SPT16_SCHPO
ID SPT16_SCHPO Reviewed; 1019 AA.
AC O94267;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=FACT complex subunit spt16;
DE AltName: Full=Facilitates chromatin transcription complex subunit spt16;
GN Name=spt16; ORFNames=SPBP8B7.19;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP INTERACTION WITH ABO1.
RX PubMed=26582768; DOI=10.15252/embr.201540476;
RA Gal C., Murton H.E., Subramanian L., Whale A.J., Moore K.M.,
RA Paszkiewicz K., Codlin S., Baehler J., Creamer K.M., Partridge J.F.,
RA Allshire R.C., Kent N.A., Whitehall S.K.;
RT "Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome
RT occupancy and organisation.";
RL EMBO Rep. 17:79-93(2016).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5B9}.
CC -!- SUBUNIT: Forms a stable heterodimer with pob3 (By similarity). The
CC spt16-pob3 dimer weakly associates with multiple molecules of nhp6 to
CC form the FACT complex (By similarity). Interacts with abo1
CC (PubMed:26582768). {ECO:0000250|UniProtKB:Q9Y5B9,
CC ECO:0000269|PubMed:26582768}.
CC -!- INTERACTION:
CC O94267; P02299: His3:CG33854; Xeno; NbExp=4; IntAct=EBI-7414132, EBI-522090;
CC O94267; P84040: His4:CG33909; Xeno; NbExp=2; IntAct=EBI-7414132, EBI-185028;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y5B9}.
CC Chromosome {ECO:0000250|UniProtKB:Q9Y5B9}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
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DR EMBL; CU329671; CAA21804.1; -; Genomic_DNA.
DR PIR; T40813; T40813.
DR RefSeq; NP_596526.1; NM_001022447.2.
DR PDB; 3CB5; X-ray; 2.05 A; A/B=1-442.
DR PDB; 3CB6; X-ray; 1.84 A; A=1-442.
DR PDBsum; 3CB5; -.
DR PDBsum; 3CB6; -.
DR AlphaFoldDB; O94267; -.
DR SMR; O94267; -.
DR BioGRID; 277866; 9.
DR DIP; DIP-44081N; -.
DR IntAct; O94267; 3.
DR MINT; O94267; -.
DR STRING; 4896.SPBP8B7.19.1; -.
DR iPTMnet; O94267; -.
DR MaxQB; O94267; -.
DR PaxDb; O94267; -.
DR PRIDE; O94267; -.
DR EnsemblFungi; SPBP8B7.19.1; SPBP8B7.19.1:pep; SPBP8B7.19.
DR GeneID; 2541355; -.
DR KEGG; spo:SPBP8B7.19; -.
DR PomBase; SPBP8B7.19; spt16.
DR VEuPathDB; FungiDB:SPBP8B7.19; -.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; O94267; -.
DR OMA; HQFFLDG; -.
DR PhylomeDB; O94267; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; O94267; -.
DR PRO; PR:O94267; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000791; C:euchromatin; EXP:PomBase.
DR GO; GO:0035101; C:FACT complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0140713; F:histone chaperone activity; EXP:PomBase.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0140597; F:protein carrier chaperone; IMP:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0140673; P:co-transcriptional chromatin reassembly; TAS:PomBase.
DR GO; GO:0140719; P:constitutive heterochromatin assembly; IMP:PomBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISO:PomBase.
DR GO; GO:0034728; P:nucleosome organization; IMP:PomBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; DNA damage; DNA repair;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1019
FT /note="FACT complex subunit spt16"
FT /id="PRO_0000245188"
FT REGION 443..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 767..799
FT /evidence="ECO:0000255"
FT COMPBIAS 468..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..992
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3CB6"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:3CB6"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:3CB6"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 178..197
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 304..323
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 384..395
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 405..416
FT /evidence="ECO:0007829|PDB:3CB6"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:3CB6"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:3CB6"
SQ SEQUENCE 1019 AA; 116451 MW; 50AD706DD6C03313 CRC64;
MAEYEIDEIT FHKRLGILLT SWKNEEDGKT LFQDCDSILV TVGAHDDTNP YQKSTALHTW
LLGYEFPSTL ILLEKHRITI LTSVNKANML TKLAETKGAA ADVNILKRTK DAEENKKLFE
KIIEYIRATN KKVGVFPKDK TQGKFINEWD SIFEPVKSEF NLVDASLGLA KCLAIKDEQE
LANIKGASRV SVAVMSKYFV DELSTYIDQG KKITHSKFSD QMESLIDNEA FFQTKSLKLG
DIDLDQLEWC YTPIIQSGGS YDLKPSAITD DRNLHGDVVL CSLGFRYKSY CSNVGRTYLF
DPDSEQQKNY SFLVALQKKL FEYCRDGAVI GDIYTKILGL IRAKRPDLEP NFVRNLGAGI
GIEFRESSLL VNAKNPRVLQ AGMTLNLSIG FGNLINPHPK NSQSKEYALL LIDTIQITRS
DPIVFTDSPK AQGDISYFFG EDDSSLEDGV KPRKPPTRGT ATISSHKGKT RSETRDLDDS
AEKRRVEHQK QLASRKQAEG LQRFAQGSVP SSGIEKPTVK RFESYKRDSQ LPQAIGELRI
LVDYRAQSII LPIFGRPVPF HISTLKNASK NDEGNFVYLR LNFVSPGQIG GKKDELPFED
PNAQFIRSFT FRSSNNSRMS QVFKDIQDMK KAATKRETER KEFADVIEQD KLIEIKNKRP
AHINDVYVRP AIDGKRLPGF IEIHQNGIRY QSPLRSDSHI DLLFSNMKHL FFQPCEGELI
VLIHVHLKAP IMVGKRKTQD VQFYREVSDI QFDETGNKKR KYMYGDEDEL EQEQEERRRR
AQLDREFKSF AEKIAEASEG RIELDIPFRE LAFNGVPFRS NVLLQPTTDC LVQLTDTPFT
VITLNEIEIA HLERVQFGLK NFDLVFIFQD FRRPPIHINT IPMEQLDNVK EWLDSCDICF
YEGPLNLNWT TIMKTVNEDP IAFFEEGGWG FLGAPSDDEG DDSVEEVSEY EASDADPSDE
EEEESEEYSE DASEEDGYSE SEVEDEESGE DWDELERKAR QEDAKHDAFE ERPSKKRHR
