Q13111 (CAF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
Short name=hp150

Gene names

Name:	CHAF1A
Synonyms:	CAF, CAF1P150

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	956 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Ref.9 Ref.11
Subunit structure	Homodimer. 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. 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. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with CBX5. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.17
Subcellular location	Nucleus. Note: DNA replication foci. Ref.5
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.
Sequence similarities	Belongs to the CHAF1A family.
Sequence caution	The sequence AAA76736.1 differs from that shown. Reason: Erroneous initiation. The sequence AAF04291.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH52620.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH52620.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 426.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome 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 Ref.4. Source: ProtInc cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Traceable author statement Ref.4. 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 PubMed 8858152. Source: UniProtKB WINAC complex Inferred from direct assay Ref.9. Source: BHF-UCL
Molecular_function	chromatin binding Traceable author statement Ref.4. Source: ProtInc unfolded protein binding Traceable author statement Ref.4. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX5	P45973	3	EBI-1020839,EBI-78219
GFI1	Q99684	4	EBI-1020839,EBI-949368
NCK1	P16333	2	EBI-1020839,EBI-389883
PCNA	P12004	2	EBI-1020839,EBI-358311

Alternative products

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

Note: 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:
     710-749: CFLETLPAQE...LPLLHGNVNG → HWVHPESRGD...CVKSTLSCFT
     750-956: Missing.

Isoform 3 (identifier: Q13111-3)

The sequence of this isoform differs from the canonical sequence as follows:
     772-944: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 956	956	Chromatin assembly factor 1 subunit A		PRO_0000089276
Regions
	Region	1 – 314	314	Binds to CBX1 chromo shadow domain
	Region	1 – 49	49	Binds to PCNA
	Region	642 – 678	37	Necessary for homodimerization and competence for chromatin assembly
	Region	660 – 956	297	Binds to p60
	Motif	233 – 246	14	PxVxL motif
	Compositional bias	323 – 453	131	Arg/Glu/Lys-rich
	Compositional bias	602 – 608	7	Poly-Glu
	Compositional bias	619 – 623	5	Poly-Asp
	Compositional bias	905 – 911	7	Poly-Glu
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.14 Ref.19
	Modified residue	123	1	Phosphoserine Ref.18
	Modified residue	138	1	Phosphoserine Ref.18
	Modified residue	141	1	Phosphoserine Ref.18 Ref.19
	Modified residue	143	1	Phosphoserine Ref.18 Ref.19
	Modified residue	206	1	Phosphoserine Ref.19
	Modified residue	224	1	Phosphoserine Ref.15 Ref.18
	Modified residue	310	1	Phosphoserine Ref.19
	Modified residue	722	1	Phosphothreonine Ref.15 Ref.18 Ref.19
	Modified residue	772	1	Phosphoserine Ref.15 Ref.18 Ref.19
	Modified residue	775	1	Phosphoserine Ref.15 Ref.19
	Modified residue	865	1	Phosphothreonine Ref.18
	Modified residue	873	1	Phosphoserine Ref.15 Ref.18
	Modified residue	951	1	Phosphoserine Ref.15 Ref.18 Ref.19
Natural variations
	Alternative sequence	710 – 749	40	CFLET…GNVNG → HWVHPESRGDVCRTLRVSSP QSRYLNRLNSCVKSTLSCFT in isoform 2.		VSP_004149
	Alternative sequence	750 – 956	207	Missing in isoform 2.		VSP_004150
	Alternative sequence	772 – 944	173	Missing in isoform 3.		VSP_004151
	Natural variant	167	1	D → V. Corresponds to variant rs35651457 [ dbSNP | Ensembl ].		VAR_055329
	Natural variant	239	1	M → V. Corresponds to variant rs2230635 [ dbSNP | Ensembl ].		VAR_055330
	Natural variant	850	1	K → R. Corresponds to variant rs8100525 [ dbSNP | Ensembl ].		VAR_055331
	Natural variant	923	1	A → V. Ref.1 Ref.4 Corresponds to variant rs9352 [ dbSNP | Ensembl ].		VAR_055332
	Natural variant	950	1	S → A. Ref.1 Ref.3 Ref.4 Ref.15 Ref.18 Ref.19 Corresponds to variant rs243383 [ dbSNP | Ensembl ].		VAR_055333
Experimental info
	Mutagenesis	240	1	V → E: Abolishes interaction with CBX5; when associated with E-242. Ref.17
	Mutagenesis	242	1	L → E: Abolishes interaction with CBX5; when associated with E-240. Ref.17
	Sequence conflict	775	1	S → T in AAA76736. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 90617F8FE8DB67B0	FASTA	956	106,926
	10 20 30 40 50 60 MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS 70 80 90 100 110 120 VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT 130 140 150 160 170 180 EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP 190 200 210 220 230 240 CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV 250 260 270 280 290 300 VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP 310 320 330 340 350 360 APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL 370 380 390 400 410 420 KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE 430 440 450 460 470 480 EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA 490 500 510 520 530 540 PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV 550 560 570 580 590 600 ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS 610 620 630 640 650 660 DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR 670 680 690 700 710 720 QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAC FLETLPAQEE 730 740 750 760 770 780 QTPKASKRER RDEQILAQLL PLLHGNVNGS KVIIREFQEH CRRGLLSNHT GSPRSPSTTY 790 800 810 820 830 840 LHTPTPSEDA AIPSKSRLKR LISENSVYEK RPDFRMCWYV HPQVLQSFQQ EHLPVPCQWS 850 860 870 880 890 900 YVTSVPSAPK EDSGSVPSTG PSQGTPISLK RKSAGSMCIT QFMKKRRHDG QIGAEDMDGF 910 920 930 940 950 QADTEEEEEE EGDCMIVDVP DAAEVQAPCG AASGAGGGVG VDTGKATLTS SPLGAS
	Isoform 2 [UniParc]. Checksum: A7176E2D8D18CA0F	FASTA	749	84,685
	10 20 30 40 50 60 MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS 70 80 90 100 110 120 VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT 130 140 150 160 170 180 EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP 190 200 210 220 230 240 CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV 250 260 270 280 290 300 VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP 310 320 330 340 350 360 APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL 370 380 390 400 410 420 KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE 430 440 450 460 470 480 EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA 490 500 510 520 530 540 PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV 550 560 570 580 590 600 ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS 610 620 630 640 650 660 DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR 670 680 690 700 710 720 QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAH WVHPESRGDV 730 740 CRTLRVSSPQ SRYLNRLNSC VKSTLSCFT
	Isoform 3 [UniParc]. Checksum: 44E39E1CCE192850	FASTA	783	88,285
	10 20 30 40 50 60 MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS 70 80 90 100 110 120 VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT 130 140 150 160 170 180 EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP 190 200 210 220 230 240 CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV 250 260 270 280 290 300 VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP 310 320 330 340 350 360 APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL 370 380 390 400 410 420 KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE 430 440 450 460 470 480 EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA 490 500 510 520 530 540 PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV 550 560 570 580 590 600 ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS 610 620 630 640 650 660 DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR 670 680 690 700 710 720 QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAC FLETLPAQEE 730 740 750 760 770 780 QTPKASKRER RDEQILAQLL PLLHGNVNGS KVIIREFQEH CRRGLLSNHT GKATLTSSPL GAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), VARIANTS VAL-923 AND ALA-950.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-950. Tissue: Brain and Ovary.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-956 (ISOFORM 1), VARIANTS VAL-923 AND ALA-950. Tissue: Cervix adenocarcinoma.
[5]	"Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin." Shibahara K., Stillman B. Cell 96:575-585(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
[6]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PCNA.
[7]	"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] [Europe PMC] [Abstract] Cited for: REVIEW.
[8]	"Dimerization of the largest subunit of chromatin assembly factor 1: importance in vitro and during Xenopus early development." Quivy J.-P., Grandi P., Almouzni G. EMBO J. 20:2015-2027(2001) [PubMed] [Europe PMC] [Abstract] Cited for: HOMODIMERIZATION.
[9]	"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome." Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S. Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[10]	"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.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MBD1 AND SETDB1.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBX5.
[13]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-722; SER-772; SER-775; SER-873 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation." Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C. Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBX5, MUTAGENESIS OF VAL-240 AND LEU-242.
[18]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-138; SER-141; SER-143; SER-224; THR-722; SER-772; THR-865; SER-873 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-141; SER-143; SER-206; SER-310; THR-722; SER-772; SER-775 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF190465 Genomic DNA. Translation: AAF04291.1. Different initiation. AC011498 Genomic DNA. No translation available. BC052620 mRNA. Translation: AAH52620.1. Sequence problems. BC067093 mRNA. Translation: AAH67093.1. U20979 mRNA. Translation: AAA76736.1. Different initiation.
IPI	IPI00023177. IPI00219363. IPI00219364.
PIR	A56731.
RefSeq	NP_005474.2. NM_005483.2.
UniGene	Hs.79018.
3D structure databases
ProteinModelPortal	Q13111.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31135N.
IntAct	Q13111. 18 interactions.
MINT	MINT-2806241.
STRING	9606.ENSP00000301280.
PTM databases
PhosphoSite	Q13111.
Polymorphism databases
DMDM	229462842.
Proteomic databases
PaxDb	Q13111.
PRIDE	Q13111.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301280; ENSP00000301280; ENSG00000167670.
GeneID	10036.
KEGG	hsa:10036.
UCSC	uc002mal.3. human.
Organism-specific databases
CTD	10036.
GeneCards	GC19P004353.
HGNC	HGNC:1910. CHAF1A.
HPA	CAB015186.
MIM	601246. gene.
neXtProt	NX_Q13111.
PharmGKB	PA26446.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG259938.
HOGENOM	HOG000111290.
HOVERGEN	HBG050779.
InParanoid	Q13111.
KO	K10750.
OMA	HMVLAPR.
OrthoDB	EOG4F4SB3.
Gene expression databases
Bgee	Q13111.
CleanEx	HS_CHAF1A.
Genevestigator	Q13111.
GermOnline	ENSG00000167670. Homo sapiens.
Family and domain databases
InterPro	IPR021644. CAF-1_p150. IPR022043. CAF1A. [Graphical view]
Pfam	PF11600. CAF-1_p150. 1 hit. PF12253. CAF1A. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10036.
NextBio	37903.
PMAP-CutDB	Q13111.
SOURCE	Search...

Entry information

Entry name

CAF1A_HUMAN

Accession

Primary (citable) accession number: Q13111
Secondary accession number(s): Q6NXG5, Q7Z7K3, Q9UJY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 5, 2009
Last modified:	May 29, 2013
This is version 127 of the entry and version 2 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.