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Protein

Chromatin assembly factor 1 subunit B

Gene

Chaf1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:Chaf1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1314881. Chaf1b.

Subcellular locationi

  • Nucleus By similarity

  • Note: DNA replication foci.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Chromatin assembly factor 1 subunit BPRO_0000050897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei426 – 4261PhosphothreonineBy similarity
Modified residuei436 – 4361PhosphoserineCombined sources
Modified residuei440 – 4401PhosphothreonineBy similarity
Modified residuei456 – 4561PhosphoserineCombined sources
Modified residuei465 – 4651PhosphoserineBy similarity
Modified residuei501 – 5011N6-acetyllysineBy similarity
Modified residuei502 – 5021PhosphothreonineSequence analysis
Modified residuei510 – 5101PhosphothreonineSequence analysis

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D0N7.
MaxQBiQ9D0N7.
PaxDbiQ9D0N7.
PRIDEiQ9D0N7.

PTM databases

iPTMnetiQ9D0N7.
PhosphoSiteiQ9D0N7.

Expressioni

Gene expression databases

BgeeiQ9D0N7.
CleanExiMM_CHAF1B.
ExpressionAtlasiQ9D0N7. baseline and differential.
GenevisibleiQ9D0N7. MM.

Interactioni

Subunit structurei

Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B (By similarity).By similarity

Protein-protein interaction databases

BioGridi225873. 1 interaction.
IntActiQ9D0N7. 2 interactions.
MINTiMINT-4614962.
STRINGi10090.ENSMUSP00000023666.

Structurei

3D structure databases

ProteinModelPortaliQ9D0N7.
SMRiQ9D0N7. Positions 3-254, 361-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 5444WD 1Add
BLAST
Repeati64 – 10340WD 2Add
BLAST
Repeati127 – 16640WD 3Add
BLAST
Repeati169 – 20840WD 4Add
BLAST
Repeati228 – 27952WD 5Add
BLAST
Repeati301 – 34747WD 6Add
BLAST
Repeati351 – 39242WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat HIR1 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1009. Eukaryota.
ENOG410XPU4. LUCA.
GeneTreeiENSGT00550000074968.
HOGENOMiHOG000183312.
HOVERGENiHBG050780.
InParanoidiQ9D0N7.
KOiK10751.
OMAiQDGYCTL.
OrthoDBiEOG79SDWV.
PhylomeDBiQ9D0N7.
TreeFamiTF313062.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029129. CAF1_p60_C.
IPR001632. Gprotein_B.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF15512. CAF-1_p60_C. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D0N7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVITCEIAW HNKEPVYSLD FQHGATWKIH RLASAGVDTA VRIWKLERGP
60 70 80 90 100
DGKAIVEFLS NLARHTKAVN VVRFSPTGEI LASGGDDAVI LLWKMNDSKE
110 120 130 140 150
PEQIAFQDEE EAQLNKENWT VVKTLRGHLE DVYDICWATD GNLMTSASVD
160 170 180 190 200
NTVIIWDVSK GQKISIFNEH KSYVQGVTWD PLGQYIATLS CDRVLRIYNT
210 220 230 240 250
QKKRVAFNIS KMLSGQGPEG EARSFRMFHD DSMKSFFRRL SFTPDGSLLL
260 270 280 290 300
TPAGCMESGE NVTNTTYVFS RKHLKRPIAH LPCPGKATLA VRCCPVYFEL
310 320 330 340 350
RPVAETEKAS EEPSPELVNL PYRMVFAVAS EDSVLLYDTQ QSFPFGYVSN
360 370 380 390 400
IHYHTLSDIS WSSDGAFLAI SSTDGYCTFV TFEKGELGIP LKEKPVLSIR
410 420 430 440 450
TPDTAKKAKN QTHQGSSPGS RSVEGTPSNR TQDPSSPCTT PSPTTQSPAP
460 470 480 490 500
SAIKDSPSAI PAGKSPLPQP SEEKTLQPAG QNMKAPQPRR VTLNTLQTWG
510 520 530 540 550
KTAPRRINLT PLKTDTVPNP QPNSGTAPST EEVQPEAPGE PPEEPPELKR
560 570
PRLEEREGDA QNLAPDDSSK TV
Length:572
Mass (Da):63,132
Last modified:June 1, 2001 - v1
Checksum:i03C2BC263591FF72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011243 mRNA. Translation: BAB27490.1.
BC013532 mRNA. Translation: AAH13532.1.
CCDSiCCDS28344.1.
RefSeqiNP_082359.1. NM_028083.4.
XP_006522910.1. XM_006522847.2.
UniGeneiMm.274222.

Genome annotation databases

EnsembliENSMUST00000023666; ENSMUSP00000023666; ENSMUSG00000022945.
ENSMUST00000117099; ENSMUSP00000113684; ENSMUSG00000022945.
GeneIDi110749.
KEGGimmu:110749.
UCSCiuc008aac.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011243 mRNA. Translation: BAB27490.1.
BC013532 mRNA. Translation: AAH13532.1.
CCDSiCCDS28344.1.
RefSeqiNP_082359.1. NM_028083.4.
XP_006522910.1. XM_006522847.2.
UniGeneiMm.274222.

3D structure databases

ProteinModelPortaliQ9D0N7.
SMRiQ9D0N7. Positions 3-254, 361-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225873. 1 interaction.
IntActiQ9D0N7. 2 interactions.
MINTiMINT-4614962.
STRINGi10090.ENSMUSP00000023666.

PTM databases

iPTMnetiQ9D0N7.
PhosphoSiteiQ9D0N7.

Proteomic databases

EPDiQ9D0N7.
MaxQBiQ9D0N7.
PaxDbiQ9D0N7.
PRIDEiQ9D0N7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023666; ENSMUSP00000023666; ENSMUSG00000022945.
ENSMUST00000117099; ENSMUSP00000113684; ENSMUSG00000022945.
GeneIDi110749.
KEGGimmu:110749.
UCSCiuc008aac.1. mouse.

Organism-specific databases

CTDi8208.
MGIiMGI:1314881. Chaf1b.

Phylogenomic databases

eggNOGiKOG1009. Eukaryota.
ENOG410XPU4. LUCA.
GeneTreeiENSGT00550000074968.
HOGENOMiHOG000183312.
HOVERGENiHBG050780.
InParanoidiQ9D0N7.
KOiK10751.
OMAiQDGYCTL.
OrthoDBiEOG79SDWV.
PhylomeDBiQ9D0N7.
TreeFamiTF313062.

Miscellaneous databases

NextBioi364585.
PROiQ9D0N7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0N7.
CleanExiMM_CHAF1B.
ExpressionAtlasiQ9D0N7. baseline and differential.
GenevisibleiQ9D0N7. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR029129. CAF1_p60_C.
IPR001632. Gprotein_B.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF15512. CAF-1_p60_C. 1 hit.
PF00400. WD40. 4 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiCAF1B_MOUSE
AccessioniPrimary (citable) accession number: Q9D0N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 126 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.