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Protein

Chromatin accessibility complex protein 1

Gene

CHRAC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1.

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • DNA-directed DNA polymerase activity Source: UniProtKB

GO - Biological processi

  • chromatin remodeling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin accessibility complex protein 1
Short name:
CHRAC-1
Alternative name(s):
Chromatin accessibility complex 15 kDa protein
Short name:
CHRAC-15
Short name:
HuCHRAC15
DNA polymerase epsilon subunit p15
Gene namesi
Name:CHRAC1
Synonyms:CHRAC15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:13544. CHRAC1.

Subcellular locationi

GO - Cellular componenti

  • CHRAC Source: UniProtKB
  • epsilon DNA polymerase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26481.

Polymorphism and mutation databases

BioMutaiCHRAC1.
DMDMi22653683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 131130Chromatin accessibility complex protein 1PRO_0000089656Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei102 – 1021N6-acetyllysineCombined sources
Modified residuei124 – 1241PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NRG0.
MaxQBiQ9NRG0.
PaxDbiQ9NRG0.
PeptideAtlasiQ9NRG0.
PRIDEiQ9NRG0.
TopDownProteomicsiQ9NRG0.

PTM databases

iPTMnetiQ9NRG0.
PhosphoSiteiQ9NRG0.

Expressioni

Tissue specificityi

Expressed in all tissues tested, including, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiQ9NRG0.
CleanExiHS_CHRAC1.
ExpressionAtlasiQ9NRG0. baseline and differential.
GenevisibleiQ9NRG0. HS.

Interactioni

Subunit structurei

Interacts with POLE3. Together with POLE3, ACF1 and ISWI/SNF2H proteins, it forms the ISWI chromatin-remodeling complex, CHRAC.

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-2795492,EBI-10175124
POLE3Q9NRF96EBI-2795492,EBI-744901

Protein-protein interaction databases

BioGridi119904. 30 interactions.
IntActiQ9NRG0. 2 interactions.
STRINGi9606.ENSP00000220913.

Structurei

3D structure databases

ProteinModelPortaliQ9NRG0.
SMRiQ9NRG0. Positions 28-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili100 – 12425Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1657. Eukaryota.
COG5208. LUCA.
GeneTreeiENSGT00510000048543.
HOGENOMiHOG000068045.
HOVERGENiHBG050946.
InParanoidiQ9NRG0.
KOiK11656.
OMAiKIRVHEF.
OrthoDBiEOG7RJPTD.
PhylomeDBiQ9NRG0.
TreeFamiTF350392.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR033048. CHRAC1.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR10252:SF47. PTHR10252:SF47. 1 hit.
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NRG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVVVGKDK GGEQRLISLP LSRIRVIMKS SPEVSSINQE ALVLTAKATE
60 70 80 90 100
LFVQCLATYS YRHGSGKEKK VLTYSDLANT AQQSETFQFL ADILPKKILA
110 120 130
SKYLKMLKEE KREEDEENDN DNESDHDEAD S
Length:131
Mass (Da):14,711
Last modified:October 1, 2000 - v1
Checksum:iBC58A99CF58ACF74
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551C → Y.
Corresponds to variant rs2231522 [ dbSNP | Ensembl ].
VAR_013755
Natural varianti126 – 1261H → R.
Corresponds to variant rs2231524 [ dbSNP | Ensembl ].
VAR_013756

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226076 mRNA. Translation: AAF72416.1.
AK023537 mRNA. Translation: BAB14601.1.
BC015891 mRNA. Translation: AAH15891.1.
CCDSiCCDS6379.1.
RefSeqiNP_059140.1. NM_017444.5.
UniGeneiHs.279704.

Genome annotation databases

EnsembliENST00000220913; ENSP00000220913; ENSG00000104472.
GeneIDi54108.
KEGGihsa:54108.
UCSCiuc003yvl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226076 mRNA. Translation: AAF72416.1.
AK023537 mRNA. Translation: BAB14601.1.
BC015891 mRNA. Translation: AAH15891.1.
CCDSiCCDS6379.1.
RefSeqiNP_059140.1. NM_017444.5.
UniGeneiHs.279704.

3D structure databases

ProteinModelPortaliQ9NRG0.
SMRiQ9NRG0. Positions 28-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119904. 30 interactions.
IntActiQ9NRG0. 2 interactions.
STRINGi9606.ENSP00000220913.

PTM databases

iPTMnetiQ9NRG0.
PhosphoSiteiQ9NRG0.

Polymorphism and mutation databases

BioMutaiCHRAC1.
DMDMi22653683.

Proteomic databases

EPDiQ9NRG0.
MaxQBiQ9NRG0.
PaxDbiQ9NRG0.
PeptideAtlasiQ9NRG0.
PRIDEiQ9NRG0.
TopDownProteomicsiQ9NRG0.

Protocols and materials databases

DNASUi54108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220913; ENSP00000220913; ENSG00000104472.
GeneIDi54108.
KEGGihsa:54108.
UCSCiuc003yvl.4. human.

Organism-specific databases

CTDi54108.
GeneCardsiCHRAC1.
HGNCiHGNC:13544. CHRAC1.
MIMi607268. gene.
neXtProtiNX_Q9NRG0.
PharmGKBiPA26481.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1657. Eukaryota.
COG5208. LUCA.
GeneTreeiENSGT00510000048543.
HOGENOMiHOG000068045.
HOVERGENiHBG050946.
InParanoidiQ9NRG0.
KOiK11656.
OMAiKIRVHEF.
OrthoDBiEOG7RJPTD.
PhylomeDBiQ9NRG0.
TreeFamiTF350392.

Miscellaneous databases

ChiTaRSiCHRAC1. human.
GenomeRNAii54108.
PROiQ9NRG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRG0.
CleanExiHS_CHRAC1.
ExpressionAtlasiQ9NRG0. baseline and differential.
GenevisibleiQ9NRG0. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR033048. CHRAC1.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR10252:SF47. PTHR10252:SF47. 1 hit.
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins."
    Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V., Becker P.B., Bickmore W.A., Varga-Weisz P.D.
    EMBO J. 19:3377-3387(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  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].
    Tissue: Uterus.
  4. "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.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHRC1_HUMAN
AccessioniPrimary (citable) accession number: Q9NRG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 127 of the entry and version 1 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 8
    Human chromosome 8: 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

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.