Retinoblastoma-like protein 1

From Wikipedia, the free encyclopedia

Retinoblastoma-like 1 (p107)

Identifiers

RBL1; PRB1; CP107; MGC40006; p107

External IDs

OMIM: 116957 MGI: 103300 HomoloGene: 2172

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• nucleus • transcription factor complex
Biological Process:	• negative regulation of transcription from RNA polymerase II promoter • transcription • regulation of transcription, DNA-dependent • cell cycle • regulation of lipid kinase activity • negative regulation of progression through cell cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002895 (mRNA)
NP_002886 (protein)

NM_011249 (mRNA)
NP_035379 (protein)

Location

Chr 20: 35.06 - 35.16 Mb

Chr 2: 156.84 - 156.9 Mb

Pubmed search

[1]

[2]

Retinoblastoma-like 1 (p107), also known as RBL1, is a human gene.^[1]

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 adenovirus E1A 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.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Pocket protein family

[edit] References

^ ^a ^b Entrez Gene: RBL1 retinoblastoma-like 1 (p107).

[edit] Further reading

Faha B, Ewen ME, Tsai LH, et al. (1992). "Interaction between human cyclin A and adenovirus E1A-associated p107 protein.". Science 255 (5040): 87–90. PMID 1532458.
Ewen ME, Xing YG, Lawrence JB, Livingston DM (1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein.". Cell 66 (6): 1155–64. PMID 1833063.
Datta PK, Raychaudhuri P, Bagchi S (1995). "Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription.". Mol. Cell. Biol. 15 (10): 5444–52. PMID 7565695.
Zhu L, Zhu L, Xie E, Chang LS (1995). "Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins.". Mol. Cell. Biol. 15 (7): 3552–62. PMID 7791762.
Sardet C, Vidal M, Cobrinik D, et al. (1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle.". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 2403–7. PMID 7892279.
Kim YW, Otterson GA, Kratzke RA, et al. (1994). "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein.". Mol. Cell. Biol. 14 (11): 7256–64. PMID 7935440.
Ginsberg D, Vairo G, Chittenden T, et al. (1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107.". Genes Dev. 8 (22): 2665–79. PMID 7958924.
Beijersbergen RL, Kerkhoven RM, Zhu L, et al. (1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo.". Genes Dev. 8 (22): 2680–90. PMID 7958925.
Beijersbergen RL, Hijmans EM, Zhu L, Bernards R (1994). "Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation.". EMBO J. 13 (17): 4080–6. PMID 8076603.
Dyson N, Dembski M, Fattaey A, et al. (1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1.". J. Virol. 67 (12): 7641–7. PMID 8230483.
Zhu L, van den Heuvel S, Helin K, et al. (1993). "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein.". Genes Dev. 7 (7A): 1111–25. PMID 8319904.
Ikeda MA, Jakoi L, Nevins JR (1996). "A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation.". Proc. Natl. Acad. Sci. U.S.A. 93 (8): 3215–20. PMID 8622916.
Xiao ZX, Ginsberg D, Ewen M, Livingston DM (1996). "Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases.". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4633–7. PMID 8643455.
Vidal M, Brachmann RK, Fattaey A, et al. (1996). "Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions.". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10315–20. PMID 8816797.
Shao Z, Siegert JL, Ruppert S, Robbins PD (1997). "Rb interacts with TAF(II)250/TFIID through multiple domains.". Oncogene 15 (4): 385–92. doi:10.1038/sj.onc.1201204. PMID 9242374.
Verona R, Moberg K, Estes S, et al. (1997). "E2F activity is regulated by cell cycle-dependent changes in subcellular localization.". Mol. Cell. Biol. 17 (12): 7268–82. PMID 9372959.
Trimarchi JM, Fairchild B, Verona R, et al. (1998). "E2F-6, a member of the E2F family that can behave as a transcriptional repressor.". Proc. Natl. Acad. Sci. U.S.A. 95 (6): 2850–5. PMID 9501179.
Sterner JM, Dew-Knight S, Musahl C, et al. (1998). "Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7.". Mol. Cell. Biol. 18 (5): 2748–57. PMID 9566894.
Woitach JT, Zhang M, Niu CH, Thorgeirsson SS (1998). "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability.". Nat. Genet. 19 (4): 371–4. doi:10.1038/1258. PMID 9697699.
Veal E, Eisenstein M, Tseng ZH, Gill G (1998). "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F.". Mol. Cell. Biol. 18 (9): 5032–41. PMID 9710587.

[edit] External links

MeSH RBL1+protein,+human

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD