Reviewed, UniProtKB/Swiss-Prot Q13111 (CAF1A_HUMAN)

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-Ip150
      Short name=hp150

Gene names

Name:	CHAF1A
Synonyms:	CAF, CAF1P150

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	956 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. The CCR4-NOT complex functions as general transcription regulation complex. 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.
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. 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. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B.
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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the CHAF1A family.
Sequence caution	The sequence AAH52620.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH52620.1 differs from that shown. Reason: Miscellaneous discrepancy. 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
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 Ref.4 Traceable author statement. Source: ProtInc cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Ref.4 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin assembly complex Ref.4 Traceable author statement. Source: ProtInc
Molecular function	chromatin binding Ref.4 Traceable author statement. Source: ProtInc unfolded protein binding Ref.4 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASF1B	Q9NVP2	1	EBI-1020839,EBI-1055650
CNOT6L	Q96LI5	1	EBI-1020839,EBI-1046635
FYN	P06241	1	EBI-1020839,EBI-515315
NCK1	P16333	1	EBI-1020839,EBI-389883
PCNA	P12004	1	EBI-1020839,EBI-358311
PIK3R1	P27986	1	EBI-1020839,EBI-79464
PLCG1	P19174	1	EBI-1020839,EBI-79387
ZNF408	Q9H9D4	1	EBI-1020839,EBI-347633

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
	Modified residue	141	1	Phosphoserine
	Modified residue	199	1	Phosphoserine
	Modified residue	203	1	Phosphoserine
	Modified residue	206	1	Phosphoserine Ref.19
	Modified residue	224	1	Phosphoserine
	Modified residue	255	1	Phosphoserine
	Modified residue	259	1	Phosphothreonine
	Modified residue	722	1	Phosphothreonine
	Modified residue	772	1	Phosphoserine
	Modified residue	775	1	Phosphoserine
	Modified residue	873	1	Phosphoserine
	Modified residue	951	1	Phosphoserine
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: dbSNP rs35651457.		VAR_055329
	Natural variant	239	1	M → V: dbSNP rs2230635.		VAR_055330
	Natural variant	850	1	K → R: dbSNP rs8100525.		VAR_055331
	Natural variant	923	1	A → V: dbSNP rs9352.		VAR_055332
	Natural variant	950	1	S → A: dbSNP rs243383.		VAR_055333
Experimental info
	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. 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. 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: 11250073] [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: 15057824] [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: 15489334] [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: 7600578] [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: 10052459] [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: 10648606] [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: 10893180] [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: 11296234] [Abstract] Cited for: HOMODIMER.
[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: 12837248] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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-141 AND SER-206, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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.
[15]	"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-65; SER-141 AND SER-772, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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-255; THR-259 AND SER-951, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"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-199; SER-203 AND SER-206, MASS SPECTROMETRY.
[18]	"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-65 AND SER-206, MASS SPECTROMETRY.
[19]	"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-224; THR-722; SER-772; SER-775; SER-873 AND SER-951, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.79018
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13111. 11 interactions.
PTM databases
PhosphoSite	Q13111.
Proteomic databases
PRIDE	Q13111.
Genome annotation databases
Ensembl	ENSG00000167670. Homo sapiens. [Contig view]
GeneID	10036.
KEGG	hsa:10036.
Organism-specific databases
GeneCards	GC19P004353.
H-InvDB	HIX0040076.
HGNC	HGNC:1910. CHAF1A.
HPA	CAB015186.
MIM	601246. gene.
PharmGKB	PA26446.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q13111.
Gene expression databases
ArrayExpress	Q13111.
Bgee	Q13111.
CleanEx	HS_CHAF1A.
GermOnline	ENSG00000167670. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)