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Protein

Chromatin assembly factor 1 subunit A

Gene

Chaf1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, DNA replication

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin assembly factor 1 subunit A
Short name:
CAF-1 subunit A
Alternative name(s):
Chromatin assembly factor I p150 subunit
Short name:
CAF-I 150 kDa subunit
Short name:
CAF-I p150
Gene namesi
Name:Chaf1a
Synonyms:Caip150
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1351331. Chaf1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi224 – 2241V → N or E: Prevents binding to CBX1 and CBX5. 1 Publication
Mutagenesisi224 – 2241V → S or D: Prevents binding to CBX1 and CBX5. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Chromatin assembly factor 1 subunit APRO_0000089277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei208 – 2081PhosphoserineBy similarity
Modified residuei838 – 8381PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9QWF0.
MaxQBiQ9QWF0.
PaxDbiQ9QWF0.
PRIDEiQ9QWF0.

PTM databases

PhosphoSiteiQ9QWF0.

Expressioni

Gene expression databases

BgeeiQ9QWF0.
CleanExiMM_CHAF1A.

Interactioni

Subunit structurei

Homodimer (By similarity). Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. CHAF1A binds directly to PCNA and to CBX1, CBX3 and CBX5. Binds MBD1. Interacts directly with CBX5 via the PxVxL motif. During DNA replication, it forms a S phase-specific complex that facilitates DNA methylation and histone H3 'Lys-9' methylation during replication-coupled chromatin assembly and is at least composed of the CHAF1A, MBD1 and SETDB1. Interacts with CBX5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbx1P839173EBI-639217,EBI-78119
Gfi1P703385EBI-639217,EBI-3954754

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205142. 16 interactions.
IntActiQ9QWF0. 17 interactions.
STRINGi10090.ENSMUSP00000002914.

Structurei

Secondary structure

1
911
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi222 – 2243Combined sources
Turni228 – 2303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4ZNMR-C210-238[»]
ProteinModelPortaliQ9QWF0.
SMRiQ9QWF0. Positions 210-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QWF0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3131Binds PCNABy similarityAdd
BLAST
Regioni176 – 327152Binds CBX1 and CBX3 chromo shadow domainsAdd
BLAST
Regioni621 – 65737Necessary for homodimerization and competence for chromatin assemblyBy similarityAdd
BLAST
Regioni639 – 911273Binds to p60By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi217 – 23014PxVxL motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi311 – 445135Arg/Glu/Lys-richAdd
BLAST
Compositional biasi546 – 64196Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi582 – 5876Poly-Glu

Domaini

Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.

Sequence similaritiesi

Belongs to the CHAF1A family.Curated

Phylogenomic databases

eggNOGiKOG4364. Eukaryota.
ENOG410ZXI9. LUCA.
GeneTreeiENSGT00440000034888.
HOGENOMiHOG000111290.
HOVERGENiHBG050779.
InParanoidiQ9QWF0.
KOiK10750.
OMAiTWNKKTA.
OrthoDBiEOG76X60P.
PhylomeDBiQ9QWF0.
TreeFamiTF350377.

Family and domain databases

InterProiIPR029105. CAF1-p150_C2.
IPR029091. CAF1-p150_N.
IPR022043. CAF1A.
[Graphical view]
PANTHERiPTHR15272. PTHR15272. 1 hit.
PfamiPF15539. CAF1-p150_C2. 1 hit.
PF15557. CAF1-p150_N. 1 hit.
PF12253. CAF1A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QWF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEEPEAATR TAAAVDCKDR PGFPVKRLIQ ARLPFKRLNL VPKEKVEEDT
60 70 80 90 100
SPKAAVESKV PDLQLSLGTF ESQCHTGSHV GLSTKLVGGQ GPIDSFLRAT
110 120 130 140 150
IKPVPSVVII DLTENCSDIP DSPEGHSELS PDTAGVVTTV EGAAKQQEHS
160 170 180 190 200
AAELCLLETP SDITCHMEEE PGSPGDPKRT GDCQAGSLQS CPELTPGSRT
210 220 230 240 250
CPTKELSSWS KAGDLLFIEK VPVVVLEDIL ATKPSIASLP MMSLDRSVTS
260 270 280 290 300
ESEILESCPE DDSILSHSST NSSSPTSSPE GPSTPPEHRG GRSSPSTPAC
310 320 330 340 350
RVAKNFVKGS TEKGRSKLHR DREQQREEKE KLREEIRRAK EEARKKKEEE
360 370 380 390 400
KELKEKERRE KREKDEKEKA EKQRLKEEKR KERQEALEAK LEEKRKKEEE
410 420 430 440 450
KRLREEEKRL REEEKRIKAE KAEITRFFQK PKTPQAPKTL AGSCGKFAPF
460 470 480 490 500
EIKEHMVLAP RCRAALDQDL CDQLDQLLQQ QSVASTFLSD LKSRLPLRSG
510 520 530 540 550
PTRVCGHDTD IMNRDVVIVE SSKVDGVSER KKFGRMKLLQ FSENHRPAYW
560 570 580 590 600
GTWNKKTAII RPRNPWAQDK DLLDYEVDSD DEWEEEEPGE SLSHSEGDED
610 620 630 640 650
DDVGEDEDED DGFFVPHGYL SEDEGVTEEC ADPENHKVHQ KLKAKEWDEL
660 670 680 690 700
LAKGKRFRVL QPVHVGCVWA SEAANCTSSD LKLLQQFTAC LLDVASPDEP
710 720 730 740 750
EPGASRREKR DQHILAQLLP LLHGNVNGSK VIIHEFQEQC RRGLLTLPSP
760 770 780 790 800
TPHLQMPNLE DAVAVPSKAR LKRLISENSA YEKRPNFRMC WYVHPEVLKS
810 820 830 840 850
FGQECLPVPC QWTYITTMPS APREDSGSAS TEGPGQSTPM LLKRKPAATM
860 870 880 890 900
CITQFMKKRR YDGQVGSGDM DGFQADTEED EEDDTDCMII DVPDVGSDVS
910
EAPIPAPTLC K
Length:911
Mass (Da):101,936
Last modified:May 1, 2000 - v1
Checksum:i67B3340010425C95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132771 mRNA. Translation: CAB55497.2.
AK034839 mRNA. Translation: BAC28848.1.
AK161016 mRNA. Translation: BAE36149.1.
CH466559 Genomic DNA. Translation: EDL23708.1.
BC053740 mRNA. Translation: AAH53740.1.
CCDSiCCDS28892.1.
RefSeqiNP_038761.1. NM_013733.3.
UniGeneiMm.391010.

Genome annotation databases

EnsembliENSMUST00000002914; ENSMUSP00000002914; ENSMUSG00000002835.
GeneIDi27221.
KEGGimmu:27221.
UCSCiuc008dar.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132771 mRNA. Translation: CAB55497.2.
AK034839 mRNA. Translation: BAC28848.1.
AK161016 mRNA. Translation: BAE36149.1.
CH466559 Genomic DNA. Translation: EDL23708.1.
BC053740 mRNA. Translation: AAH53740.1.
CCDSiCCDS28892.1.
RefSeqiNP_038761.1. NM_013733.3.
UniGeneiMm.391010.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4ZNMR-C210-238[»]
ProteinModelPortaliQ9QWF0.
SMRiQ9QWF0. Positions 210-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205142. 16 interactions.
IntActiQ9QWF0. 17 interactions.
STRINGi10090.ENSMUSP00000002914.

PTM databases

PhosphoSiteiQ9QWF0.

Proteomic databases

EPDiQ9QWF0.
MaxQBiQ9QWF0.
PaxDbiQ9QWF0.
PRIDEiQ9QWF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002914; ENSMUSP00000002914; ENSMUSG00000002835.
GeneIDi27221.
KEGGimmu:27221.
UCSCiuc008dar.1. mouse.

Organism-specific databases

CTDi10036.
MGIiMGI:1351331. Chaf1a.

Phylogenomic databases

eggNOGiKOG4364. Eukaryota.
ENOG410ZXI9. LUCA.
GeneTreeiENSGT00440000034888.
HOGENOMiHOG000111290.
HOVERGENiHBG050779.
InParanoidiQ9QWF0.
KOiK10750.
OMAiTWNKKTA.
OrthoDBiEOG76X60P.
PhylomeDBiQ9QWF0.
TreeFamiTF350377.

Miscellaneous databases

ChiTaRSiChaf1a. mouse.
EvolutionaryTraceiQ9QWF0.
NextBioi305130.
PROiQ9QWF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QWF0.
CleanExiMM_CHAF1A.

Family and domain databases

InterProiIPR029105. CAF1-p150_C2.
IPR029091. CAF1-p150_N.
IPR022043. CAF1A.
[Graphical view]
PANTHERiPTHR15272. PTHR15272. 1 hit.
PfamiPF15539. CAF1-p150_C2. 1 hit.
PF15557. CAF1-p150_N. 1 hit.
PF12253. CAF1A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins."
    Murzina N.V., Verreault A., Laue E.D., Stillman B.
    Mol. Cell 4:529-540(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, INTERACTION WITH HP1 PROTEINS.
  2. "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: Embryo and Head.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Limb.
  5. "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1."
    Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.
    Mol. Cell. Biol. 23:3226-3236(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD1.

Entry informationi

Entry nameiCAF1A_MOUSE
AccessioniPrimary (citable) accession number: Q9QWF0
Secondary accession number(s): Q3TU22, Q544M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 122 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.