Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32558

- SPT16_YEAST

UniProt

P32558 - SPT16_YEAST

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 - Molecular functioni

    1. protein binding Source: IntAct

    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

    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.

    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

    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.
    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. 169 interactions.
    DIPiDIP-2546N.
    IntActiP32558. 57 interactions.
    MINTiMINT-427889.
    STRINGi4932.YGL207W.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI     50
    LHNWLLSYEF PATLIALVPG KVIIITSSAK AKHLQKAIDL FKDPESKITL 100
    ELWQRNNKEP ELNKKLFDDV IALINSAGKT VGIPEKDSYQ GKFMTEWNPV 150
    WEAAVKENEF NVIDISLGLS KVWEVKDVNE QAFLSVSSKG SDKFMDLLSN 200
    EMVRAVDEEL KITNAKLSDK IENKIDDVKF LKQLSPDLSA LCPPNYKFNF 250
    DLLDWTYSPI IQSGKKFDLR VSARSTNDQL YGNGCILASC GIRYNNYCSN 300
    ITRTFLIDPS EEMANNYDFL LTLQKEIVTN ILKPGRTPKE VYESVIEYIE 350
    KTKPELVPNF TKNIGSLIGL EFRDSNFILN VKNDYRKIQR GDCFNISFGF 400
    NNLKDSQSAN NYALQLADTV QIPLDETEPP RFLTNYTKAK SQISFYFNNE 450
    EEDNNKKKSS PATKVPSKPD RNSKILRTKL RGEARGGAED AQKEQIRKEN 500
    QKKLHEKLEK NGLLRFSAAD ANGPDSEPRQ YFKKYESYVR DSQLPTNIRD 550
    LRIHVDWKSQ TIILPIYGRP VPFHINSYKN GSKNEEGEYT YLRLNFNSPG 600
    SSGGISKKVE ELPYEESADN QFVRSITLRS KDGDRMSETF KQIADLKKEA 650
    TKREQERKAL ADVVQQDKLI ENKTGRTKRL DQIFVRPNPD TKRVPSTVFI 700
    HENGIRFQSP LRTDSRIDIL FSNIKNLIFQ SCKGELIVVI HIHLKNPILM 750
    GKKKIQDVQF YREASDMSVD ETGGGRRGQS RFRRYGDEDE LEQEQEERRK 800
    RAALDKEFKY FADAIAEASN GLLTVENTFR DLGFQGVPNR SAVFCMPTTD 850
    CLVQLIEPPF LVINLEEVEI CILERVQFGL KNFDMVFVYK DFNKPVTHIN 900
    TVPIESLDFL KQWLTDMDIP YTVSTINLNW ATIMKSLQDD PYQFFLDGGW 950
    NFLATGSDDE ASDESEEEVS EYEASEDDVS DESAFSEDEE GSEVDDDISG 1000
    DESEDYTGDE SEEGEDWDEL EKKAARADRG ANFRD 1035
    Length:1,035
    Mass (Da):118,630
    Last modified:October 1, 1993 - v1
    Checksum:i4F01C772E299E2E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 169 interactions.
    DIPi DIP-2546N.
    IntActi P32558. 57 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.
    OMAi NDEVASY.
    OrthoDBi EOG7SFJ58.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30684-MONOMER.

    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

    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: October 1, 2014
    This is version 125 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