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Protein

Histone chaperone ASF1A

Gene

ASF1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.7 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • histone binding Source: MGI

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • DNA repair Source: MGI
  • DNA replication-dependent nucleosome assembly Source: UniProtKB
  • DNA replication-independent nucleosome assembly Source: UniProtKB
  • muscle cell differentiation Source: Ensembl
  • negative regulation of chromatin silencing Source: UniProtKB
  • nucleosome assembly Source: MGI
  • osteoblast differentiation Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111875-MONOMER.
ReactomeiR-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone ASF1A
Alternative name(s):
Anti-silencing function protein 1 homolog A
Short name:
hAsf1
Short name:
hAsf1a
CCG1-interacting factor A
Short name:
CIA
Short name:
hCIA
Gene namesi
Name:ASF1A
ORF Names:CGI-98, HSPC146
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20995. ASF1A.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36 – 37ED → AA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. 2 Publications2
Mutagenesisi37D → A: Abrogates interaction with CHAF1B and HIRA. 1 Publication1
Mutagenesisi54D → R: Reduces interaction with histone H3. 1 Publication1
Mutagenesisi62 – 64VGP → AAA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. 2 Publications3
Mutagenesisi94V → R: Abrogates interaction with histone H3 and histone H4. 1 Publication1
Mutagenesisi108R → E: Reduces interaction with histone H3. 1 Publication1

Organism-specific databases

DisGeNETi25842.
OpenTargetsiENSG00000111875.
PharmGKBiPA128394636.

Chemistry databases

ChEMBLiCHEMBL3392950.

Polymorphism and mutation databases

BioMutaiASF1A.
DMDMi74735206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002840121 – 204Histone chaperone ASF1AAdd BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei192Phosphoserine; by TLK21 Publication1

Post-translational modificationi

Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y294.
MaxQBiQ9Y294.
PaxDbiQ9Y294.
PeptideAtlasiQ9Y294.
PRIDEiQ9Y294.

PTM databases

iPTMnetiQ9Y294.
PhosphoSitePlusiQ9Y294.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000111875.
CleanExiHS_ASF1A.
GenevisibleiQ9Y294. HS.

Organism-specific databases

HPAiHPA030502.

Interactioni

Subunit structurei

Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex. Interacts with CABIN1, HAT1, HIRA, NASP, TAF1, TLK1, TLK2 and UBN1. Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1 and H4. Interacts with CREBBP.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-749553,EBI-78473
HIRAP541987EBI-749553,EBI-372342
HIST2H4BP628056EBI-749553,EBI-302023
PRR3P795223EBI-749553,EBI-2803328

GO - Molecular functioni

  • histone binding Source: MGI

Protein-protein interaction databases

BioGridi117368. 55 interactors.
DIPiDIP-29241N.
IntActiQ9Y294. 36 interactors.
MINTiMINT-1385638.
STRINGi9606.ENSP00000229595.

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi15 – 17Combined sources3
Beta strandi22 – 32Combined sources11
Beta strandi34 – 36Combined sources3
Beta strandi38 – 46Combined sources9
Helixi51 – 53Combined sources3
Beta strandi54 – 62Combined sources9
Beta strandi67 – 76Combined sources10
Helixi81 – 83Combined sources3
Helixi86 – 89Combined sources4
Beta strandi90 – 101Combined sources12
Beta strandi104 – 119Combined sources16
Helixi120 – 124Combined sources5
Helixi132 – 134Combined sources3
Beta strandi135 – 139Combined sources5
Beta strandi145 – 148Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TEYNMR-A1-156[»]
2I32X-ray2.70A/B1-157[»]
2IIJNMR-A1-156[»]
2IO5X-ray2.70A1-172[»]
3AADX-ray3.30B/D1-155[»]
5C3IX-ray3.50A/E/I/M/Q/U1-175[»]
ProteinModelPortaliQ9Y294.
SMRiQ9Y294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y294.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 156Interaction with histone H3, CHAF1B, and HIRAAdd BLAST156
Regioni155 – 204Required for interaction with HIRAAdd BLAST50

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi31 – 37Required for interaction with HIRA7

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9Y294.
KOiK10753.
OMAiFNPFQFE.
OrthoDBiEOG091G0K07.
PhylomeDBiQ9Y294.
TreeFamiTF106429.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9Y294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES
60 70 80 90 100
EEYDQVLDSV LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT
110 120 130 140 150
YRGQEFIRVG YYVNNEYTET ELRENPPVKP DFSKLQRNIL ASNPRVTRFH
160 170 180 190 200
INWEDNTEKL EDAESSNPNL QSLLSTDALP SASKGWSTSE NSLNVMLESH

MDCM
Length:204
Mass (Da):22,969
Last modified:November 1, 1999 - v1
Checksum:i9819D531D3A9FC68
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74F → I in AAF29110 (PubMed:11042152).Curated1
Sequence conflicti204M → I in CAG33628 (Ref. 7) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028628 mRNA. Translation: BAA96542.1.
AF279306 mRNA. Translation: AAK82972.1.
AF151856 mRNA. Translation: AAD34093.1.
AF161495 mRNA. Translation: AAF29110.1.
AL050261 mRNA. Translation: CAB43363.1.
AK025738 mRNA. Translation: BAB15228.1.
CR457347 mRNA. Translation: CAG33628.1.
AC022098 Genomic DNA. No translation available.
BC010878 mRNA. Translation: AAH10878.1.
CCDSiCCDS47469.1.
PIRiT08661.
RefSeqiNP_054753.1. NM_014034.2.
UniGeneiHs.292316.

Genome annotation databases

EnsembliENST00000229595; ENSP00000229595; ENSG00000111875.
GeneIDi25842.
KEGGihsa:25842.
UCSCiuc011ebn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028628 mRNA. Translation: BAA96542.1.
AF279306 mRNA. Translation: AAK82972.1.
AF151856 mRNA. Translation: AAD34093.1.
AF161495 mRNA. Translation: AAF29110.1.
AL050261 mRNA. Translation: CAB43363.1.
AK025738 mRNA. Translation: BAB15228.1.
CR457347 mRNA. Translation: CAG33628.1.
AC022098 Genomic DNA. No translation available.
BC010878 mRNA. Translation: AAH10878.1.
CCDSiCCDS47469.1.
PIRiT08661.
RefSeqiNP_054753.1. NM_014034.2.
UniGeneiHs.292316.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TEYNMR-A1-156[»]
2I32X-ray2.70A/B1-157[»]
2IIJNMR-A1-156[»]
2IO5X-ray2.70A1-172[»]
3AADX-ray3.30B/D1-155[»]
5C3IX-ray3.50A/E/I/M/Q/U1-175[»]
ProteinModelPortaliQ9Y294.
SMRiQ9Y294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117368. 55 interactors.
DIPiDIP-29241N.
IntActiQ9Y294. 36 interactors.
MINTiMINT-1385638.
STRINGi9606.ENSP00000229595.

Chemistry databases

ChEMBLiCHEMBL3392950.

PTM databases

iPTMnetiQ9Y294.
PhosphoSitePlusiQ9Y294.

Polymorphism and mutation databases

BioMutaiASF1A.
DMDMi74735206.

Proteomic databases

EPDiQ9Y294.
MaxQBiQ9Y294.
PaxDbiQ9Y294.
PeptideAtlasiQ9Y294.
PRIDEiQ9Y294.

Protocols and materials databases

DNASUi25842.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229595; ENSP00000229595; ENSG00000111875.
GeneIDi25842.
KEGGihsa:25842.
UCSCiuc011ebn.3. human.

Organism-specific databases

CTDi25842.
DisGeNETi25842.
GeneCardsiASF1A.
HGNCiHGNC:20995. ASF1A.
HPAiHPA030502.
MIMi609189. gene.
neXtProtiNX_Q9Y294.
OpenTargetsiENSG00000111875.
PharmGKBiPA128394636.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9Y294.
KOiK10753.
OMAiFNPFQFE.
OrthoDBiEOG091G0K07.
PhylomeDBiQ9Y294.
TreeFamiTF106429.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111875-MONOMER.
ReactomeiR-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

EvolutionaryTraceiQ9Y294.
GeneWikiiASF1A.
GenomeRNAii25842.
PROiQ9Y294.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111875.
CleanExiHS_ASF1A.
GenevisibleiQ9Y294. HS.

Family and domain databases

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

Entry informationi

Entry nameiASF1A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y294
Secondary accession number(s): Q6IA08, Q9P014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.