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0RBL1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRBL1
DescriptionRetinoblastoma-like protein 1 (107 kda retinoblastoma-associated protein) (prb1) (p107).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0000074 regulation of progression through cell cycle (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Retinoblastoma-like and retinoblastoma-associated proteins may have a function in cell cycle regulation. They form a complex with adenovirus E1A and SV40 large T antigen.nd may bind and modulate the function of certain cellular proteins with which T and E1A compete for pocket binding. The proteins may act as tumor suppressors.nd are potent inhibitors of E2F-mediated trans-activation. This domain has the cyclin fold . The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif.hared by other Rb-binding viral and cellular proteins.hows that the LxCxE peptide binds a highly conserved groove on the B-box portion of the pocket; the A-box portion appears to be required for the stable folding of the B box (see ). Also highly conserved is the extensive A-B interface.uggesting that it may be an additional protein-binding site. The A and B boxes each contain the cyclin-fold structural motif.ith the LxCxE-binding site on the B-box cyclin fold being similar to a Cdk2-binding site of cyclin A and to a TBP-binding site of TFIIB . The A and B boxes are found at the C-terminal end of the protein; the A-box is on N-terminal side of the B-box.
  IPR002720:Retinoblastoma-associated protein, A-box
Retinoblastoma-like and retinoblastoma-associated proteins may have a function in cell cycle regulation. They form a complex with adenovirus E1A and SV40 large T antigen.nd may bind and modulate the function of certain cellular proteins with which T and E1A compete for pocket binding. The proteins may act as tumor suppressors.nd are potent inhibitors of E2F-mediated trans-activation. This domain has the cyclin fold . The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif.hared by other Rb-binding viral and cellular proteins.hows that the LxCxE peptide binds a highly conserved groove on the B-box portion of the pocket; the A-box portion (see ) appears to be required for the stable folding of the B box. Also highly conserved is the extensive A-B interface.uggesting that it may be an additional protein-binding site. The A and B boxes each contain the cyclin-fold structural motif.ith the LxCxE-binding site on the B-box cyclin fold being similar to a Cdk2-binding site of cyclin A and to a TBP-binding site of TFIIB . The A and B boxes are found at the C-terminal end of the protein; the B-box is on C-terminal side of the A-box.
  IPR002719:Retinoblastoma-associated protein, B-box
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles .nd regulate cyclin dependent kinases (CDKs). Cyclins.ogether with the p34 (cdc2) or cdk2 kinases.orm the Maturation Promoting Factor (MPF). There are two main groups of cyclins.1/S cyclins.hich are essential for the control of the cell cycle at the G1/S (start) transition.nd G2/M cyclins.hich are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species.here are multiple forms of G1 and G2 cyclins. For example.n vertebrates.here are two G2 cyclins. and B.nd at least three G1 cyclins...nd E.Cyclin homologues have been found in various viruses.ncluding herpesvirus saimiri and Kaposis sarcoma-associated herpesvirus. These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus .This domain is also found as the core domain in transcription factor IIB (TFIIB) and in the retinoblastoma tumour suppressor.
  IPR013763:Cyclin-related
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles .nd regulate cyclin dependent kinases (CDKs). Cyclins.ogether with the p34 (cdc2) or cdk2 kinases.orm the Maturation Promoting Factor (MPF). There are two main groups of cyclins.1/S cyclins.hich are essential for the control of the cell cycle at the G1/S (start) transition.nd G2/M cyclins.hich are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species.here are multiple forms of G1 and G2 cyclins. For example.n vertebrates.here are two G2 cyclins. and B.nd at least three G1 cyclins...nd E.Cyclin homologues have been found in various viruses.ncluding herpesvirus saimiri and Kaposis sarcoma-associated herpesvirus. These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus .This domain is also found in transcription factor IIB (TFIIB) and retinoblastoma.
  IPR006670:Cyclin
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles .nd regulate cyclin dependent kinases (CDKs). Cyclins.ogether with the p34 (cdc2) or cdk2 kinases.orm the Maturation Promoting Factor (MPF). There are two main groups of cyclins.1/S cyclins.hich are essential for the control of the cell cycle at the G1/S (start) transition.nd G2/M cyclins.hich are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species.here are multiple forms of G1 and G2 cyclins. For example.n vertebrates.here are two G2 cyclins. and B.nd at least three G1 cyclins...nd E.Cyclin homologues have been found in various viruses.ncluding herpesvirus saimiri and Kaposis sarcoma-associated herpesvirus. These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus .This domain is also found as the core domain in transcription factor IIB (TFIIB) and in the retinoblastoma tumour suppressor.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011028:Cyclin-like
IPR002720:RB_A 
Evalue:-121.080924987793 
Location:385-578IPR002719:RB_B 
Evalue:-110.130767822266 
Location:786-944
SequencesProtein: RBL1_HUMAN (1068 aa)
mRNA: NM_002895
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK04681
  Level 3 annotation:
    retinoblastoma-like
  Level 2 annotation:
    TGF-beta signaling pathway
    Cell cycle
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 385 residues, 35059592-35060746Exon2: 57 residues, 35065518-35065683Exon3: 51 residues, 35069227-35069376Exon4: 32 residues, 35080095-35080186Exon5: 26 residues, 35082475-35082547Exon6: 61 residues, 35084466-35084643Exon7: 72 residues, 35094481-35094693Exon8: 91 residues, 35097058-35097325Exon9: 46 residues, 35101969-35102102Exon10: 57 residues, 35105902-35106067Exon11: 48 residues, 35108869-35109007Exon12: 36 residues, 35117369-35117473Exon13: 39 residues, 35117962-35118075Exon14: 57 residues, 35122919-35123086Exon15: 64 residues, 35123900-35124087Exon16: 18 residues, 35127240-35127290Exon17: 55 residues, 35128540-35128701Exon18: 45 residues, 35128809-35128938Exon19: 23 residues, 35129049-35129114Exon20: 69 residues, 35129802-35130003Exon21: 46 residues, 35150805-35150939Exon22: 80 residues, 35157589-35157824Exon23: 2 residues, -Jump to RBL1_HUMAN  
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Loci Cluster (Details)Loci: 3252 34357716-34590449 ~-233K 23020(DLGAP4)(+)Loci: 3253 34667580-34674372 ~-7K 23028(C20orf24)(+)Loci: 4521 35059592-35157824 ~-98K 23045(RBL1)(-)Loci: 3254 35406501-35467233 ~-61K 23056(SRC)(+)Loci: 3251 34144067-34284134 ~-140K 23014(EPB41L1)(+)Link out to UCSC