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Protein

FACT complex subunit POB3

Gene

POB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

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

GO - Molecular functioni

GO - Biological processi

  • DNA-dependent DNA replication Source: SGD
  • DNA repair Source: UniProtKB-KW
  • DNA replication-independent nucleosome organization Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Biological processDNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32664-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 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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML069W
SGDiS000004534 POB3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20R → H in pob3-11; causes severe defects in rate of growth; when associated with C-109. 1 Publication1
Mutagenesisi78L → R in pob3-1; causes severe defects in rate of growth; when associated with K-419 and T-489. 1 Publication1
Mutagenesisi109R → C in pob3-11; causes severe defects in rate of growth; when associated with H-20. 1 Publication1
Mutagenesisi308Q → A or D: No effect. 1 Publication1
Mutagenesisi308Q → K: Confers sensitivity to HU indicating a disturbed activity in DNA replication; confers a SPT- phenotype indicating a disturbed activity in transcription. 1 Publication1
Mutagenesisi308Q → R: Confers sensitivity to HU indicating a disturbed activity in DNA replication. 1 Publication1
Mutagenesisi311T → A: No change of sensitivity to HU; confers a SPT- phenotype indicating a disturbed activity in transcription. 1 Publication1
Mutagenesisi419M → K in pob3-1; causes severe defects in rate of growth; when associated with R-78 and T-489. 1 Publication1
Mutagenesisi489S → T in pob3-1; causes severe defects in rate of growth; when associated with R-78 and K-419. 1 Publication1
Mutagenesisi547K → M in pob3-21; causes severe defects in rate of growth. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002032501 – 552FACT complex subunit POB3Add BLAST552

Proteomic databases

MaxQBiQ04636
PaxDbiQ04636
PRIDEiQ04636

PTM databases

iPTMnetiQ04636

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

Show more details

Protein-protein interaction databases

BioGridi35097, 660 interactors
ComplexPortaliCPX-3215 FACT complex
DIPiDIP-4083N
IntActiQ04636, 49 interactors
MINTiQ04636
STRINGi4932.YML069W

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 10Combined sources10
Beta strandi17 – 22Combined sources6
Beta strandi25 – 30Combined sources6
Turni35 – 37Combined sources3
Helixi38 – 41Combined sources4
Beta strandi45 – 48Combined sources4
Helixi49 – 51Combined sources3
Beta strandi52 – 59Combined sources8
Beta strandi61 – 73Combined sources13
Beta strandi75 – 81Combined sources7
Helixi83 – 85Combined sources3
Helixi86 – 97Combined sources12
Turni107 – 110Combined sources4
Beta strandi242 – 252Combined sources11
Beta strandi255 – 261Combined sources7
Beta strandi263 – 269Combined sources7
Beta strandi274 – 278Combined sources5
Helixi279 – 281Combined sources3
Beta strandi282 – 289Combined sources8
Beta strandi293 – 308Combined sources16
Beta strandi311 – 321Combined sources11
Beta strandi325 – 329Combined sources5
Helixi334 – 340Combined sources7
Turni341 – 344Combined sources4
Beta strandi347 – 352Combined sources6
Helixi353 – 365Combined sources13
Beta strandi384 – 388Combined sources5
Beta strandi391 – 397Combined sources7
Beta strandi399 – 408Combined sources10
Beta strandi410 – 413Combined sources4
Helixi414 – 416Combined sources3
Beta strandi417 – 423Combined sources7
Beta strandi434 – 441Combined sources8
Helixi442 – 444Combined sources3
Beta strandi447 – 454Combined sources8
Helixi455 – 457Combined sources3
Helixi458 – 467Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04636

Family & Domainsi

Sequence similaritiesi

Belongs to the SSRP1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00560000076898
HOGENOMiHOG000180790
InParanoidiQ04636
KOiK09272
OMAiTGDAICI
OrthoDBiEOG092C355W

Family and domain databases

Gene3Di2.30.29.220, 1 hit
2.30.29.30, 2 hits
InterProiView protein in InterPro
IPR013719 DUF1747
IPR011993 PH-like_dom_sf
IPR035417 POB3_N
IPR000969 SSrcognition
IPR024954 SSRP1_dom
IPR038167 SSRP1_sf
PfamiView protein in Pfam
PF17292 POB3_N, 1 hit
PF08512 Rtt106, 1 hit
PF03531 SSrecog, 1 hit
PRINTSiPR00887 SSRCOGNITION
SMARTiView protein in SMART
SM01287 Rtt106, 1 hit

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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiPOB3_YEAST
AccessioniPrimary (citable) accession number: Q04636
Secondary accession number(s): D6VZA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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