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Protein

Histone chaperone ASF1A

Gene

Asf1a

Organism
Mus musculus (Mouse)
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. 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.By similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-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
Gene namesi
Name:Asf1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1913653. Asf1a.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Histone chaperone ASF1APRO_0000284013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Phosphoserine; by TLK2By similarity

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9CQE6.
MaxQBiQ9CQE6.
PaxDbiQ9CQE6.
PRIDEiQ9CQE6.

PTM databases

iPTMnetiQ9CQE6.
PhosphoSiteiQ9CQE6.

Expressioni

Gene expression databases

BgeeiQ9CQE6.
GenevisibleiQ9CQE6. MM.

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 (By similarity). Interacts with CDAN1 (By similarity). Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1 and H4. Interacts with CREBBP (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211447. 2 interactions.
IntActiQ9CQE6. 5 interactions.
STRINGi10090.ENSMUSP00000020004.

Structurei

3D structure databases

ProteinModelPortaliQ9CQE6.
SMRiQ9CQE6. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156Interaction with histone H3, CHAF1B, and HIRABy similarityAdd
BLAST
Regioni155 – 20450Required for interaction with HIRABy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi31 – 377Required for interaction with HIRABy similarity

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9CQE6.
KOiK10753.
OMAiKINWDYG.
OrthoDBiEOG7B5WWX.
PhylomeDBiQ9CQE6.
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.

Q9CQE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES
60 70 80 90 100
EEYDQVLDSV LVGPVPAGRH MFVFQADAPN AGLIPDADAV 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):22,943
Last modified:June 1, 2001 - v1
Checksum:i9803653A63B8FC68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007804 mRNA. Translation: BAB25269.1.
AK010210 mRNA. Translation: BAB26770.1.
AK012376 mRNA. Translation: BAB28198.1.
AK088618 mRNA. Translation: BAC40457.1.
BC027628 mRNA. Translation: AAH27628.1.
CCDSiCCDS23847.1.
RefSeqiNP_079817.1. NM_025541.3.
UniGeneiMm.272989.

Genome annotation databases

EnsembliENSMUST00000020004; ENSMUSP00000020004; ENSMUSG00000019857.
GeneIDi66403.
KEGGimmu:66403.
UCSCiuc007fbr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007804 mRNA. Translation: BAB25269.1.
AK010210 mRNA. Translation: BAB26770.1.
AK012376 mRNA. Translation: BAB28198.1.
AK088618 mRNA. Translation: BAC40457.1.
BC027628 mRNA. Translation: AAH27628.1.
CCDSiCCDS23847.1.
RefSeqiNP_079817.1. NM_025541.3.
UniGeneiMm.272989.

3D structure databases

ProteinModelPortaliQ9CQE6.
SMRiQ9CQE6. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211447. 2 interactions.
IntActiQ9CQE6. 5 interactions.
STRINGi10090.ENSMUSP00000020004.

PTM databases

iPTMnetiQ9CQE6.
PhosphoSiteiQ9CQE6.

Proteomic databases

EPDiQ9CQE6.
MaxQBiQ9CQE6.
PaxDbiQ9CQE6.
PRIDEiQ9CQE6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020004; ENSMUSP00000020004; ENSMUSG00000019857.
GeneIDi66403.
KEGGimmu:66403.
UCSCiuc007fbr.1. mouse.

Organism-specific databases

CTDi25842.
MGIiMGI:1913653. Asf1a.

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9CQE6.
KOiK10753.
OMAiKINWDYG.
OrthoDBiEOG7B5WWX.
PhylomeDBiQ9CQE6.
TreeFamiTF106429.

Enzyme and pathway databases

ReactomeiR-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

NextBioi321579.
PROiQ9CQE6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQE6.
GenevisibleiQ9CQE6. MM.

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...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Pancreas, Thymus and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiASF1A_MOUSE
AccessioniPrimary (citable) accession number: Q9CQE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2001
Last modified: April 13, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.