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Q04636 (POB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FACT complex subunit POB3
Alternative name(s):
Facilitates chromatin transcription complex subunit POB3
Gene names
Name:POB3
Ordered Locus Names:YML069W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.9 Ref.12 Ref.16 Ref.19 Ref.21 Ref.22 Ref.24

Subunit structure

Forms a stable heterodimer with SPT16. 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. Interacts directly with RFA1. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.11 Ref.13 Ref.14 Ref.24

Subcellular location

Nucleus. Chromosome. Note: Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. Ref.6 Ref.16 Ref.20

Miscellaneous

In contrast to the orthologous protein in animals and plants, this protein does not contain a HMG box DNA-binding domain. This function may instead be provided by the HMG box of the associated NHP6A/NHP6B proteins in the FACT complex of yeast.

Present with 22400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SSRP1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RFA1P223363EBI-27863,EBI-14971
SPT16P325589EBI-27863,EBI-4334

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552FACT complex subunit POB3
PRO_0000203250

Experimental info

Mutagenesis201R → H in pob3-11; causes severe defects in rate of growth; when associated with C-109. Ref.8
Mutagenesis781L → R in pob3-1; causes severe defects in rate of growth; when associated with K-419 and T-489. Ref.8
Mutagenesis1091R → C in pob3-11; causes severe defects in rate of growth; when associated with H-20. Ref.8
Mutagenesis3081Q → A or D: No effect. Ref.24
Mutagenesis3081Q → K: Confers sensitivity to HU indicating a disturbed activity in DNA replication; confers a SPT- phenotype indicating a disturbed activity in transcription. Ref.24
Mutagenesis3081Q → R: Confers sensitivity to HU indicating a disturbed activity in DNA replication. Ref.24
Mutagenesis3111T → A: No change of sensitivity to HU; confers a SPT- phenotype indicating a disturbed activity in transcription. Ref.24
Mutagenesis4191M → K in pob3-1; causes severe defects in rate of growth; when associated with R-78 and T-489. Ref.8
Mutagenesis4891S → T in pob3-1; causes severe defects in rate of growth; when associated with R-78 and K-419. Ref.8
Mutagenesis5471K → M in pob3-21; causes severe defects in rate of growth. Ref.8

Secondary structure

............................................................. 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04636 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 02C04F620C7B1450

FASTA55262,994
        10         20         30         40         50         60 
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG 

        70         80         90        100        110        120 
CRGYDLKINT KNQGVIQLDG FSQDDYNLIK NDFHRRFNIQ VEQREHSLRG WNWGKTDLAR 

       130        140        150        160        170        180 
NEMVFALNGK PTFEIPYARI NNTNLTSKNE VGIEFNIQDE EYQPAGDELV EMRFYIPGVI 

       190        200        210        220        230        240 
QTNVDENMTK KEESSNEVVP KKEDGAEGED VQMAVEEKSM AEAFYEELKE KADIGEVAGD 

       250        260        270        280        290        300 
AIVSFQDVFF TTPRGRYDID IYKNSIRLRG KTYEYKLQHR QIQRIVSLPK ADDIHHLLVL 

       310        320        330        340        350        360 
AIEPPLRQGQ TTYPFLVLQF QKDEETEVQL NLEDEDYEEN YKDKLKKQYD AKTHIVLSHV 

       370        380        390        400        410        420 
LKGLTDRRVI VPGEYKSKYD QCAVSCSFKA NEGYLYPLDN AFFFLTKPTL YIPFSDVSMV 

       430        440        450        460        470        480 
NISRAGQTST SSRTFDLEVV LRSNRGSTTF ANISKEEQQL LEQFLKSKNL RVKNEDREVQ 

       490        500        510        520        530        540 
ERLQTALGSD SDEEDINMGS AGEDDESVDE DFQVSSDNDA DEVAEEFDSD AALSDAEGGS 

       550 
DEERPSKKPK VE 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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 SPT16.
[5]"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 SPT16.
[6]"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 SPT16, SUBCELLULAR LOCATION.
[7]"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.
[8]"POB3 is required for both transcription and replication in the yeast Saccharomyces cerevisiae."
Schlesinger M.B., Formosa T.
Genetics 155:1593-1606(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-20; LEU-78; ARG-109; MET-419; SER-489 AND LYS-547.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]Erratum
Mason P.B., Struhl K.
Mol. Cell. Biol. 24:6536-6536(2004)
[18]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition."
Vandemark A.P., Blanksma M., Ferris E., Heroux A., Hill C.P., Formosa T.
Mol. Cell 22:363-374(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-478, FUNCTION, INTERACTION WITH RFA1, MUTAGENESIS OF GLN-308 AND THR-311.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38114 Genomic DNA. Translation: CAA86251.1.
BK006946 Genomic DNA. Translation: DAA09828.1.
PIRS48328.
RefSeqNP_013642.1. NM_001182428.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GCJX-ray2.55A/B/C/D220-478[»]
2GCLX-ray2.21A/B220-478[»]
3F5RX-ray1.70A1-168[»]
4PQ0X-ray1.65A232-473[»]
ProteinModelPortalQ04636.
SMRQ04636. Positions 1-178, 232-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35097. 188 interactions.
DIPDIP-4083N.
IntActQ04636. 46 interactions.
MINTMINT-559116.
STRING4932.YML069W.

Proteomic databases

MaxQBQ04636.
PaxDbQ04636.
PeptideAtlasQ04636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML069W; YML069W; YML069W.
GeneID854933.
KEGGsce:YML069W.

Organism-specific databases

CYGDYML069w.
SGDS000004534. POB3.

Phylogenomic databases

eggNOGCOG5165.
GeneTreeENSGT00560000076898.
HOGENOMHOG000180790.
KOK09272.
OMAIIQLDGF.
OrthoDBEOG7P2Z26.

Enzyme and pathway databases

BioCycYEAST:G3O-32664-MONOMER.

Gene expression databases

GenevestigatorQ04636.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR013719. DUF1747.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamPF08512. Rtt106. 1 hit.
PF03531. SSrecog. 2 hits.
[Graphical view]
PRINTSPR00887. SSRCOGNITION.
ProtoNetSearch...

Other

EvolutionaryTraceQ04636.
NextBio977968.
PROQ04636.

Entry information

Entry namePOB3_YEAST
AccessionPrimary (citable) accession number: Q04636
Secondary accession number(s): D6VZA4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references