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Protein

Transcription elongation factor SPT4

Gene

spt4

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates transcription elongation by RNA polymerase II. DSIF enhances transcriptional pausing at sites proximal to the promoter, which may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF may also promote transcriptional elongation within coding regions. DSIF is required for the transcriptional induction of heat shock response genes and regulation of genes which control anterior-posterior patterning during embryonic development (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 3621C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-113418. Formation of the Early 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:
Transcription elongation factor SPT4
Alternative name(s):
DRB sensitivity-inducing factor small subunit
Short name:
DSIF small subunit
dSpt4
Gene namesi
Name:spt4
ORF Names:CG12372
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0028683. spt4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • polytene chromosome interband Source: UniProtKB
  • polytene chromosome puff Source: UniProtKB
  • transcription elongation factor complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Transcription elongation factor SPT4PRO_0000210332Add
BLAST

Proteomic databases

PaxDbiQ9TVQ5.
PRIDEiQ9TVQ5.

Expressioni

Gene expression databases

BgeeiQ9TVQ5.
GenevisibleiQ9TVQ5. DM.

Interactioni

Subunit structurei

Interacts with Spt5 to form DSIF. DSIF interacts with TRX, RNA polymerase II and with the FACT complex, which is composed of DRE4/SPT16 and SSRP/SSRP1. DSIF can also interact with the exosome, a complex with 3'-5' exoribonuclease activity which is composed of at least Csl4, Dis3, Mtr3, Rrp4, Rrp6, Rrp40, Rrp42, Rrp46 and Ski6. DSIF may also interact with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of Cdk9 and cyclin-T (CycT).1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi62161. 2 interactions.
MINTiMINT-813567.
STRINGi7227.FBpp0086953.

Structurei

3D structure databases

ProteinModelPortaliQ9TVQ5.
SMRiQ9TVQ5. Positions 2-112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4040Interaction with Spt5By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the SPT4 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 3621C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3490. Eukaryota.
COG5204. LUCA.
GeneTreeiENSGT00390000018559.
InParanoidiQ9TVQ5.
KOiK15171.
OMAiACMLCGI.
OrthoDBiEOG7RFTK7.
PhylomeDBiQ9TVQ5.

Family and domain databases

InterProiIPR029040. RPABC4/Spt4.
IPR009287. Spt4.
IPR016046. Spt4-like.
IPR022800. Spt4/RpoE2_Znf.
[Graphical view]
PANTHERiPTHR12882. PTHR12882. 1 hit.
PfamiPF06093. Spt4. 1 hit.
[Graphical view]
PIRSFiPIRSF025023. Spt4. 1 hit.
SMARTiSM01389. Spt4. 1 hit.
[Graphical view]
SUPFAMiSSF63393. SSF63393. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9TVQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFDAIPKDL RGLRACLVCS LVKSFDQFET DGCENCEEFL RMKNNKDNVY
60 70 80 90 100
DHTSNNFDGI IALTTPTDSW VAKWQRLSRF TRGIYAISVS GTLPQSTLRD
110
MKNRGIVYKS RDRSQR
Length:116
Mass (Da):13,332
Last modified:May 1, 2000 - v1
Checksum:iA4EF4580DCAA8A57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108353 mRNA. Translation: AAF14223.1.
AF109133 Genomic DNA. Translation: AAF14224.1.
AE013599 Genomic DNA. Translation: AAF58482.2.
AY075424 mRNA. Translation: AAL68240.1.
RefSeqiNP_610802.1. NM_136958.5.
UniGeneiDm.19918.

Genome annotation databases

EnsemblMetazoaiFBtr0087840; FBpp0086953; FBgn0028683.
GeneIDi36387.
KEGGidme:Dmel_CG12372.
UCSCiCG12372-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108353 mRNA. Translation: AAF14223.1.
AF109133 Genomic DNA. Translation: AAF14224.1.
AE013599 Genomic DNA. Translation: AAF58482.2.
AY075424 mRNA. Translation: AAL68240.1.
RefSeqiNP_610802.1. NM_136958.5.
UniGeneiDm.19918.

3D structure databases

ProteinModelPortaliQ9TVQ5.
SMRiQ9TVQ5. Positions 2-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62161. 2 interactions.
MINTiMINT-813567.
STRINGi7227.FBpp0086953.

Proteomic databases

PaxDbiQ9TVQ5.
PRIDEiQ9TVQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087840; FBpp0086953; FBgn0028683.
GeneIDi36387.
KEGGidme:Dmel_CG12372.
UCSCiCG12372-RA. d. melanogaster.

Organism-specific databases

CTDi36387.
FlyBaseiFBgn0028683. spt4.

Phylogenomic databases

eggNOGiKOG3490. Eukaryota.
COG5204. LUCA.
GeneTreeiENSGT00390000018559.
InParanoidiQ9TVQ5.
KOiK15171.
OMAiACMLCGI.
OrthoDBiEOG7RFTK7.
PhylomeDBiQ9TVQ5.

Enzyme and pathway databases

ReactomeiR-DME-112382. Formation of RNA Pol II elongation complex.
R-DME-113418. Formation of the Early 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

GenomeRNAii36387.
PROiQ9TVQ5.

Gene expression databases

BgeeiQ9TVQ5.
GenevisibleiQ9TVQ5. DM.

Family and domain databases

InterProiIPR029040. RPABC4/Spt4.
IPR009287. Spt4.
IPR016046. Spt4-like.
IPR022800. Spt4/RpoE2_Znf.
[Graphical view]
PANTHERiPTHR12882. PTHR12882. 1 hit.
PfamiPF06093. Spt4. 1 hit.
[Graphical view]
PIRSFiPIRSF025023. Spt4. 1 hit.
SMARTiSM01389. Spt4. 1 hit.
[Graphical view]
SUPFAMiSSF63393. SSF63393. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of Drosophila homolog of SPT4."
    Chiang P.-W.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Analysis of polymerase II elongation complexes by native gel electrophoresis. Evidence for a novel carboxyl-terminal domain-mediated termination mechanism."
    Zhang Z., Wu C.-H., Gilmour D.S.
    J. Biol. Chem. 279:23223-23228(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPT5 AND RNA POLYMERASE II.

Entry informationi

Entry nameiSPT4H_DROME
AccessioniPrimary (citable) accession number: Q9TVQ5
Secondary accession number(s): Q9V6E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.