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Protein

FACT complex subunit spt16

Gene

spt16

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-SPO-674695. RNA Polymerase II Pre-transcription Events.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit spt16
Alternative name(s):
Facilitates chromatin transcription complex subunit spt16
Gene namesi
Name:spt16
ORF Names:SPBP8B7.19
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP8B7.19.
PomBaseiSPBP8B7.19. spt16.

Subcellular locationi

GO - Cellular componenti

  • FACT complex Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10191019FACT complex subunit spt16PRO_0000245188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei444 – 4441Phosphoserine1 Publication
Modified residuei445 – 4451Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94267.

PTM databases

iPTMnetiO94267.

Interactioni

Subunit structurei

Forms a stable heterodimer with pob3. The spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to form the FACT complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi277866. 4 interactions.
DIPiDIP-44081N.
IntActiO94267. 1 interaction.
MINTiMINT-4682716.

Structurei

Secondary structure

1
1019
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2316Combined sources
Helixi25 – 306Combined sources
Beta strandi36 – 427Combined sources
Helixi53 – 6210Combined sources
Beta strandi67 – 748Combined sources
Beta strandi77 – 837Combined sources
Helixi84 – 874Combined sources
Turni88 – 903Combined sources
Helixi91 – 944Combined sources
Beta strandi100 – 1089Combined sources
Helixi112 – 12716Combined sources
Turni128 – 1303Combined sources
Beta strandi131 – 1355Combined sources
Helixi144 – 15310Combined sources
Turni154 – 1563Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1645Combined sources
Helixi166 – 1749Combined sources
Helixi178 – 19720Combined sources
Helixi199 – 20911Combined sources
Helixi215 – 2239Combined sources
Helixi224 – 2274Combined sources
Helixi229 – 2324Combined sources
Helixi235 – 2373Combined sources
Helixi244 – 2463Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi276 – 2838Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi294 – 3018Combined sources
Helixi304 – 32320Combined sources
Helixi330 – 34415Combined sources
Helixi346 – 3516Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi361 – 3644Combined sources
Helixi367 – 3693Combined sources
Beta strandi384 – 39512Combined sources
Beta strandi405 – 41612Combined sources
Beta strandi419 – 4213Combined sources
Helixi432 – 4354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CB5X-ray2.05A/B1-442[»]
3CB6X-ray1.84A1-442[»]
ProteinModelPortaliO94267.
SMRiO94267. Positions 1-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94267.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili767 – 79933Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi945 – 101167Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M24 family. SPT16 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000209079.
InParanoidiO94267.
OMAiYANIDAI.
OrthoDBiEOG7SFJ58.
PhylomeDBiO94267.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SMARTiSM01285. FACT-Spt16_Nlob. 1 hit.
SM01287. Rtt106. 1 hit.
SM01286. SPT16. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Complete.

O94267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYEIDEIT FHKRLGILLT SWKNEEDGKT LFQDCDSILV TVGAHDDTNP
60 70 80 90 100
YQKSTALHTW LLGYEFPSTL ILLEKHRITI LTSVNKANML TKLAETKGAA
110 120 130 140 150
ADVNILKRTK DAEENKKLFE KIIEYIRATN KKVGVFPKDK TQGKFINEWD
160 170 180 190 200
SIFEPVKSEF NLVDASLGLA KCLAIKDEQE LANIKGASRV SVAVMSKYFV
210 220 230 240 250
DELSTYIDQG KKITHSKFSD QMESLIDNEA FFQTKSLKLG DIDLDQLEWC
260 270 280 290 300
YTPIIQSGGS YDLKPSAITD DRNLHGDVVL CSLGFRYKSY CSNVGRTYLF
310 320 330 340 350
DPDSEQQKNY SFLVALQKKL FEYCRDGAVI GDIYTKILGL IRAKRPDLEP
360 370 380 390 400
NFVRNLGAGI GIEFRESSLL VNAKNPRVLQ AGMTLNLSIG FGNLINPHPK
410 420 430 440 450
NSQSKEYALL LIDTIQITRS DPIVFTDSPK AQGDISYFFG EDDSSLEDGV
460 470 480 490 500
KPRKPPTRGT ATISSHKGKT RSETRDLDDS AEKRRVEHQK QLASRKQAEG
510 520 530 540 550
LQRFAQGSVP SSGIEKPTVK RFESYKRDSQ LPQAIGELRI LVDYRAQSII
560 570 580 590 600
LPIFGRPVPF HISTLKNASK NDEGNFVYLR LNFVSPGQIG GKKDELPFED
610 620 630 640 650
PNAQFIRSFT FRSSNNSRMS QVFKDIQDMK KAATKRETER KEFADVIEQD
660 670 680 690 700
KLIEIKNKRP AHINDVYVRP AIDGKRLPGF IEIHQNGIRY QSPLRSDSHI
710 720 730 740 750
DLLFSNMKHL FFQPCEGELI VLIHVHLKAP IMVGKRKTQD VQFYREVSDI
760 770 780 790 800
QFDETGNKKR KYMYGDEDEL EQEQEERRRR AQLDREFKSF AEKIAEASEG
810 820 830 840 850
RIELDIPFRE LAFNGVPFRS NVLLQPTTDC LVQLTDTPFT VITLNEIEIA
860 870 880 890 900
HLERVQFGLK NFDLVFIFQD FRRPPIHINT IPMEQLDNVK EWLDSCDICF
910 920 930 940 950
YEGPLNLNWT TIMKTVNEDP IAFFEEGGWG FLGAPSDDEG DDSVEEVSEY
960 970 980 990 1000
EASDADPSDE EEEESEEYSE DASEEDGYSE SEVEDEESGE DWDELERKAR
1010
QEDAKHDAFE ERPSKKRHR
Length:1,019
Mass (Da):116,451
Last modified:May 1, 1999 - v1
Checksum:i50AD706DD6C03313
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21804.1.
PIRiT40813.
RefSeqiNP_596526.1. NM_001022447.2.

Genome annotation databases

EnsemblFungiiSPBP8B7.19.1; SPBP8B7.19.1:pep; SPBP8B7.19.
GeneIDi2541355.
KEGGispo:SPBP8B7.19.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21804.1.
PIRiT40813.
RefSeqiNP_596526.1. NM_001022447.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CB5X-ray2.05A/B1-442[»]
3CB6X-ray1.84A1-442[»]
ProteinModelPortaliO94267.
SMRiO94267. Positions 1-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277866. 4 interactions.
DIPiDIP-44081N.
IntActiO94267. 1 interaction.
MINTiMINT-4682716.

PTM databases

iPTMnetiO94267.

Proteomic databases

MaxQBiO94267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP8B7.19.1; SPBP8B7.19.1:pep; SPBP8B7.19.
GeneIDi2541355.
KEGGispo:SPBP8B7.19.

Organism-specific databases

EuPathDBiFungiDB:SPBP8B7.19.
PomBaseiSPBP8B7.19. spt16.

Phylogenomic databases

HOGENOMiHOG000209079.
InParanoidiO94267.
OMAiYANIDAI.
OrthoDBiEOG7SFJ58.
PhylomeDBiO94267.

Enzyme and pathway databases

ReactomeiR-SPO-674695. RNA Polymerase II Pre-transcription Events.

Miscellaneous databases

EvolutionaryTraceiO94267.
NextBioi20802464.
PROiO94267.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view]
SMARTiSM01285. FACT-Spt16_Nlob. 1 hit.
SM01287. Rtt106. 1 hit.
SM01286. SPT16. 1 hit.
[Graphical view]
SUPFAMiSSF55920. SSF55920. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSPT16_SCHPO
AccessioniPrimary (citable) accession number: O94267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  4. 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.