Retinoblastom 1

RBL1
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 1H28, 4YOO, 4YOS, 4YOZ
Identifikatori
Aliasi	RBL1
Vanjski ID-jevi	OMIM: 116957 MGI: 103300 HomoloGene: 2172 GeneCards: RBL1
Lokacija gena (čovjek) Hrom. Hromosom 20 (čovjek)[1] Bend 20q11.23 Početak 36,996,349 bp[1] Kraj 37,095,997 bp[1]
Lokacija gena (miš) Hrom. Hromosom 2 (miš)[2] Bend 2 H1|2 78.05 cM Početak 156,987,813 bp[2] Kraj 157,046,454 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • transcription factor binding • GO:0001948, GO:0016582 vezivanje za proteine • promoter-specific chromatin binding • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific Ćelijska komponenta • jedro • transcription regulator complex • nukleoplazma • Hromatin Biološki proces • regulation of cell cycle • GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II • ćelijski ciklus • GO:0022415 viral process • GO:0009373 regulation of transcription, DNA-templated • GO:1901227 negative regulation of transcription by RNA polymerase II • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II • regulation of lipid kinase activity • negative regulation of gene expression • transcription, DNA-templated • negative regulation of cellular senescence • GO:0031497, GO:0006336, GO:0034724, GO:0001301, GO:0007580, GO:0034652, GO:0010847 chromatin organization • regulation of mitotic cell cycle • Ćelijska diferencijacija • regulation of cell division • GO:1990376 negative regulation of G1/S transition of mitotic cell cycle Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	5933	19650
Ensembl	ENSG00000080839	ENSMUSG00000027641
UniProt	P28749	Q64701
RefSeq (mRNK)	NM_002895 NM_183404 NM_001323281 NM_001323282	NM_001139516 NM_011249
RefSeq (bjelančevina)	NP_001310210 NP_001310211 NP_002886 NP_899662	NP_001132988 NP_035379
Lokacija (UCSC)	Chr 20: 37 – 37.1 Mb	Chr 2: 156.99 – 157.05 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Retinoblastomoliki protein 1 (p107), znan i kao RBL1, jest protein koji je kod ljudi kodiran genom RBL1 sa hromosoma 20.^[5][6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.068 aminokiselina, a molekulska težina 120.847 Da.^[5]

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MFEDKPHAEG		AAVVAAAGEA		LQALCQELNL		DEGSAAEALD		DFTAIRGNYS
LEGEVTHWLA		CSLYVACRKS		IIPTVGKGIM		EGNCVSLTRI		LRSAKLSLIQ
FFSKMKKWMD		MSNLPQEFRE		RIERLERNFE		VSTVIFKKYE		PIFLDIFQNP
YEEPPKLPRS		RKQRRIPCSV		KDLFNFCWTL		FVYTKGNFRM		IGDDLVNSYH
LLLCCLDLIF		ANAIMCPNRQ		DLLNPSFKGL		PSDFHTADFT		ASEEPPCIIA
VLCELHDGLL		VEAKGIKEHY		FKPYISKLFD		RKILKGECLL		DLSSFTDNSK
AVNKEYEEYV		LTVGDFDERI		FLGADAEEEI		GTPRKFTRDT		PLGKLTAQAN
VEYNLQQHFE		KKRSFAPSTP		LTGRRYLREK		EAVITPVASA		TQSVSRLQSI
VAGLKNAPSD		QLINIFESCV		RNPVENIMKI		LKGIGETFCQ		HYTQSTDEQP
GSHIDFAVNR		LKLAEILYYK		ILETVMVQET		RRLHGMDMSV		LLEQDIFHRS
LMACCLEIVL		FAYSSPRTFP		WIIEVLNLQP		FYFYKVIEVV		IRSEEGLSRD
MVKHLNSIEE		QILESLAWSH		DSALWEALQV		SANKVPTCEE		VIFPNNFETG
NGGNVQGHLP		LMPMSPLMHP		RVKEVRTDSG		SLRRDMQPLS		PISVHERYSS
PTAGSAKRRL		FGEDPPKEML		MDKIITEGTK		LKIAPSSSIT		AENVSILPGQ
TLLTMATAPV		TGTTGHKVTI		PLHGVANDAG		EITLIPLSMN		TNQESKVKSP
VSLTAHSLIG		ASPKQTNLTK		AQEVHSTGIN		RPKRTGSLAL		FYRKVYHLAS
VRLRDLCLKL		DVSNELRRKI		WTCFEFTLVH		CPDLMKDRHL		DQLLLCAFYI
MAKVTKEERT		FQEIMKSYRN		QPQANSHVYR		SVLLKSIPRE		VVAYNKNIND
DFEMIDCDLE		DATKTPDCSS		GPVKEERGDL		IKFYNTIYVG		RVKSFALKYD
LANQDHMMDA		PPLSPFPHIK		QQPGSPRRIS		QQHSIYISPH		KNGSGLTPRS
ALLYKFNGSP		SKSLKDINNM		IRQGEQRTKK		RVIAIDSDAE		SPAKRVCQEN
DDVLLKRLQD		VVSERANH

Funkcija

Protein koji je kodiran ovim genom sličan je po sekvenci i možda funkciji produktu retinoblastomskog 1 (RB1) gena. RB1 genski proizvod je protein za supresiju tumora koji se je uključen u regulaciju ćelijskog ciklusa, budući da je fosforiliran u S u M faznoj tranziciji i defosforiliran u G1 fazi ćelijskog ciklusa. I protein RB1 i proizvod ovog gena mogu formirati kompleks sa adenovirusnim E1A proteinom i SV40 veliki T-antigen, sa SV40 velikim T-antigenom, vezujući se samo za nefosforilirani oblik svakog proteina. Osim toga, oba proteina mogu inhibirati transkripciju gena ćelijskog ciklusa koji sadrže E2F mjesta vezanja u svojim promotorima. Zbog sekvencne i biohemijskih sličnosti sa RB1 proteinom, smatra se da protein kodiran ovim genom takođe može biti supresor tumora. Za ovaj gen, pronađene su dvije varijante transkripta koje kodiraju različite izoforme.^[5]

Interakcije

Pokazalo se da protein 1 sličan retinoblastomu reaguje sa:

• BEGAIN,^[7]
• BRCA1,^[8]
• BRF1,^[9]
• Ciklin A2,^[10][11]
• Ciklin-ovisna kinaza 2,^[12][13]
• E2F1,^[10]
• HDAC1,^[14][15]
• MYBL2^[11][16]
• Majke protiv dekapentaplegijskog homologa 3,^[17]
• Prohibitin,^[18] i
• RBBP8.^[7][19]

Također pogledajte

• Porodica džepnih proteina

Reference

1. GRCh38: Ensembl release 89: ENSG00000080839 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027641 - Ensembl, maj 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: RBL1 retinoblastoma-like 1 (p107)".
6. 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. PMID 1833063. S2CID 27478008.
7. Rual 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. PMID 16189514. S2CID 4427026.
8. Fan S, Yuan R, Ma YX, Xiong J, Meng Q, Erdos M, Zhao JN, Goldberg ID, Pestell RG, Rosen EM (Aug 2001). "Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding". Oncogene. 20 (35): 4827–41. doi:10.1038/sj.onc.1204666. PMID 11521194.
9. Sutcliffe JE, Cairns CA, McLees A, Allison SJ, Tosh K, White RJ (Jun 1999). "RNA polymerase III transcription factor IIIB is a target for repression by pocket proteins p107 and p130". Molecular and Cellular Biology. 19 (6): 4255–61. doi:10.1128/mcb.19.6.4255. PMC 104385. PMID 10330166.
10. Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (Dec 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". Journal of Virology. 67 (12): 7641–7. doi:10.1128/JVI.67.12.7641-7647.1993. PMC 238233. PMID 8230483.
11. Joaquin 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. PMID 12439743.
12. Shanahan F, Seghezzi W, Parry D, Mahony D, Lees E (Feb 1999). "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest". Molecular and Cellular Biology. 19 (2): 1460–9. doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079.
13. Leng X, Noble M, Adams PD, Qin J, Harper JW (Apr 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Molecular and Cellular Biology. 22 (7): 2242–54. doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
14. Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (Oct 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.
15. Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (Sep 1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proceedings of the National Academy of Sciences of the United States of America. 95 (18): 10493–8. Bibcode:1998PNAS...9510493F. doi:10.1073/pnas.95.18.10493. PMC 27922. PMID 9724731.
16. Joaquin M, Watson RJ (Nov 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". The Journal of Biological Chemistry. 278 (45): 44255–64. doi:10.1074/jbc.M308953200. PMID 12947099.
17. Chen CR, Kang Y, Siegel PM, Massagué J (Jul 2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell. 110 (1): 19–32. doi:10.1016/s0092-8674(02)00801-2. PMID 12150994. S2CID 8945574.
18. 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. PMID 10376528.
19. 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. PMID 9721205.

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

Dopunska literatura

• Faha B, Ewen ME, Tsai LH, Livingston DM, Harlow E (Jan 1992). "Interaction between human cyclin A and adenovirus E1A-associated p107 protein". Science. 255 (5040): 87–90. Bibcode:1992Sci...255...87F. doi:10.1126/science.1532458. PMID 1532458.
• 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. PMID 1833063. S2CID 27478008.
• Datta PK, Raychaudhuri P, Bagchi S (Oct 1995). "Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription". Molecular and Cellular Biology. 15 (10): 5444–52. doi:10.1128/mcb.15.10.5444. PMC 230794. PMID 7565695.
• Zhu L, Zhu L, Xie E, Chang LS (Jul 1995). "Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins". Molecular and Cellular Biology. 15 (7): 3552–62. doi:10.1128/mcb.15.7.3552. PMC 230592. PMID 7791762.
• Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (Mar 1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle". Proceedings of the National Academy of Sciences of the United States of America. 92 (6): 2403–7. Bibcode:1995PNAS...92.2403S. doi:10.1073/pnas.92.6.2403. PMC 42492. PMID 7892279.
• Kim YW, Otterson GA, Kratzke RA, Coxon AB, Kaye FJ (Nov 1994). "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein". Molecular and Cellular Biology. 14 (11): 7256–64. doi:10.1128/mcb.14.11.7256. PMC 359260. PMID 7935440.
• Ginsberg D, Vairo G, Chittenden T, Xiao ZX, Xu G, Wydner KL, DeCaprio JA, Lawrence JB, Livingston DM (Nov 1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107". Genes & Development. 8 (22): 2665–79. doi:10.1101/gad.8.22.2665. PMID 7958924.
• Beijersbergen RL, Kerkhoven RM, Zhu L, Carlée L, Voorhoeve PM, Bernards R (Nov 1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo". Genes & Development. 8 (22): 2680–90. doi:10.1101/gad.8.22.2680. PMID 7958925.
• Beijersbergen RL, Hijmans EM, Zhu L, Bernards R (Sep 1994). "Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation". The EMBO Journal. 13 (17): 4080–6. doi:10.1002/j.1460-2075.1994.tb06725.x. PMC 395329. PMID 8076603.
• Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (Dec 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". Journal of Virology. 67 (12): 7641–7. doi:10.1128/JVI.67.12.7641-7647.1993. PMC 238233. PMID 8230483.
• Zhu L, van den Heuvel S, Helin K, Fattaey A, Ewen M, Livingston D, Dyson N, Harlow E (Jul 1993). "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein". Genes & Development. 7 (7A): 1111–25. doi:10.1101/gad.7.7a.1111. PMID 8319904.
• Ikeda MA, Jakoi L, Nevins JR (Apr 1996). "A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation". Proceedings of the National Academy of Sciences of the United States of America. 93 (8): 3215–20. Bibcode:1996PNAS...93.3215I. doi:10.1073/pnas.93.8.3215. PMC 39585. PMID 8622916.
• Xiao ZX, Ginsberg D, Ewen M, Livingston DM (maj 1996). "Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 4633–7. Bibcode:1996PNAS...93.4633X. doi:10.1073/pnas.93.10.4633. PMC 39330. PMID 8643455.
• Vidal M, Brachmann RK, Fattaey A, Harlow E, Boeke JD (Sep 1996). "Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions". Proceedings of the National Academy of Sciences of the United States of America. 93 (19): 10315–20. Bibcode:1996PNAS...9310315V. doi:10.1073/pnas.93.19.10315. PMC 38381. PMID 8816797.
• Shao Z, Siegert JL, Ruppert S, Robbins PD (Jul 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, Starz M, Vernon JP, Lees JA (Dec 1997). "E2F activity is regulated by cell cycle-dependent changes in subcellular localization". Molecular and Cellular Biology. 17 (12): 7268–82. doi:10.1128/mcb.17.12.7268. PMC 232584. PMID 9372959.
• Trimarchi JM, Fairchild B, Verona R, Moberg K, Andon N, Lees JA (Mar 1998). "E2F-6, a member of the E2F family that can behave as a transcriptional repressor". Proceedings of the National Academy of Sciences of the United States of America. 95 (6): 2850–5. Bibcode:1998PNAS...95.2850T. doi:10.1073/pnas.95.6.2850. PMC 19658. PMID 9501179.
• Sterner JM, Dew-Knight S, Musahl C, Kornbluth S, Horowitz JM (maj 1998). "Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7". Molecular and Cellular Biology. 18 (5): 2748–57. doi:10.1128/mcb.18.5.2748. PMC 110654. PMID 9566894.
• 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. PMID 9697699. S2CID 11374970.
• Veal E, Eisenstein M, Tseng ZH, Gill G (Sep 1998). "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F". Molecular and Cellular Biology. 18 (9): 5032–41. doi:10.1128/mcb.18.9.5032. PMC 109088. PMID 9710587.

Vanjski linkovi

• RBL1 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)