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Protein

Histone chaperone cia1

Gene

cia1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.1 Publication

GO - Molecular functioni

GO - Biological processi

  • chromatin assembly Source: PomBase
  • chromatin organization Source: PomBase
  • chromatin silencing Source: PomBase
  • histone acetylation Source: PomBase
  • histone exchange Source: PomBase
  • nucleosome disassembly Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone cia1
Alternative name(s):
Anti-silencing function protein 1
Gene namesi
Name:cia1
Synonyms:asf1
ORF Names:SPCC663.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC663.05c.
PomBaseiSPCC663.05c. cia1.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Histone chaperone cia1PRO_0000089743Add
BLAST

Proteomic databases

MaxQBiO74515.

Interactioni

Subunit structurei

Interacts with histone H3 and histone H4.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi276128. 72 interactions.
MINTiMINT-4679711.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Beta strandi15 – 173Combined sources
Beta strandi22 – 309Combined sources
Beta strandi38 – 4710Combined sources
Helixi51 – 533Combined sources
Beta strandi54 – 629Combined sources
Beta strandi67 – 7610Combined sources
Helixi81 – 833Combined sources
Beta strandi84 – 863Combined sources
Helixi87 – 904Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi105 – 11814Combined sources
Helixi123 – 1253Combined sources
Helixi128 – 1314Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi151 – 1544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU9X-ray1.80A1-161[»]
2DZEX-ray1.80A/B1-161[»]
2Z34X-ray2.40A/B1-161[»]
2Z3FX-ray2.70A/B/C/D/E/F/G/H1-161[»]
ProteinModelPortaliO74515.
SMRiO74515. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74515.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili173 – 19624Sequence analysisAdd
BLAST
Coiled coili223 – 25331Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi176 – 25984Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000197425.
InParanoidiO74515.
KOiK10753.
OMAiCAYEDNE.
OrthoDBiEOG70CRJQ.
PhylomeDBiO74515.

Family and domain databases

Gene3Di2.60.40.1490. 1 hit.
InterProiIPR006818. ASF1-like.
IPR017282. Hist_deposition_Asf1.
[Graphical view]
PANTHERiPTHR12040. PTHR12040. 1 hit.
PfamiPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
PIRSFiPIRSF037759. Histone_Asf1. 1 hit.
SUPFAMiSSF101546. SSF101546. 1 hit.

Sequencei

Sequence statusi: Complete.

O74515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVNILSVN VLNNPAKFSD PYKFEITFEC LEPLKSDLEW KLTYVGSATS
60 70 80 90 100
QSYDQILDTL LVGPIPIGIN KFVFEADPPN IDLLPQLSDV LGVTVILLSC
110 120 130 140 150
AYEDNEFVRV GYYVNNEMEG LNLQEMDDAE IKKVKVDISK VWRSILAEKP
160 170 180 190 200
RVTRFNIQWD NPDFDDAPPV QPDADEEEEE EEADEMEEEF DEEGEGDEEE
210 220 230 240 250
EEEDDGDGDG EGDGDGEGEN DGKGSEEEEE EEIDIEEEEE ESALANASAA
260
EEKPEEKPET SQ
Length:262
Mass (Da):29,431
Last modified:November 1, 1998 - v1
Checksum:iFA4E491BC8B49171
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031397 Genomic DNA. Translation: BAB82475.1.
CU329672 Genomic DNA. Translation: CAA20365.1.
PIRiT41536.
RefSeqiNP_588267.1. NM_001023257.2.

Genome annotation databases

EnsemblFungiiSPCC663.05c.1; SPCC663.05c.1:pep; SPCC663.05c.
GeneIDi2539568.
KEGGispo:SPCC663.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031397 Genomic DNA. Translation: BAB82475.1.
CU329672 Genomic DNA. Translation: CAA20365.1.
PIRiT41536.
RefSeqiNP_588267.1. NM_001023257.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CU9X-ray1.80A1-161[»]
2DZEX-ray1.80A/B1-161[»]
2Z34X-ray2.40A/B1-161[»]
2Z3FX-ray2.70A/B/C/D/E/F/G/H1-161[»]
ProteinModelPortaliO74515.
SMRiO74515. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276128. 72 interactions.
MINTiMINT-4679711.

Proteomic databases

MaxQBiO74515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC663.05c.1; SPCC663.05c.1:pep; SPCC663.05c.
GeneIDi2539568.
KEGGispo:SPCC663.05c.

Organism-specific databases

EuPathDBiFungiDB:SPCC663.05c.
PomBaseiSPCC663.05c. cia1.

Phylogenomic databases

HOGENOMiHOG000197425.
InParanoidiO74515.
KOiK10753.
OMAiCAYEDNE.
OrthoDBiEOG70CRJQ.
PhylomeDBiO74515.

Miscellaneous databases

EvolutionaryTraceiO74515.
PROiO74515.

Family and domain databases

Gene3Di2.60.40.1490. 1 hit.
InterProiIPR006818. ASF1-like.
IPR017282. Hist_deposition_Asf1.
[Graphical view]
PANTHERiPTHR12040. PTHR12040. 1 hit.
PfamiPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
PIRSFiPIRSF037759. Histone_Asf1. 1 hit.
SUPFAMiSSF101546. SSF101546. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro."
    Umehara T., Chimura T., Ichikawa N., Horikoshi M.
    Genes Cells 7:59-73(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiASF1_SCHPO
AccessioniPrimary (citable) accession number: O74515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.