SSBP4_HUMAN
ID SSBP4_HUMAN Reviewed; 385 AA.
AC Q9BWG4; Q9BWW5;
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 4;
GN Name=SSBP4;
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], GENE STRUCTURE, AND ALTERNATIVE SPLICING
RP (ISOFORM 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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355, 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 [5]
RP IDENTIFICATION BY 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355, AND IDENTIFICATION BY
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341 AND THR-355, 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).
CC -!- INTERACTION:
CC Q9BWG4; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-744719, EBI-14103818;
CC Q9BWG4; Q9UBH0: IL36RN; NbExp=4; IntAct=EBI-744719, EBI-465156;
CC Q9BWG4; Q86U70-2: LDB1; NbExp=4; IntAct=EBI-744719, EBI-11979761;
CC Q9BWG4; Q92569: PIK3R3; NbExp=3; IntAct=EBI-744719, EBI-79893;
CC Q9BWG4; Q13526: PIN1; NbExp=4; IntAct=EBI-744719, EBI-714158;
CC Q9BWG4; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-744719, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BWG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWG4-2; Sequence=VSP_054113;
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; AY026292; AAK20020.1; -; Genomic_DNA.
DR EMBL; AY026276; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026277; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026278; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026279; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026280; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026281; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026282; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026283; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026284; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026285; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026286; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026287; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026288; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026289; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026290; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AY026291; AAK20020.1; JOINED; Genomic_DNA.
DR EMBL; AC008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000274; AAH00274.1; -; mRNA.
DR CCDS; CCDS12378.1; -. [Q9BWG4-1]
DR CCDS; CCDS32960.1; -. [Q9BWG4-2]
DR RefSeq; NP_001009998.1; NM_001009998.3. [Q9BWG4-2]
DR RefSeq; NP_116016.1; NM_032627.4. [Q9BWG4-1]
DR AlphaFoldDB; Q9BWG4; -.
DR SMR; Q9BWG4; -.
DR BioGRID; 128006; 41.
DR IntAct; Q9BWG4; 28.
DR MINT; Q9BWG4; -.
DR STRING; 9606.ENSP00000270061; -.
DR GlyConnect; 2076; 1 N-Linked glycan (1 site).
DR GlyGen; Q9BWG4; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9BWG4; -.
DR PhosphoSitePlus; Q9BWG4; -.
DR BioMuta; SSBP4; -.
DR DMDM; 27734580; -.
DR EPD; Q9BWG4; -.
DR jPOST; Q9BWG4; -.
DR MassIVE; Q9BWG4; -.
DR MaxQB; Q9BWG4; -.
DR PaxDb; Q9BWG4; -.
DR PeptideAtlas; Q9BWG4; -.
DR PRIDE; Q9BWG4; -.
DR ProteomicsDB; 79275; -. [Q9BWG4-1]
DR ProteomicsDB; 79333; -.
DR Antibodypedia; 28035; 78 antibodies from 17 providers.
DR DNASU; 170463; -.
DR Ensembl; ENST00000270061.12; ENSP00000270061.5; ENSG00000130511.16. [Q9BWG4-1]
DR Ensembl; ENST00000348495.10; ENSP00000252807.7; ENSG00000130511.16. [Q9BWG4-2]
DR GeneID; 170463; -.
DR KEGG; hsa:170463; -.
DR MANE-Select; ENST00000270061.12; ENSP00000270061.5; NM_032627.5; NP_116016.1.
DR UCSC; uc002niy.4; human. [Q9BWG4-1]
DR CTD; 170463; -.
DR DisGeNET; 170463; -.
DR GeneCards; SSBP4; -.
DR HGNC; HGNC:15676; SSBP4.
DR HPA; ENSG00000130511; Low tissue specificity.
DR MIM; 607391; gene.
DR neXtProt; NX_Q9BWG4; -.
DR OpenTargets; ENSG00000130511; -.
DR PharmGKB; PA38018; -.
DR VEuPathDB; HostDB:ENSG00000130511; -.
DR eggNOG; KOG4594; Eukaryota.
DR GeneTree; ENSGT00950000183049; -.
DR HOGENOM; CLU_053914_1_0_1; -.
DR InParanoid; Q9BWG4; -.
DR OMA; YTIMNPM; -.
DR OrthoDB; 907486at2759; -.
DR PhylomeDB; Q9BWG4; -.
DR TreeFam; TF318961; -.
DR PathwayCommons; Q9BWG4; -.
DR SignaLink; Q9BWG4; -.
DR BioGRID-ORCS; 170463; 35 hits in 1078 CRISPR screens.
DR ChiTaRS; SSBP4; human.
DR GenomeRNAi; 170463; -.
DR Pharos; Q9BWG4; Tdark.
DR PRO; PR:Q9BWG4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BWG4; protein.
DR Bgee; ENSG00000130511; Expressed in right uterine tube and 163 other tissues.
DR ExpressionAtlas; Q9BWG4; baseline and differential.
DR Genevisible; Q9BWG4; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..385
FT /note="Single-stranded DNA-binding protein 4"
FT /id="PRO_0000123832"
FT DOMAIN 17..49
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 122..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
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 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 123..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054113"
SQ SEQUENCE 385 AA; 39388 MW; F55FD3470B810742 CRC64;
MYAKGGKGSA VPSDSQAREK LALYVYEYLL HIGAQKSAQT FLSEIRWEKN ITLGEPPGFL
HSWWCVFWDL YCAAPDRREA CEHSGEAKAF QDYSAAAAPS PVMGSMAPGD TMAAGSMAAG
FFQGPPGSQP SPHNPNAPMM GPHGQPFMSP RFPGGPRPTL RMPSQPPAGL PGSQPLLPGA
MEPSPRAQGH PSMGGPMQRV TPPRGMASVG PQSYGGGMRP PPNSLAGPGL PAMNMGPGVR
GPWASPSGNS IPYSSSSPGS YTGPPGGGGP PGTPIMPSPG DSTNSSENMY TIMNPIGQGA
GRANFPLGPG PEGPMAAMSA MEPHHVNGSL GSGDMDGLPK SSPGAVAGLS NAPGTPRDDG
EMAAAGTFLH PFPSESYSPG MTMSV
