Q05344 (SSRP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Ssrp
Synonyms:	CF5, SSRP1
ORF Names:	CG4817

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.6
Subunit structure	Component of the FACT complex, a stable heterodimer of dre4/spt16 and Ssrp. Interacts with CHD1 and TRL/GAGA. Ref.6 Ref.7
Subcellular location	Nucleus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.7 Ref.8
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.
Sequence similarities	Belongs to the SSRP1 family. Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Ligand	DNA-binding RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW regulation of DNA binding Inferred from mutant phenotype. Source: FlyBase regulation of chromatin assembly or disassembly Inferred from mutant phenotype Ref.6. Source: FlyBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	FACT complex Inferred from direct assay. Source: FlyBase chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleosomal DNA binding Inferred from direct assay. Source: FlyBase protein self-association Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 723

723

FACT complex subunit Ssrp1

PRO_0000048604

Regions

DNA binding

555 – 621

67

HMG box

Compositional bias

437 – 516

80

Asp-rich (acidic)

Compositional bias

519 – 698

180

Lys-rich (basic)

Amino acid modifications

Modified residue

443

1

Phosphoserine Ref.9 Ref.10

Modified residue

628

1

Phosphoserine Ref.9

Modified residue

664

1

Phosphoserine Ref.10

Modified residue

668

1

Phosphoserine Ref.10

Modified residue

669

1

Phosphothreonine Ref.10

Modified residue

670

1

Phosphoserine Ref.10

Modified residue

671

1

Phosphoserine Ref.10

Experimental info

Sequence conflict

13

1

E → Q in AAA28914. Ref.1

Sequence conflict

33

1

K → E in AAA28914. Ref.1

Sequence conflict

212

1

G → R in AAA28914. Ref.1

Sequence conflict

428

1

M → T in AAA28914. Ref.1

Sequence conflict

498

1

V → E in AAA28914. Ref.1

Sequence conflict

504

1

D → E in AAA28914. Ref.1

Sequence conflict

573

1

I → Y in AAA28914. Ref.1

Sequence conflict

681

1

K → T in AAO45187. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

723

Helix Strand Turn

Details...

Helix

561 – 576

16

Helix

582 – 594

13

Helix

599 – 614

16

Turn

615 – 617

3

Helix

618 – 620

3

Sequences

	Sequence		Length	Mass (Da)
	Q05344 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: DE8017F75C6CA207	FASTA	723	81,533
	10 20 30 40 50 60 MTDSLEYNDI NAEVRGVLCS GRLKMTEQNI IFKNTKTGKV EQISAEDIDL INSQKFVGTW 70 80 90 100 110 120 GLRVFTKGGV LHRFTGFRDS EHEKLGKFIK AAYSQEMVEK EMCVKGWNWG TARFMGSVLS 130 140 150 160 170 180 FDKESKTIFE VPLSHVSQCV TGKNEVTLEF HQNDDAPVGL LEMRFHIPAV ESAEEDPVDK 190 200 210 220 230 240 FHQNVMSKAS VISASGESIA IFREIQILTP RGRYDIKIFS TFFQLHGKTF DYKIPMDSVL 250 260 270 280 290 300 RLFMLPHKDS RQMFFVLSLD PPIKQGQTRY HYLVLLFAPD EETTIELPFS EAELRDKYEG 310 320 330 340 350 360 KLEKEISGPV YEVMGKVMKV LIGRKITGPG NFIGHSGTAA VGCSFKAAAG YLYPLERGFI 370 380 390 400 410 420 YIHKPPLHIR FEEISSVNFA RSGGSTRSFD FEVTLKNGTV HIFSSIEKEE YAKLFDYITQ 430 440 450 460 470 480 KKLHVSNMGK DKSGYKDVDF GDSDNENEPD AYLARLKAEA REKEEDDDDG DSDEESTDED 490 500 510 520 530 540 FKPNENESDV AEEYDSNVES DSDDDSDASG GGGDSDGAKK KKEKKSEKKE KKEKKHKEKE 550 560 570 580 590 600 RTKKPSKKKK DSGKPKRATT AFMLWLNDTR ESIKRENPGI KVTEIAKKGG EMWKELKDKS 610 620 630 640 650 660 KWEDAAAKDK QRYHDEMRNY KPEAGGDSDN EKGGKSSKKR KTEPSPSKKA NTSGSGFKSK 670 680 690 700 710 720 EYISDDDSTS SDDEKDNEPA KKKSKPPSDG DAKKKKAKSE SEPEESEEDS NASDEDEEDE ASD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7688122] [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: 8479916] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	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 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: 12815073] [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: 10199952] [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: 12934007] [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: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-628, 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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-664; SER-668; THR-669; SER-670 AND SER-671, 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: 16041486] [Abstract] Cited for: STRUCTURE BY NMR OF 555-624.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L08825 mRNA. Translation: AAA28914.1.
X68408 mRNA. Translation: CAA48471.1.
AE013599 Genomic DNA. Translation: AAF47064.1.
BT004831 mRNA. Translation: AAO45187.1.

PIR

A48217.
S33688.

RefSeq

NP_523830.2. NM_079106.2.

UniGene

Dm.3383.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WXL	NMR	-	A	555-624	[»]

ProteinModelPortal

Q05344.

SMR

Q05344. Positions 195-428, 552-624.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q05344. 1 interaction.

STRING

Q05344.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0072242; FBpp0072151; FBgn0010278.

GeneID

37767.

KEGG

dme:Dmel_CG4817.

NMPDR

fig|7227.3.peg.7134.

Organism-specific databases

CTD

37767.

FlyBase

FBgn0010278. Ssrp.

Phylogenomic databases

eggNOG

inNOG08394.

GeneTree

EMGT00050000003536.

InParanoid

Q05344.

OMA

PVEVKKG.

OrthoDB

EOG40CFZ2.

PhylomeDB

Q05344.

Gene expression databases

Bgee

Q05344.

GermOnline

CG4817. Drosophila melanogaster.

Family and domain databases

InterPro

IPR000910. HMG_HMG1/HMG2.
IPR009071. HMG_superfamily.
IPR000969. SSrcognition.
[Graphical view]

Gene3D

G3DSA:1.10.30.10. HMG-box. 1 hit.

KO

K09272.

Pfam

PF00505. HMG_box. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]

PRINTS

PR00887. SSRCOGNITION.

SMART

SM00398. HMG. 1 hit.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 1 hit.

PROSITE

PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

805310.

Entry information

Entry name

SSRP1_DROME

Accession

Primary (citable) accession number: Q05344
Secondary accession number(s): Q86NM5, Q9W1J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project