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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: 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

  • DNA-dependent DNA replication Source: SGD
  • DNA repair Source: UniProtKB-KW
  • DNA replication-independent nucleosome organization Source: SGD
  • nucleosome assembly Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: GO_Central
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  • 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.
ReactomeiR-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL207W.
SGDiS000003175. SPT16.

Subcellular locationi

  • Nucleus
  • Chromosome

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

GO - Cellular componenti

  • FACT complex Source: SGD
  • nuclear chromatin Source: SGD
  • replication fork protection complex Source: SGD
  • transcription elongation factor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi565P → S in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with L-570. 1 Publication1
Mutagenesisi570P → L in spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with S-565. 1 Publication1
Mutagenesisi836G → D in cdc68-1; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication1
Mutagenesisi848 – 850TTD → IIY in spt16-7; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication3
Mutagenesisi920P → L in spt16-6; induces a spt phenotype characterized by depletion of many mRNAs. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000894481 – 1035FACT complex subunit SPT16Add BLAST1035

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei526PhosphoserineCombined sources1
Modified residuei765PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32558.
PRIDEiP32558.

PTM databases

iPTMnetiP32558.

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. 190 interactors.
DIPiDIP-2546N.
IntActiP32558. 61 interactors.
MINTiMINT-427889.

Structurei

Secondary structure

11035
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 21Combined sources14
Helixi22 – 24Combined sources3
Beta strandi30 – 36Combined sources7
Helixi47 – 56Combined sources10
Beta strandi61 – 68Combined sources8
Beta strandi71 – 77Combined sources7
Helixi78 – 84Combined sources7
Helixi85 – 91Combined sources7
Beta strandi92 – 95Combined sources4
Beta strandi99 – 105Combined sources7
Helixi110 – 127Combined sources18
Beta strandi129 – 133Combined sources5
Helixi142 – 158Combined sources17
Beta strandi161 – 164Combined sources4
Helixi166 – 172Combined sources7
Helixi178 – 207Combined sources30
Helixi214 – 223Combined sources10
Helixi224 – 226Combined sources3
Helixi228 – 239Combined sources12
Helixi250 – 252Combined sources3
Beta strandi253 – 257Combined sources5
Beta strandi260 – 262Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi283 – 290Combined sources8
Beta strandi292 – 294Combined sources3
Beta strandi301 – 308Combined sources8
Helixi311 – 330Combined sources20
Helixi338 – 352Combined sources15
Helixi354 – 359Combined sources6
Beta strandi365 – 367Combined sources3
Beta strandi369 – 372Combined sources4
Helixi375 – 377Combined sources3
Beta strandi378 – 380Combined sources3
Beta strandi393 – 403Combined sources11
Turni406 – 408Combined sources3
Beta strandi412 – 421Combined sources10
Beta strandi431 – 433Combined sources3
Helixi440 – 443Combined sources4
Beta strandi679 – 686Combined sources8
Beta strandi689 – 691Combined sources3
Beta strandi696 – 700Combined sources5
Beta strandi702 – 707Combined sources6
Helixi712 – 714Combined sources3
Beta strandi717 – 720Combined sources4
Helixi721 – 723Combined sources3
Beta strandi724 – 730Combined sources7
Beta strandi735 – 750Combined sources16
Beta strandi753 – 763Combined sources11
Helixi790 – 818Combined sources29
Turni819 – 821Combined sources3
Beta strandi825 – 827Combined sources3
Helixi830 – 832Combined sources3
Beta strandi834 – 841Combined sources8
Beta strandi843 – 847Combined sources5
Beta strandi849 – 854Combined sources6
Beta strandi856 – 859Combined sources4
Beta strandi861 – 864Combined sources4
Helixi865 – 867Combined sources3
Beta strandi868 – 874Combined sources7
Beta strandi881 – 891Combined sources11
Beta strandi897 – 903Combined sources7
Helixi904 – 906Combined sources3
Helixi907 – 916Combined sources10
Beta strandi921 – 923Combined sources3
Helixi931 – 939Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BIPX-ray1.94A/B1-465[»]
3BIQX-ray1.73A1-465[»]
3BITX-ray1.90A/B1-451[»]
4IOYX-ray1.94X675-958[»]
4WNNX-ray1.80T958-972[»]
ProteinModelPortaliP32558.
SMRiP32558.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32558.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili208 – 234Sequence analysisAdd BLAST27
Coiled coili636 – 666Sequence analysisAdd BLAST31
Coiled coili959 – 983Sequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi958 – 1021Asp/Glu-rich (acidic)Add BLAST64

Sequence similaritiesi

Belongs to the peptidase M24 family. SPT16 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000014495.
HOGENOMiHOG000209079.
InParanoidiP32558.
OMAiKEFRYFA.
OrthoDBiEOG092C0U5S.

Family and domain databases

CDDicd01091. CDC68-like. 1 hit.
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.
IPR033825. SPT16.
[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.

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.
PIRiS18512.
RefSeqiNP_011308.1. NM_001181072.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BIPX-ray1.94A/B1-465[»]
3BIQX-ray1.73A1-465[»]
3BITX-ray1.90A/B1-451[»]
4IOYX-ray1.94X675-958[»]
4WNNX-ray1.80T958-972[»]
ProteinModelPortaliP32558.
SMRiP32558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33049. 190 interactors.
DIPiDIP-2546N.
IntActiP32558. 61 interactors.
MINTiMINT-427889.

PTM databases

iPTMnetiP32558.

Proteomic databases

MaxQBiP32558.
PRIDEiP32558.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL207W.
SGDiS000003175. SPT16.

Phylogenomic databases

GeneTreeiENSGT00390000014495.
HOGENOMiHOG000209079.
InParanoidiP32558.
OMAiKEFRYFA.
OrthoDBiEOG092C0U5S.

Enzyme and pathway databases

BioCyciYEAST:G3O-30684-MONOMER.
ReactomeiR-SCE-674695. RNA Polymerase II Pre-transcription Events.
R-SCE-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

Miscellaneous databases

EvolutionaryTraceiP32558.
PROiP32558.

Family and domain databases

CDDicd01091. CDC68-like. 1 hit.
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.
IPR033825. SPT16.
[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...

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 30, 2016
This is version 149 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

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.