Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone chaperone ASF1B

Gene

ASF1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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. Required for spermatogenesis.5 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Chromatin regulator, Developmental protein
Biological processDifferentiation, Spermatogenesis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone ASF1B
Alternative name(s):
Anti-silencing function protein 1 homolog B
Short name:
hAsf1
Short name:
hAsf1b
CCG1-interacting factor A-II
Short name:
CIA-II
Short name:
hCIA-II
Gene namesi
Name:ASF1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105011.8
HGNCiHGNC:20996 ASF1B
MIMi609190 gene
neXtProtiNX_Q9NVP2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36D → A: Abolishes CDAN1 interaction. 1 Publication1
Mutagenesisi37D → A: Abolishes CDAN1 interaction. 1 Publication1

Organism-specific databases

DisGeNETi55723
OpenTargetsiENSG00000105011
PharmGKBiPA134931112

Polymorphism and mutation databases

BioMutaiASF1B

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002840151 – 202Histone chaperone ASF1BAdd BLAST202

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198Phosphoserine; by TLK21 Publication1

Post-translational modificationi

Phosphorylated by TLK1 and TLK2.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NVP2
MaxQBiQ9NVP2
PaxDbiQ9NVP2
PeptideAtlasiQ9NVP2
PRIDEiQ9NVP2
ProteomicsDBi82838

PTM databases

iPTMnetiQ9NVP2
PhosphoSitePlusiQ9NVP2

Expressioni

Tissue specificityi

Highly expressed in testis and at lower levels in colon, small intestine and thymus.1 Publication

Gene expression databases

BgeeiENSG00000105011
CleanExiHS_ASF1B
ExpressionAtlasiQ9NVP2 baseline and differential
GenevisibleiQ9NVP2 HS

Organism-specific databases

HPAiHPA054036

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. Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4. Interacts with CREBBP.9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120845, 63 interactors
CORUMiQ9NVP2
DIPiDIP-29242N
IntActiQ9NVP2, 37 interactors
MINTiQ9NVP2
STRINGi9606.ENSP00000263382

Structurei

Secondary structure

1202
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 – 45Combined sources8
Helixi51 – 53Combined sources3
Beta strandi54 – 62Combined sources9
Beta strandi67 – 76Combined sources10
Helixi81 – 83Combined sources3
Helixi86 – 89Combined sources4
Beta strandi90 – 101Combined sources12
Beta strandi104 – 117Combined sources14
Helixi120 – 124Combined sources5
Helixi132 – 134Combined sources3
Beta strandi135 – 139Combined sources5
Beta strandi145 – 148Combined sources4

3D structure databases

ProteinModelPortaliQ9NVP2
SMRiQ9NVP2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 156Interaction with histone H3By similarityAdd BLAST156
Regioni1 – 155Interaction with CHAF1BAdd BLAST155

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiKOG3265 Eukaryota
COG5137 LUCA
GeneTreeiENSGT00390000004692
HOGENOMiHOG000197425
HOVERGENiHBG105617
InParanoidiQ9NVP2
KOiK10753
OMAiHINWEGC
OrthoDBiEOG091G0K07
PhylomeDBiQ9NVP2
TreeFamiTF106429

Family and domain databases

Gene3Di2.60.40.1490, 1 hit
InterProiView protein in InterPro
IPR006818 ASF1-like
IPR036747 ASF1-like_sf
PANTHERiPTHR12040 PTHR12040, 1 hit
PfamiView protein in Pfam
PF04729 ASF1_hist_chap, 1 hit
SUPFAMiSSF101546 SSF101546, 1 hit

Sequencei

Sequence statusi: Complete.

Q9NVP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES
60 70 80 90 100
EEFDQILDSV LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT
110 120 130 140 150
YHGQEFIRVG YYVNNEYLNP ELRENPPMKP DFSQLQRNIL ASNPRVTRFH
160 170 180 190 200
INWDNNMDRL EAIETQDPSL GCGLPLNCTP IKGLGLPGCI PGLLPENSMD

CI
Length:202
Mass (Da):22,434
Last modified:October 1, 2000 - v1
Checksum:iBD62F726610E3A70
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11V → A in BAA91602 (PubMed:14702039).Curated1
Sequence conflicti23R → Q in BAD96800 (Ref. 5) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279307 mRNA Translation: AAK82973.1
AB104486 mRNA Translation: BAC87709.1
CR457235 mRNA Translation: CAG33516.1
AK001288 mRNA Translation: BAA91602.1
AK001466 mRNA Translation: BAA91708.1
AK223080 mRNA Translation: BAD96800.1
AC022098 Genomic DNA No translation available.
BC007726 mRNA Translation: AAH07726.1
BC010014 mRNA Translation: AAH10014.1
BC036521 mRNA Translation: AAH36521.1
CCDSiCCDS12306.1
RefSeqiNP_060624.1, NM_018154.2
UniGeneiHs.26516

Genome annotation databases

EnsembliENST00000263382; ENSP00000263382; ENSG00000105011
GeneIDi55723
KEGGihsa:55723
UCSCiuc002mye.4 human

Similar proteinsi

Entry informationi

Entry nameiASF1B_HUMAN
AccessioniPrimary (citable) accession number: Q9NVP2
Secondary accession number(s): Q53G51, Q9NVZ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: July 18, 2018
This is version 146 of the entry and version 1 of the sequence. See 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 19
    Human chromosome 19: 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health