RCC1

Last updated
RCC1
Protein RCC1 PDB 1a12.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RCC1 , CHC1, RCC1-I, SNHG3-regulator of chromosome condensation 1
External IDs OMIM: 179710 MGI: 1913989 HomoloGene: 55567 GeneCards: RCC1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001197082
NM_133878

RefSeq (protein)

NP_001184011
NP_598639

Location (UCSC) Chr 1: 28.51 – 28.54 Mb Chr 4: 132.06 – 132.08 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Regulator of chromosome condensation 1, also known as RCC1, Ran guanine nucleotide exchange factor and RanGEF, is the name for a human gene and protein. [5]

Contents

RCC1 also functions as a guanine nucleotide exchange factor for Ran GTPase.

Interactions

RCC1 has been shown to interact with RANBP3 [6] [7] and Ran (biology). [8] [9] [10] [11]

Related Research Articles

<span class="mw-page-title-main">Ran (protein)</span> GTPase functioning in nuclear transport

Ran also known as GTP-binding nuclear protein Ran is a protein that in humans is encoded by the RAN gene. Ran is a small 25 kDa protein that is involved in transport into and out of the cell nucleus during interphase and also involved in mitosis. It is a member of the Ras superfamily.

<span class="mw-page-title-main">Guanine nucleotide exchange factor</span> Proteins which remove GDP from GTPases

Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP). A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase.

<span class="mw-page-title-main">RANBP2</span> Protein-coding gene in the species Homo sapiens

RAN binding protein 2 (RANBP2) is protein which in humans is encoded by the RANBP2 gene. It is also known as nucleoporin 358 (Nup358) since it is a member nucleoporin family that makes up the nuclear pore complex. RanBP2 has a mass of 358 kDa.

<span class="mw-page-title-main">Cyclin E1</span> Protein-coding gene in the species Homo sapiens

G1/S-specific cyclin-E1 is a protein that in humans is encoded by the CCNE1 gene.

<span class="mw-page-title-main">ILF3</span> Protein-coding gene in the species Homo sapiens

Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.

<span class="mw-page-title-main">RAB3A</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene. It is involved in calcium-triggered exocytosis in neurons.

<span class="mw-page-title-main">T-cell lymphoma invasion and metastasis-inducing protein 1</span> Protein-coding gene in the species Homo sapiens

Rho guanine nucleotide exchange factor TIAM1 is a protein that in humans is encoded by the TIAM1 gene.

<span class="mw-page-title-main">RAPGEF3</span> Protein-coding gene in the species Homo sapiens

Rap guanine nucleotide exchange factor 3 also known as exchange factor directly activated by cAMP 1 (EPAC1) or cAMP-regulated guanine nucleotide exchange factor I (cAMP-GEFI) is a protein that in humans is encoded by the RAPGEF3 gene.

<span class="mw-page-title-main">RANGAP1</span> Protein-coding gene in the species Homo sapiens

Ran GTPase-activating protein 1 is an enzyme that in humans is encoded by the RANGAP1 gene.

<span class="mw-page-title-main">Dock180</span> Protein-coding gene in the species Homo sapiens

Dock180, also known as DOCK1, is a large protein involved in intracellular signalling networks. It is the mammalian ortholog of the C. elegans protein CED-5 and belongs to the DOCK family of Guanine nucleotide exchange factors (GEFs).

<span class="mw-page-title-main">ARHGEF1</span> Protein-coding gene in the species Homo sapiens

Rho guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the ARHGEF1 gene. This protein is also called RhoGEF1 or p115-RhoGEF.

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

RhoG is a small monomeric GTP-binding protein, and is an important component of many intracellular signalling pathways. It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG.

<span class="mw-page-title-main">RANBP1</span> Protein-coding gene in the species Homo sapiens

Ran-specific binding protein 1 is an enzyme that in humans is encoded by the RANBP1 gene.

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

Triple functional domain protein is a protein that in humans is encoded by the TRIO gene.

<span class="mw-page-title-main">RANBP3</span> Protein-coding gene in the species Homo sapiens

Ran-binding protein 3 is a protein that in humans is encoded by the RANBP3 gene.

<span class="mw-page-title-main">RCBTB1</span> Protein-coding gene in the species Homo sapiens

RCC1 and BTB domain-containing protein 1 is a protein that in humans is encoded by the RCBTB1 gene.

<span class="mw-page-title-main">RAPGEF5</span> Protein-coding gene in the species Homo sapiens

Rap guanine nucleotide exchange factor 5 is a protein that in humans is encoded by the RAPGEF5 gene.

<span class="mw-page-title-main">GNA12</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide-binding protein subunit alpha-12 is a protein that in humans is encoded by the GNA12 gene.

<span class="mw-page-title-main">RCBTB2</span> Protein-coding gene in the species Homo sapiens

RCC1 and BTB domain-containing protein 2 is a protein that in humans is encoded by the RCBTB2 gene.

<span class="mw-page-title-main">Mary Dasso</span> American biochemist

Mary C. Dasso is an American biochemist known for research on chromosome segregation and the discovery of Ran GTPase. She is the acting scientific director of the division of intramural research and a senior investigator in the section on cell cycle regulation at the Eunice Kennedy Shriver National Institute of Child Health and Human Development.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000180198 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028896 - 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. "Entrez Gene: RCC1 Regulator of chromosome condensation 1".
  6. Nemergut ME, Lindsay ME, Brownawell AM, Macara IG (May 2002). "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor". The Journal of Biological Chemistry. 277 (20): 17385–8. doi: 10.1074/jbc.C100620200 . PMID   11932251.
  7. Mueller L, Cordes VC, Bischoff FR, Ponstingl H (May 1998). "Human RanBP3, a group of nuclear RanGTP binding proteins". FEBS Letters. 427 (3): 330–6. doi: 10.1016/S0014-5793(98)00459-1 . PMID   9637251.
  8. Steggerda SM, Paschal BM (July 2000). "The mammalian Mog1 protein is a guanine nucleotide release factor for Ran". The Journal of Biological Chemistry. 275 (30): 23175–80. doi: 10.1074/jbc.C000252200 . PMID   10811801.
  9. Renault L, Kuhlmann J, Henkel A, Wittinghofer A (April 2001). "Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)". Cell. 105 (2): 245–55. doi: 10.1016/S0092-8674(01)00315-4 . PMID   11336674. S2CID   12827419.
  10. Azuma Y, Renault L, García-Ranea JA, Valencia A, Nishimoto T, Wittinghofer A (June 1999). "Model of the ran-RCC1 interaction using biochemical and docking experiments". Journal of Molecular Biology. 289 (4): 1119–30. doi:10.1006/jmbi.1999.2820. PMID   10369786.
  11. Ren M, Villamarin A, Shih A, Coutavas E, Moore MS, LoCurcio M, Clarke V, Oppenheim JD, D'Eustachio P, Rush MG (April 1995). "Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing". Molecular and Cellular Biology. 15 (4): 2117–24. doi:10.1128/MCB.15.4.2117. PMC   230439 . PMID   7891706.

Further reading