Chromatin assembly factor 1 subunit B

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Q13112 (CAF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chromatin assembly factor 1 subunit B
Short name=CAF-1 subunit B

Alternative name(s):
Chromatin assembly factor I p60 subunit
Short name=CAF-I 60 kDa subunit
Short name=CAF-I p60
M-phase phosphoprotein 7

Gene names

Name:	CHAF1B
Synonyms:	CAF1A, CAF1P60, MPHOSPH7, MPP7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Complex that is 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. The CCR4-NOT complex functions as general transcription regulation complex. Ref.6
Subunit structure	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. In G2 and S phase also monomeric CHAF1B is detected. Subunit of the CCR4-NOT core complex that contains CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8.
Subcellular location	Nucleus. Cytoplasm. Note: DNA replication foci. Cytoplasmic in M phase. Ref.7
Developmental stage	Active complex is found in G1, S and G2 phases.
Post-translational modification	Differentially phosphorylated during cell cycle. During mitosis the p60 subunit of inactive CAF-1 is hyperphosphorylated and displaced into the cytosol. Progressivly dephosphorylated from G1 to S and G2 phase. Phosphorylated p60 is recruited to chromatin undergoing DNA repair after UV irradiation in G1, S or G2 phases. Ref.5 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Sequence similarities	Belongs to the WD repeat HIR1 family. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW DNA replication-dependent nucleosome assembly Traceable author statement. Source: ProtInc cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	CAF-1 complex Inferred from direct assay. Source: UniProtKB centrosome Inferred from direct assay. Source: HPA
Molecular function	chromatin binding Traceable author statement. Source: ProtInc histone binding Non-traceable author statement Ref.1. Source: UniProtKB unfolded protein binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNOT6L	Q96LI5	2	EBI-1052944,EBI-1046635

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 559

559

Chromatin assembly factor 1 subunit B

PRO_0000050896

Regions

Repeat

11 – 54

WD 1

Repeat

64 – 103

WD 2

Repeat

127 – 166

WD 3

Repeat

169 – 208

WD 4

Repeat

228 – 279

WD 5

Repeat

299 – 340

WD 6

Repeat

344 – 385

WD 7

Amino acid modifications

Modified residue

409

Phosphoserine Ref.15

Modified residue

419

Phosphothreonine Ref.15

Modified residue

428

Phosphoserine Ref.16

Modified residue

429

Phosphoserine Ref.10 Ref.13 Ref.15 Ref.16 Ref.17

Modified residue

432

Phosphothreonine Ref.16

Modified residue

433

Phosphothreonine Ref.15 Ref.16

Modified residue

458

Phosphoserine Ref.11 Ref.14

Modified residue

485

Phosphothreonine Ref.12

Modified residue

494

N6-acetyllysine Ref.18

Modified residue

495

Phosphothreonine Potential

Modified residue

503

Phosphothreonine Ref.15

Modified residue

509

Phosphothreonine Potential

Modified residue

521

Phosphothreonine Potential

Modified residue

524

Phosphothreonine Ref.15 Ref.16

Modified residue

529

Phosphoserine Ref.16

Modified residue

531

Phosphothreonine Potential

Modified residue

538

Phosphoserine Ref.10 Ref.15 Ref.16 Ref.17

Natural variations

Natural variant

506

K → Q.
Corresponds to variant rs2230638 [ dbSNP | Ensembl ].

VAR_053387

Experimental info

Sequence conflict

494

K → N in CAA66915. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q13112 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AD1846CC81B8DC9F
Show »

FASTA

559

61,493

        10         20         30         40         50         60 
MKVITCEIAW HNKEPVYSLD FQHGTAGRIH RLASAGVDTN VRIWKVEKGP DGKAIVEFLS 

        70         80         90        100        110        120 
NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKVNDNKE PEQIAFQDED EAQLNKENWT 

       130        140        150        160        170        180 
VVKTLRGHLE DVYDICWATD GNLMASASVD NTAIIWDVSK GQKISIFNEH KSYVQGVTWD 

       190        200        210        220        230        240 
PLGQYVATLS CDRVLRVYSI QKKRVAFNVS KMLSGIGAEG EARSYRMFHD DSMKSFFRRL 

       250        260        270        280        290        300 
SFTPDGSLLL TPAGCVESGE NVMNTTYVFS RKNLKRPIAH LPCPGKATLA VRCCPVYFEL 

       310        320        330        340        350        360 
RPVVETGVEL MSLPYRLVFA VASEDSVLLY DTQQSFPFGY VSNIHYHTLS DISWSSDGAF 

       370        380        390        400        410        420 
LAISSTDGYC SFVTFEKDEL GIPLKEKPVL NMRTPDTAKK TKSQTHRGSS PGPRPVEGTP 

       430        440        450        460        470        480 
ASRTQDPSSP GTTPPQARQA PAPTVIRDPP SITPAVKSPL PGPSEEKTLQ PSSQNTKAHP 

       490        500        510        520        530        540 
SRRVTLNTLQ AWSKTTPRRI NLTPLKTDTP PSSVPTSVIS TPSTEEIQSE TPGDAQGSPP 

       550 
ELKRPRLDEN KGGTESLDP

« Hide

References

	« Hide 'large scale' referencesShow '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], PROTEIN SEQUENCE OF 100-123.
[2]	"Genomic sequencing of 1.2-Mb region on human chromosome 21q22.2." Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Nakatoh E., Shintani A., Asakawa S., Shimizu N. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[5]	"Identification of novel M phase phosphoproteins by expression cloning." Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M. Mol. Biol. Cell 7:1455-1469(1996) [PubMed: 8885239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 474-559, PHOSPHORYLATION. Tissue: Lymphoblast.
[6]	"Recruitment of phosphorylated chromatin assembly factor 1 to chromatin after UV irradiation of human cells." Martini E., Roche D.M., Marheineke K., Verreault A., Almouzni G. J. Cell Biol. 143:563-575(1998) [PubMed: 9813080] [Abstract] Cited for: FUNCTION.
[7]	"Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle." Marheineke K., Krude T. J. Biol. Chem. 273:15279-15286(1998) [PubMed: 9614144] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[8]	"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.
[9]	"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.
[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-429 AND SER-538, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-458, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-429, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-409; THR-419; SER-429; THR-433; THR-503; THR-524 AND SER-538, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-429; THR-432; THR-433; THR-524; SER-529 AND SER-538, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND SER-538, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-494, MASS SPECTROMETRY.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U20980 mRNA. Translation: AAA76737.1. AP000694 Genomic DNA. Translation: BAA89426.1. AP001725 Genomic DNA. Translation: BAA95549.1. BC021218 mRNA. Translation: AAH21218.1. X98262 mRNA. Translation: CAA66915.1.
IPI	IPI00011857.
PIR	B56731.
RefSeq	NP_005432.1. NM_005441.2.
UniGene	Hs.75238.
3D structure databases
ProteinModelPortal	Q13112.
SMR	Q13112. Positions 8-199, 344-376.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29243N.
IntAct	Q13112. 8 interactions.
STRING	Q13112.
PTM databases
PhosphoSite	Q13112.
Polymorphism databases
DMDM	3121829.
Proteomic databases
PRIDE	Q13112.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000314103; ENSP00000315700; ENSG00000159259.
GeneID	8208.
KEGG	hsa:8208.
UCSC	uc002yvj.1. human.
Organism-specific databases
CTD	8208.
GeneCards	GC21P037757.
H-InvDB	HIX0016103.
HGNC	HGNC:1911. CHAF1B.
HPA	HPA016698. HPA021679. HPA029538.
MIM	601245. gene.
neXtProt	NX_Q13112.
PharmGKB	PA26447.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08122.
GeneTree	ENSGT00550000074968.
HOGENOM	HBG715018.
HOVERGEN	HBG050780.
InParanoid	Q13112.
OMA	DFQHGTA.
OrthoDB	EOG4G4GQD.
PhylomeDB	Q13112.
Gene expression databases
ArrayExpress	Q13112.
Bgee	Q13112.
CleanEx	HS_CHAF1B. HS_MPP7.
Genevestigator	Q13112.
GermOnline	ENSG00000159259. Homo sapiens.
Family and domain databases
InterPro	IPR001632. Gprotein_B. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K10751.
Pfam	PF00400. WD40. 5 hits. [Graphical view]
PRINTS	PR00319. GPROTEINB.
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 3 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	30919.
SOURCE	Search...

Entry information

Entry name

CAF1B_HUMAN

Accession

Primary (citable) accession number: Q13112
Secondary accession number(s): Q99548

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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Human chromosome 21: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents