Reviewed,
UniProtKB/Swiss-Prot Q9W420 (SPT6H_DROME)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Transcription elongation factor SPT6 | ||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| 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 | 1831 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Acts to stimulate transcriptional elongation by RNA polymerase II By similarity. |
| Subunit structure | Self associates. Interacts with RNA polymerase II. Interacts with the FACT complex, which is composed of dre4/Spt16 and Ssrp/Ssrp1. Interacts 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. Interacts with the DRB sensitivity-inducing factor complex (the DSIF complex), which is composed of Spt4 and Spt5. Ref.7 Ref.8 |
| Subcellular location | Nucleus. Note: Recruited to sites of active transcription where it colocalizes with the elongating form of RNA polymerase II. Ref.7 Ref.8 Ref.5 Ref.6 |
| Sequence similarities | Belongs to the SPT6 family. Contains 1 S1 motif domain. Contains 1 SH2 domain. |
| Sequence caution | The sequence AAF14115.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1831 | 1831 | Transcription elongation factor SPT6 | PRO_0000072170 | |||||
Regions | |||||||||
| Domain | 1217 – 1286 | 70 | S1 motif | ||||||
| Domain | 1329 – 1440 | 112 | SH2 1 | ||||||
| Coiled coil | 7 – 59 | 53 | Potential | ||||||
| Coiled coil | 467 – 494 | 28 | Potential | ||||||
| Compositional bias | 6 – 245 | 240 | Asp/Glu-rich | ||||||
| Compositional bias | 489 – 512 | 24 | Glu-rich | ||||||
| Compositional bias | 1552 – 1682 | 131 | Ser-rich | ||||||
| Compositional bias | 1675 – 1702 | 28 | Gly-rich | ||||||
| Compositional bias | 1771 – 1783 | 13 | Poly-Gly | ||||||
Amino acid modifications | |||||||||
| Modified residue | 34 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 36 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 37 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 66 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 70 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 124 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 151 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 156 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 159 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 171 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 173 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 1661 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 1664 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 1815 | 1 | Phosphoserine Ref.10 | ||||||
Experimental info | |||||||||
| Sequence conflict | 1194 | 1 | L → I in AAF14114. Ref.1 | ||||||
| Sequence conflict | 1194 | 1 | L → I in AAF14115. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of Drosophila SPT6 homolog." 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. Venter J.C.Science 287:2185-2195(2000) [PubMed: 10731132] [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. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. |
| [4] | "A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-1831. Strain: Berkeley. Tissue: Embryo. |
| [5] | "Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster." Kaplan C.D., Morris J.R., Wu C.-T., Winston F. Genes Dev. 14:2623-2634(2000) [PubMed: 11040216] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [6] | "High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation." Andrulis E.D., Guzman E., Doering P., Werner J., Lis J.T. Genes Dev. 14:2635-2649(2000) [PubMed: 11040217] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [7] | "The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila." Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P., Lis J.T. Nature 420:837-841(2002) [PubMed: 12490954] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH SPT5 AND THE EXOSOME COMPLEX, SUBCELLULAR LOCATION. |
| [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: INTERACTION WITH SPT5; RNA POLYMERASE II AND THE FACT COMPLEX, 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-124, 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-34; SER-36; SER-37; SER-66; SER-70; SER-75; SER-151; SER-156; SER-159; THR-171; SER-173; SER-1661; SER-1664 AND SER-1815, MASS SPECTROMETRY. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF104400 mRNA. Translation: AAF14114.1. AF104401 Genomic DNA. Translation: AAF14115.1. Sequence problems. AE014298 Genomic DNA. Translation: AAF46140.1. AY052030 mRNA. Translation: AAK93454.1. Different initiation. | |
| RefSeq | NP_651962.2. |
| UniGene | Dm.7373 |
3D structure databases | |
| HSSP | HSSP built from PDB template 5RXN based on UniProtKB P00268. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9W420. |
Genome annotation databases | |
| Ensembl | FBgn0028982. Drosophila melanogaster. [Contig view] |
| GeneID | 44000. |
| KEGG | dme:Dmel_CG12225. |
| NMPDR | fig|7227.3.peg.16696. |
Organism-specific databases | |
| FlyBase | FBgn0028982. Spt6. |
Phylogenomic databases | |
| HOGENOM | Q9W420. |
| OMA | Q9W420. QHFEVPF. |
Gene expression databases | |
| ArrayExpress | Q9W420. |
| GermOnline | CG12225. Drosophila melanogaster. |
Family and domain databases | |
| InterPro | IPR012340. NA-bd_OB-fold. IPR003029. Rbsml_prot_S1_RNA-bd_dom. IPR006641. Resolv_RNaseH-like. IPR000980. SH2. IPR017072. TF_Spt6. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| Pfam | PF00575. S1. 1 hit. [Graphical view] |
| PIRSF | PIRSF036947. Spt6. 1 hit. |
| SMART | SM00252. SH2. 2 hits. SM00732. YqgFc. 1 hit. [Graphical view] |
| PROSITE | PS50126. S1. 1 hit. PS50001. SH2. False negative. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 836551. |
Entry information
| Entry name | SPT6H_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9W420 Secondary accession number(s): Q960J2, Q9U8B5, Q9U8B6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


