Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13111

- CAF1A_HUMAN

UniProt

Q13111 - CAF1A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Chromatin assembly factor 1 subunit A

Gene

CHAF1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  1. chromatin binding Source: ProtInc
  2. chromo shadow domain binding Source: BHF-UCL
  3. identical protein binding Source: IntAct
  4. unfolded protein binding Source: ProtInc

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. chromatin assembly Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. DNA replication Source: UniProtKB-KW
  5. DNA replication-dependent nucleosome assembly Source: UniProt
  6. protein complex assembly Source: ProtInc
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

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 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 namesi
Name:CHAF1A
Synonyms:CAF, CAF1P150
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1910. CHAF1A.

Subcellular locationi

Nucleus 1 Publication
Note: DNA replication foci.

GO - Cellular componenti

  1. CAF-1 complex Source: UniProtKB
  2. nuclear chromatin Source: UniProt
  3. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi240 – 2401V → E: Abolishes interaction with CBX5; when associated with E-242. 1 Publication
Mutagenesisi242 – 2421L → E: Abolishes interaction with CBX5; when associated with E-240. 1 Publication

Organism-specific databases

PharmGKBiPA26446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 956956Chromatin assembly factor 1 subunit APRO_0000089276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine2 Publications
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei141 – 1411Phosphoserine2 Publications
Modified residuei143 – 1431Phosphoserine2 Publications
Modified residuei206 – 2061Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine2 Publications
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei722 – 7221Phosphothreonine3 Publications
Modified residuei772 – 7721Phosphoserine3 Publications
Modified residuei775 – 7751Phosphoserine2 Publications
Modified residuei865 – 8651Phosphothreonine1 Publication
Modified residuei873 – 8731Phosphoserine2 Publications
Modified residuei951 – 9511Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13111.
PaxDbiQ13111.
PRIDEiQ13111.

PTM databases

PhosphoSiteiQ13111.

Miscellaneous databases

PMAP-CutDBQ13111.

Expressioni

Developmental stagei

Active complex is found in G1, S and G2 phases.

Gene expression databases

BgeeiQ13111.
CleanExiHS_CHAF1A.
ExpressionAtlasiQ13111. baseline and differential.
GenevestigatoriQ13111.

Organism-specific databases

HPAiCAB015186.

Interactioni

Subunit structurei

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 CBX5.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1020839,EBI-1020839
CBX5P459737EBI-1020839,EBI-78219
GFI1Q996844EBI-1020839,EBI-949368
MBD1Q9UIS93EBI-1020839,EBI-867196
NCK1P163332EBI-1020839,EBI-389883
PCNAP120043EBI-1020839,EBI-358311

Protein-protein interaction databases

BioGridi115349. 66 interactions.
DIPiDIP-31135N.
IntActiQ13111. 32 interactions.
MINTiMINT-2806241.
STRINGi9606.ENSP00000301280.

Structurei

3D structure databases

ProteinModelPortaliQ13111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 314314Binds to CBX1 chromo shadow domainAdd
BLAST
Regioni1 – 4949Binds to PCNAAdd
BLAST
Regioni642 – 67837Necessary for homodimerization and competence for chromatin assemblyAdd
BLAST
Regioni660 – 956297Binds to p60Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi233 – 24614PxVxL motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi323 – 453131Arg/Glu/Lys-richAdd
BLAST
Compositional biasi602 – 6087Poly-Glu
Compositional biasi619 – 6235Poly-Asp
Compositional biasi905 – 9117Poly-Glu

Domaini

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 similaritiesi

Belongs to the CHAF1A family.Curated

Phylogenomic databases

eggNOGiNOG259938.
GeneTreeiENSGT00440000034888.
HOGENOMiHOG000111290.
HOVERGENiHBG050779.
InParanoidiQ13111.
KOiK10750.
OMAiHMVLAPR.
OrthoDBiEOG76X60P.
PhylomeDBiQ13111.
TreeFamiTF350377.

Family and domain databases

InterProiIPR029105. CAF1-p150_C2.
IPR029091. CAF1-p150_N.
IPR022043. CAF1A.
[Graphical view]
PfamiPF15539. CAF1-p150_C2. 1 hit.
PF15557. CAF1-p150_N. 1 hit.
PF12253. CAF1A. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q13111-1) [UniParc]FASTAAdd to Basket

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.

« Hide

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

SPLGAS
Length:956
Mass (Da):106,926
Last modified:May 5, 2009 - v2
Checksum:i90617F8FE8DB67B0
GO
Isoform 2 (identifier: Q13111-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     710-749: CFLETLPAQE...LPLLHGNVNG → HWVHPESRGD...CVKSTLSCFT
     750-956: Missing.

Show »
Length:749
Mass (Da):84,685
Checksum:iA7176E2D8D18CA0F
GO
Isoform 3 (identifier: Q13111-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:783
Mass (Da):88,285
Checksum:i44E39E1CCE192850
GO

Sequence cautioni

The sequence AAA76736.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF04291.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH52620.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 426.Curated
The sequence AAH52620.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti775 – 7751S → T in AAA76736. (PubMed:7600578)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671D → V.
Corresponds to variant rs35651457 [ dbSNP | Ensembl ].
VAR_055329
Natural varianti239 – 2391M → V.
Corresponds to variant rs2230635 [ dbSNP | Ensembl ].
VAR_055330
Natural varianti850 – 8501K → R.
Corresponds to variant rs8100525 [ dbSNP | Ensembl ].
VAR_055331
Natural varianti923 – 9231A → V.2 Publications
Corresponds to variant rs9352 [ dbSNP | Ensembl ].
VAR_055332
Natural varianti950 – 9501S → A.7 Publications
Corresponds to variant rs243383 [ dbSNP | Ensembl ].
VAR_055333

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei710 – 74940CFLET…GNVNG → HWVHPESRGDVCRTLRVSSP QSRYLNRLNSCVKSTLSCFT in isoform 2. CuratedVSP_004149Add
BLAST
Alternative sequencei750 – 956207Missing in isoform 2. CuratedVSP_004150Add
BLAST
Alternative sequencei772 – 944173Missing in isoform 3. CuratedVSP_004151Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32875.1. [Q13111-1]
PIRiA56731.
RefSeqiNP_005474.2. NM_005483.2.
UniGeneiHs.79018.

Genome annotation databases

EnsembliENST00000301280; ENSP00000301280; ENSG00000167670.
GeneIDi10036.
KEGGihsa:10036.
UCSCiuc002mal.3. human. [Q13111-1]

Polymorphism databases

DMDMi229462842.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS32875.1. [Q13111-1 ]
PIRi A56731.
RefSeqi NP_005474.2. NM_005483.2.
UniGenei Hs.79018.

3D structure databases

ProteinModelPortali Q13111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115349. 66 interactions.
DIPi DIP-31135N.
IntActi Q13111. 32 interactions.
MINTi MINT-2806241.
STRINGi 9606.ENSP00000301280.

PTM databases

PhosphoSitei Q13111.

Polymorphism databases

DMDMi 229462842.

Proteomic databases

MaxQBi Q13111.
PaxDbi Q13111.
PRIDEi Q13111.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301280 ; ENSP00000301280 ; ENSG00000167670 .
GeneIDi 10036.
KEGGi hsa:10036.
UCSCi uc002mal.3. human. [Q13111-1 ]

Organism-specific databases

CTDi 10036.
GeneCardsi GC19P004402.
HGNCi HGNC:1910. CHAF1A.
HPAi CAB015186.
MIMi 601246. gene.
neXtProti NX_Q13111.
PharmGKBi PA26446.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259938.
GeneTreei ENSGT00440000034888.
HOGENOMi HOG000111290.
HOVERGENi HBG050779.
InParanoidi Q13111.
KOi K10750.
OMAi HMVLAPR.
OrthoDBi EOG76X60P.
PhylomeDBi Q13111.
TreeFami TF350377.

Miscellaneous databases

GeneWikii CHAF1A.
GenomeRNAii 10036.
NextBioi 37903.
PMAP-CutDB Q13111.
PROi Q13111.
SOURCEi Search...

Gene expression databases

Bgeei Q13111.
CleanExi HS_CHAF1A.
ExpressionAtlasi Q13111. baseline and differential.
Genevestigatori Q13111.

Family and domain databases

InterProi IPR029105. CAF1-p150_C2.
IPR029091. CAF1-p150_N.
IPR022043. CAF1A.
[Graphical view ]
Pfami PF15539. CAF1-p150_C2. 1 hit.
PF15557. CAF1-p150_N. 1 hit.
PF12253. CAF1A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. 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].

Entry informationi

Entry nameiCAF1A_HUMAN
AccessioniPrimary (citable) accession number: Q13111
Secondary accession number(s): Q6NXG5, Q7Z7K3, Q9UJY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3