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Protein

FACT complex subunit Ssrp1

Gene

Ssrp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi555 – 62167HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • nucleosomal DNA binding Source: FlyBase
  • nucleosome binding Source: FlyBase
  • protein self-association Source: FlyBase
  • single-stranded DNA binding Source: FlyBase
  • single-stranded RNA binding Source: FlyBase

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • DNA replication Source: UniProtKB-KW
  • neurogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • regulation of chromatin assembly or disassembly Source: FlyBase
  • regulation of DNA binding Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-DME-75955. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit Ssrp1
Alternative name(s):
Chorion-factor 5
Facilitates chromatin transcription complex subunit Ssrp1
Recombination signal sequence recognition protein
Single-strand recognition protein
dSSRP1
Gene namesi
Name:Ssrp
Synonyms:CF5, SSRP1
ORF Names:CG4817
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010278. Ssrp.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • FACT complex Source: FlyBase
  • nucleolus Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723FACT complex subunit Ssrp1PRO_0000048604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei443 – 4431Phosphoserine2 Publications
Modified residuei628 – 6281Phosphoserine1 Publication
Modified residuei664 – 6641Phosphoserine1 Publication
Modified residuei668 – 6681Phosphoserine1 Publication
Modified residuei669 – 6691Phosphothreonine1 Publication
Modified residuei670 – 6701Phosphoserine1 Publication
Modified residuei671 – 6711Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ05344.

PTM databases

iPTMnetiQ05344.

Expressioni

Tissue specificityi

Expressed at highest levels in nurse cells of the ovary.

Developmental stagei

Abundant throughout oogenesis and embryogenesis, decreases during larval stages and increases again in pupae.

Gene expression databases

BgeeiQ05344.
ExpressionAtlasiQ05344. differential.
GenevisibleiQ05344. DM.

Interactioni

Subunit structurei

Component of the FACT complex, a stable heterodimer of dre4/spt16 and Ssrp. Interacts with CHD1 and TRL/GAGA.2 Publications

GO - Molecular functioni

  • nucleosomal DNA binding Source: FlyBase
  • nucleosome binding Source: FlyBase
  • protein self-association Source: FlyBase

Protein-protein interaction databases

BioGridi63363. 7 interactions.
IntActiQ05344. 1 interaction.
STRINGi7227.FBpp0072151.

Structurei

Secondary structure

1
723
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi561 – 57616Combined sources
Helixi582 – 59413Combined sources
Helixi599 – 61416Combined sources
Turni615 – 6173Combined sources
Helixi618 – 6203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXLNMR-A555-624[»]
DisProtiDP00720.
ProteinModelPortaliQ05344.
SMRiQ05344. Positions 21-169, 197-427, 521-624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05344.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi437 – 51680Asp-rich (acidic)Add
BLAST
Compositional biasi519 – 698180Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the SSRP1 family.Curated
Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0526. Eukaryota.
COG5165. LUCA.
GeneTreeiENSGT00560000076898.
InParanoidiQ05344.
KOiK09272.
OMAiEQNIIFK.
OrthoDBiEOG7B31MG.
PhylomeDBiQ05344.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM00398. HMG. 1 hit.
SM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL
60 70 80 90 100
INSQKFVGTW GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK
110 120 130 140 150
EMCVKGWNWG TARFMGSVLS FDKESKTIFE VPLSHVSQCV TGKNEVTLEF
160 170 180 190 200
HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK FHQNVMSKAS VISASGESIA
210 220 230 240 250
IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL RLFMLPHKDS
260 270 280 290 300
RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG
310 320 330 340 350
KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG
360 370 380 390 400
YLYPLERGFI YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV
410 420 430 440 450
HIFSSIEKEE YAKLFDYITQ KKLHVSNMGK DKSGYKDVDF GDSDNENEPD
460 470 480 490 500
AYLARLKAEA REKEEDDDDG DSDEESTDED FKPNENESDV AEEYDSNVES
510 520 530 540 550
DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE RTKKPSKKKK
560 570 580 590 600
DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS
610 620 630 640 650
KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA
660 670 680 690 700
NTSGSGFKSK EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE
710 720
SEPEESEEDS NASDEDEEDE ASD
Length:723
Mass (Da):81,533
Last modified:December 1, 2000 - v2
Checksum:iDE8017F75C6CA207
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131E → Q in AAA28914 (PubMed:7688122).Curated
Sequence conflicti33 – 331K → E in AAA28914 (PubMed:7688122).Curated
Sequence conflicti212 – 2121G → R in AAA28914 (PubMed:7688122).Curated
Sequence conflicti428 – 4281M → T in AAA28914 (PubMed:7688122).Curated
Sequence conflicti498 – 4981V → E in AAA28914 (PubMed:7688122).Curated
Sequence conflicti504 – 5041D → E in AAA28914 (PubMed:7688122).Curated
Sequence conflicti573 – 5731I → Y in AAA28914 (PubMed:7688122).Curated
Sequence conflicti681 – 6811K → T in AAO45187 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08825 mRNA. Translation: AAA28914.1.
X68408 mRNA. Translation: CAA48471.1.
AE013599 Genomic DNA. Translation: AAF47064.1.
BT004831 mRNA. Translation: AAO45187.1.
PIRiA48217.
S33688.
RefSeqiNP_523830.2. NM_079106.3.
UniGeneiDm.3383.

Genome annotation databases

EnsemblMetazoaiFBtr0072242; FBpp0072151; FBgn0010278.
GeneIDi37767.
KEGGidme:Dmel_CG4817.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08825 mRNA. Translation: AAA28914.1.
X68408 mRNA. Translation: CAA48471.1.
AE013599 Genomic DNA. Translation: AAF47064.1.
BT004831 mRNA. Translation: AAO45187.1.
PIRiA48217.
S33688.
RefSeqiNP_523830.2. NM_079106.3.
UniGeneiDm.3383.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXLNMR-A555-624[»]
DisProtiDP00720.
ProteinModelPortaliQ05344.
SMRiQ05344. Positions 21-169, 197-427, 521-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63363. 7 interactions.
IntActiQ05344. 1 interaction.
STRINGi7227.FBpp0072151.

PTM databases

iPTMnetiQ05344.

Proteomic databases

PaxDbiQ05344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072242; FBpp0072151; FBgn0010278.
GeneIDi37767.
KEGGidme:Dmel_CG4817.

Organism-specific databases

CTDi37767.
FlyBaseiFBgn0010278. Ssrp.

Phylogenomic databases

eggNOGiKOG0526. Eukaryota.
COG5165. LUCA.
GeneTreeiENSGT00560000076898.
InParanoidiQ05344.
KOiK09272.
OMAiEQNIIFK.
OrthoDBiEOG7B31MG.
PhylomeDBiQ05344.

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-DME-75955. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

EvolutionaryTraceiQ05344.
GenomeRNAii37767.
PROiQ05344.

Gene expression databases

BgeeiQ05344.
ExpressionAtlasiQ05344. differential.
GenevisibleiQ05344. DM.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR009071. HMG_box_dom.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM00398. HMG. 1 hit.
SM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus."
    Hsu T., King D.L., Labonne C., Kafatos F.C.
    Proc. Natl. Acad. Sci. U.S.A. 90:6488-6492(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. "Isolation and characterization of cDNA clones encoding the Drosophila homolog of the HMG-box SSRP family that recognizes specific DNA structures."
    Bruhn S.L., Housman D.E., Lippard S.J.
    Nucleic Acids Res. 21:1643-1646(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor."
    Shimojima T., Okada M., Nakayama T., Ueda H., Okawa K., Iwamatsu A., Handa H., Hirose S.
    Genes Dev. 17:1605-1616(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 68-74; 305-309; 326-334 AND 414-420, FUNCTION, INTERACTION WITH DRE4 AND TRL.
  7. "CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin."
    Kelley D.E., Stokes D.G., Perry R.P.
    Chromosoma 108:10-25(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CHD1.
  8. "Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo."
    Saunders A., Werner J., Andrulis E.D., Nakayama T., Hirose S., Reinberg D., Lis J.T.
    Science 301:1094-1096(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-628, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-664; SER-668; THR-669; SER-670 AND SER-671, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "Solution structure of the HMG-box domain in the SSRP1 subunit of FACT."
    Kasai N., Tsunaka Y., Ohki I., Hirose S., Morikawa K., Tate S.
    J. Biomol. NMR 32:83-88(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 555-624.

Entry informationi

Entry nameiSSRP1_DROME
AccessioniPrimary (citable) accession number: Q05344
Secondary accession number(s): Q86NM5, Q9W1J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.