ID   SSBP3_MOUSE             Reviewed;         388 AA.
AC   Q9D032; Q99LC6; Q9EQP3;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   02-SEP-2026, entry version 182.
DE   RecName: Full=Single-stranded DNA-binding protein 3;
DE   AltName: Full=Lck-associated signal transducer;
DE   AltName: Full=Sequence-specific single-stranded-DNA-binding protein;
GN   Name=Ssbp3; Synonyms=Last, Ssdp1;
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 [MRNA] (ISOFORM 2).
RC   TISSUE=T-cell lymphoma;
RA   Park C., Choi Y.B., Park D., Hur E.M., Yun Y.D.;
RT   "LAST, a novel protein binding to the SH2 domain of Lck/Src, mediates
RT   signaling events of the Src-type tyrosine kinase.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=12479417; DOI=10.1016/s1570-9639(02)00376-x;
RA   Bayarsaihan D.;
RT   "SSDP1 gene encodes a protein with a conserved N-terminal FORWARD domain.";
RL   Biochim. Biophys. Acta 1599:152-155(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C3H/HeJ;
RX   PubMed=12642495; DOI=10.1242/dev.00389;
RA   van Meyel D.J., Thomas J.B., Agulnick A.D.;
RT   "Ssdp proteins bind to LIM-interacting co-factors and regulate the activity
RT   of LIM-homeodomain protein complexes in vivo.";
RL   Development 130:1915-1925(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-360, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-355 AND THR-360, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, and Spleen;
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   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161 AND ARG-165, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May be involved in transcription regulation of the alpha 2(I)
CC       collagen gene where it binds to the single-stranded polypyrimidine
CC       sequences in the promoter region. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D032-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D032-2; Sequence=VSP_006262;
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DR   EMBL; AF170906; AAG43403.1; -; mRNA.
DR   EMBL; AF500117; AAM22102.1; -; mRNA.
DR   EMBL; AY167987; AAN87333.1; -; mRNA.
DR   EMBL; AK011853; BAB27882.1; -; mRNA.
DR   EMBL; BC003430; AAH03430.1; -; mRNA.
DR   CCDS; CCDS18427.1; -. [Q9D032-1]
DR   CCDS; CCDS18428.1; -. [Q9D032-2]
DR   RefSeq; NP_076161.2; NM_023672.2. [Q9D032-1]
DR   RefSeq; NP_940840.1; NM_198438.1. [Q9D032-2]
DR   AlphaFoldDB; Q9D032; -.
DR   SMR; Q9D032; -.
DR   BioGRID; 215389; 43.
DR   DIP; DIP-42843N; -.
DR   FunCoup; Q9D032; 930.
DR   IntAct; Q9D032; 28.
DR   MINT; Q9D032; -.
DR   STRING; 10090.ENSMUSP00000030367; -.
DR   GlyGen; Q9D032; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q9D032; -.
DR   PhosphoSitePlus; Q9D032; -.
DR   jPOST; Q9D032; -.
DR   PaxDb; 10090-ENSMUSP00000030367; -.
DR   ProteomicsDB; 257417; -. [Q9D032-1]
DR   ProteomicsDB; 257418; -. [Q9D032-2]
DR   Pumba; Q9D032; -.
DR   Antibodypedia; 33182; 120 antibodies from 17 providers.
DR   DNASU; 72475; -.
DR   Ensembl; ENSMUST00000030367.15; ENSMUSP00000030367.9; ENSMUSG00000061887.15. [Q9D032-1]
DR   Ensembl; ENSMUST00000072753.13; ENSMUSP00000072536.7; ENSMUSG00000061887.15. [Q9D032-2]
DR   GeneID; 72475; -.
DR   KEGG; mmu:72475; -.
DR   UCSC; uc008tyx.1; mouse. [Q9D032-1]
DR   UCSC; uc008tyy.1; mouse. [Q9D032-2]
DR   AGR; MGI:1919725; -.
DR   CTD; 23648; -.
DR   MGI; MGI:1919725; Ssbp3.
DR   VEuPathDB; HostDB:ENSMUSG00000061887; -.
DR   eggNOG; KOG4594; Eukaryota.
DR   GeneTree; ENSGT00950000183049; -.
DR   InParanoid; Q9D032; -.
DR   OMA; HRMGTPN; -.
DR   OrthoDB; 5600002at2759; -.
DR   PhylomeDB; Q9D032; -.
DR   BioGRID-ORCS; 72475; 8 hits in 77 CRISPR screens.
DR   PRO; PR:Q9D032; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9D032; protein.
DR   Bgee; ENSMUSG00000061887; Expressed in cortical plate and 254 other cell types or tissues.
DR   ExpressionAtlas; Q9D032; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0030154; P:cell differentiation; TAS:MGI.
DR   GO; GO:0060322; P:head development; IGI:UniProtKB.
DR   GO; GO:0060323; P:head morphogenesis; IMP:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR   GO; GO:0021547; P:midbrain-hindbrain boundary initiation; IMP:UniProtKB.
DR   GO; GO:2000744; P:positive regulation of anterior head development; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0021501; P:prechordal plate formation; IMP:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR061917; LisH_SSDP.
DR   InterPro; IPR008116; SSDP_DNA-bd.
DR   PANTHER; PTHR12610; SINGLE STRANDED DNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR12610:SF22; SINGLE-STRANDED DNA-BINDING PROTEIN 3; 1.
DR   Pfam; PF30097; LisH_SSDP; 1.
DR   Pfam; PF04503; SSDP; 1.
DR   PRINTS; PR01743; SSDNABINDING.
DR   SMART; SM00667; LisH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..388
FT                   /note="Single-stranded DNA-binding protein 3"
FT                   /id="PRO_0000123829"
FT   DOMAIN          16..48
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          101..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..209
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..268
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..325
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..357
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT   MOD_RES         155
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT   MOD_RES         161
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         165
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         360
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT   VAR_SEQ         122..148
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12479417,
FT                   ECO:0000303|PubMed:12642495, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.1"
FT                   /id="VSP_006262"
FT   CONFLICT        243
FT                   /note="A -> D (in Ref. 1; AAG43403)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="A -> V (in Ref. 4; BAB27882)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="L -> V (in Ref. 1; AAG43403)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   388 AA;  40421 MW;  DBBB169D4EE10536 CRC64;
     MFAKGKGSAV PSDGQAREKL ALYVYEYLLH VGAQKSAQTF LSEIRWEKNI TLGEPPGFLH
     SWWCVFWDLY CAAPERRDTC EHSSEAKAFH DYSAAAAPSP VLGNIPPNDG MPGGPIPPGF
     FQGPPGSQPS PHAQPPPHNP SSMMGPHSQP FMSPRYAGGP RPPIRMGNQP PGGVPGTQPL
     LPNSMDPTRQ QGHPNMGGSM QRMNPPRGMG PMGPGPQNYG SGMRPPPNSL GPAMPGINMG
     PGAGRPWPNP NSANSIPYSS SSPGTYVGPP GGGGPPGTPI MPSPADSTNS SDNIYTMINP
     VPPGGSRSNF PMGPGSDGPM GGMGGMEPHH MNGSLGSGDI DGLPKNSPNN ISGISNPPGT
     PRDDGELGGN FLHSFQNDNY SPSMTMSV
//