SSBP3_HUMAN
ID SSBP3_HUMAN Reviewed; 388 AA.
AC Q9BWW4; A8K0A9; Q5T860; Q5T861; Q9BTM0; Q9BWW3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Single-stranded DNA-binding protein 3;
DE AltName: Full=Sequence-specific single-stranded-DNA-binding protein;
GN Name=SSBP3; Synonyms=SSDP, SSDP1;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RX PubMed=12079286; DOI=10.1006/geno.2002.6805;
RA Castro P.D., Liang H., Liang J.C., Nagarajan L.;
RT "A novel, evolutionarily conserved gene family with putative sequence-
RT specific single-stranded DNA-binding activity.";
RL Genomics 80:78-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Bayarsaihan D.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-352; THR-360;
RP SER-381 AND SER-387, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; THR-360 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND SER-352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-360, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-155; ARG-161 AND ARG-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 -!- INTERACTION:
CC Q9BWW4; P51451: BLK; NbExp=3; IntAct=EBI-2902395, EBI-2105445;
CC Q9BWW4; O60941-5: DTNB; NbExp=3; IntAct=EBI-2902395, EBI-11984733;
CC Q9BWW4; Q01844: EWSR1; NbExp=3; IntAct=EBI-2902395, EBI-739737;
CC Q9BWW4; Q9UBH0: IL36RN; NbExp=8; IntAct=EBI-2902395, EBI-465156;
CC Q9BWW4; Q86U70: LDB1; NbExp=4; IntAct=EBI-2902395, EBI-677177;
CC Q9BWW4; Q86U70-2: LDB1; NbExp=5; IntAct=EBI-2902395, EBI-11979761;
CC Q9BWW4; O43679: LDB2; NbExp=4; IntAct=EBI-2902395, EBI-2865580;
CC Q9BWW4; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-2902395, EBI-752122;
CC Q9BWW4; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-2902395, EBI-10698339;
CC Q9BWW4; Q13526: PIN1; NbExp=6; IntAct=EBI-2902395, EBI-714158;
CC Q9BWW4; O75177-5: SS18L1; NbExp=3; IntAct=EBI-2902395, EBI-12035119;
CC Q9BWW4; Q9NUY8: TBC1D23; NbExp=3; IntAct=EBI-2902395, EBI-2853126;
CC Q9BWW4; Q9NUY8-2: TBC1D23; NbExp=3; IntAct=EBI-2902395, EBI-10314276;
CC Q9BWW4; P07947: YES1; NbExp=6; IntAct=EBI-2902395, EBI-515331;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BWW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWW4-2; Sequence=VSP_006260;
CC Name=3;
CC IsoId=Q9BWW4-3; Sequence=VSP_006261;
CC -!- TISSUE SPECIFICITY: Highly expressed in all hematopoietic tissues,
CC including spleen, lymph node, peripheral blood, bone marrow, thymus,
CC and fetal liver, with highest expression in thymus and fetal liver.
CC Expression is also high in heart, brain, kidney, and skeletal muscle.
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DR EMBL; AY026310; AAK21984.1; -; Genomic_DNA.
DR EMBL; AY026293; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026294; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026295; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026296; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026297; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026298; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026299; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026300; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026301; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026302; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026303; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026304; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026305; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026306; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026307; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026308; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026309; AAK21984.1; JOINED; Genomic_DNA.
DR EMBL; AY026310; AAK21985.1; -; Genomic_DNA.
DR EMBL; AY026293; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026294; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026295; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026296; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026297; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026299; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026300; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026301; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026302; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026303; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026304; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026305; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026306; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026307; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026308; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AY026309; AAK21985.1; JOINED; Genomic_DNA.
DR EMBL; AF500116; AAM22101.1; -; mRNA.
DR EMBL; AK289474; BAF82163.1; -; mRNA.
DR EMBL; CH471059; EAX06692.1; -; Genomic_DNA.
DR EMBL; AL035415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003605; AAH03605.1; -; mRNA.
DR EMBL; BC066365; AAH66365.1; -; mRNA.
DR CCDS; CCDS30726.1; -. [Q9BWW4-2]
DR CCDS; CCDS590.1; -. [Q9BWW4-3]
DR CCDS; CCDS591.1; -. [Q9BWW4-1]
DR RefSeq; NP_001009955.1; NM_001009955.3. [Q9BWW4-2]
DR RefSeq; NP_060540.2; NM_018070.4. [Q9BWW4-3]
DR RefSeq; NP_663768.1; NM_145716.3. [Q9BWW4-1]
DR AlphaFoldDB; Q9BWW4; -.
DR SMR; Q9BWW4; -.
DR BioGRID; 117175; 84.
DR DIP; DIP-48897N; -.
DR IntAct; Q9BWW4; 67.
DR MINT; Q9BWW4; -.
DR STRING; 9606.ENSP00000360371; -.
DR GlyGen; Q9BWW4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWW4; -.
DR PhosphoSitePlus; Q9BWW4; -.
DR BioMuta; SSBP3; -.
DR DMDM; 27734581; -.
DR EPD; Q9BWW4; -.
DR jPOST; Q9BWW4; -.
DR MassIVE; Q9BWW4; -.
DR MaxQB; Q9BWW4; -.
DR PaxDb; Q9BWW4; -.
DR PeptideAtlas; Q9BWW4; -.
DR PRIDE; Q9BWW4; -.
DR ProteomicsDB; 79330; -. [Q9BWW4-1]
DR ProteomicsDB; 79331; -. [Q9BWW4-2]
DR ProteomicsDB; 79332; -. [Q9BWW4-3]
DR Antibodypedia; 33182; 125 antibodies from 18 providers.
DR DNASU; 23648; -.
DR Ensembl; ENST00000357475.9; ENSP00000350067.4; ENSG00000157216.16. [Q9BWW4-3]
DR Ensembl; ENST00000371319.8; ENSP00000360370.3; ENSG00000157216.16. [Q9BWW4-2]
DR Ensembl; ENST00000610401.5; ENSP00000479674.2; ENSG00000157216.16. [Q9BWW4-1]
DR GeneID; 23648; -.
DR KEGG; hsa:23648; -.
DR UCSC; uc001cxe.5; human. [Q9BWW4-1]
DR CTD; 23648; -.
DR DisGeNET; 23648; -.
DR GeneCards; SSBP3; -.
DR HGNC; HGNC:15674; SSBP3.
DR HPA; ENSG00000157216; Low tissue specificity.
DR MIM; 607390; gene.
DR neXtProt; NX_Q9BWW4; -.
DR OpenTargets; ENSG00000157216; -.
DR PharmGKB; PA38017; -.
DR VEuPathDB; HostDB:ENSG00000157216; -.
DR eggNOG; KOG4594; Eukaryota.
DR GeneTree; ENSGT00950000183049; -.
DR HOGENOM; CLU_053914_1_0_1; -.
DR InParanoid; Q9BWW4; -.
DR OMA; MPGDFPM; -.
DR OrthoDB; 907486at2759; -.
DR PhylomeDB; Q9BWW4; -.
DR TreeFam; TF318961; -.
DR PathwayCommons; Q9BWW4; -.
DR SignaLink; Q9BWW4; -.
DR BioGRID-ORCS; 23648; 229 hits in 1087 CRISPR screens.
DR ChiTaRS; SSBP3; human.
DR GeneWiki; SSBP3; -.
DR GenomeRNAi; 23648; -.
DR Pharos; Q9BWW4; Tbio.
DR PRO; PR:Q9BWW4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BWW4; protein.
DR Bgee; ENSG00000157216; Expressed in cortical plate and 185 other tissues.
DR ExpressionAtlas; Q9BWW4; baseline and differential.
DR Genevisible; Q9BWW4; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0048382; P:mesendoderm development; IEA:Ensembl.
DR GO; GO:0021547; P:midbrain-hindbrain boundary initiation; IEA:Ensembl.
DR GO; GO:2000744; P:positive regulation of anterior head development; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021501; P:prechordal plate formation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
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_0000123828"
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:0007744|PubMed:22814378"
FT MOD_RES 155
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
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:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D032"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 123..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006260"
FT VAR_SEQ 150..169
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_006261"
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
