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Protein

Histone chaperone ASF1B

Gene

Asf1b

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. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA.1 Publication

GO - Molecular functioni

  • histone binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone ASF1B
Alternative name(s):
Anti-silencing function protein 1 homolog B
Short name:
mCIA-II
Gene namesi
Name:Asf1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1914179. Asf1b.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • chromatin Source: MGI
  • nuclear chromatin Source: MGI
  • nucleoplasm Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Histone chaperone ASF1BPRO_0000284016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphoserine; by TLK2By similarity

Post-translational modificationi

Phosphorylated by TLK2 (By similarity). Phosphorylated by TLK1.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9DAP7.
MaxQBiQ9DAP7.
PaxDbiQ9DAP7.
PRIDEiQ9DAP7.

PTM databases

iPTMnetiQ9DAP7.
PhosphoSiteiQ9DAP7.

Expressioni

Tissue specificityi

Highly expressed in testis. Restricted to premeiotic to meiotic stages during spermatogenesis.1 Publication

Gene expression databases

BgeeiQ9DAP7.
GenevisibleiQ9DAP7. 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 HAT1, NASP, TAF1, TLK1 and TLK2 (By similarity). Interacts with CDAN1 (By similarity). Found in a cytosolic complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4. Interacts with CREBBP (By similarity).By similarity

GO - Molecular functioni

  • histone binding Source: MGI

Protein-protein interaction databases

IntActiQ9DAP7. 5 interactions.
MINTiMINT-4615967.
STRINGi10090.ENSMUSP00000005607.

Structurei

3D structure databases

ProteinModelPortaliQ9DAP7.
SMRiQ9DAP7. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156Interaction with histone H3 and CHAF1BBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9DAP7.
KOiK10753.
OMAiFIFQADA.
OrthoDBiEOG7B5WWX.
PhylomeDBiQ9DAP7.
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.

Q9DAP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALSDDLEW KIIYVGSAES
60 70 80 90 100
EEFDQILDSV LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT
110 120 130 140 150
YHGQEFIRVG YYVNNEYPDP ELRENPPPKP DFSQLQRNIL ASNPRVTRFH
160 170 180 190 200
INWDNNPDSL EAIENQDPNV DFSLSLSCTP VKSLGLPSCI PGLLPENSMD

CI
Length:202
Mass (Da):22,464
Last modified:June 1, 2001 - v1
Checksum:iA02546180DA18A48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931T → N in BAC36978 (PubMed:16141072).Curated
Sequence conflicti155 – 1551N → K in BAC36978 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005646 mRNA. Translation: BAB24166.1.
AK019594 mRNA. Translation: BAB31809.1.
AK077005 mRNA. Translation: BAC36561.1.
AK077718 mRNA. Translation: BAC36978.1.
AK134906 mRNA. Translation: BAE22334.1.
AK150818 mRNA. Translation: BAE29881.1.
AK151951 mRNA. Translation: BAE30824.1.
AK165322 mRNA. Translation: BAE38137.1.
BC003428 mRNA. Translation: AAH03428.1.
CCDSiCCDS22462.1.
RefSeqiNP_077146.1. NM_024184.2.
UniGeneiMm.29680.

Genome annotation databases

EnsembliENSMUST00000005607; ENSMUSP00000005607; ENSMUSG00000005470.
GeneIDi66929.
KEGGimmu:66929.
UCSCiuc009mlk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005646 mRNA. Translation: BAB24166.1.
AK019594 mRNA. Translation: BAB31809.1.
AK077005 mRNA. Translation: BAC36561.1.
AK077718 mRNA. Translation: BAC36978.1.
AK134906 mRNA. Translation: BAE22334.1.
AK150818 mRNA. Translation: BAE29881.1.
AK151951 mRNA. Translation: BAE30824.1.
AK165322 mRNA. Translation: BAE38137.1.
BC003428 mRNA. Translation: AAH03428.1.
CCDSiCCDS22462.1.
RefSeqiNP_077146.1. NM_024184.2.
UniGeneiMm.29680.

3D structure databases

ProteinModelPortaliQ9DAP7.
SMRiQ9DAP7. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DAP7. 5 interactions.
MINTiMINT-4615967.
STRINGi10090.ENSMUSP00000005607.

PTM databases

iPTMnetiQ9DAP7.
PhosphoSiteiQ9DAP7.

Proteomic databases

EPDiQ9DAP7.
MaxQBiQ9DAP7.
PaxDbiQ9DAP7.
PRIDEiQ9DAP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005607; ENSMUSP00000005607; ENSMUSG00000005470.
GeneIDi66929.
KEGGimmu:66929.
UCSCiuc009mlk.1. mouse.

Organism-specific databases

CTDi55723.
MGIiMGI:1914179. Asf1b.

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9DAP7.
KOiK10753.
OMAiFIFQADA.
OrthoDBiEOG7B5WWX.
PhylomeDBiQ9DAP7.
TreeFamiTF106429.

Miscellaneous databases

PROiQ9DAP7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAP7.
GenevisibleiQ9DAP7. 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

« Hide 'large scale' publications
  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.
    Tissue: Bone marrow, Embryo, Olfactory bulb, Spleen and Testis.
  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: Czech II.
    Tissue: Mammary tumor.
  3. "Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis."
    Umehara T., Horikoshi M.
    J. Biol. Chem. 278:35660-35667(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "TLK1B promotes repair of UV-damaged DNA through chromatin remodeling by Asf1."
    Sen S.P., De Benedetti A.
    BMC Mol. Biol. 7:37-37(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY TLK1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiASF1B_MOUSE
AccessioniPrimary (citable) accession number: Q9DAP7
Secondary accession number(s): Q8BP41, Q9CTX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 102 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.