3D; 2.40.50.140; -; 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; Complete proteome;
KW Direct protein sequencing; DNA replication; DNA-binding;
KW Mitochondrion; Mitochondrion nucleoid; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1 16 Mitochondrion.
FT CHAIN 17 148 Single-stranded DNA-binding protein,
FT mitochondrial.
FT /FTId=PRO_0000033263.
FT DOMAIN 30 141 SSB.
FT MOD_RES 79 79 Phosphoserine.
FT MOD_RES 113 113 N6-acetyllysine.
FT STRAND 30 39
FT STRAND 44 46
FT STRAND 48 51
FT STRAND 54 65
FT STRAND 79 89
FT HELIX 94 101
FT STRAND 107 115
FT STRAND 119 126
FT STRAND 130 138
SQ SEQUENCE 148 AA; 17260 MW; 98EE9E396D5636C2 CRC64;
MFRRPVLQVL RQFVRHESET TTSLVLERSL NRVHLLGRVG QDPVLRQVEG KNPVTIFSLA
TNEMWRSGDS EVYQLGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGSRIYL EGKIDYGEYM
DKNNVRRQAT TIIADNIIFL SDQTKEKE
//
MIM
600439
*RECORD*
*FIELD* NO
600439
*FIELD* TI
*600439 SINGLE-STRANDED DNA-BINDING PROTEIN 1; SSBP1
;;SSBP;;
SENSOR OF SINGLE-STRANDED DNA COMPLEX, SUBUNIT B1; SOSSB1;;
read moreSOSS COMPLEX, SUBUNIT B1
*FIELD* TX
DESCRIPTION
SSBP1 is a housekeeping gene involved in mitochondrial biogenesis
(Tiranti et al., 1995). It is also a subunit of a single-stranded DNA
(ssDNA)-binding complex involved in the maintenance of genome stability
(Huang et al., 2009).
CLONING
Tiranti et al. (1995) determined that the SSBP gene encodes a
mitochondrial ssDNA-binding protein, which is also known as mtSSB. The
mature SSBP product is a 132-amino acid protein.
GENE FUNCTION
Tiranti et al. (1995) found that mature SSBP acted as a homotetramer to
stabilize the displaced single strand of the normal and expanded
displacement loop (D loop) during mtDNA replication, thus preventing
formation of secondary single-stranded DNA structures, which could stop
the gamma-DNA polymerase.
Mitochondrial nucleoids are large complexes containing, on average, 5 to
7 mtDNA genomes and several proteins involved in mtDNA replication and
transcription, as well as related processes. Bogenhagen et al. (2008)
had previously shown that SSBP1 was associated with native purified HeLa
cell nucleoids. Using a formaldehyde crosslinking technique, they found
that SSBP1 copurified with mtDNA and was a core nucleoid protein.
Bogenhagen et al. (2008) confirmed these findings by Western blot
analysis.
Using HEK293 cells for tandem affinity purification, Huang et al. (2009)
identified SOSSA (INTS3; 611347) and SOSSC (613273) as common components
of 2 distinct and complementary ssDNA-binding heterotrimeric complexes
defined by their inclusion of either SOSSB1 (SSBP1) or SOSSB2 (SSBP2;
607389), but not both. Coimmunoprecipitation analysis confirmed that
SOSS complexes formed in HeLa cells independent of DNA damage.
Recombinant heterotrimeric SOSS complexes specifically bound ssDNA, but
not double-stranded DNA. SOSSA served as the central assembly factor,
and SOSSB and SOSSC bound overlapping regions on SOSSA, but they did not
interact directly with each other. Depletion of SOSSA by small
interfering RNA led to dramatic decreases in SOSSB1 and SOSSB2 protein
levels, abrogated targeting of SOSSB1 and SOSSB2 to chromatin, increased
ionizing radiation sensitivity, caused defective G2/M checkpoint, and
impaired homologous recombination repair. Huang et al. (2009)
demonstrated that both SOSS complexes and the CTIP (RBBP8; 604124)/RPA
(see RPA1; 179835) complex acted downstream of the MRE11 (600814)-RAD50
(604040)-NBS1 (NBN; 602667) complex and functioned in DNA damage repair.
MAPPING
By a PCR-based screening of a somatic cell hybrid panel and by
fluorescence in situ hybridization, Tiranti et al. (1995) assigned the
SSBP gene to 7q34.
*FIELD* RF
1. Bogenhagen, D. F.; Rousseau, D.; Burke, S.: The layered structure
of human mitochondrial DNA nucleoids. J. Biol. Chem. 283: 3665-3675,
2008.
2. Huang, J.; Gong, Z.; Ghosal, G.; Chen, J.: SOSS complexes participate
in the maintenance of genomic stability. Molec. Cell 35: 384-393,
2009.
3. Tiranti, V.; Rossi, E.; Ruiz-Carrillo, A.; Rossi, G.; Rocchi, M.;
DiDonato, S.; Zuffardi, O.; Zeviani, M.: Chromosomal localization
of mitochondrial transcription factor A (TCF6), single-stranded DNA-binding
protein (SSBP), and endonuclease G (ENDOG), three human housekeeping
genes involved in mitochondrial biogenesis. Genomics 25: 559-564,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 2/19/2010
Patricia A. Hartz - updated: 9/24/2008
*FIELD* CD
Victor A. McKusick: 3/6/1995
*FIELD* ED
mgross: 02/22/2010
terry: 2/19/2010
mgross: 9/25/2008
terry: 9/24/2008
mgross: 12/3/2002
carol: 11/26/2002
carol: 3/7/1995
carol: 3/6/1995
*RECORD*
*FIELD* NO
600439
*FIELD* TI
*600439 SINGLE-STRANDED DNA-BINDING PROTEIN 1; SSBP1
;;SSBP;;
SENSOR OF SINGLE-STRANDED DNA COMPLEX, SUBUNIT B1; SOSSB1;;
read moreSOSS COMPLEX, SUBUNIT B1
*FIELD* TX
DESCRIPTION
SSBP1 is a housekeeping gene involved in mitochondrial biogenesis
(Tiranti et al., 1995). It is also a subunit of a single-stranded DNA
(ssDNA)-binding complex involved in the maintenance of genome stability
(Huang et al., 2009).
CLONING
Tiranti et al. (1995) determined that the SSBP gene encodes a
mitochondrial ssDNA-binding protein, which is also known as mtSSB. The
mature SSBP product is a 132-amino acid protein.
GENE FUNCTION
Tiranti et al. (1995) found that mature SSBP acted as a homotetramer to
stabilize the displaced single strand of the normal and expanded
displacement loop (D loop) during mtDNA replication, thus preventing
formation of secondary single-stranded DNA structures, which could stop
the gamma-DNA polymerase.
Mitochondrial nucleoids are large complexes containing, on average, 5 to
7 mtDNA genomes and several proteins involved in mtDNA replication and
transcription, as well as related processes. Bogenhagen et al. (2008)
had previously shown that SSBP1 was associated with native purified HeLa
cell nucleoids. Using a formaldehyde crosslinking technique, they found
that SSBP1 copurified with mtDNA and was a core nucleoid protein.
Bogenhagen et al. (2008) confirmed these findings by Western blot
analysis.
Using HEK293 cells for tandem affinity purification, Huang et al. (2009)
identified SOSSA (INTS3; 611347) and SOSSC (613273) as common components
of 2 distinct and complementary ssDNA-binding heterotrimeric complexes
defined by their inclusion of either SOSSB1 (SSBP1) or SOSSB2 (SSBP2;
607389), but not both. Coimmunoprecipitation analysis confirmed that
SOSS complexes formed in HeLa cells independent of DNA damage.
Recombinant heterotrimeric SOSS complexes specifically bound ssDNA, but
not double-stranded DNA. SOSSA served as the central assembly factor,
and SOSSB and SOSSC bound overlapping regions on SOSSA, but they did not
interact directly with each other. Depletion of SOSSA by small
interfering RNA led to dramatic decreases in SOSSB1 and SOSSB2 protein
levels, abrogated targeting of SOSSB1 and SOSSB2 to chromatin, increased
ionizing radiation sensitivity, caused defective G2/M checkpoint, and
impaired homologous recombination repair. Huang et al. (2009)
demonstrated that both SOSS complexes and the CTIP (RBBP8; 604124)/RPA
(see RPA1; 179835) complex acted downstream of the MRE11 (600814)-RAD50
(604040)-NBS1 (NBN; 602667) complex and functioned in DNA damage repair.
MAPPING
By a PCR-based screening of a somatic cell hybrid panel and by
fluorescence in situ hybridization, Tiranti et al. (1995) assigned the
SSBP gene to 7q34.
*FIELD* RF
1. Bogenhagen, D. F.; Rousseau, D.; Burke, S.: The layered structure
of human mitochondrial DNA nucleoids. J. Biol. Chem. 283: 3665-3675,
2008.
2. Huang, J.; Gong, Z.; Ghosal, G.; Chen, J.: SOSS complexes participate
in the maintenance of genomic stability. Molec. Cell 35: 384-393,
2009.
3. Tiranti, V.; Rossi, E.; Ruiz-Carrillo, A.; Rossi, G.; Rocchi, M.;
DiDonato, S.; Zuffardi, O.; Zeviani, M.: Chromosomal localization
of mitochondrial transcription factor A (TCF6), single-stranded DNA-binding
protein (SSBP), and endonuclease G (ENDOG), three human housekeeping
genes involved in mitochondrial biogenesis. Genomics 25: 559-564,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 2/19/2010
Patricia A. Hartz - updated: 9/24/2008
*FIELD* CD
Victor A. McKusick: 3/6/1995
*FIELD* ED
mgross: 02/22/2010
terry: 2/19/2010
mgross: 9/25/2008
terry: 9/24/2008
mgross: 12/3/2002
carol: 11/26/2002
carol: 3/7/1995
carol: 3/6/1995