BRCT domain

Last updated
BRCA1 C Terminus (BRCT) domain
PDB 1cdz EBI.jpg
Structure of an XRCC1 BRCT domain. [1]
Identifiers
SymbolBRCT
Pfam PF00533
InterPro IPR001357
SCOP2 1cdz / SCOPe / SUPFAM
CDD cd00027
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 2azm B:1906-1957 2ado B:1906-1957 2etx A:1906-1957

1kzy C:1795-1835 1l0b A:1589-1669 1t2v C:1646-1723 1n5o X:1646-1723 1t2u A:1646-1723 1jnx X:1646-1723 1t15 A:1646-1723 1t29 A:1646-1723 1y98 A:1646-1723 2cou A:91-166 1l7b A:589-664 2cok A:385-463 1wf6 A:354-431 1ik9 C:681-717 1cdz A:538-616

Contents

1oqa A:1756-1842 2coe A:27-111

BRCA1 C Terminus (BRCT) domain is a family of evolutionarily related proteins. It is named after the C-terminal domain of BRCA1, a DNA-repair protein that serves as a marker of breast cancer susceptibility.

The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage, [2] for example as found in the breast cancer DNA-repair protein BRCA1. The domain is an approximately 100 amino acid tandem repeat, which appears to act as a phospho-protein binding domain. [3]

Examples

Human proteins containing this domain include:

Related Research Articles

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The SRC Homology 3 Domain is a small protein domain of about 60 amino acid residues. Initially, SH3 was described as a conserved sequence in the viral adaptor protein v-Crk. This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25. SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. The SH3 proteins interact with adaptor proteins and tyrosine kinases. Interacting with tyrosine kinases, SH3 proteins usually bind far away from the active site. Approximately 300 SH3 domains are found in proteins encoded in the human genome. In addition to that, the SH3 domain was responsible for controlling protein-protein interactions in the signal transduction pathways and regulating the interactions of proteins involved in the cytoplasmic signaling.

<span class="mw-page-title-main">BRCA1</span> Gene known for its role in breast cancer

Breast cancer type 1 susceptibility protein is a protein that in humans is encoded by the BRCA1 gene. Orthologs are common in other vertebrate species, whereas invertebrate genomes may encode a more distantly related gene. BRCA1 is a human tumor suppressor gene and is responsible for repairing DNA.

<span class="mw-page-title-main">BRCA2</span> Gene known for its role in breast cancer

BRCA2 and BRCA2 are human genes and their protein products, respectively. The official symbol and the official name are maintained by the HUGO Gene Nomenclature Committee. One alternative symbol, FANCD1, recognizes its association with the FANC protein complex. Orthologs, styled Brca2 and Brca2, are common in other vertebrate species. BRCA2 is a human tumor suppressor gene, found in all humans; its protein, also called by the synonym breast cancer type 2 susceptibility protein, is responsible for repairing DNA.

<span class="mw-page-title-main">14-3-3 protein</span> Family of conserved regulatory molecules

14-3-3 proteins are a family of conserved regulatory molecules that are expressed in all eukaryotic cells. 14-3-3 proteins have the ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors. More than 200 signaling proteins have been reported as 14-3-3 ligands.

<span class="mw-page-title-main">Poly (ADP-ribose) polymerase</span> Family of proteins

Poly (ADP-ribose) polymerase (PARP) is a family of proteins involved in a number of cellular processes such as DNA repair, genomic stability, and programmed cell death.

<span class="mw-page-title-main">ATM serine/threonine kinase</span> Mammalian protein found in Homo sapiens

ATM serine/threonine kinase or Ataxia-telangiectasia mutated, symbol ATM, is a serine/threonine protein kinase that is recruited and activated by DNA double-strand breaks, oxidative stress, topoisomerase cleavage complexes, splicing intermediates, R-loops and in some cases by single-strand DNA breaks. It phosphorylates several key proteins that initiate activation of the DNA damage checkpoint, leading to cell cycle arrest, DNA repair or apoptosis. Several of these targets, including p53, CHK2, BRCA1, NBS1 and H2AX are tumor suppressors.

<span class="mw-page-title-main">CHEK2</span> Protein-coding gene in humans

CHEK2 is a tumor suppressor gene that encodes the protein CHK2, a serine-threonine kinase. CHK2 is involved in DNA repair, cell cycle arrest or apoptosis in response to DNA damage. Mutations to the CHEK2 gene have been linked to a wide range of cancers.

<span class="mw-page-title-main">MRE11A</span> Protein-coding gene in the species Homo sapiens

Double-strand break repair protein MRE11 is an enzyme that in humans is encoded by the MRE11 gene. The gene has been designated MRE11A to distinguish it from the pseudogene MRE11B that is nowadays named MRE11P1.

<span class="mw-page-title-main">BARD1</span> Protein-coding gene in the species Homo sapiens

BRCA1-associated RING domain protein 1 is a protein that in humans is encoded by the BARD1 gene. The human BARD1 protein is 777 amino acids long and contains a RING finger domain, four ankyrin repeats, and two tandem BRCT domains.

<span class="mw-page-title-main">RAD9A</span> Protein-coding gene in the species Homo sapiens

Cell cycle checkpoint control protein RAD9A is a protein that in humans is encoded by the RAD9A gene.Rad9 has been shown to induce G2 arrest in the cell cycle in response to DNA damage in yeast cells. Rad9 was originally found in budding yeast cells but a human homolog has also been found and studies have suggested that the molecular mechanisms of the S and G2 checkpoints are conserved in eukaryotes. Thus, what is found in yeast cells are likely to be similar in human cells.

<span class="mw-page-title-main">TP53BP1</span> Protein-coding gene in the species Homo sapiens

Tumor suppressor p53-binding protein 1 also known as p53-binding protein 1 or 53BP1 is a protein that in humans is encoded by the TP53BP1 gene.

<span class="mw-page-title-main">TOPBP1</span> Protein-coding gene in the species Homo sapiens

DNA topoisomerase 2-binding protein 1 (TOPBP1) is a scaffold protein that in humans is encoded by the TOPBP1 gene.

<span class="mw-page-title-main">MDC1</span> Protein-coding gene in the species Homo sapiens

Mediator of DNA damage checkpoint protein 1 is a 2080 amino acid long protein that in humans is encoded by the MDC1 gene located on the short arm (p) of chromosome 6. MDC1 protein is a regulator of the Intra-S phase and the G2/M cell cycle checkpoints and recruits repair proteins to the site of DNA damage. It is involved in determining cell survival fate in association with tumor suppressor protein p53. This protein also goes by the name Nuclear Factor with BRCT Domain 1 (NFBD1).

<span class="mw-page-title-main">RBBP8</span> Protein-coding gene in the species Homo sapiens

Retinoblastoma-binding protein 8 is a protein that in humans is encoded by the RBBP8 gene.

<span class="mw-page-title-main">BRIP1</span> Mammalian protein found in Homo sapiens

Fanconi anemia group J protein is a protein that in humans is encoded by the BRCA1-interacting protein 1 (BRIP1) gene.

<span class="mw-page-title-main">WD40 repeat</span> Short protein motif that forms a solenoid domain

The WD40 repeat is a short structural motif of approximately 40 amino acids, often terminating in a tryptophan-aspartic acid (W-D) dipeptide. Tandem copies of these repeats typically fold together to form a type of circular solenoid protein domain called the WD40 domain.

<span class="mw-page-title-main">Forkhead-associated domain</span>

In molecular biology, the forkhead-associated domain is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich, which sometimes contains small helical insertions between the loops connecting the strands.

<span class="mw-page-title-main">HORMA domain</span>

In molecular biology, the HORMA domain is a protein domain that has been suggested to recognise chromatin states resulting from DNA adducts, double stranded breaks or non-attachment to the spindle and act as an adaptor that recruits other proteins. Hop1 is a meiosis-specific protein, Rev7 is required for DNA damage induced mutagenesis, and MAD2 is a spindle checkpoint protein which prevents progression of the cell cycle upon detection of a defect in mitotic spindle integrity.

<span class="mw-page-title-main">DNA ligase 3</span> Protein-coding gene in the species Homo sapiens

DNA ligase 3 also DNA ligase III, is an enzyme that, in humans, is encoded by the LIG3 gene. LIG3 encodes ATP-dependent DNA ligases that seal interruptions in the phosphodiester backbone of duplex DNA.

<span class="mw-page-title-main">Solenoid protein domain</span>

Solenoid protein domains are a highly modular type of protein domain. They consist of a chain of nearly identical folds, often simply called tandem repeats. They are extremely common among all types of proteins, though exact figures are unknown.

References

  1. Zhang X, Moréra S, Bates PA, et al. (November 1998). "Structure of an XRCC1 BRCT domain: a new protein-protein interaction module". EMBO J. 17 (21): 6404–11. doi:10.1093/emboj/17.21.6404. PMC   1170965 . PMID   9799248.
  2. Bork P, Hofmann K, Koonin EV, Bucher P, Neuwald AF, Altschul SF (1997). "A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins". FASEB J. 11 (1): 68–76. doi: 10.1096/fasebj.11.1.9034168 . PMID   9034168. S2CID   16457619.
  3. Yu X, Chini CC, He M, Mer G, Chen J (2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID   14576433. S2CID   29407635.
This article incorporates text from the public domain Pfam and InterPro: IPR001357