SSBP3_MOUSE
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 03-AUG-2022, entry version 163.
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;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 42.
DR DIP; DIP-42843N; -.
DR IntAct; Q9D032; 28.
DR MINT; Q9D032; -.
DR STRING; 10090.ENSMUSP00000030367; -.
DR iPTMnet; Q9D032; -.
DR PhosphoSitePlus; Q9D032; -.
DR jPOST; Q9D032; -.
DR MaxQB; Q9D032; -.
DR PaxDb; Q9D032; -.
DR PRIDE; Q9D032; -.
DR ProteomicsDB; 257417; -. [Q9D032-1]
DR ProteomicsDB; 257418; -. [Q9D032-2]
DR Antibodypedia; 33182; 125 antibodies from 18 providers.
DR DNASU; 72475; -.
DR Ensembl; ENSMUST00000030367; ENSMUSP00000030367; ENSMUSG00000061887. [Q9D032-1]
DR Ensembl; ENSMUST00000072753; ENSMUSP00000072536; ENSMUSG00000061887. [Q9D032-2]
DR GeneID; 72475; -.
DR KEGG; mmu:72475; -.
DR UCSC; uc008tyx.1; mouse. [Q9D032-1]
DR UCSC; uc008tyy.1; mouse. [Q9D032-2]
DR CTD; 23648; -.
DR MGI; MGI:1919725; Ssbp3.
DR VEuPathDB; HostDB:ENSMUSG00000061887; -.
DR eggNOG; KOG4594; Eukaryota.
DR GeneTree; ENSGT00950000183049; -.
DR InParanoid; Q9D032; -.
DR OMA; MPGDFPM; -.
DR OrthoDB; 907486at2759; -.
DR PhylomeDB; Q9D032; -.
DR TreeFam; TF318961; -.
DR BioGRID-ORCS; 72475; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Ssbp3; mouse.
DR PRO; PR:Q9D032; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D032; protein.
DR Bgee; ENSMUSG00000061887; Expressed in cortical plate and 251 other tissues.
DR ExpressionAtlas; Q9D032; baseline and differential.
DR Genevisible; Q9D032; MM.
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:0048382; P:mesendoderm development; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP: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; IPR008116; SSDP_DNA-bd.
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 110..143
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..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
