Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q04636

- POB3_YEAST

UniProt

Q04636 - POB3_YEAST

(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)

Protein

FACT complex subunit POB3

Gene

POB3

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.9 Publications

GO - Molecular functioni

  1. DNA binding Source: InterPro

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. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  5. regulation of transcription by chromatin organization Source: SGD
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-32664-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FACT complex subunit POB3
Alternative name(s):
Facilitates chromatin transcription complex subunit POB3
Gene namesi
Name:POB3
Ordered Locus Names:YML069W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYML069w.
SGDiS000004534. POB3.

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
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201R → H in pob3-11; causes severe defects in rate of growth; when associated with C-109. 1 Publication
Mutagenesisi78 – 781L → R in pob3-1; causes severe defects in rate of growth; when associated with K-419 and T-489. 1 Publication
Mutagenesisi109 – 1091R → C in pob3-11; causes severe defects in rate of growth; when associated with H-20. 1 Publication
Mutagenesisi308 – 3081Q → A or D: No effect. 1 Publication
Mutagenesisi308 – 3081Q → K: Confers sensitivity to HU indicating a disturbed activity in DNA replication; confers a SPT- phenotype indicating a disturbed activity in transcription. 1 Publication
Mutagenesisi308 – 3081Q → R: Confers sensitivity to HU indicating a disturbed activity in DNA replication. 1 Publication
Mutagenesisi311 – 3111T → A: No change of sensitivity to HU; confers a SPT- phenotype indicating a disturbed activity in transcription. 1 Publication
Mutagenesisi419 – 4191M → K in pob3-1; causes severe defects in rate of growth; when associated with R-78 and T-489. 1 Publication
Mutagenesisi489 – 4891S → T in pob3-1; causes severe defects in rate of growth; when associated with R-78 and K-419. 1 Publication
Mutagenesisi547 – 5471K → M in pob3-21; causes severe defects in rate of growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552FACT complex subunit POB3PRO_0000203250Add
BLAST

Proteomic databases

MaxQBiQ04636.
PaxDbiQ04636.
PeptideAtlasiQ04636.

Expressioni

Gene expression databases

GenevestigatoriQ04636.

Interactioni

Subunit structurei

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 RFA1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RFA1P223363EBI-27863,EBI-14971
SPT16P325589EBI-27863,EBI-4334

Protein-protein interaction databases

BioGridi35097. 190 interactions.
DIPiDIP-4083N.
IntActiQ04636. 46 interactions.
MINTiMINT-559116.
STRINGi4932.YML069W.

Structurei

Secondary structure

552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 1010
Beta strandi17 – 226
Beta strandi25 – 306
Turni35 – 373
Helixi38 – 414
Beta strandi45 – 484
Helixi49 – 513
Beta strandi52 – 598
Beta strandi61 – 7313
Beta strandi75 – 817
Helixi83 – 853
Helixi86 – 9712
Turni107 – 1104
Beta strandi242 – 25211
Beta strandi255 – 2617
Beta strandi263 – 2697
Beta strandi274 – 2785
Helixi279 – 2813
Beta strandi282 – 2898
Beta strandi293 – 30816
Beta strandi311 – 32111
Beta strandi325 – 3295
Helixi334 – 3407
Turni341 – 3444
Beta strandi347 – 3526
Helixi353 – 36513
Beta strandi384 – 3885
Beta strandi391 – 3977
Beta strandi399 – 40810
Beta strandi410 – 4134
Helixi414 – 4163
Beta strandi417 – 4237
Beta strandi434 – 4418
Helixi442 – 4443
Beta strandi447 – 4548
Helixi455 – 4573
Helixi458 – 46710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GCJX-ray2.55A/B/C/D220-478[»]
2GCLX-ray2.21A/B220-478[»]
3F5RX-ray1.70A1-168[»]
4PQ0X-ray1.65A232-473[»]
ProteinModelPortaliQ04636.
SMRiQ04636. Positions 1-178, 232-473.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04636.

Family & Domainsi

Sequence similaritiesi

Belongs to the SSRP1 family.Curated

Phylogenomic databases

eggNOGiCOG5165.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
InParanoidiQ04636.
KOiK09272.
OMAiIIQLDGF.
OrthoDBiEOG7P2Z26.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
PF03531. SSrecog. 2 hits.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.

Sequencei

Sequence statusi: Complete.

Q04636-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT
60 70 80 90 100
ELSTVQWSRG CRGYDLKINT KNQGVIQLDG FSQDDYNLIK NDFHRRFNIQ
110 120 130 140 150
VEQREHSLRG WNWGKTDLAR NEMVFALNGK PTFEIPYARI NNTNLTSKNE
160 170 180 190 200
VGIEFNIQDE EYQPAGDELV EMRFYIPGVI QTNVDENMTK KEESSNEVVP
210 220 230 240 250
KKEDGAEGED VQMAVEEKSM AEAFYEELKE KADIGEVAGD AIVSFQDVFF
260 270 280 290 300
TTPRGRYDID IYKNSIRLRG KTYEYKLQHR QIQRIVSLPK ADDIHHLLVL
310 320 330 340 350
AIEPPLRQGQ TTYPFLVLQF QKDEETEVQL NLEDEDYEEN YKDKLKKQYD
360 370 380 390 400
AKTHIVLSHV LKGLTDRRVI VPGEYKSKYD QCAVSCSFKA NEGYLYPLDN
410 420 430 440 450
AFFFLTKPTL YIPFSDVSMV NISRAGQTST SSRTFDLEVV LRSNRGSTTF
460 470 480 490 500
ANISKEEQQL LEQFLKSKNL RVKNEDREVQ ERLQTALGSD SDEEDINMGS
510 520 530 540 550
AGEDDESVDE DFQVSSDNDA DEVAEEFDSD AALSDAEGGS DEERPSKKPK

VE
Length:552
Mass (Da):62,994
Last modified:November 1, 1997 - v1
Checksum:i02C04F620C7B1450
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38114 Genomic DNA. Translation: CAA86251.1.
BK006946 Genomic DNA. Translation: DAA09828.1.
PIRiS48328.
RefSeqiNP_013642.1. NM_001182428.1.

Genome annotation databases

EnsemblFungiiYML069W; YML069W; YML069W.
GeneIDi854933.
KEGGisce:YML069W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38114 Genomic DNA. Translation: CAA86251.1 .
BK006946 Genomic DNA. Translation: DAA09828.1 .
PIRi S48328.
RefSeqi NP_013642.1. NM_001182428.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GCJ X-ray 2.55 A/B/C/D 220-478 [» ]
2GCL X-ray 2.21 A/B 220-478 [» ]
3F5R X-ray 1.70 A 1-168 [» ]
4PQ0 X-ray 1.65 A 232-473 [» ]
ProteinModelPortali Q04636.
SMRi Q04636. Positions 1-178, 232-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35097. 190 interactions.
DIPi DIP-4083N.
IntActi Q04636. 46 interactions.
MINTi MINT-559116.
STRINGi 4932.YML069W.

Proteomic databases

MaxQBi Q04636.
PaxDbi Q04636.
PeptideAtlasi Q04636.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YML069W ; YML069W ; YML069W .
GeneIDi 854933.
KEGGi sce:YML069W.

Organism-specific databases

CYGDi YML069w.
SGDi S000004534. POB3.

Phylogenomic databases

eggNOGi COG5165.
GeneTreei ENSGT00560000076898.
HOGENOMi HOG000180790.
InParanoidi Q04636.
KOi K09272.
OMAi IIQLDGF.
OrthoDBi EOG7P2Z26.

Enzyme and pathway databases

BioCyci YEAST:G3O-32664-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q04636.
NextBioi 977968.
PROi Q04636.

Gene expression databases

Genevestigatori Q04636.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR013719. DUF1747.
IPR011993. PH_like_dom.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view ]
Pfami PF08512. Rtt106. 1 hit.
PF03531. SSrecog. 2 hits.
[Graphical view ]
PRINTSi PR00887. SSRCOGNITION.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. 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.

Entry informationi

Entry nameiPOB3_YEAST
AccessioniPrimary (citable) accession number: Q04636
Secondary accession number(s): D6VZA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3