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P32558

- SPT16_YEAST

UniProt

P32558 - SPT16_YEAST

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Protein

FACT complex subunit SPT16

Gene

SPT16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 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. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.7 Publications

GO - Biological processi

  1. DNA-dependent DNA replication Source: SGD
  2. DNA repair Source: UniProtKB-KW
  3. DNA replication-independent nucleosome organization Source: SGD
  4. nucleosome assembly Source: SGD
  5. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  6. positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  7. regulation of transcription by chromatin organization Source: SGD
  8. transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-30684-MONOMER.
ReactomeiREACT_250507. RNA Polymerase II Pre-transcription Events.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit SPT16
Alternative name(s):
Cell division control protein 68
Facilitates chromatin transcription complex subunit SPT16
Suppressor of Ty protein 16
Gene namesi
Name:SPT16
Synonyms:CDC68, SSF1
Ordered Locus Names:YGL207W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL207w.
SGDiS000003175. SPT16.

Subcellular locationi

Nucleus. Chromosome
Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.

GO - Cellular componenti

  1. FACT complex Source: SGD
  2. nuclear chromatin Source: SGD
  3. replication fork protection complex Source: SGD
  4. transcription elongation factor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi565 – 5651P → S in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with L-570. 1 Publication
Mutagenesisi570 – 5701P → L in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with S-565. 1 Publication
Mutagenesisi836 – 8361G → D in cdc68-1; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication
Mutagenesisi848 – 8503TTD → IIY in spt16-7; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication
Mutagenesisi920 – 9201P → L in spt16-6; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10351035FACT complex subunit SPT16PRO_0000089448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei526 – 5261Phosphoserine1 Publication
Modified residuei765 – 7651Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32558.
PaxDbiP32558.
PeptideAtlasiP32558.

Expressioni

Gene expression databases

GenevestigatoriP32558.

Interactioni

Subunit structurei

Forms a stable heterodimer with POB3. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex. The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73. The FACT complex interacts with the PAF1 complex. SPT16 interacts with SAS3 and POL1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POB3Q046369EBI-4334,EBI-27863

Protein-protein interaction databases

BioGridi33049. 170 interactions.
DIPiDIP-2546N.
IntActiP32558. 60 interactions.
MINTiMINT-427889.
STRINGi4932.YGL207W.

Structurei

Secondary structure

1
1035
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2114Combined sources
Helixi22 – 243Combined sources
Beta strandi30 – 367Combined sources
Helixi47 – 5610Combined sources
Beta strandi61 – 688Combined sources
Beta strandi71 – 777Combined sources
Helixi78 – 847Combined sources
Helixi85 – 917Combined sources
Beta strandi92 – 954Combined sources
Beta strandi99 – 1057Combined sources
Helixi110 – 12718Combined sources
Beta strandi129 – 1335Combined sources
Helixi142 – 15817Combined sources
Beta strandi161 – 1644Combined sources
Helixi166 – 1727Combined sources
Helixi178 – 20730Combined sources
Helixi214 – 22310Combined sources
Helixi224 – 2263Combined sources
Helixi228 – 23912Combined sources
Helixi250 – 2523Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi283 – 2908Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi301 – 3088Combined sources
Helixi311 – 33020Combined sources
Helixi338 – 35215Combined sources
Helixi354 – 3596Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi369 – 3724Combined sources
Helixi375 – 3773Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi393 – 40311Combined sources
Turni406 – 4083Combined sources
Beta strandi412 – 42110Combined sources
Beta strandi431 – 4333Combined sources
Helixi440 – 4434Combined sources
Beta strandi679 – 6868Combined sources
Beta strandi689 – 6913Combined sources
Beta strandi696 – 7005Combined sources
Beta strandi702 – 7076Combined sources
Helixi712 – 7143Combined sources
Beta strandi717 – 7204Combined sources
Helixi721 – 7233Combined sources
Beta strandi724 – 7307Combined sources
Beta strandi735 – 75016Combined sources
Beta strandi753 – 76311Combined sources
Helixi790 – 81829Combined sources
Turni819 – 8213Combined sources
Beta strandi825 – 8273Combined sources
Helixi830 – 8323Combined sources
Beta strandi834 – 8418Combined sources
Beta strandi843 – 8475Combined sources
Beta strandi849 – 8546Combined sources
Beta strandi856 – 8594Combined sources
Beta strandi861 – 8644Combined sources
Helixi865 – 8673Combined sources
Beta strandi868 – 8747Combined sources
Beta strandi881 – 89111Combined sources
Beta strandi897 – 9037Combined sources
Helixi904 – 9063Combined sources
Helixi907 – 91610Combined sources
Beta strandi921 – 9233Combined sources
Helixi931 – 9399Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BIPX-ray1.94A/B1-465[»]
3BIQX-ray1.73A1-465[»]
3BITX-ray1.90A/B1-451[»]
4IOYX-ray1.94X675-958[»]
ProteinModelPortaliP32558.
SMRiP32558. Positions 1-447, 533-652, 677-941.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32558.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili208 – 23427Sequence AnalysisAdd
BLAST
Coiled coili636 – 66631Sequence AnalysisAdd
BLAST
Coiled coili959 – 98325Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi958 – 102164Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M24 family. SPT16 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5406.
GeneTreeiENSGT00390000014495.
HOGENOMiHOG000209079.
InParanoidiP32558.
OMAiNDEVASY.
OrthoDBiEOG7SFJ58.

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]
SUPFAMiSSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Complete.

P32558-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI
60 70 80 90 100
LHNWLLSYEF PATLIALVPG KVIIITSSAK AKHLQKAIDL FKDPESKITL
110 120 130 140 150
ELWQRNNKEP ELNKKLFDDV IALINSAGKT VGIPEKDSYQ GKFMTEWNPV
160 170 180 190 200
WEAAVKENEF NVIDISLGLS KVWEVKDVNE QAFLSVSSKG SDKFMDLLSN
210 220 230 240 250
EMVRAVDEEL KITNAKLSDK IENKIDDVKF LKQLSPDLSA LCPPNYKFNF
260 270 280 290 300
DLLDWTYSPI IQSGKKFDLR VSARSTNDQL YGNGCILASC GIRYNNYCSN
310 320 330 340 350
ITRTFLIDPS EEMANNYDFL LTLQKEIVTN ILKPGRTPKE VYESVIEYIE
360 370 380 390 400
KTKPELVPNF TKNIGSLIGL EFRDSNFILN VKNDYRKIQR GDCFNISFGF
410 420 430 440 450
NNLKDSQSAN NYALQLADTV QIPLDETEPP RFLTNYTKAK SQISFYFNNE
460 470 480 490 500
EEDNNKKKSS PATKVPSKPD RNSKILRTKL RGEARGGAED AQKEQIRKEN
510 520 530 540 550
QKKLHEKLEK NGLLRFSAAD ANGPDSEPRQ YFKKYESYVR DSQLPTNIRD
560 570 580 590 600
LRIHVDWKSQ TIILPIYGRP VPFHINSYKN GSKNEEGEYT YLRLNFNSPG
610 620 630 640 650
SSGGISKKVE ELPYEESADN QFVRSITLRS KDGDRMSETF KQIADLKKEA
660 670 680 690 700
TKREQERKAL ADVVQQDKLI ENKTGRTKRL DQIFVRPNPD TKRVPSTVFI
710 720 730 740 750
HENGIRFQSP LRTDSRIDIL FSNIKNLIFQ SCKGELIVVI HIHLKNPILM
760 770 780 790 800
GKKKIQDVQF YREASDMSVD ETGGGRRGQS RFRRYGDEDE LEQEQEERRK
810 820 830 840 850
RAALDKEFKY FADAIAEASN GLLTVENTFR DLGFQGVPNR SAVFCMPTTD
860 870 880 890 900
CLVQLIEPPF LVINLEEVEI CILERVQFGL KNFDMVFVYK DFNKPVTHIN
910 920 930 940 950
TVPIESLDFL KQWLTDMDIP YTVSTINLNW ATIMKSLQDD PYQFFLDGGW
960 970 980 990 1000
NFLATGSDDE ASDESEEEVS EYEASEDDVS DESAFSEDEE GSEVDDDISG
1010 1020 1030
DESEDYTGDE SEEGEDWDEL EKKAARADRG ANFRD
Length:1,035
Mass (Da):118,630
Last modified:October 1, 1993 - v1
Checksum:i4F01C772E299E2E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73533 Genomic DNA. No translation available.
Z72729 Genomic DNA. Translation: CAA96920.1.
M27174 Genomic DNA. No translation available.
BK006941 Genomic DNA. Translation: DAA07909.1.
PIRiS18512.
RefSeqiNP_011308.1. NM_001181072.1.

Genome annotation databases

EnsemblFungiiYGL207W; YGL207W; YGL207W.
GeneIDi852665.
KEGGisce:YGL207W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73533 Genomic DNA. No translation available.
Z72729 Genomic DNA. Translation: CAA96920.1 .
M27174 Genomic DNA. No translation available.
BK006941 Genomic DNA. Translation: DAA07909.1 .
PIRi S18512.
RefSeqi NP_011308.1. NM_001181072.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BIP X-ray 1.94 A/B 1-465 [» ]
3BIQ X-ray 1.73 A 1-465 [» ]
3BIT X-ray 1.90 A/B 1-451 [» ]
4IOY X-ray 1.94 X 675-958 [» ]
ProteinModelPortali P32558.
SMRi P32558. Positions 1-447, 533-652, 677-941.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33049. 170 interactions.
DIPi DIP-2546N.
IntActi P32558. 60 interactions.
MINTi MINT-427889.
STRINGi 4932.YGL207W.

Proteomic databases

MaxQBi P32558.
PaxDbi P32558.
PeptideAtlasi P32558.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL207W ; YGL207W ; YGL207W .
GeneIDi 852665.
KEGGi sce:YGL207W.

Organism-specific databases

CYGDi YGL207w.
SGDi S000003175. SPT16.

Phylogenomic databases

eggNOGi COG5406.
GeneTreei ENSGT00390000014495.
HOGENOMi HOG000209079.
InParanoidi P32558.
OMAi NDEVASY.
OrthoDBi EOG7SFJ58.

Enzyme and pathway databases

BioCyci YEAST:G3O-30684-MONOMER.
Reactomei REACT_250507. RNA Polymerase II Pre-transcription Events.

Miscellaneous databases

EvolutionaryTracei P32558.
NextBioi 971957.
PROi P32558.

Gene expression databases

Genevestigatori P32558.

Family and domain databases

Gene3Di 3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProi IPR029149. Creatin/AminoP/Spt16_NTD.
IPR013719. DUF1747.
IPR029148. FACT-Spt16_Nlobe.
IPR013953. FACT_Spt16p.
IPR000994. Pept_M24_structural-domain.
[Graphical view ]
Pfami PF14826. FACT-Spt16_Nlob. 1 hit.
PF00557. Peptidase_M24. 1 hit.
PF08512. Rtt106. 1 hit.
PF08644. SPT16. 1 hit.
[Graphical view ]
SUPFAMi SSF55920. SSF55920. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "CDC68, a yeast gene that affects regulation of cell proliferation and transcription, encodes a protein with a highly acidic carboxyl terminus."
    Rowley A., Singer R.A., Johnston G.C.
    Mol. Cell. Biol. 11:5718-5726(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutations in SPT16/CDC68 suppress cis- and trans-acting mutations that affect promoter function in Saccharomyces cerevisiae."
    Malone E.A., Clark C.D., Chiang A., Winston F.
    Mol. Cell. Biol. 11:5710-5717(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes."
    Feuermann M., Simeonava L., Souciet J.-L., Potier S.
    Yeast 13:475-477(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex."
    Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S.
    Gene 79:59-70(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  7. "The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein."
    Wittmeyer J., Formosa T.
    Mol. Cell. Biol. 17:4178-4190(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POL1.
  8. "The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain."
    Evans D.R.H., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C., Singer R.A.
    Genetics 150:1393-1405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POB3, MUTAGENESIS OF GLY-836.
  9. "Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3 proteins that regulates yeast transcriptional activation and chromatin repression."
    Brewster N.K., Johnston G.C., Singer R.A.
    J. Biol. Chem. 273:21972-21979(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POB3.
  10. "Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha."
    Wittmeyer J., Joss L., Formosa T.
    Biochemistry 38:8961-8971(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POB3, SUBCELLULAR LOCATION.
  11. "The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex."
    John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L.
    Genes Dev. 14:1196-1208(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAS3.
  12. "Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN."
    Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J.
    EMBO J. 20:3506-3517(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B AND NUCLEOSOMES, FUNCTION OF THE FACT COMPLEX, MUTAGENESIS OF PRO-565; PRO-570; 848-THR--ASP-850 AND PRO-920.
  13. "A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription."
    Brewster N.K., Johnston G.C., Singer R.A.
    Mol. Cell. Biol. 21:3491-3502(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
  14. "The Paf1 complex physically and functionally associates with transcription elongation factors in vivo."
    Squazzo S.L., Costa P.J., Lindstrom D.L., Kumer K.E., Simic R., Jennings J.L., Link A.J., Arndt K.M., Hartzog G.A.
    EMBO J. 21:1764-1774(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAF1 COMPLEX.
  15. "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure."
    Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., Rhoades A.R., Kaufman P.D., Stillman D.J.
    Genetics 162:1557-1571(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE FACT COMPLEX.
  16. "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach."
    Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F.
    Mol. Cell. Biol. 22:6979-6992(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD1; CTR9; PAF1; CDC73; CKA1; CKA2; CKB1; CKB2 AND HISTONES.
  17. "Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes."
    Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., Arndt K.M.
    EMBO J. 22:1846-1856(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD1.
  18. "Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes."
    Ruone S., Rhoades A.R., Formosa T.
    J. Biol. Chem. 278:45288-45295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SPT16-POB3 DIMER WITH NHP6A/B.
  19. "The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo."
    Mason P.B., Struhl K.
    Mol. Cell. Biol. 23:8323-8333(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE FACT COMPLEX, SUBCELLULAR LOCATION.
  20. Erratum
    Mason P.B., Struhl K.
    Mol. Cell. Biol. 24:6536-6536(2004)
  21. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  22. "Transcription elongation factors repress transcription initiation from cryptic sites."
    Kaplan C.D., Laprade L., Winston F.
    Science 301:1096-1099(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE FACT COMPLEX.
  23. "Transitions in RNA polymerase II elongation complexes at the 3' ends of genes."
    Kim M., Ahn S.-H., Krogan N.J., Greenblatt J.F., Buratowski S.
    EMBO J. 23:354-364(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  24. "Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6."
    Rhoades A.R., Ruone S., Formosa T.
    Mol. Cell. Biol. 24:3907-3917(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE FACT COMPLEX.
  25. "The yeast FACT complex has a role in transcriptional initiation."
    Biswas D., Yu Y., Prall M., Formosa T., Stillman D.J.
    Mol. Cell. Biol. 25:5812-5822(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE FACT COMPLEX.
  26. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-765, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPT16_YEAST
AccessioniPrimary (citable) accession number: P32558
Secondary accession number(s): D6VTU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18500 molecules/cell in log phase SD medium.1 Publication

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. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3