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Reviewed, UniProtKB/Swiss-Prot Q13111 (CAF1A_HUMAN)

Last modified November 25, 2008. Version 77. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chromatin assembly factor 1 subunit A
      Short name=CAF-1 subunit A
Alternative name(s):
    Chromatin assembly factor I p150 subunit
    CAF-I 150 kDa subunit
    CAF-Ip150
Gene names
Name: CHAF1A
Synonyms: CAF, CAF1P150
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. The CCR4-NOT complex functions as general transcription regulation complex.

Subunit structure

Part 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. Part of the CCR4-NOT core complex that contains CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8. CHAF1A binds directly to PCNA and to CBX1. 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.

Subcellular location

Nucleus. Note= DNA replication foci.

Developmental stage

Active complex is found in G1, S and G2 phases.

Domain

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.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence caution

The sequence AAH52620.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence starting in position 408.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Notes: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q13111-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13111-2)

The sequence of this isoform differs from the canonical sequence as follows:
     692-731: CFLETLPAQE...LPLLHGNVNG → HWVHPESRGD...CVKSTLSCFT
     732-938: Missing.
Isoform 3 (identifier: Q13111-3)

The sequence of this isoform differs from the canonical sequence as follows:
     754-926: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 938938Chromatin assembly factor 1 subunit A
PRO_0000089276

Regions

Region1 – 296296Binds to CBX1 chromo shadow domain
Region1 – 3131Binds to PCNA
Region642 – 938297Binds to p60
Motif215 – 22814PxVxL motif
Compositional bias305 – 435131Arg/Glu/Lys-rich
Compositional bias584 – 5907Poly-Glu
Compositional bias601 – 6055Poly-Asp
Compositional bias887 – 8937Poly-Glu

Amino acid modifications

Modified residue471Phosphoserine
Modified residue1231Phosphoserine
Modified residue1811Phosphoserine
Modified residue1851Phosphoserine
Modified residue1881Phosphoserine
Modified residue2061Phosphoserine
Modified residue2371Phosphoserine
Modified residue2411Phosphothreonine
Modified residue7041Phosphothreonine
Modified residue7541Phosphoserine
Modified residue8551Phosphoserine
Modified residue9331Phosphoserine

Natural variations

Alternative sequence692 – 73140CFLET…GNVNG → HWVHPESRGDVCRTLRVSSP QSRYLNRLNSCVKSTLSCFT in isoform 2.
VSP_004149
Alternative sequence732 – 938207Missing in isoform 2.
VSP_004150
Alternative sequence754 – 926173Missing in isoform 3.
VSP_004151

Experimental info

Sequence conflict7571T → S in AAF04291. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DBD01B9F1A0E28B7

FASTA938105,223
        10         20         30         40         50         60 
MDCKDRPAFP VKKLIQARLP FKRLNLVPKG KADDMSDDQG TSVQSKSPDL EASLDTLENN 

        70         80         90        100        110        120 
CHVGSDIDFR PKLVNGKGPL DNFLRNRIET SIGQSTVIID LTEDSNEQPD SLVDHNKLNS 

       130        140        150        160        170        180 
EASPSREAIN GQREDTGDQQ GLLKAIQNDK LAFPGETLSD IPCKTEEEGV GCGGAGRRGD 

       190        200        210        220        230        240 
SQECSPRSCP ELTSGPRMCP RKEQDSWSEA GGILFKGKVP MVVLQDILAV RPPQIKSLPA 

       250        260        270        280        290        300 
TPQGKNMTPE SEVLESFPEE DSVLSHSSLS SPSSTSSPEG PPAPPKQHSS TSPFPTSTPL 

       310        320        330        340        350        360 
RRITKKFVKG STEKNKLRLQ RDQERLGKQL KLRAEREEKE KLKEEAKRAK EEAKKKKEEE 

       370        380        390        400        410        420 
KELKEKERRE KREKDEKEKA EKQRLKEERR KERQEALEAK LEEKRKKEEE KRLREEEKRI 

       430        440        450        460        470        480 
KAEKAEITRF FQKPKTPQAP KTLAGSCGKF APFEIKEHMV LAPRRRTAFH PDLCSQLDQL 

       490        500        510        520        530        540 
LQQQSGEFSF LKDLKGRQPL RSGPTHVSTR NADIFNSDVV IVERGKGDGV PERRKFGRMK 

       550        560        570        580        590        600 
LLQFCENHRP AYWGTWNKKT ALIRARDPWA QDTKLLDYEV DSDEEWEEEE PGESLSHSEG 

       610        620        630        640        650        660 
DDDDDMGEDE DEDDGFFVPH GYLSEDEGVT EECADPENHK VRQKLKAKEW DEFLAKGKRF 

       670        680        690        700        710        720 
RVLQPVKIGC VWAADRDCAG DDLKVLQQFA ACFLETLPAQ EEQTPKASKR ERRDEQILAQ 

       730        740        750        760        770        780 
LLPLLHGNVN GSKVIIREFQ EHCRRGLLSN HTGSPRTPST TYLHTPTPSE DAAIPSKSRL 

       790        800        810        820        830        840 
KRLISENSVY EKRPDFRMCW YVHPQVLQSF QQEHLPVPCQ WSYVTSVPSA PKEDSGSVPS 

       850        860        870        880        890        900 
TGPSQGTPIS LKRKSAGSMC ITQFMKKRRH DGQIGAEDMD GFQADTEEEE EEEGDCMIVD 

       910        920        930 
VPDAVEVQAP CGAASGAGGG VGVDTGKATL TASPLGAS 

« Hide

Isoform 2 [UniParc].

Checksum: F7572877A06B9A70
Show »

73182,956
Isoform 3 [UniParc].

Checksum: 8E56019C48629C6C
Show »

76586,540

References

« Hide 'large scale' references
[1]"The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication."
Kaufman P.D., Kobayashi R., Kessler N., Stillman B.
Cell 81:1105-1114(1995) [PubMed: 7600578] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix adenocarcinoma.
[2]"Genomic sequence and expression analyses of human chromatin assembly factor 1 p150 gene."
Dong H., Lin W., Zhang C.-K., Xiong H., Fu G., Jin W.-R., Chen R., Chen Z., Qi Z.-T., Huang G.M.
Gene 264:187-196(2001) [PubMed: 11250073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-407.
Tissue: Ovary.
[4]"Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin."
Shibahara K., Stillman B.
Cell 96:575-585(1999) [PubMed: 10052459] [Abstract]
Cited for: INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
[5]"A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage."
Moggs J.G., Grandi P., Quivy J.P., Jonsson Z.O., Hubscher U., Becker P.B., Almouzni G.
Mol. Cell. Biol. 20:1206-1218(2000) [PubMed: 10648606] [Abstract]
Cited for: INTERACTION WITH PCNA.
[6]"CAF-1 and the inheritance of chromatin states: at the crossroads of DNA replication and repair."
Ridgway P., Almouzni G.
J. Cell Sci. 113:2647-2658(2000) [PubMed: 10893180] [Abstract]
Cited for: REVIEW.
[7]"BTG2 antiproliferative protein interacts with the human CCR4 complex existing in vivo in three cell-cycle-regulated forms."
Morel A.-P., Sentis S., Bianchin C., Le Romancer M., Jonard L., Rostan M.-C., Rimokh R., Corbo L.
J. Cell Sci. 116:2929-2936(2003) [PubMed: 12771185] [Abstract]
Cited for: INTERACTION WITH THE CCR4-NOT COMPLEX.
[8]"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: 12697822] [Abstract]
Cited for: INTERACTION WITH MBD1.
[9]"Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
Sarraf S.A., Stancheva I.
Mol. Cell 15:595-605(2004) [PubMed: 15327775] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MBD1 AND SETDB1.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-188, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed: 15882967] [Abstract]
Cited for: INTERACTION WITH CBX5.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-123 AND SER-754, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; THR-241 AND SER-933, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-185 AND SER-188, MASS SPECTROMETRY.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-188, MASS SPECTROMETRY.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; THR-704; SER-754; SER-855 AND SER-933, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U20979 mRNA. Translation: AAA76736.1.
AF190465 Genomic DNA. Translation: AAF04291.1.
BC052620 mRNA. Translation: AAH52620.1. Sequence problems.
PIRA56731.
RefSeqNP_005474.2.
UniGeneHs.79018

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ13111.

PTM databases

PhosphoSiteQ13111.

Genome annotation databases

EnsemblENSG00000167670. Homo sapiens. [Contig view]
GeneID10036.
KEGGhsa:10036.

Organism-specific databases

H-InvDBHIX0040076.
HGNCHGNC:1910. CHAF1A.
HPACAB015186.
MIM601246. gene.
PharmGKBPA26446.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ13111.

Gene expression databases

ArrayExpressQ13111.
CleanExHS_CHAF1A.
GermOnlineENSG00000167670. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio37903.
SOURCESearch...

Entry information

Entry nameCAF1A_HUMAN
AccessionPrimary (citable) accession number: Q13111
Secondary accession number(s): Q7Z7K3, Q9UJY8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents