| General information | | DisProt: | DP00721 | | Name: | FACT complex subunit spt16 | | Synonym(s): | SPT16_DROME
Facilitates chromatin transcription complex subunit SPT16
dSPT16
| | First appeared in release: | Release 5.9 (02/23/2012) | | UniProt: | Q8IRG6 | | UniGene: | | | SwissProt: | SPT16_DROME | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Drosophila melanogaster (Fruit fly) | | Sequence length: | 1083 | | Percent disordered: | 14% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSSFVLDKEA FVRRVKRLYT EWRAPSIGHD DALRNLDCIM SIVGVEEDVM YSKSMALQLW - 60
LLGYELTDTI SVFCSDAVYF LTSKKKIEFL KQTQNITEEG FPEINLLVRD RTDKDQGNFE - 120
KLIKALQNSK KGKRLGVFAK DAYPGEFSEA WKKSLTASKF EHVDISTIIA YLMCPKDESE - 180
INNIRKASLV SMDIFNKYLK DEIMDIIDSD RKVKHNKLSD GCEAAIGEKK YTSGLDPRLL - 240
DMAYPPIIQS GGAYSLKFSA VADKNPLHFG VIVCSLGARY KSYCSNISRT FLVNPTEAMQ - 300
ENYTFLVSVQ EEILKLLVPG TKLCDVYEKT LDFVKKEKPS MVDNLPKSFG FAMGLEFREN - 360
SIVIGPKCQA LLKKNMVFNL HVGISNLTNP EATDKEGKNY ALFIGDTVLV GEQSPASVMT - 420
PSKKKIKNVG IFIKDDSDEE DVDDKKTAKE DQGTEILGRS KRNAVLESKL RNEINTEEKR - 480
KEHQRELAQQ LNERAKDRLA RQGNSKEVEK VRKNTVSYKS ISQMPREPEV KELKLYVDKK - 540
YETVIMPVFG IQVPFHISTI KNISQSVEGE YTYLRINFFH PGATMGRNEG GLYPQPEATF - 600
VKEVTYRSSN VKEHGEVGAP SANLNNAFRL IKEVQKRFKT REAEEREKED LVKQDTLILS - 660
QNKGNPKLKD LYIRPNIVTK RMTGSLEAHS NGFRYISVRG DKVDILYNNI KSAFFQPCDG - 720
EMIILLHFHL KYAIMFGKKK HVDVQFYTEV GEITTDLGKH QHMHDRDDLA AEQAERELRH - 780
KLKTAFKSFC EKVETMTKSV VEFDTPFREL GFPGAPFRST VTLQPTSGSL VNLTEWPPFV - 840
ITLDDVELVH FERVQFHLRN FDMIFVFKEY NKKVAMVNAI PMNMLDHVKE WLNSCDIRYS - 900
EGVQSLNWQK IMKTITDDPE GFFEQGGWTF LDPESGSEGE NETAESEEDE AYNPTDAESD - 960
EESDEDSEYS EASEDSEESD EDLGSDEESG KDWSDLEREA AEEDRNHDYA ADDKPRNGKF - 1020
DSKKHGKSSK HSPSKSSKDK YNSRDKHHSS SSSGNKSSSK DKDRKRSRDD SRDNGHKSKK - 1080
SRH
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| Functional narrative |
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.
SUBUNIT: Component of the FACT complex, a stable heterodimer of dre4/spt16 and Ssrp. Interacts with TRL/GAGA.
Subcellular Location: Nucleus. Chromosome. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Event=Alternative splicing; Named isoforms=2; Name=B; IsoId=Q8IRG6-1; Sequence=Displayed; Name=A; IsoId=Q8IRG6-2; Sequence=VSP_019625;
SIMILARITY: 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=AAB80935.1; Type=Frameshift; Positions=Several; Sequence=AAB80936.1; Type=Frameshift; Positions=Several;
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | Acidic C-terminal | | Location: | 889 - 1044 | | Length: | 156 | | Region sequence: |
KEWLNSCDIRYSEGVQSLNWQKIMKTITDDPEGFFEQGGWTFLDPESGSEGENETAESEE
DEAYNPTDAESDEESDEDSEYSEASEDSEESDEDLGSDEESGKDWSDLEREAAEEDRNHD
YAADDKPRNGKFDSKKHGKSSKHSPSKSSKDKYNSR | | Modification type: | Complex
Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Transactivation (transcriptional activation)
| Detection methods:
- Atomic force microscopy (AFM) (pH: 7.5; Buffer A (Tris-HCl, NaCl, glycerol, ME); FACT complex (FACT subunits SSRP1 and SPT16 in Buffer A) 2 uL; KCl (Buffer B for AFM observation) 50 mM; MgCl2 (Buffer B for AFM observation) 10 mM; Tris-HCl (Buffer B for AFM observation) 20 mM)
| References:
- Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. "Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy." Chemphyschem. 2008; 9(13): 1859-66. PubMed: 18698566
- Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. "Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements." J. Biol. Chem.. 2009; 284(36): 24610-21. PubMed: 19605348
| Comments:
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| Comments |
Verification request sent 2-22-2012 (PMID: 186985660)
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