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FACT complex subunit Ssrp1 (Chorion-factor 5) (Facilitates chromatin transcription complex subunit Ssrp1) (Recombination signal sequence recognition protein) (Single-strand recognition protein) (dSSRP1)

 SSRP1_DROME             Reviewed;         723 AA.
Q05344; Q86NM5; Q9W1J4;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
28-MAR-2018, entry version 163.
RecName: Full=FACT complex subunit Ssrp1;
AltName: Full=Chorion-factor 5;
AltName: Full=Facilitates chromatin transcription complex subunit Ssrp1;
AltName: Full=Recombination signal sequence recognition protein;
AltName: Full=Single-strand recognition protein;
AltName: Full=dSSRP1;
Name=Ssrp; Synonyms=CF5, SSRP1; ORFNames=CG4817;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=7688122; DOI=10.1073/pnas.90.14.6488;
Hsu T., King D.L., Labonne C., Kafatos F.C.;
"A Drosophila single-strand DNA/RNA-binding factor contains a high-
mobility-group box and is enriched in the nucleolus.";
Proc. Natl. Acad. Sci. U.S.A. 90:6488-6492(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8479916; DOI=10.1093/nar/21.7.1643;
Bruhn S.L., Housman D.E., Lippard S.J.;
"Isolation and characterization of cDNA clones encoding the Drosophila
homolog of the HMG-box SSRP family that recognizes specific DNA
structures.";
Nucleic Acids Res. 21:1643-1646(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 68-74; 305-309; 326-334 AND 414-420, FUNCTION, AND
INTERACTION WITH DRE4 AND TRL.
PubMed=12815073; DOI=10.1101/gad.1086803;
Shimojima T., Okada M., Nakayama T., Ueda H., Okawa K., Iwamatsu A.,
Handa H., Hirose S.;
"Drosophila FACT contributes to Hox gene expression through physical
and functional interactions with GAGA factor.";
Genes Dev. 17:1605-1616(2003).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH CHD1.
PubMed=10199952; DOI=10.1007/s004120050347;
Kelley D.E., Stokes D.G., Perry R.P.;
"CHD1 interacts with SSRP1 and depends on both its chromodomain and
its ATPase/helicase-like domain for proper association with
chromatin.";
Chromosoma 108:10-25(1999).
[8]
SUBCELLULAR LOCATION.
PubMed=12934007; DOI=10.1126/science.1085712;
Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S.,
Reinberg D., Lis J.T.;
"Tracking FACT and the RNA polymerase II elongation complex through
chromatin in vivo.";
Science 301:1094-1096(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-628, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-664; SER-668;
THR-669; SER-670 AND SER-671, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[11]
STRUCTURE BY NMR OF 555-624.
PubMed=16041486; DOI=10.1007/s10858-005-3662-3;
Kasai N., Tsunaka Y., Ohki I., Hirose S., Morikawa K., Tate S.;
"Solution structure of the HMG-box domain in the SSRP1 subunit of
FACT.";
J. Biomol. NMR 32:83-88(2005).
-!- FUNCTION: Component of the FACT complex, a general chromatin
factor that acts to reorganize nucleosomes. The FACT complex is
involved in multiple processes that require DNA as a template such
as mRNA elongation, DNA replication and DNA repair. During
transcription elongation the FACT complex acts as a histone
chaperone that both destabilizes and restores nucleosomal
structure. It facilitates the passage of RNA polymerase II and
transcription by promoting the dissociation of one histone H2A-H2B
dimer from the nucleosome, then subsequently promotes the
reestablishment of the nucleosome following the passage of RNA
polymerase II. Binds specifically to single-stranded DNA and RNA
with highest affinity for nucleotides G and U. The FACT complex is
required for expression of Hox genes.
{ECO:0000269|PubMed:12815073}.
-!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
dre4/spt16 and Ssrp. Interacts with CHD1 and TRL/GAGA.
{ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:12815073}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12934007,
ECO:0000303|PubMed:10199952}. Chromosome
{ECO:0000269|PubMed:12934007, ECO:0000303|PubMed:10199952}.
Nucleus, nucleolus {ECO:0000269|PubMed:12934007}. Note=Colocalizes
with RNA polymerase II on chromatin. Recruited to actively
transcribed loci. {ECO:0000269|PubMed:12934007}.
-!- TISSUE SPECIFICITY: Expressed at highest levels in nurse cells of
the ovary.
-!- DEVELOPMENTAL STAGE: Abundant throughout oogenesis and
embryogenesis, decreases during larval stages and increases again
in pupae.
-!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L08825; AAA28914.1; -; mRNA.
EMBL; X68408; CAA48471.1; -; mRNA.
EMBL; AE013599; AAF47064.1; -; Genomic_DNA.
EMBL; BT004831; AAO45187.1; -; mRNA.
PIR; A48217; A48217.
PIR; S33688; S33688.
RefSeq; NP_523830.2; NM_079106.3.
UniGene; Dm.3383; -.
PDB; 1WXL; NMR; -; A=555-624.
PDBsum; 1WXL; -.
DisProt; DP00720; -.
ProteinModelPortal; Q05344; -.
SMR; Q05344; -.
BioGrid; 63363; 10.
IntAct; Q05344; 2.
STRING; 7227.FBpp0072151; -.
iPTMnet; Q05344; -.
PaxDb; Q05344; -.
PRIDE; Q05344; -.
EnsemblMetazoa; FBtr0072242; FBpp0072151; FBgn0010278.
GeneID; 37767; -.
KEGG; dme:Dmel_CG4817; -.
CTD; 37767; -.
FlyBase; FBgn0010278; Ssrp.
eggNOG; KOG0526; Eukaryota.
eggNOG; COG5165; LUCA.
GeneTree; ENSGT00560000076898; -.
InParanoid; Q05344; -.
KO; K09272; -.
OMA; TGDAICI; -.
OrthoDB; EOG091G04JP; -.
PhylomeDB; Q05344; -.
Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
EvolutionaryTrace; Q05344; -.
GenomeRNAi; 37767; -.
PRO; PR:Q05344; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0010278; -.
ExpressionAtlas; Q05344; differential.
Genevisible; Q05344; DM.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0035101; C:FACT complex; IDA:FlyBase.
GO; GO:0005730; C:nucleolus; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0070087; F:chromo shadow domain binding; IMP:CAFA.
GO; GO:0031492; F:nucleosomal DNA binding; IDA:FlyBase.
GO; GO:0031491; F:nucleosome binding; IDA:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0043621; F:protein self-association; IDA:FlyBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0001672; P:regulation of chromatin assembly or disassembly; IMP:FlyBase.
GO; GO:0051101; P:regulation of DNA binding; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 1.
Gene3D; 2.30.29.220; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR013719; DUF1747.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR035417; POB3_N.
InterPro; IPR000969; SSrcognition.
InterPro; IPR024954; SSRP1_dom.
InterPro; IPR038167; SSRP1_sf.
Pfam; PF00505; HMG_box; 1.
Pfam; PF17292; POB3_N; 1.
Pfam; PF08512; Rtt106; 1.
Pfam; PF03531; SSrecog; 1.
PRINTS; PR00887; SSRCOGNITION.
SMART; SM00398; HMG; 1.
SMART; SM01287; Rtt106; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; DNA replication;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
Transcription; Transcription regulation.
CHAIN 1 723 FACT complex subunit Ssrp1.
/FTId=PRO_0000048604.
DNA_BIND 555 621 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
COMPBIAS 437 516 Asp-rich (acidic).
COMPBIAS 519 698 Lys-rich (basic).
MOD_RES 443 443 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 669 669 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 13 13 E -> Q (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 33 33 K -> E (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 212 212 G -> R (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 428 428 M -> T (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 498 498 V -> E (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 504 504 D -> E (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 573 573 I -> Y (in Ref. 1; AAA28914).
{ECO:0000305}.
CONFLICT 681 681 K -> T (in Ref. 5; AAO45187).
{ECO:0000305}.
HELIX 561 576 {ECO:0000244|PDB:1WXL}.
HELIX 582 594 {ECO:0000244|PDB:1WXL}.
HELIX 599 614 {ECO:0000244|PDB:1WXL}.
TURN 615 617 {ECO:0000244|PDB:1WXL}.
HELIX 618 620 {ECO:0000244|PDB:1WXL}.
SEQUENCE 723 AA; 81533 MW; DE8017F75C6CA207 CRC64;
MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL INSQKFVGTW
GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK EMCVKGWNWG TARFMGSVLS
FDKESKTIFE VPLSHVSQCV TGKNEVTLEF HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK
FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL
RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG
KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI
YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDYITQ
KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEDDDDG DSDEESTDED
FKPNENESDV AEEYDSNVES DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE
RTKKPSKKKK DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS
KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA NTSGSGFKSK
EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE SEPEESEEDS NASDEDEEDE
ASD


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