Reviewed,
UniProtKB/Swiss-Prot Q8IRG6 (SPT16_DROME)
Last modified
June 16, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: FACT complex subunit spt16 Alternative name(s): Facilitates chromatin transcription complex subunit SPT16 dSPT16 | ||||||
| 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 | 1083 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. 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 | Chromosomal protein Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: UniProtKB-KW regulation of chromatin assembly or disassembly Ref.5Inferred from mutant phenotype. Source: FlyBase regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | FACT complex Traceable author statement. Source: FlyBase chromosomeInferred from electronic annotation. Source: UniProtKB-KW |
| 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
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References
| « Hide '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. 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, ALTERNATIVE SPLICING. |
| [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. 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: 12815073] [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: 1551577] [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: 12934007] [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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, MASS SPECTROMETRY. Tissue: Embryo. |
Cross-references
Sequence databases | |
|---|---|
| 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. NP_728686.2. |
| UniGene | Dm.5723 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | FBgn0002183. Drosophila melanogaster. [Contig view] |
| GeneID | 38248. |
| KEGG | dme:Dmel_CG1828. |
| NMPDR | fig|7227.3.peg.7676. |
Organism-specific databases | |
| FlyBase | FBgn0002183. dre4. |
Phylogenomic databases | |
| OMA | Q8IRG6. FENIKHV. |
Gene expression databases | |
| ArrayExpress | Q8IRG6. |
| GermOnline | CG1828. Drosophila melanogaster. |
Family and domain databases | |
| InterPro | IPR013719. DUF1747_euk. IPR013953. FACT_Spt16p. IPR000994. Pept_M24_structural-domain. [Graphical view] |
| Gene3D | G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit. |
| Pfam | PF00557. Peptidase_M24. 1 hit. PF08512. Rtt106. 1 hit. PF08644. SPT16. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 807718. |
Entry information
| Entry name | SPT16_DROME | ||||||||
| Accession | Primary (citable) accession number: Q8IRG6 Secondary accession number(s): O17045 Q9W071 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


