SPT16_YEAST
ID SPT16_YEAST Reviewed; 1035 AA.
AC P32558; D6VTU8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=Cell division control protein 68;
DE AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
DE AltName: Full=Suppressor of Ty protein 16;
GN Name=SPT16; Synonyms=CDC68, SSF1; OrderedLocusNames=YGL207W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1833637; DOI=10.1128/mcb.11.11.5718-5726.1991;
RA Rowley A., Singer R.A., Johnston G.C.;
RT "CDC68, a yeast gene that affects regulation of cell proliferation and
RT transcription, encodes a protein with a highly acidic carboxyl terminus.";
RL Mol. Cell. Biol. 11:5718-5726(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1922073; DOI=10.1128/mcb.11.11.5710-5717.1991;
RA Malone E.A., Clark C.D., Chiang A., Winston F.;
RT "Mutations in SPT16/CDC68 suppress cis- and trans-acting mutations that
RT affect promoter function in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 11:5710-5717(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9153757;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT reveals 11 open reading frames: two correspond to new genes.";
RL Yeast 13:475-477(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=2570735; DOI=10.1016/0378-1119(89)90092-9;
RA Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S.;
RT "Organization of the yeast URA2 gene: identification of a defective
RT dihydroorotase-like domain in the multifunctional carbamoylphosphate
RT synthetase-aspartate transcarbamylase complex.";
RL Gene 79:59-70(1989).
RN [7]
RP INTERACTION WITH POL1.
RX PubMed=9199353; DOI=10.1128/mcb.17.7.4178;
RA Wittmeyer J., Formosa T.;
RT "The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit
RT interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like
RT protein.";
RL Mol. Cell. Biol. 17:4178-4190(1997).
RN [8]
RP INTERACTION WITH POB3, AND MUTAGENESIS OF GLY-836.
RX PubMed=9832518; DOI=10.1093/genetics/150.4.1393;
RA Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C.,
RA Singer R.A.;
RT "The yeast protein complex containing cdc68 and pob3 mediates core-promoter
RT repression through the cdc68 N-terminal domain.";
RL Genetics 150:1393-1405(1998).
RN [9]
RP INTERACTION WITH POB3.
RX PubMed=9705338; DOI=10.1074/jbc.273.34.21972;
RA Brewster N.K., Johnston G.C., Singer R.A.;
RT "Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3
RT proteins that regulates yeast transcriptional activation and chromatin
RT repression.";
RL J. Biol. Chem. 273:21972-21979(1998).
RN [10]
RP FUNCTION, INTERACTION WITH POB3, AND SUBCELLULAR LOCATION.
RX PubMed=10413469; DOI=10.1021/bi982851d;
RA Wittmeyer J., Joss L., Formosa T.;
RT "Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant
RT heterodimer that is nuclear, chromatin-associated, and copurifies with DNA
RT polymerase alpha.";
RL Biochemistry 38:8961-8971(1999).
RN [11]
RP INTERACTION WITH SAS3.
RX PubMed=10817755;
RA John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L.;
RT "The something about silencing protein, Sas3, is the catalytic subunit of
RT NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16
RT subunit of the yeast CP (Cdc68/Pob3)-FACT complex.";
RL Genes Dev. 14:1196-1208(2000).
RN [12]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B AND NUCLEOSOMES, FUNCTION
RP OF THE FACT COMPLEX, AND MUTAGENESIS OF PRO-565; PRO-570; 848-THR--ASP-850
RP AND PRO-920.
RX PubMed=11432837; DOI=10.1093/emboj/20.13.3506;
RA Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J.;
RT "Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding
RT factor SPN.";
RL EMBO J. 20:3506-3517(2001).
RN [13]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
RX PubMed=11313475; DOI=10.1128/mcb.21.10.3491-3502.2001;
RA Brewster N.K., Johnston G.C., Singer R.A.;
RT "A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins
RT modulates transcription.";
RL Mol. Cell. Biol. 21:3491-3502(2001).
RN [14]
RP INTERACTION WITH PAF1 COMPLEX.
RX PubMed=11927560; DOI=10.1093/emboj/21.7.1764;
RA Squazzo S.L., Costa P.J., Lindstrom D.L., Kumer K.E., Simic R.,
RA Jennings J.L., Link A.J., Arndt K.M., Hartzog G.A.;
RT "The Paf1 complex physically and functionally associates with transcription
RT elongation factors in vivo.";
RL EMBO J. 21:1764-1774(2002).
RN [15]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=12524332; DOI=10.1093/genetics/162.4.1557;
RA Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y.,
RA Rhoades A.R., Kaufman P.D., Stillman D.J.;
RT "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause
RT dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin
RT structure.";
RL Genetics 162:1557-1571(2002).
RN [16]
RP INTERACTION WITH CHD1; CTR9; PAF1; CDC73; CKA1; CKA2; CKB1; CKB2 AND
RP HISTONES.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [17]
RP INTERACTION WITH CHD1.
RX PubMed=12682017; DOI=10.1093/emboj/cdg179;
RA Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J.,
RA Johnson A.D., Hartzog G.A., Arndt K.M.;
RT "Chromatin remodeling protein Chd1 interacts with transcription elongation
RT factors and localizes to transcribed genes.";
RL EMBO J. 22:1846-1856(2003).
RN [18]
RP ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
RX PubMed=12952948; DOI=10.1074/jbc.m307291200;
RA Ruone S., Rhoades A.R., Formosa T.;
RT "Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT
RT complexes and to reorganize nucleosomes.";
RL J. Biol. Chem. 278:45288-45295(2003).
RN [19]
RP FUNCTION OF THE FACT COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=14585989; DOI=10.1128/mcb.23.22.8323-8333.2003;
RA Mason P.B., Struhl K.;
RT "The FACT complex travels with elongating RNA polymerase II and is
RT important for the fidelity of transcriptional initiation in vivo.";
RL Mol. Cell. Biol. 23:8323-8333(2003).
RN [20]
RP ERRATUM OF PUBMED:14585989.
RA Mason P.B., Struhl K.;
RL Mol. Cell. Biol. 24:6536-6536(2004).
RN [21]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [22]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=12934008; DOI=10.1126/science.1087374;
RA Kaplan C.D., Laprade L., Winston F.;
RT "Transcription elongation factors repress transcription initiation from
RT cryptic sites.";
RL Science 301:1096-1099(2003).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=14739930; DOI=10.1038/sj.emboj.7600053;
RA Kim M., Ahn S.-H., Krogan N.J., Greenblatt J.F., Buratowski S.;
RT "Transitions in RNA polymerase II elongation complexes at the 3' ends of
RT genes.";
RL EMBO J. 23:354-364(2004).
RN [24]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=15082784; DOI=10.1128/mcb.24.9.3907-3917.2004;
RA Rhoades A.R., Ruone S., Formosa T.;
RT "Structural features of nucleosomes reorganized by yeast FACT and its HMG
RT box component, Nhp6.";
RL Mol. Cell. Biol. 24:3907-3917(2004).
RN [25]
RP FUNCTION OF THE FACT COMPLEX.
RX PubMed=15987999; DOI=10.1128/mcb.25.14.5812-5822.2005;
RA Biswas D., Yu Y., Prall M., Formosa T., Stillman D.J.;
RT "The yeast FACT complex has a role in transcriptional initiation.";
RL Mol. Cell. Biol. 25:5812-5822(2005).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [29]
RP INTERACTION WITH YTA7.
RX PubMed=22156209; DOI=10.1101/gad.173427.111;
RA Kurat C.F., Lambert J.P., van Dyk D., Tsui K., van Bakel H.,
RA Kaluarachchi S., Friesen H., Kainth P., Nislow C., Figeys D.,
RA Fillingham J., Andrews B.J.;
RT "Restriction of histone gene transcription to S phase by phosphorylation of
RT a chromatin boundary protein.";
RL Genes Dev. 25:2489-2501(2011).
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. Transcription elongation is promoted
CC by the repression of transcription initiation from cryptic sites. Also
CC acts in establishing transcription initiation complexes and promotes
CC SPT15/TBP-binding to a TATA box. Together with replication factor-A
CC protein (RPA), FACT may play a role in nucleosome deposition during DNA
CC replication. {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:11432837,
CC ECO:0000269|PubMed:12524332, ECO:0000269|PubMed:12934008,
CC ECO:0000269|PubMed:14585989, ECO:0000269|PubMed:15082784,
CC ECO:0000269|PubMed:15987999}.
CC -!- SUBUNIT: Forms a stable heterodimer with POB3 (PubMed:9832518,
CC PubMed:9705338, PubMed:10413469). The SPT16-POB3 dimer weakly
CC associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the
CC FACT (yFACT or SNP) complex (PubMed:11432837, PubMed:11313475,
CC PubMed:12952948). The FACT complex interacts with the CK2 (casein
CC kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the
CC components of the transcription machinery CHD1, CTR9, PAF1 and CDC73
CC (PubMed:12682017, PubMed:12242279). The FACT complex interacts with the
CC PAF1 complex (PubMed:11927560). Interacts with POL1 (PubMed:9199353).
CC Interacts with SAS3 (PubMed:10817755). Interacts with YTA7
CC (PubMed:22156209). {ECO:0000269|PubMed:10413469,
CC ECO:0000269|PubMed:10817755, ECO:0000269|PubMed:11313475,
CC ECO:0000269|PubMed:11432837, ECO:0000269|PubMed:11927560,
CC ECO:0000269|PubMed:12242279, ECO:0000269|PubMed:12682017,
CC ECO:0000269|PubMed:12952948, ECO:0000269|PubMed:22156209,
CC ECO:0000269|PubMed:9199353, ECO:0000269|PubMed:9705338,
CC ECO:0000269|PubMed:9832518}.
CC -!- INTERACTION:
CC P32558; Q04636: POB3; NbExp=8; IntAct=EBI-4334, EBI-27863;
CC P32558; P32908: SMC1; NbExp=2; IntAct=EBI-4334, EBI-17402;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10413469}. Chromosome
CC {ECO:0000269|PubMed:10413469}. Note=Colocalizes with RNA polymerase II
CC on chromatin (PubMed:10413469, PubMed:14585989, PubMed:14739930).
CC Recruited to actively transcribed loci (PubMed:14585989). Associates
CC with the coding region of HTA1 (PubMed:19683497).
CC {ECO:0000269|PubMed:10413469, ECO:0000269|PubMed:14585989,
CC ECO:0000269|PubMed:14739930, ECO:0000269|PubMed:19683497}.
CC -!- MISCELLANEOUS: Present with 18500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M73533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72729; CAA96920.1; -; Genomic_DNA.
DR EMBL; M27174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006941; DAA07909.1; -; Genomic_DNA.
DR PIR; S18512; S18512.
DR RefSeq; NP_011308.1; NM_001181072.1.
DR PDB; 3BIP; X-ray; 1.94 A; A/B=1-465.
DR PDB; 3BIQ; X-ray; 1.73 A; A=1-465.
DR PDB; 3BIT; X-ray; 1.90 A; A/B=1-451.
DR PDB; 4IOY; X-ray; 1.94 A; X=675-958.
DR PDB; 4WNN; X-ray; 1.80 A; T=958-972.
DR PDB; 7NKY; EM; 3.20 A; Q=1-1035.
DR PDBsum; 3BIP; -.
DR PDBsum; 3BIQ; -.
DR PDBsum; 3BIT; -.
DR PDBsum; 4IOY; -.
DR PDBsum; 4WNN; -.
DR PDBsum; 7NKY; -.
DR AlphaFoldDB; P32558; -.
DR SMR; P32558; -.
DR BioGRID; 33049; 474.
DR ComplexPortal; CPX-3215; FACT complex.
DR DIP; DIP-2546N; -.
DR IntAct; P32558; 68.
DR MINT; P32558; -.
DR STRING; 4932.YGL207W; -.
DR iPTMnet; P32558; -.
DR MaxQB; P32558; -.
DR PaxDb; P32558; -.
DR PRIDE; P32558; -.
DR DNASU; 852665; -.
DR EnsemblFungi; YGL207W_mRNA; YGL207W; YGL207W.
DR GeneID; 852665; -.
DR KEGG; sce:YGL207W; -.
DR SGD; S000003175; SPT16.
DR VEuPathDB; FungiDB:YGL207W; -.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; P32558; -.
DR OMA; HQFFLDG; -.
DR BioCyc; YEAST:G3O-30684-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR EvolutionaryTrace; P32558; -.
DR PRO; PR:P32558; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32558; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0035101; C:FACT complex; IGI:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IPI:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IDA:SGD.
DR GO; GO:0034728; P:nucleosome organization; IC:ComplexPortal.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:1902275; P:regulation of chromatin organization; IC:ComplexPortal.
DR GO; GO:0007063; P:regulation of sister chromatid cohesion; IDA:SGD.
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; Activator; Chromosome; Coiled coil; DNA damage; DNA repair;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1035
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000089448"
FT REGION 448..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..234
FT /evidence="ECO:0000255"
FT COILED 636..666
FT /evidence="ECO:0000255"
FT COILED 959..983
FT /evidence="ECO:0000255"
FT COMPBIAS 470..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1017
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 565
FT /note="P->S: In spt16-4; induces a spt phenotype
FT characterized by depletion of many mRNAs; when associated
FT with L-570."
FT /evidence="ECO:0000269|PubMed:11432837"
FT MUTAGEN 570
FT /note="P->L: In spt16-4; induces a spt phenotype
FT characterized by depletion of many mRNAs; when associated
FT with S-565."
FT /evidence="ECO:0000269|PubMed:11432837"
FT MUTAGEN 836
FT /note="G->D: In cdc68-1; induces a spt phenotype
FT characterized by depletion of many mRNAs."
FT /evidence="ECO:0000269|PubMed:9832518"
FT MUTAGEN 848..850
FT /note="TTD->IIY: In spt16-7; induces a spt phenotype
FT characterized by depletion of many mRNAs."
FT /evidence="ECO:0000269|PubMed:11432837"
FT MUTAGEN 920
FT /note="P->L: In spt16-6; induces a spt phenotype
FT characterized by depletion of many mRNAs."
FT /evidence="ECO:0000269|PubMed:11432837"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3BIP"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 178..207
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 311..330
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 393..403
FT /evidence="ECO:0007829|PDB:3BIQ"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:3BIT"
FT STRAND 412..421
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3BIQ"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3BIQ"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:7NKY"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 561..575
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 578..586
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:7NKY"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:7NKY"
FT HELIX 613..616
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:7NKY"
FT HELIX 636..646
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 679..686
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 721..723
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 724..730
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 735..750
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 753..763
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 790..818
FT /evidence="ECO:0007829|PDB:4IOY"
FT TURN 819..821
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 830..832
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 834..841
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 843..847
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 849..854
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 861..864
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 865..867
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 868..874
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 881..891
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 897..903
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 904..906
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 907..916
FT /evidence="ECO:0007829|PDB:4IOY"
FT STRAND 921..923
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 931..939
FT /evidence="ECO:0007829|PDB:4IOY"
FT HELIX 943..946
FT /evidence="ECO:0007829|PDB:7NKY"
FT HELIX 949..953
FT /evidence="ECO:0007829|PDB:7NKY"
SQ SEQUENCE 1035 AA; 118630 MW; 4F01C772E299E2E6 CRC64;
MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI LHNWLLSYEF
PATLIALVPG KVIIITSSAK AKHLQKAIDL FKDPESKITL ELWQRNNKEP ELNKKLFDDV
IALINSAGKT VGIPEKDSYQ GKFMTEWNPV WEAAVKENEF NVIDISLGLS KVWEVKDVNE
QAFLSVSSKG SDKFMDLLSN EMVRAVDEEL KITNAKLSDK IENKIDDVKF LKQLSPDLSA
LCPPNYKFNF DLLDWTYSPI IQSGKKFDLR VSARSTNDQL YGNGCILASC GIRYNNYCSN
ITRTFLIDPS EEMANNYDFL LTLQKEIVTN ILKPGRTPKE VYESVIEYIE KTKPELVPNF
TKNIGSLIGL EFRDSNFILN VKNDYRKIQR GDCFNISFGF NNLKDSQSAN NYALQLADTV
QIPLDETEPP RFLTNYTKAK SQISFYFNNE EEDNNKKKSS PATKVPSKPD RNSKILRTKL
RGEARGGAED AQKEQIRKEN QKKLHEKLEK NGLLRFSAAD ANGPDSEPRQ YFKKYESYVR
DSQLPTNIRD LRIHVDWKSQ TIILPIYGRP VPFHINSYKN GSKNEEGEYT YLRLNFNSPG
SSGGISKKVE ELPYEESADN QFVRSITLRS KDGDRMSETF KQIADLKKEA TKREQERKAL
ADVVQQDKLI ENKTGRTKRL DQIFVRPNPD TKRVPSTVFI HENGIRFQSP LRTDSRIDIL
FSNIKNLIFQ SCKGELIVVI HIHLKNPILM GKKKIQDVQF YREASDMSVD ETGGGRRGQS
RFRRYGDEDE LEQEQEERRK RAALDKEFKY FADAIAEASN GLLTVENTFR DLGFQGVPNR
SAVFCMPTTD CLVQLIEPPF LVINLEEVEI CILERVQFGL KNFDMVFVYK DFNKPVTHIN
TVPIESLDFL KQWLTDMDIP YTVSTINLNW ATIMKSLQDD PYQFFLDGGW NFLATGSDDE
ASDESEEEVS EYEASEDDVS DESAFSEDEE GSEVDDDISG DESEDYTGDE SEEGEDWDEL
EKKAARADRG ANFRD
