Retinoblastoma-like 1 (p107), also known as RBL1, is a
protein that in humans is encoded by the RBL1gene.[5][6]
Function
The protein encoded by this gene is similar in sequence and possibly function to the product of the
retinoblastoma 1 (
RB1) gene. The RB1 gene product is a
tumor suppressor protein that appears to be involved in
cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with
adenovirusE1A protein and
SV40 Large T-antigen, with the
SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing
E2F binding sites in their
promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different
isoforms have been found for this gene.[5]
Interactions
Retinoblastoma-like protein 1 has been shown to
interact with:
^Ewen ME, Xing YG, Lawrence JB, Livingston DM (Sep 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell. 66 (6): 1155–64.
doi:
10.1016/0092-8674(91)90038-Z.
PMID1833063.
S2CID27478008.
^
abRual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
^
abJoaquin M, Bessa M, Saville MK, Watson RJ (Nov 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene. 21 (52): 7923–32.
doi:
10.1038/sj.onc.1206001.
PMID12439743.
S2CID21761703.
^Wang S, Nath N, Adlam M, Chellappan S (Jun 1999). "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene. 18 (23): 3501–10.
doi:
10.1038/sj.onc.1202684.
PMID10376528.
S2CID33828482.
^Fusco C, Reymond A, Zervos AS (Aug 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics. 51 (3): 351–8.
doi:
10.1006/geno.1998.5368.
PMID9721205.
Woitach JT, Zhang M, Niu CH, Thorgeirsson SS (Aug 1998). "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability". Nature Genetics. 19 (4): 371–4.
doi:
10.1038/1258.
PMID9697699.
S2CID11374970.
Retinoblastoma-like 1 (p107), also known as RBL1, is a
protein that in humans is encoded by the RBL1gene.[5][6]
Function
The protein encoded by this gene is similar in sequence and possibly function to the product of the
retinoblastoma 1 (
RB1) gene. The RB1 gene product is a
tumor suppressor protein that appears to be involved in
cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with
adenovirusE1A protein and
SV40 Large T-antigen, with the
SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing
E2F binding sites in their
promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different
isoforms have been found for this gene.[5]
Interactions
Retinoblastoma-like protein 1 has been shown to
interact with:
^Ewen ME, Xing YG, Lawrence JB, Livingston DM (Sep 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell. 66 (6): 1155–64.
doi:
10.1016/0092-8674(91)90038-Z.
PMID1833063.
S2CID27478008.
^
abRual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8.
Bibcode:
2005Natur.437.1173R.
doi:
10.1038/nature04209.
PMID16189514.
S2CID4427026.
^
abJoaquin M, Bessa M, Saville MK, Watson RJ (Nov 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene. 21 (52): 7923–32.
doi:
10.1038/sj.onc.1206001.
PMID12439743.
S2CID21761703.
^Wang S, Nath N, Adlam M, Chellappan S (Jun 1999). "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene. 18 (23): 3501–10.
doi:
10.1038/sj.onc.1202684.
PMID10376528.
S2CID33828482.
^Fusco C, Reymond A, Zervos AS (Aug 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics. 51 (3): 351–8.
doi:
10.1006/geno.1998.5368.
PMID9721205.
Woitach JT, Zhang M, Niu CH, Thorgeirsson SS (Aug 1998). "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability". Nature Genetics. 19 (4): 371–4.
doi:
10.1038/1258.
PMID9697699.
S2CID11374970.