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Protein

Histone chaperone ASF1B

Gene

ASF1B

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. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for spermatogenesis.5 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator, Developmental protein

Keywords - Biological processi

Differentiation, 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

HGNCiHGNC:20996. ASF1B.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361D → A: Abolishes CDAN1 interaction. 1 Publication
Mutagenesisi37 – 371D → A: Abolishes CDAN1 interaction. 1 Publication

Organism-specific databases

PharmGKBiPA134931112.

Polymorphism and mutation databases

BioMutaiASF1B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Histone chaperone ASF1BPRO_0000284015Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphoserine; by TLK21 Publication

Post-translational modificationi

Phosphorylated by TLK1 and TLK2.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NVP2.
MaxQBiQ9NVP2.
PaxDbiQ9NVP2.
PeptideAtlasiQ9NVP2.
PRIDEiQ9NVP2.

PTM databases

iPTMnetiQ9NVP2.
PhosphoSiteiQ9NVP2.

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

Protein-protein interaction databases

BioGridi120845. 60 interactions.
DIPiDIP-29242N.
IntActiQ9NVP2. 15 interactions.
MINTiMINT-3075078.
STRINGi9606.ENSP00000263382.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi15 – 173Combined sources
Beta strandi22 – 3211Combined sources
Beta strandi34 – 363Combined sources
Beta strandi38 – 458Combined sources
Helixi51 – 533Combined sources
Beta strandi54 – 629Combined sources
Beta strandi67 – 7610Combined sources
Helixi81 – 833Combined sources
Helixi86 – 894Combined sources
Beta strandi90 – 10112Combined sources
Beta strandi104 – 11714Combined sources
Helixi120 – 1245Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi145 – 1484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BNXX-ray2.31D1-158[»]
5BO0X-ray2.91D1-158[»]
ProteinModelPortaliQ9NVP2.
SMRiQ9NVP2. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156Interaction with histone H3By similarityAdd
BLAST
Regioni1 – 155155Interaction with CHAF1BAdd
BLAST

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiKOG3265. Eukaryota.
COG5137. LUCA.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9NVP2.
KOiK10753.
OMAiFIFQADA.
OrthoDBiEOG091G0K07.
PhylomeDBiQ9NVP2.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → A in BAA91602 (PubMed:14702039).Curated
Sequence conflicti23 – 231R → Q in BAD96800 (Ref. 5) Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BNXX-ray2.31D1-158[»]
5BO0X-ray2.91D1-158[»]
ProteinModelPortaliQ9NVP2.
SMRiQ9NVP2. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120845. 60 interactions.
DIPiDIP-29242N.
IntActiQ9NVP2. 15 interactions.
MINTiMINT-3075078.
STRINGi9606.ENSP00000263382.

PTM databases

iPTMnetiQ9NVP2.
PhosphoSiteiQ9NVP2.

Polymorphism and mutation databases

BioMutaiASF1B.

Proteomic databases

EPDiQ9NVP2.
MaxQBiQ9NVP2.
PaxDbiQ9NVP2.
PeptideAtlasiQ9NVP2.
PRIDEiQ9NVP2.

Protocols and materials databases

DNASUi55723.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55723.
GeneCardsiASF1B.
HGNCiHGNC:20996. ASF1B.
HPAiHPA054036.
MIMi609190. gene.
neXtProtiNX_Q9NVP2.
PharmGKBiPA134931112.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiASF1B. human.
GeneWikiiASF1B.
GenomeRNAii55723.
PROiQ9NVP2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105011.
CleanExiHS_ASF1B.
ExpressionAtlasiQ9NVP2. baseline and differential.
GenevisibleiQ9NVP2. 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 nameiASF1B_HUMAN
AccessioniPrimary (citable) accession number: Q9NVP2
Secondary accession number(s): Q53G51, Q9NVZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 130 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 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

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.