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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: 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

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
Complete GO annotation...

Keywords - Biological processi

DNA 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

GO - Cellular componenti

  • FACT complex Source: SGD
  • nuclear chromatin Source: SGD
  • 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.

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

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

Protein-protein interaction databases

BioGridi35097. 192 interactions.
DIPiDIP-4083N.
IntActiQ04636. 47 interactions.
MINTiMINT-559116.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
InParanoidiQ04636.
KOiK09272.
OMAiNWYSTAL.
OrthoDBiEOG092C355W.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi35097. 192 interactions.
DIPiDIP-4083N.
IntActiQ04636. 47 interactions.
MINTiMINT-559116.

PTM databases

iPTMnetiQ04636.

Proteomic databases

MaxQBiQ04636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YML069W.
SGDiS000004534. POB3.

Phylogenomic databases

GeneTreeiENSGT00560000076898.
HOGENOMiHOG000180790.
InParanoidiQ04636.
KOiK09272.
OMAiNWYSTAL.
OrthoDBiEOG092C355W.

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.

Miscellaneous databases

EvolutionaryTraceiQ04636.
PROiQ04636.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR013719. DUF1747.
IPR011993. PH_dom-like.
IPR000969. SSrcognition.
IPR024954. SSRP1_dom.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
PF03531. SSrecog. 1 hit.
[Graphical view]
PRINTSiPR00887. SSRCOGNITION.
SMARTiSM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

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: September 7, 2016
This is version 138 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

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.