SSBP_MOUSE
ID SSBP_MOUSE Reviewed; 152 AA.
AC Q9CYR0;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Single-stranded DNA-binding protein, mitochondrial;
DE Short=Mt-SSB;
DE Short=MtSSB;
DE Flags: Precursor;
GN Name=Ssbp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC single-stranded DNA (ss-DNA). In vitro, required to maintain the copy
CC number of mitochondrial DNA (mtDNA) and plays a crucial role during
CC mtDNA replication by stimulating the activity of the replisome
CC components POLG and TWNK at the replication fork. Promotes the activity
CC of the gamma complex polymerase POLG, largely by organizing the
CC template DNA and eliminating secondary structures to favor ss-DNA
CC conformations that facilitate POLG activity. In addition it is able to
CC promote the 5'-3' unwinding activity of the mtDNA helicase TWNK. May
CC also function in mtDNA repair. {ECO:0000250|UniProtKB:Q04837}.
CC -!- SUBUNIT: Homotetramer. Interacts with MPG/AAG, through inhibition of
CC its glycosylase activity it potentially prevents formation of DNA
CC breaks in ssDNA, ensuring that base removal primarily occurs in dsDNA.
CC Interacts with POLDIP2. Interacts with PRIMPOL.
CC {ECO:0000250|UniProtKB:Q04837}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:31298765}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:31298765}.
CC -!- TISSUE SPECIFICITY: Expressed in all the layers of the retina (at
CC protein level). {ECO:0000269|PubMed:31298765}.
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DR EMBL; AK013425; BAB28850.1; -; mRNA.
DR CCDS; CCDS20030.1; -.
DR RefSeq; NP_082634.1; NM_028358.2.
DR RefSeq; NP_997633.1; NM_212468.3.
DR RefSeq; XP_006506392.1; XM_006506329.2.
DR RefSeq; XP_017177153.1; XM_017321664.1.
DR AlphaFoldDB; Q9CYR0; -.
DR SMR; Q9CYR0; -.
DR BioGRID; 238075; 24.
DR IntAct; Q9CYR0; 4.
DR MINT; Q9CYR0; -.
DR STRING; 10090.ENSMUSP00000031971; -.
DR iPTMnet; Q9CYR0; -.
DR PhosphoSitePlus; Q9CYR0; -.
DR EPD; Q9CYR0; -.
DR MaxQB; Q9CYR0; -.
DR PaxDb; Q9CYR0; -.
DR PeptideAtlas; Q9CYR0; -.
DR PRIDE; Q9CYR0; -.
DR ProteomicsDB; 263350; -.
DR Antibodypedia; 1260; 179 antibodies from 30 providers.
DR Ensembl; ENSMUST00000031971; ENSMUSP00000031971; ENSMUSG00000029911.
DR GeneID; 381760; -.
DR KEGG; mmu:381760; -.
DR UCSC; uc009bmr.1; mouse.
DR CTD; 6742; -.
DR MGI; MGI:1920040; Ssbp1.
DR VEuPathDB; HostDB:ENSMUSG00000029911; -.
DR eggNOG; KOG1653; Eukaryota.
DR GeneTree; ENSGT00390000002796; -.
DR InParanoid; Q9CYR0; -.
DR OrthoDB; 1304218at2759; -.
DR PhylomeDB; Q9CYR0; -.
DR TreeFam; TF314629; -.
DR BioGRID-ORCS; 381760; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Ssbp1; mouse.
DR PRO; PR:Q9CYR0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CYR0; protein.
DR Bgee; ENSMUSG00000029911; Expressed in ventricular zone and 147 other tissues.
DR ExpressionAtlas; Q9CYR0; baseline and differential.
DR Genevisible; Q9CYR0; MM.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:MGI.
DR GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
DR GO; GO:1905776; P:positive regulation of DNA helicase activity; ISO:MGI.
DR GO; GO:0051096; P:positive regulation of helicase activity; ISO:MGI.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS: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 Acetylation; DNA replication; DNA-binding; Mitochondrion;
KW Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q04837"
FT CHAIN 17..152
FT /note="Single-stranded DNA-binding protein, mitochondrial"
FT /id="PRO_0000033264"
FT DOMAIN 30..141
FT /note="SSB"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04837"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04837"
FT MOD_RES 122
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 152 AA; 17319 MW; 719B9F03C4C0D1EE CRC64;
MFRRPVLQVF RQFVRHESEV ASSLVLERSL NRVQLLGRVG QDPVMRQVEG KNPVTIFSLA
TNEMWRSGDS EVYQMGDVSQ KTTWHRISVF RPGLRDVAYQ YVKKGARIFV EGKVDYGEYM
DKNNVRRQAT TIIAGKKLVV HSVSGCSLEG LA
