Q8IRG6 (SPT16_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FACT complex subunit spt16

Alternative name(s):
Facilitates chromatin transcription complex subunit SPT16
dSPT16

Gene names

Name:	dre4
Synonyms:	spt16
ORF Names:	CG1828

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1083 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. The FACT complex is required for expression of Hox genes. Ref.5 Ref.6
Subunit structure	Component of the FACT complex, a stable heterodimer of dre4/spt16 and Ssrp. Interacts with TRL/GAGA. Ref.5
Subcellular location	Nucleus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.7
Sequence similarities	Belongs to the peptidase M24 family. SPT16 subfamily.
Caution	Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.
Sequence caution	The sequence AAB80935.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAB80936.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	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 neurogenesis Inferred from mutant phenotype PubMed 21549331. Source: FlyBase positive regulation of transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17174895. Source: FlyBase regulation of chromatin assembly or disassembly Inferred from mutant phenotype Ref.5. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	FACT complex Inferred from direct assay PubMed 19605348. Source: FlyBase chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chromatin binding Inferred from direct assay PubMed 17174895. Source: FlyBase
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: Q8IRG6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A (identifier: Q8IRG6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1031-1031: H → HSRRDREEARSSSHSKKHKSNSSSSSSHLKSSSSKHGSSS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1083	1083	FACT complex subunit spt16		PRO_0000245174
Regions
	Coiled coil	466 – 504	39	Potential
	Compositional bias	934 – 1003	70	Glu-rich (acidic)
	Compositional bias	1028 – 1059	32	Ser-rich
Amino acid modifications
	Modified residue	437	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1031	1	H → HSRRDREEARSSSHSKKHKS NSSSSSSHLKSSSSKHGSSS in isoform A.		VSP_019625
Experimental info
	Sequence conflict	345	1	L → V in AAB80935. Ref.1
	Sequence conflict	345	1	L → V in AAB80936. Ref.1
	Sequence conflict	598	1	A → R in AAB80935. Ref.1
	Sequence conflict	598	1	A → R in AAB80936. Ref.1
	Sequence conflict	1057	1	S → I in AAB80935. Ref.1
	Sequence conflict	1057	1	S → I in AAB80936. Ref.1
	Sequence conflict	1080 – 1081	2	KS → NA in AAB80935. Ref.1
	Sequence conflict	1080 – 1081	2	KS → NA in AAB80936. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 6A2AF4012D93D449	FASTA	1,083	123,583
	10 20 30 40 50 60 MSSFVLDKEA FVRRVKRLYT EWRAPSIGHD DALRNLDCIM SIVGVEEDVM YSKSMALQLW 70 80 90 100 110 120 LLGYELTDTI SVFCSDAVYF LTSKKKIEFL KQTQNITEEG FPEINLLVRD RTDKDQGNFE 130 140 150 160 170 180 KLIKALQNSK KGKRLGVFAK DAYPGEFSEA WKKSLTASKF EHVDISTIIA YLMCPKDESE 190 200 210 220 230 240 INNIRKASLV SMDIFNKYLK DEIMDIIDSD RKVKHNKLSD GCEAAIGEKK YTSGLDPRLL 250 260 270 280 290 300 DMAYPPIIQS GGAYSLKFSA VADKNPLHFG VIVCSLGARY KSYCSNISRT FLVNPTEAMQ 310 320 330 340 350 360 ENYTFLVSVQ EEILKLLVPG TKLCDVYEKT LDFVKKEKPS MVDNLPKSFG FAMGLEFREN 370 380 390 400 410 420 SIVIGPKCQA LLKKNMVFNL HVGISNLTNP EATDKEGKNY ALFIGDTVLV GEQSPASVMT 430 440 450 460 470 480 PSKKKIKNVG IFIKDDSDEE DVDDKKTAKE DQGTEILGRS KRNAVLESKL RNEINTEEKR 490 500 510 520 530 540 KEHQRELAQQ LNERAKDRLA RQGNSKEVEK VRKNTVSYKS ISQMPREPEV KELKLYVDKK 550 560 570 580 590 600 YETVIMPVFG IQVPFHISTI KNISQSVEGE YTYLRINFFH PGATMGRNEG GLYPQPEATF 610 620 630 640 650 660 VKEVTYRSSN VKEHGEVGAP SANLNNAFRL IKEVQKRFKT REAEEREKED LVKQDTLILS 670 680 690 700 710 720 QNKGNPKLKD LYIRPNIVTK RMTGSLEAHS NGFRYISVRG DKVDILYNNI KSAFFQPCDG 730 740 750 760 770 780 EMIILLHFHL KYAIMFGKKK HVDVQFYTEV GEITTDLGKH QHMHDRDDLA AEQAERELRH 790 800 810 820 830 840 KLKTAFKSFC EKVETMTKSV VEFDTPFREL GFPGAPFRST VTLQPTSGSL VNLTEWPPFV 850 860 870 880 890 900 ITLDDVELVH FERVQFHLRN FDMIFVFKEY NKKVAMVNAI PMNMLDHVKE WLNSCDIRYS 910 920 930 940 950 960 EGVQSLNWQK IMKTITDDPE GFFEQGGWTF LDPESGSEGE NETAESEEDE AYNPTDAESD 970 980 990 1000 1010 1020 EESDEDSEYS EASEDSEESD EDLGSDEESG KDWSDLEREA AEEDRNHDYA ADDKPRNGKF 1030 1040 1050 1060 1070 1080 DSKKHGKSSK HSPSKSSKDK YNSRDKHHSS SSSGNKSSSK DKDRKRSRDD SRDNGHKSKK SRH
	Isoform A [UniParc]. Checksum: 2313A44E1EA1A300	FASTA	1,122	127,781
	10 20 30 40 50 60 MSSFVLDKEA FVRRVKRLYT EWRAPSIGHD DALRNLDCIM SIVGVEEDVM YSKSMALQLW 70 80 90 100 110 120 LLGYELTDTI SVFCSDAVYF LTSKKKIEFL KQTQNITEEG FPEINLLVRD RTDKDQGNFE 130 140 150 160 170 180 KLIKALQNSK KGKRLGVFAK DAYPGEFSEA WKKSLTASKF EHVDISTIIA YLMCPKDESE 190 200 210 220 230 240 INNIRKASLV SMDIFNKYLK DEIMDIIDSD RKVKHNKLSD GCEAAIGEKK YTSGLDPRLL 250 260 270 280 290 300 DMAYPPIIQS GGAYSLKFSA VADKNPLHFG VIVCSLGARY KSYCSNISRT FLVNPTEAMQ 310 320 330 340 350 360 ENYTFLVSVQ EEILKLLVPG TKLCDVYEKT LDFVKKEKPS MVDNLPKSFG FAMGLEFREN 370 380 390 400 410 420 SIVIGPKCQA LLKKNMVFNL HVGISNLTNP EATDKEGKNY ALFIGDTVLV GEQSPASVMT 430 440 450 460 470 480 PSKKKIKNVG IFIKDDSDEE DVDDKKTAKE DQGTEILGRS KRNAVLESKL RNEINTEEKR 490 500 510 520 530 540 KEHQRELAQQ LNERAKDRLA RQGNSKEVEK VRKNTVSYKS ISQMPREPEV KELKLYVDKK 550 560 570 580 590 600 YETVIMPVFG IQVPFHISTI KNISQSVEGE YTYLRINFFH PGATMGRNEG GLYPQPEATF 610 620 630 640 650 660 VKEVTYRSSN VKEHGEVGAP SANLNNAFRL IKEVQKRFKT REAEEREKED LVKQDTLILS 670 680 690 700 710 720 QNKGNPKLKD LYIRPNIVTK RMTGSLEAHS NGFRYISVRG DKVDILYNNI KSAFFQPCDG 730 740 750 760 770 780 EMIILLHFHL KYAIMFGKKK HVDVQFYTEV GEITTDLGKH QHMHDRDDLA AEQAERELRH 790 800 810 820 830 840 KLKTAFKSFC EKVETMTKSV VEFDTPFREL GFPGAPFRST VTLQPTSGSL VNLTEWPPFV 850 860 870 880 890 900 ITLDDVELVH FERVQFHLRN FDMIFVFKEY NKKVAMVNAI PMNMLDHVKE WLNSCDIRYS 910 920 930 940 950 960 EGVQSLNWQK IMKTITDDPE GFFEQGGWTF LDPESGSEGE NETAESEEDE AYNPTDAESD 970 980 990 1000 1010 1020 EESDEDSEYS EASEDSEESD EDLGSDEESG KDWSDLEREA AEEDRNHDYA ADDKPRNGKF 1030 1040 1050 1060 1070 1080 DSKKHGKSSK HSRRDREEAR SSSHSKKHKS NSSSSSSHLK SSSSKHGSSS SPSKSSKDKY 1090 1100 1110 1120 NSRDKHHSSS SSGNKSSSKD KDRKRSRDDS RDNGHKSKKS RH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Washington A.V., Robinson P., Sliter T.J. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]	"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.
[3]	"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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[4]	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 (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Testis.
[5]	"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: NUCLEOTIDE SEQUENCE [MRNA] OF 40-1083 (ISOFORM B), PROTEIN SEQUENCE OF 134-410; 613-627; 670-678; 703-710 AND 760-771, FUNCTION, INTERACTION WITH SSRP AND TRL.
[6]	"Developmental arrest and ecdysteroid deficiency resulting from mutations at the dre4 locus of Drosophila." Sliter T.J., Gilbert L.I. Genetics 130:555-568(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY FUNCTION.
[7]	"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.
[8]	"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-437, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF023269 mRNA. Translation: AAB80935.1. Frameshift. AF023270 mRNA. Translation: AAB80936.1. Frameshift. AE014296 Genomic DNA. Translation: AAF47587.2. AE014296 Genomic DNA. Translation: AAN11502.2. BT010116 mRNA. Translation: AAQ22585.1. AB083008 mRNA. Translation: BAC54898.1.
PIR	T13928. T13929.
RefSeq	NP_476610.2. NM_057262.4. NP_728686.2. NM_167922.3.
UniGene	Dm.5723.
3D structure databases
ProteinModelPortal	Q8IRG6.
SMR	Q8IRG6. Positions 1-436.
ModBase	Search...
Proteomic databases
PaxDb	Q8IRG6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0072865; FBpp0072744; FBgn0002183.
GeneID	38248.
KEGG	dme:Dmel_CG1828.
Organism-specific databases
CTD	38248.
FlyBase	FBgn0002183. dre4.
Phylogenomic databases
eggNOG	COG5406.
GeneTree	ENSGT00390000014495.
InParanoid	Q8IRG6.
OMA	GARYKNY.
OrthoDB	EOG40CFXV.
Gene expression databases
Bgee	Q8IRG6.
GermOnline	CG1828. Drosophila melanogaster.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR013719. DUF1747. IPR013953. FACT_Spt16p. IPR000994. Pept_M24_structural-domain. [Graphical view]
Pfam	PF00557. Peptidase_M24. 1 hit. PF08512. Rtt106. 1 hit. PF08644. SPT16. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	38248.
NextBio	807718.

Entry information

Entry name

SPT16_DROME

Accession

Primary (citable) accession number: Q8IRG6
Secondary accession number(s): O17045 , O17046, Q7YTY1, Q86SB9, Q9W071

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project