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Q13111 (CAF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Short name=CAF-I 150 kDa subunit
Short name=CAF-I p150
Short name=hp150
Gene names
Name:CHAF1A
Synonyms:CAF, CAF1P150
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length956 AA.
Sequence statusComplete.
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. 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 processCell cycle
DNA damage
DNA repair
DNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

chromatin assembly

Inferred from direct assay PubMed 8858152. Source: UniProtKB

protein complex assembly

Traceable author statement Ref.4. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCAF-1 complex

Inferred from direct assay PubMed 8858152. Source: UniProtKB

WINAC complex

Inferred from direct assay Ref.9. Source: BHF-UCL

   Molecular_functionchromatin binding

Traceable author statement Ref.4. Source: ProtInc

chromo shadow domain binding

Inferred from physical interaction Ref.12. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 16826239. Source: IntAct

unfolded protein binding

Traceable author statement Ref.4. Source: ProtInc

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 956956Chromatin assembly factor 1 subunit A
PRO_0000089276

Regions

Region1 – 314314Binds to CBX1 chromo shadow domain
Region1 – 4949Binds to PCNA
Region642 – 67837Necessary for homodimerization and competence for chromatin assembly
Region660 – 956297Binds to p60
Motif233 – 24614PxVxL motif
Compositional bias323 – 453131Arg/Glu/Lys-rich
Compositional bias602 – 6087Poly-Glu
Compositional bias619 – 6235Poly-Asp
Compositional bias905 – 9117Poly-Glu

Amino acid modifications

Modified residue651Phosphoserine Ref.14 Ref.19
Modified residue1231Phosphoserine Ref.18
Modified residue1381Phosphoserine Ref.18
Modified residue1411Phosphoserine Ref.18 Ref.19
Modified residue1431Phosphoserine Ref.18 Ref.19
Modified residue2061Phosphoserine Ref.19
Modified residue2241Phosphoserine Ref.15 Ref.18
Modified residue3101Phosphoserine Ref.19
Modified residue7221Phosphothreonine Ref.15 Ref.18 Ref.19
Modified residue7721Phosphoserine Ref.15 Ref.18 Ref.19
Modified residue7751Phosphoserine Ref.15 Ref.19
Modified residue8651Phosphothreonine Ref.18
Modified residue8731Phosphoserine Ref.15 Ref.18
Modified residue9511Phosphoserine Ref.15 Ref.18 Ref.19

Natural variations

Alternative sequence710 – 74940CFLET…GNVNG → HWVHPESRGDVCRTLRVSSP QSRYLNRLNSCVKSTLSCFT in isoform 2.
VSP_004149
Alternative sequence750 – 956207Missing in isoform 2.
VSP_004150
Alternative sequence772 – 944173Missing in isoform 3.
VSP_004151
Natural variant1671D → V.
Corresponds to variant rs35651457 [ dbSNP | Ensembl ].
VAR_055329
Natural variant2391M → V.
Corresponds to variant rs2230635 [ dbSNP | Ensembl ].
VAR_055330
Natural variant8501K → R.
Corresponds to variant rs8100525 [ dbSNP | Ensembl ].
VAR_055331
Natural variant9231A → V. Ref.1 Ref.4
Corresponds to variant rs9352 [ dbSNP | Ensembl ].
VAR_055332
Natural variant9501S → A. Ref.1 Ref.3 Ref.4 Ref.15 Ref.18 Ref.19 Ref.20
Corresponds to variant rs243383 [ dbSNP | Ensembl ].
VAR_055333

Experimental info

Mutagenesis2401V → E: Abolishes interaction with CBX5; when associated with E-242. Ref.17
Mutagenesis2421L → E: Abolishes interaction with CBX5; when associated with E-240. Ref.17
Sequence conflict7751S → T in AAA76736. Ref.4

Sequences

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

Last modified May 5, 2009. Version 2.
Checksum: 90617F8FE8DB67B0

FASTA956106,926
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A7176E2D8D18CA0F
Show »

FASTA74984,685
Isoform 3 [UniParc].

Checksum: 44E39E1CCE192850
Show »

FASTA78388,285

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRA56731.
RefSeqNP_005474.2. NM_005483.2.
UniGeneHs.79018.

3D structure databases

ProteinModelPortalQ13111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115349. 65 interactions.
DIPDIP-31135N.
IntActQ13111. 32 interactions.
MINTMINT-2806241.
STRING9606.ENSP00000301280.

PTM databases

PhosphoSiteQ13111.

Polymorphism databases

DMDM229462842.

Proteomic databases

PaxDbQ13111.
PRIDEQ13111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301280; ENSP00000301280; ENSG00000167670. [Q13111-1]
GeneID10036.
KEGGhsa:10036.
UCSCuc002mal.3. human. [Q13111-1]

Organism-specific databases

CTD10036.
GeneCardsGC19P004402.
HGNCHGNC:1910. CHAF1A.
HPACAB015186.
MIM601246. gene.
neXtProtNX_Q13111.
PharmGKBPA26446.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259938.
HOGENOMHOG000111290.
HOVERGENHBG050779.
InParanoidQ13111.
KOK10750.
OMAHMVLAPR.
OrthoDBEOG76X60P.
PhylomeDBQ13111.
TreeFamTF350377.

Gene expression databases

ArrayExpressQ13111.
BgeeQ13111.
CleanExHS_CHAF1A.
GenevestigatorQ13111.

Family and domain databases

InterProIPR022043. CAF1A.
[Graphical view]
PfamPF12253. CAF1A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCHAF1A.
GenomeRNAi10036.
NextBio37903.
PMAP-CutDBQ13111.
PROQ13111.
SOURCESearch...

Entry information

Entry nameCAF1A_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

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