STAG1

Last updated
STAG1
Identifiers
Aliases STAG1 , SA1, SCC3A, stromal antigen 1, MRD47
External IDs OMIM: 604358 MGI: 1098658 HomoloGene: 21191 GeneCards: STAG1
Orthologs
SpeciesHumanMouse
Entrez

10274

20842

Ensembl

ENSG00000118007

ENSMUSG00000037286

UniProt

Q8WVM7

Q9D3E6

RefSeq (mRNA)

NM_005862

NM_009282
NM_001357264
NM_001357265

RefSeq (protein)

NP_005853

NP_033308
NP_001344193
NP_001344194

Location (UCSC) Chr 3: 136.34 – 136.75 Mb Chr 9: 100.48 – 100.84 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cohesin subunit SA-1 (SA1) is a protein that in humans is encoded by the STAG1 gene. [5] [6] SA1 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. In somatic cells cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2 whereas in meiosis, cohesin is formed of SMC3, SMC1B, REC8 and SA3. There is a nonprofit community formed for those with a STAG1 Gene mutation at www.stag1gene.org.

Contents

Structure

Structure of SA2 (blue) and RAD21 (green) (PDB 4PK7) Structure of SA2 (blue) and RAD21 (green) (PDB 4PK7).png
Structure of SA2 (blue) and RAD21 (green) (PDB 4PK7)

SA1 is one of three human homologues of the yeast protein Scc3 which is a core subunit of the cohesin complex (the three human paralogues are SA1, SA2 and SA3). SA1 and SA2 are expressed in somatic cells whereas SA3 is the main SA paralogue in meiotic cells. In humans, SA2 has been shown to be more abundant than SA1; however, in other cell types, SA1 is the dominant form. [7]

SA1 stably binds to cohesin via the RAD21 subunit and functions as a platform for other regulatory subunits. The sequences of SA1 and SA2 are 75% conserved. They demonstrate a distinction between the N-terminal region and the C-terminal region. [8] SA1 has an evident AT-hook at the N-terminal region. [9]

Function

SA1 has roles in regulating both cohesin loading and release. [6] SA1 functions specifically in telomere cohesion. [10]

In mice, SA1 is required for embryonic development and has been shown to be lethal if not expressed. [11]

Related Research Articles

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

Separase, also known as separin, is a cysteine protease responsible for triggering anaphase by hydrolysing cohesin, which is the protein responsible for binding sister chromatids during the early stage of anaphase. In humans, separin is encoded by the ESPL1 gene.

SMC complexes represent a large family of ATPases that participate in many aspects of higher-order chromosome organization and dynamics. SMC stands for Structural Maintenance of Chromosomes.

<span class="mw-page-title-main">Cohesin</span> Protein complex that regulates the separation of sister chromatids during cell division

Cohesin is a protein complex that mediates sister chromatid cohesion, homologous recombination, and DNA looping. Cohesin is formed of SMC3, SMC1, SCC1 and SCC3. Cohesin holds sister chromatids together after DNA replication until anaphase when removal of cohesin leads to separation of sister chromatids. The complex forms a ring-like structure and it is believed that sister chromatids are held together by entrapment inside the cohesin ring. Cohesin is a member of the SMC family of protein complexes which includes Condensin, MukBEF and SMC-ScpAB.

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

Nipped-B-like protein (NIPBL), also known as SCC2 or delangin is a protein that in humans is encoded by the NIPBL gene. NIPBL is required for the association of cohesin with DNA and is the major subunit of the cohesin loading complex. Heterozygous mutations in NIPBL account for an estimated 60% of case of Cornelia de Lange Syndrome.

<span class="mw-page-title-main">SMC1A</span> Protein-coding gene in humans

Structural maintenance of chromosomes protein 1A (SMC1A) is a protein that in humans is encoded by the SMC1A gene. SMC1A is a subunit of the cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. In somatic cells, cohesin is formed of SMC1A, SMC3, RAD21 and either SA1 or SA2 whereas in meiosis, cohesin is formed of SMC3, SMC1B, REC8 and SA3.

<span class="mw-page-title-main">RAD21</span> Protein-coding gene in humans

Double-strand-break repair protein rad21 homolog is a protein that in humans is encoded by the RAD21 gene. RAD21, an essential gene, encodes a DNA double-strand break (DSB) repair protein that is evolutionarily conserved in all eukaryotes from budding yeast to humans. RAD21 protein is a structural component of the highly conserved cohesin complex consisting of RAD21, SMC1A, SMC3, and SCC3 [ STAG1 (SA1) and STAG2 (SA2) in multicellular organisms] proteins, involved in sister chromatid cohesion.

<span class="mw-page-title-main">SMC3</span> Protein-coding gene in humans

Structural maintenance of chromosomes protein 3 (SMC3) is a protein that in humans is encoded by the SMC3 gene. SMC3 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. In humans, SMC3 is present in all cohesin complexes whereas there are multiple paralogs for the other subunits.

<span class="mw-page-title-main">STAG2</span> Protein-coding gene in humans

Cohesin subunit SA-2 (SA2) is a protein that in humans is encoded by the STAG2 gene. SA2 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. In somatic cells cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2 whereas in meiosis, cohesin is formed of SMC3, SMC1B, REC8 and SA3.

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

Wings apart-like protein homolog (WAPL) is a protein that in humans is encoded by the WAPAL gene. WAPL is a key regulator of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. Cohesin has a ring-like arrangement and it is thought that it associates with the chromosome by entrapping it whether as a loop of DNA, a single strand or a pair of sister chromosomes. WAPL forms a complex with PDS5A or PDS5B and releases cohesin from DNA by opening the interface between SMC3 and RAD21.

<span class="mw-page-title-main">Shugoshin 1</span> Protein-coding gene in the species Homo sapiens

Shugoshin 1 or Shugoshin-like 1, is a protein that in humans is encoded by the SGO1 gene.

<span class="mw-page-title-main">SMC6</span> Protein-coding gene in the species Homo sapiens

Structural maintenance of chromosomes protein 6 is a protein that in humans is encoded by the SMC6 gene.

<span class="mw-page-title-main">Shugoshin 2</span> Protein-coding gene in the species Homo sapiens

Shugoshin 2(Shugoshin-2), also known as Shugoshin-like 2, is a protein which in humans is encoded by the SGO2 gene.

<span class="mw-page-title-main">PDS5B</span> Protein-coding gene in the species Homo sapiens

Sister chromatid cohesion protein PDS5 homolog B(PDS5B) is a protein that in humans is encoded by the PDS5B gene. It is a regulatory subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. The core cohesin complex is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. PDS5 associates with WAPL to stimulate the release of cohesin from DNA but during DNA replication PDS5 promotes acetylation of SMC3 by ESCO1 and ESCO2.

<span class="mw-page-title-main">SMC5</span> Protein-coding gene in the species Homo sapiens

Structural maintenance of chromosomes protein 5 is a protein encoded by the SMC5 gene in human.

<span class="mw-page-title-main">PDS5A</span> Protein-coding gene in the species Homo sapiens

Sister chromatid cohesion protein PDS5 homolog A is a protein that in humans is encoded by the PDS5A gene.

<span class="mw-page-title-main">REC8</span> Protein-coding gene in the species Homo sapiens

Meiotic recombination protein REC8 homolog is a protein that in humans is encoded by the REC8 gene.

Sister chromatid cohesion refers to the process by which sister chromatids are paired and held together during certain phases of the cell cycle. Establishment of sister chromatid cohesion is the process by which chromatin-associated cohesin protein becomes competent to physically bind together the sister chromatids. In general, cohesion is established during S phase as DNA is replicated, and is lost when chromosomes segregate during mitosis and meiosis. Some studies have suggested that cohesion aids in aligning the kinetochores during mitosis by forcing the kinetochores to face opposite cell poles.

<span class="mw-page-title-main">NCAPH2</span> Protein-coding gene in the species Homo sapiens

Condensin-2 complex subunit H2, also known as chromosome-associated protein H2 (CAP-H2) or non-SMC condensin II complex subunit H2 (NCAPH2), is a protein that in humans is encoded by the NCAPH2 gene. CAP-H2 is a subunit of condensin II, a large protein complex involved in chromosome condensation.

<span class="mw-page-title-main">SMC1B</span> Protein-coding gene in the species Homo sapiens

Structural maintenance of chromosomes protein 1B (SMC-1B) is a protein that in humans is encoded by the SMC1B gene. SMC proteins engage in chromosome organization and can be broken into 3 groups based on function which are cohesins, condensins, and DNA repair.SMC-1B belongs to a family of proteins required for chromatid cohesion and DNA recombination during meiosis and mitosis. SMC1ß protein appears to participate with other cohesins REC8, STAG3 and SMC3 in sister-chromatid cohesion throughout the whole meiotic process in human oocytes.

<span class="mw-page-title-main">STAG3 (gene)</span> Protein-coding gene in the species Homo sapiens

Stromal antigen 3 is a protein that in humans is encoded by the STAG3 gene. STAG3 protein is a component of a cohesin complex that regulates the separation of sister chromatids specifically during meiosis. STAG3 appears to be paramount in sister-chromatid cohesion throughout the meiotic process in human oocytes and spermatocytes.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000118007 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000037286 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Carramolino L, Lee BC, Zaballos A, Peled A, Barthelemy I, Shav-Tal Y, et al. (August 1997). "SA-1, a nuclear protein encoded by one member of a novel gene family: molecular cloning and detection in hemopoietic organs". Gene. 195 (2): 151–159. doi:10.1016/S0378-1119(97)00121-2. PMID   9305759.
  6. 1 2 "Entrez Gene: STAG1 stromal antigen 1".
  7. ↑ Cuadrado A, Losada A (April 2020). "Specialized functions of cohesins STAG1 and STAG2 in 3D genome architecture". Current Opinion in Genetics & Development. Genome Architecture and Expression. 61: 9–16. doi:10.1016/j.gde.2020.02.024. PMID   32294612.
  8. ↑ Arruda NL, Carico ZM, Justice M, Liu YF, Zhou J, Stefan HC, Dowen JM (August 2020). "Distinct and overlapping roles of STAG1 and STAG2 in cohesin localization and gene expression in embryonic stem cells". Epigenetics & Chromatin. 13 (1): 32. doi:10.1186/s13072-020-00353-9. PMC   7418333 . PMID   32778134.
  9. ↑ Lin J, Countryman P, Chen H, Pan H, Fan Y, Jiang Y, et al. (July 2016). "Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing". Nucleic Acids Research. 44 (13): 6363–6376. doi:10.1093/nar/gkw518. PMC   5291270 . PMID   27298259.
  10. ↑ Canudas S, Smith S (October 2009). "Differential regulation of telomere and centromere cohesion by the Scc3 homologues SA1 and SA2, respectively, in human cells". The Journal of Cell Biology. 187 (2): 165–173. doi:10.1083/jcb.200903096. PMC   2768842 . PMID   19822671.
  11. ↑ Remeseiro S, Cuadrado A, Gómez-López G, Pisano DG, Losada A (May 2012). "A unique role of cohesin-SA1 in gene regulation and development". The EMBO Journal. 31 (9): 2090–2102. doi:10.1038/emboj.2012.60. PMC   3343463 . PMID   22415368.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.