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P06400

- RB_HUMAN

UniProt

P06400 - RB_HUMAN

Protein

Retinoblastoma-associated protein

Gene

RB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 199 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex By similarity. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.By similarity1 Publication

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. core promoter binding Source: UniProtKB
    3. DNA binding Source: ProtInc
    4. identical protein binding Source: IntAct
    5. kinase binding Source: UniProtKB
    6. phosphoprotein binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. sequence-specific DNA binding transcription factor activity Source: ProtInc
    9. transcription coactivator activity Source: UniProtKB
    10. transcription factor binding Source: UniProtKB
    11. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. cell cycle arrest Source: BHF-UCL
    3. cell cycle checkpoint Source: ProtInc
    4. cell morphogenesis involved in neuron differentiation Source: Ensembl
    5. chromatin remodeling Source: BHF-UCL
    6. digestive tract development Source: Ensembl
    7. enucleate erythrocyte differentiation Source: Ensembl
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. glial cell apoptotic process Source: Ensembl
    10. hepatocyte apoptotic process Source: Ensembl
    11. maintenance of mitotic sister chromatid cohesion Source: BHF-UCL
    12. mitotic cell cycle Source: Reactome
    13. mitotic cell cycle checkpoint Source: BHF-UCL
    14. myoblast differentiation Source: UniProtKB
    15. negative regulation of epithelial cell proliferation Source: Ensembl
    16. negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
    17. negative regulation of protein kinase activity Source: UniProtKB
    18. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    19. negative regulation of smoothened signaling pathway Source: Ensembl
    20. negative regulation of transcription, DNA-templated Source: UniProtKB
    21. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: BHF-UCL
    22. negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Ensembl
    23. neuron apoptotic process Source: Ensembl
    24. neuron maturation Source: Ensembl
    25. neuron projection development Source: Ensembl
    26. positive regulation of macrophage differentiation Source: Ensembl
    27. positive regulation of mitotic metaphase/anaphase transition Source: BHF-UCL
    28. positive regulation of transcription, DNA-templated Source: UniProtKB
    29. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    30. protein localization to chromosome, centromeric region Source: BHF-UCL
    31. Ras protein signal transduction Source: BHF-UCL
    32. regulation of centromere complex assembly Source: BHF-UCL
    33. regulation of cohesin localization to chromatin Source: BHF-UCL
    34. regulation of lipid kinase activity Source: UniProtKB
    35. regulation of mitotic cell cycle Source: BHF-UCL
    36. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
    37. sister chromatid biorientation Source: BHF-UCL
    38. skeletal muscle cell differentiation Source: Ensembl
    39. striated muscle cell differentiation Source: Ensembl
    40. transcription, DNA-templated Source: UniProtKB-KW
    41. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1156. Orc1 removal from chromatin.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_821. Cyclin D associated events in G1.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinkiP06400.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoblastoma-associated protein
    Alternative name(s):
    p105-Rb
    pRb
    Short name:
    Rb
    pp110
    Gene namesi
    Name:RB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:9884. RB1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. chromatin Source: ProtInc
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB
    5. Rb-E2F complex Source: BHF-UCL
    6. spindle Source: Ensembl
    7. SWI/SNF complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Childhood cancer retinoblastoma (RB) [MIM:180200]: Congenital malignant tumor that arises from the nuclear layers of the retina. It occurs in about 1:20'000 live births and represents about 2% of childhood malignancies. It is bilateral in about 30% of cases. Although most RB appear sporadically, about 20% are transmitted as an autosomal dominant trait with incomplete penetrance. The diagnosis is usually made before the age of 2 years when strabismus or a gray to yellow reflex from pupil ('cat eye') is investigated.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721E → Q in RB. 1 Publication
    VAR_005572
    Natural varianti137 – 1371E → D in RB; unilateral form. 1 Publication
    VAR_005573
    Natural varianti185 – 1851I → T in RB. 1 Publication
    VAR_005574
    Natural varianti310 – 3101G → E in RB; unknown pathological significance. 1 Publication
    VAR_010045
    Natural varianti358 – 3581R → G in RB. 1 Publication
    VAR_010046
    Natural varianti358 – 3581R → Q in RB.
    VAR_005575
    Natural varianti447 – 4471K → Q in RB. 1 Publication
    VAR_010048
    Natural varianti457 – 4571M → R in RB. 1 Publication
    VAR_005576
    Natural varianti480 – 4801Missing in RB; mild form. 1 Publication
    VAR_005577
    Natural varianti500 – 5001R → G in RB. 1 Publication
    VAR_011580
    Natural varianti530 – 5301K → R in RB. 1 Publication
    VAR_010049
    Natural varianti549 – 5491H → Y in RB. 1 Publication
    VAR_005578
    Natural varianti567 – 5671S → L in RB. 2 Publications
    VAR_005579
    Natural varianti616 – 6161K → E in RB. 1 Publication
    VAR_011581
    Natural varianti635 – 6351A → P in RB. 1 Publication
    VAR_005580
    Natural varianti654 – 6541V → E in RB. 1 Publication
    VAR_005581
    Natural varianti657 – 6571L → P in RB. 1 Publication
    VAR_010050
    Natural varianti661 – 6611R → W in RB; mild form. 4 Publications
    VAR_005582
    Natural varianti662 – 6621L → P in RB. 1 Publication
    VAR_005583
    Natural varianti673 – 6731H → P in RB.
    VAR_005584
    Natural varianti685 – 6851Q → P in RB. 1 Publication
    VAR_005585
    Natural varianti706 – 7061C → Y in RB.
    VAR_005586
    Natural varianti712 – 7121C → R in RB. 1 Publication
    VAR_005587
    Natural varianti803 – 8031N → K in RB. 1 Publication
    VAR_005588
    Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Osteogenic sarcoma (OSRC) [MIM:259500]: A sarcoma originating in bone-forming cells, affecting the ends of long bones.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi821 – 8211T → A: Abolishes interaction with Pocket domain; when associated with A-826. 2 Publications
    Mutagenesisi826 – 8261T → A: Abolishes interaction with Pocket domain; when associated with A-821. 2 Publications
    Mutagenesisi860 – 8601K → R: Abolishes monomethylation by SMYD2 and subsequent interaction with L3MBTL1. 2 Publications
    Mutagenesisi870 – 8701K → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. 2 Publications
    Mutagenesisi873 – 8742KK → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. 1 Publication
    Mutagenesisi873 – 8742KK → RR: Does not alter Rb localization in cycling cells, but mislocalizes to the cytoplasm during keratinocytes differentiation. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi109800. phenotype.
    180200. phenotype.
    259500. phenotype.
    Orphaneti357027. Familial retinoblastoma.
    1587. Monosomy 13q14.
    357034. Unilateral retinoblastoma.
    PharmGKBiPA295.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 928927Retinoblastoma-associated proteinPRO_0000167836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N-dimethylprolineBy similarity
    Modified residuei37 – 371Phosphoserine2 Publications
    Modified residuei249 – 2491Phosphoserine; by CDK15 Publications
    Modified residuei252 – 2521Phosphothreonine; by CDK13 Publications
    Modified residuei356 – 3561Phosphothreonine1 Publication
    Modified residuei373 – 3731Phosphothreonine; by CDK12 Publications
    Modified residuei567 – 5671Phosphoserine; by CDK21 Publication
    Modified residuei612 – 6121Phosphoserine; by CHEK2 and CHEK12 Publications
    Modified residuei795 – 7951PhosphoserineBy similarity
    Modified residuei807 – 8071Phosphoserine; by CDK1 and CDK34 Publications
    Modified residuei810 – 8101N6-methyllysine; by SMYD21 Publication
    Modified residuei811 – 8111Phosphoserine; by CDK1 and CDK33 Publications
    Modified residuei821 – 8211Phosphothreonine; by CDK63 Publications
    Modified residuei823 – 8231Phosphothreonine1 Publication
    Modified residuei826 – 8261Phosphothreonine; by CDK44 Publications
    Modified residuei841 – 8411Phosphothreonine1 Publication
    Modified residuei860 – 8601N6-methyllysine; by SMYD21 Publication
    Modified residuei873 – 8731N6-acetyllysine; by PCAF1 Publication
    Modified residuei874 – 8741N6-acetyllysine; by PCAF1 Publication

    Post-translational modificationi

    Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-567 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. SV40 large T antigen, HPV E7 and adenovirus E1A bind to the underphosphorylated, active form of pRb. Phosphorylation at Thr-821 and Thr-826 promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-795 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-807 and Ser-811 is required for G0-G1 transition. Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis By similarity.By similarity
    N-terminus is methylated by METTL11A/NTM1 By similarity. Monomethylation at Lys-810 by SMYD2 enhances phosphorylation at Ser-807 and Ser-811, and promotes cell cycle progression. Monomethylation at Lys-860 by SMYD2 promotes interaction with L3MBTL1.By similarity14 Publications
    Acetylation at Lys-873 and Lys-874 regulates subcellular localization, at least during keratinocytes differentiation.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06400.
    PaxDbiP06400.
    PeptideAtlasiP06400.
    PRIDEiP06400.

    PTM databases

    PhosphoSiteiP06400.

    Miscellaneous databases

    PMAP-CutDBP06400.

    Expressioni

    Tissue specificityi

    Expressed in the retina.

    Gene expression databases

    ArrayExpressiP06400.
    BgeeiP06400.
    CleanExiHS_RB1.
    GenevestigatoriP06400.

    Organism-specific databases

    HPAiCAB000095.
    CAB016687.

    Interactioni

    Subunit structurei

    Interacts with ATAD5. Interacts with PRMT2, CDK1 and CDK2 By similarity. The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor. Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of TAF1. Interacts with SNW1, AATF, DNMT1, LIN9, LMNA, SUV420H1, SUV420H2, PELP1, UHRF2 and TMPO-alpha. May interact with NDC80. Interacts with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 AND HDAC1 By similarity. Interacts with adenovirus E1A protein, HPV E7 protein and SV40 large T antigen. Interacts with PSMA3 and USP4. Interacts (when methylated at Lys-860) with L3MBTL1. Interacts with CHEK2; phosphorylates RB1. Interacts with human cytomegalovirus/HHV-5 protein UL123.By similarity34 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-491274,EBI-491274
    P030706EBI-491274,EBI-617698From a different organism.
    P032558EBI-491274,EBI-2603114From a different organism.
    P03255-12EBI-491274,EBI-6692439From a different organism.
    P03255-23EBI-491274,EBI-6859460From a different organism.
    CDK2P249413EBI-491274,EBI-375096
    Cdk4P302852EBI-491274,EBI-847225From a different organism.
    CenpfQ155P74EBI-491274,EBI-2211248From a different organism.
    CHEK1O147573EBI-491274,EBI-974488
    CHEK2O960173EBI-491274,EBI-1180783
    DGKZQ13574-26EBI-491274,EBI-715527
    DYRK1AQ136273EBI-491274,EBI-1053596
    DYRK1BQ9Y4633EBI-491274,EBI-634187
    E2F1Q0109420EBI-491274,EBI-448924
    E2F2Q142093EBI-491274,EBI-718476
    E2F3O007164EBI-491274,EBI-765551
    E7A0MPS72EBI-491274,EBI-7014709From a different organism.
    E7P0312921EBI-491274,EBI-866453From a different organism.
    E7P040202EBI-491274,EBI-7005254From a different organism.
    E7P064642EBI-491274,EBI-6944797From a different organism.
    E7P064652EBI-491274,EBI-963841From a different organism.
    E7P067882EBI-491274,EBI-1776887From a different organism.
    FRKP426853EBI-491274,EBI-1383583
    HBP1O603812EBI-491274,EBI-954175
    HDAC1Q135474EBI-491274,EBI-301834
    Hmga2P529275EBI-491274,EBI-912574From a different organism.
    Ifi202Q9R0025EBI-491274,EBI-3043899From a different organism.
    IRF3Q146532EBI-491274,EBI-2650369
    MAPK14Q165394EBI-491274,EBI-73946
    MDM2Q009874EBI-491274,EBI-389668
    MDM4O151514EBI-491274,EBI-398437
    NCOA6Q146863EBI-491274,EBI-78670
    NEFMP071972EBI-491274,EBI-1105035
    ospFQ8VSP92EBI-491274,EBI-6506625From a different organism.
    PA2G4Q9UQ804EBI-491274,EBI-924893
    PPP1CAP621362EBI-491274,EBI-357253
    PRMT2P553453EBI-491274,EBI-78458
    PURAQ005776EBI-491274,EBI-1045860
    RAF1P040493EBI-491274,EBI-365996
    RNF40O751503EBI-491274,EBI-744408
    SETD7Q8WTS64EBI-491274,EBI-1268586
    Sirt1Q923E44EBI-491274,EBI-1802585From a different organism.
    Smarca4Q3TKT44EBI-491274,EBI-1210244From a different organism.
    UHRF2Q96PU44EBI-491274,EBI-625304
    USP7Q930098EBI-491274,EBI-302474

    Protein-protein interaction databases

    BioGridi111860. 206 interactions.
    DIPiDIP-582N.
    IntActiP06400. 85 interactions.
    MINTiMINT-98847.
    STRINGi9606.ENSP00000267163.

    Structurei

    Secondary structure

    1
    928
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi55 – 639
    Helixi68 – 8215
    Helixi95 – 11016
    Helixi117 – 1248
    Helixi128 – 1358
    Helixi142 – 17231
    Beta strandi180 – 1823
    Helixi188 – 20417
    Beta strandi207 – 2093
    Helixi212 – 22817
    Helixi232 – 2343
    Turni237 – 2404
    Helixi241 – 2433
    Helixi272 – 28110
    Helixi285 – 29410
    Helixi296 – 2994
    Helixi302 – 3065
    Helixi314 – 32815
    Helixi333 – 3386
    Helixi341 – 3433
    Helixi347 – 3537
    Helixi382 – 39110
    Helixi398 – 4058
    Beta strandi407 – 4093
    Helixi412 – 43423
    Helixi436 – 4383
    Helixi439 – 46830
    Helixi474 – 4774
    Helixi480 – 50122
    Turni504 – 5063
    Beta strandi511 – 5133
    Helixi516 – 5216
    Helixi525 – 5295
    Helixi532 – 5387
    Helixi544 – 55916
    Helixi561 – 5633
    Beta strandi564 – 5663
    Helixi569 – 5779
    Helixi602 – 6076
    Helixi645 – 66925
    Helixi676 – 69015
    Helixi692 – 6954
    Helixi700 – 71415
    Helixi721 – 7288
    Beta strandi731 – 7333
    Helixi737 – 7404
    Beta strandi741 – 7433
    Beta strandi745 – 7473
    Beta strandi748 – 7503
    Helixi752 – 7587
    Helixi760 – 77011
    Beta strandi773 – 7753
    Beta strandi830 – 8367
    Turni838 – 8403
    Helixi841 – 85313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AD6X-ray2.30A378-562[»]
    1GH6X-ray3.20B379-577[»]
    B645-772[»]
    1GUXX-ray1.85A372-589[»]
    B636-787[»]
    1H25X-ray2.50E868-878[»]
    1N4MX-ray2.20A/B380-785[»]
    1O9KX-ray2.60A/C/E/G372-589[»]
    B/D/F/H636-787[»]
    1PJMX-ray2.50A858-881[»]
    2AZEX-ray2.55C829-874[»]
    2QDJX-ray2.00A52-355[»]
    2R7GX-ray1.67A/C380-787[»]
    3N5UX-ray3.20C870-882[»]
    3POMX-ray2.50A/B380-577[»]
    A/B643-783[»]
    4ELJX-ray2.70A53-787[»]
    4ELLX-ray1.98A/B380-787[»]
    ProteinModelPortaliP06400.
    SMRiP06400. Positions 53-786, 829-872.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06400.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni373 – 771399Pocket; binds T and E1AAdd
    BLAST
    Regioni373 – 579207Domain AAdd
    BLAST
    Regioni580 – 63960SpacerAdd
    BLAST
    Regioni640 – 771132Domain BAdd
    BLAST
    Regioni763 – 928166Interaction with LIMD1Add
    BLAST
    Regioni771 – 928158Domain C; mediates interaction with E4F1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi870 – 8767Nuclear localization signalCurated

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 189Poly-Ala
    Compositional biasi20 – 2910Poly-Pro

    Domaini

    The Pocket domain binds to the threonine-phosphorylated domain C, thereby preventing interaction with heterodimeric E2F/DP transcription factor complexes.

    Sequence similaritiesi

    Belongs to the retinoblastoma protein (RB) family.Curated

    Phylogenomic databases

    eggNOGiNOG296920.
    HOVERGENiHBG008967.
    InParanoidiP06400.
    KOiK06618.
    OMAiTNILQYA.
    OrthoDBiEOG7P5T04.
    PhylomeDBiP06400.
    TreeFamiTF105568.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view]
    PANTHERiPTHR13742. PTHR13742. 1 hit.
    PfamiPF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    PF08934. Rb_C. 1 hit.
    [Graphical view]
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06400-1 [UniParc]FASTAAdd to Basket

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    MPPKTPRKTA ATAAAAAAEP PAPPPPPPPE EDPEQDSGPE DLPLVRLEFE    50
    ETEEPDFTAL CQKLKIPDHV RERAWLTWEK VSSVDGVLGG YIQKKKELWG 100
    ICIFIAAVDL DEMSFTFTEL QKNIEISVHK FFNLLKEIDT STKVDNAMSR 150
    LLKKYDVLFA LFSKLERTCE LIYLTQPSSS ISTEINSALV LKVSWITFLL 200
    AKGEVLQMED DLVISFQLML CVLDYFIKLS PPMLLKEPYK TAVIPINGSP 250
    RTPRRGQNRS ARIAKQLEND TRIIEVLCKE HECNIDEVKN VYFKNFIPFM 300
    NSLGLVTSNG LPEVENLSKR YEEIYLKNKD LDARLFLDHD KTLQTDSIDS 350
    FETQRTPRKS NLDEEVNVIP PHTPVRTVMN TIQQLMMILN SASDQPSENL 400
    ISYFNNCTVN PKESILKRVK DIGYIFKEKF AKAVGQGCVE IGSQRYKLGV 450
    RLYYRVMESM LKSEEERLSI QNFSKLLNDN IFHMSLLACA LEVVMATYSR 500
    STSQNLDSGT DLSFPWILNV LNLKAFDFYK VIESFIKAEG NLTREMIKHL 550
    ERCEHRIMES LAWLSDSPLF DLIKQSKDRE GPTDHLESAC PLNLPLQNNH 600
    TAADMYLSPV RSPKKKGSTT RVNSTANAET QATSAFQTQK PLKSTSLSLF 650
    YKKVYRLAYL RLNTLCERLL SEHPELEHII WTLFQHTLQN EYELMRDRHL 700
    DQIMMCSMYG ICKVKNIDLK FKIIVTAYKD LPHAVQETFK RVLIKEEEYD 750
    SIIVFYNSVF MQRLKTNILQ YASTRPPTLS PIPHIPRSPY KFPSSPLRIP 800
    GGNIYISPLK SPYKISEGLP TPTKMTPRSR ILVSIGESFG TSEKFQKINQ 850
    MVCNSDRVLK RSAEGSNPPK PLKKLRFDIE GSDEADGSKH LPGESKFQQK 900
    LAEMTSTRTR MQKQKMNDSM DTSNKEEK 928
    Length:928
    Mass (Da):106,159
    Last modified:January 1, 1990 - v2
    Checksum:iC8E746111E19CC32
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti500 – 5012RS → SN in AAN64133. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721E → Q in RB. 1 Publication
    VAR_005572
    Natural varianti133 – 1331N → H.
    Corresponds to variant rs3092900 [ dbSNP | Ensembl ].
    VAR_051909
    Natural varianti137 – 1371E → D in RB; unilateral form. 1 Publication
    VAR_005573
    Natural varianti173 – 1731Y → H.1 Publication
    VAR_069376
    Natural varianti185 – 1851I → T in RB. 1 Publication
    VAR_005574
    Natural varianti310 – 3101G → E in RB; unknown pathological significance. 1 Publication
    VAR_010045
    Natural varianti358 – 3581R → G in RB. 1 Publication
    VAR_010046
    Natural varianti358 – 3581R → Q in RB.
    VAR_005575
    Natural varianti436 – 4361Q → K.1 Publication
    Corresponds to variant rs4151534 [ dbSNP | Ensembl ].
    VAR_019379
    Natural varianti447 – 4471K → Q in RB. 1 Publication
    VAR_010048
    Natural varianti457 – 4571M → R in RB. 1 Publication
    VAR_005576
    Natural varianti480 – 4801Missing in RB; mild form. 1 Publication
    VAR_005577
    Natural varianti500 – 5001R → G in RB. 1 Publication
    VAR_011580
    Natural varianti525 – 5251A → G.1 Publication
    Corresponds to variant rs4151539 [ dbSNP | Ensembl ].
    VAR_019380
    Natural varianti530 – 5301K → R in RB. 1 Publication
    VAR_010049
    Natural varianti549 – 5491H → Y in RB. 1 Publication
    VAR_005578
    Natural varianti567 – 5671S → L in RB. 2 Publications
    VAR_005579
    Natural varianti569 – 5691L → F.
    Corresponds to variant rs3092895 [ dbSNP | Ensembl ].
    VAR_051910
    Natural varianti616 – 6161K → E in RB. 1 Publication
    VAR_011581
    Natural varianti635 – 6351A → P in RB. 1 Publication
    VAR_005580
    Natural varianti654 – 6541V → E in RB. 1 Publication
    VAR_005581
    Natural varianti657 – 6571L → P in RB. 1 Publication
    VAR_010050
    Natural varianti661 – 6611R → W in RB; mild form. 4 Publications
    VAR_005582
    Natural varianti662 – 6621L → P in RB. 1 Publication
    VAR_005583
    Natural varianti673 – 6731H → P in RB.
    VAR_005584
    Natural varianti685 – 6851Q → P in RB. 1 Publication
    VAR_005585
    Natural varianti697 – 6971D → E.
    Corresponds to variant rs3092903 [ dbSNP | Ensembl ].
    VAR_051911
    Natural varianti706 – 7061C → Y in RB.
    VAR_005586
    Natural varianti712 – 7121C → R in RB. 1 Publication
    VAR_005587
    Natural varianti746 – 7461E → G.
    Corresponds to variant rs3092905 [ dbSNP | Ensembl ].
    VAR_034442
    Natural varianti803 – 8031N → K in RB. 1 Publication
    VAR_005588

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15400 mRNA. Translation: AAA69807.1. Sequence problems.
    M28419 mRNA. Translation: AAA69808.1.
    M33647 mRNA. Translation: AAA69806.1.
    L41870 mRNA. Translation: AAB59465.1.
    M27866
    , M27845, M27846, M27847, M27849, M27850, M27851, L35146, M27852, M27853, M27854, M27855, M27856, M27857, M27858, M27859, M27860, L35147, M27862, M27863, M27864, M27865 Genomic DNA. Translation: AAA53484.1.
    L41889 Genomic DNA. Translation: AAB59467.1.
    L41890 Genomic DNA. Translation: AAA65735.1.
    L41891 Genomic DNA. Translation: AAA65736.1.
    L41893 Genomic DNA. Translation: AAA65737.1.
    L41894 Genomic DNA. Translation: AAA65738.1.
    L41895 Genomic DNA. Translation: AAA65739.1.
    L41896 Genomic DNA. Translation: AAA65740.1.
    L41897 Genomic DNA. Translation: AAA65741.1.
    L41898 Genomic DNA. Translation: AAB59471.1.
    L41899 Genomic DNA. Translation: AAB59473.1.
    L41997 Genomic DNA. Translation: AAB59482.1.
    X16439 Genomic DNA. Translation: CAA34462.1.
    AF551763 Genomic DNA. Translation: AAN64133.1.
    AK291258 mRNA. Translation: BAF83947.1.
    AL136960, AL392048 Genomic DNA. Translation: CAH70901.1.
    AL392048, AL136960 Genomic DNA. Translation: CAH72243.1.
    CH471075 Genomic DNA. Translation: EAX08793.1.
    BC039060 mRNA. Translation: AAH39060.1.
    BC040540 mRNA. Translation: AAH40540.1.
    L11910 Genomic DNA. Translation: AAA53483.1.
    CCDSiCCDS31973.1.
    PIRiJS0276. RBHU.
    RefSeqiNP_000312.2. NM_000321.2.
    UniGeneiHs.408528.

    Genome annotation databases

    EnsembliENST00000267163; ENSP00000267163; ENSG00000139687.
    GeneIDi5925.
    KEGGihsa:5925.
    UCSCiuc001vcb.3. human.

    Polymorphism databases

    DMDMi132164.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    RB1base

    RB1 mutation db

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs
    Wikipedia

    Retinoblastoma protein entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15400 mRNA. Translation: AAA69807.1 . Sequence problems.
    M28419 mRNA. Translation: AAA69808.1 .
    M33647 mRNA. Translation: AAA69806.1 .
    L41870 mRNA. Translation: AAB59465.1 .
    M27866
    , M27845 , M27846 , M27847 , M27849 , M27850 , M27851 , L35146 , M27852 , M27853 , M27854 , M27855 , M27856 , M27857 , M27858 , M27859 , M27860 , L35147 , M27862 , M27863 , M27864 , M27865 Genomic DNA. Translation: AAA53484.1 .
    L41889 Genomic DNA. Translation: AAB59467.1 .
    L41890 Genomic DNA. Translation: AAA65735.1 .
    L41891 Genomic DNA. Translation: AAA65736.1 .
    L41893 Genomic DNA. Translation: AAA65737.1 .
    L41894 Genomic DNA. Translation: AAA65738.1 .
    L41895 Genomic DNA. Translation: AAA65739.1 .
    L41896 Genomic DNA. Translation: AAA65740.1 .
    L41897 Genomic DNA. Translation: AAA65741.1 .
    L41898 Genomic DNA. Translation: AAB59471.1 .
    L41899 Genomic DNA. Translation: AAB59473.1 .
    L41997 Genomic DNA. Translation: AAB59482.1 .
    X16439 Genomic DNA. Translation: CAA34462.1 .
    AF551763 Genomic DNA. Translation: AAN64133.1 .
    AK291258 mRNA. Translation: BAF83947.1 .
    AL136960 , AL392048 Genomic DNA. Translation: CAH70901.1 .
    AL392048 , AL136960 Genomic DNA. Translation: CAH72243.1 .
    CH471075 Genomic DNA. Translation: EAX08793.1 .
    BC039060 mRNA. Translation: AAH39060.1 .
    BC040540 mRNA. Translation: AAH40540.1 .
    L11910 Genomic DNA. Translation: AAA53483.1 .
    CCDSi CCDS31973.1.
    PIRi JS0276. RBHU.
    RefSeqi NP_000312.2. NM_000321.2.
    UniGenei Hs.408528.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AD6 X-ray 2.30 A 378-562 [» ]
    1GH6 X-ray 3.20 B 379-577 [» ]
    B 645-772 [» ]
    1GUX X-ray 1.85 A 372-589 [» ]
    B 636-787 [» ]
    1H25 X-ray 2.50 E 868-878 [» ]
    1N4M X-ray 2.20 A/B 380-785 [» ]
    1O9K X-ray 2.60 A/C/E/G 372-589 [» ]
    B/D/F/H 636-787 [» ]
    1PJM X-ray 2.50 A 858-881 [» ]
    2AZE X-ray 2.55 C 829-874 [» ]
    2QDJ X-ray 2.00 A 52-355 [» ]
    2R7G X-ray 1.67 A/C 380-787 [» ]
    3N5U X-ray 3.20 C 870-882 [» ]
    3POM X-ray 2.50 A/B 380-577 [» ]
    A/B 643-783 [» ]
    4ELJ X-ray 2.70 A 53-787 [» ]
    4ELL X-ray 1.98 A/B 380-787 [» ]
    ProteinModelPortali P06400.
    SMRi P06400. Positions 53-786, 829-872.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111860. 206 interactions.
    DIPi DIP-582N.
    IntActi P06400. 85 interactions.
    MINTi MINT-98847.
    STRINGi 9606.ENSP00000267163.

    Chemistry

    BindingDBi P06400.
    ChEMBLi CHEMBL5288.
    DrugBanki DB00047. Insulin Glargine recombinant.
    DB00046. Insulin Lyspro recombinant.
    DB00030. Insulin recombinant.
    DB00071. Insulin, porcine.

    PTM databases

    PhosphoSitei P06400.

    Polymorphism databases

    DMDMi 132164.

    Proteomic databases

    MaxQBi P06400.
    PaxDbi P06400.
    PeptideAtlasi P06400.
    PRIDEi P06400.

    Protocols and materials databases

    DNASUi 5925.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267163 ; ENSP00000267163 ; ENSG00000139687 .
    GeneIDi 5925.
    KEGGi hsa:5925.
    UCSCi uc001vcb.3. human.

    Organism-specific databases

    CTDi 5925.
    GeneCardsi GC13P048877.
    GeneReviewsi RB1.
    HGNCi HGNC:9884. RB1.
    HPAi CAB000095.
    CAB016687.
    MIMi 109800. phenotype.
    180200. phenotype.
    259500. phenotype.
    614041. gene.
    neXtProti NX_P06400.
    Orphaneti 357027. Familial retinoblastoma.
    1587. Monosomy 13q14.
    357034. Unilateral retinoblastoma.
    PharmGKBi PA295.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296920.
    HOVERGENi HBG008967.
    InParanoidi P06400.
    KOi K06618.
    OMAi TNILQYA.
    OrthoDBi EOG7P5T04.
    PhylomeDBi P06400.
    TreeFami TF105568.

    Enzyme and pathway databases

    Reactomei REACT_1156. Orc1 removal from chromatin.
    REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_821. Cyclin D associated events in G1.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinki P06400.

    Miscellaneous databases

    ChiTaRSi RB1. human.
    EvolutionaryTracei P06400.
    GeneWikii Retinoblastoma_protein.
    GenomeRNAii 5925.
    NextBioi 23076.
    PMAP-CutDB P06400.
    PROi P06400.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06400.
    Bgeei P06400.
    CleanExi HS_RB1.
    Genevestigatori P06400.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view ]
    PANTHERi PTHR13742. PTHR13742. 1 hit.
    Pfami PF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    PF08934. Rb_C. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNA binding activity."
      Lee W.-H., Shew J.-Y., Hong F.D., Sery T.W., Donoso L.A., Young L.-J.S., Bookstein R., Lee E.Y.-H.P.
      Nature 329:642-645(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human retinoblastoma susceptibility gene: cloning, identification, and sequence."
      Lee W.-H., Bookstein R., Hong F.D., Young L.-J., Shew J.-Y., Lee E.Y.-H.P.
      Science 235:1394-1399(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Deletions of a DNA sequence in retinoblastomas and mesenchymal tumors: organization of the sequence and its encoded protein."
      Friend S.H., Horowitz J.M., Gerber M.R., Wang X.-F., Bogenmann E., Li F.P., Weinberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 84:9059-9063(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structure and partial genomic sequence of the human retinoblastoma susceptibility gene."
      McGee T.L., Yandell D.W., Dryja T.P.
      Gene 80:119-128(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Detection of heterozygous mutations in the RB1 gene in retinoblastoma patients using single-strand conformation polymorphism analysis and polymerase chain reaction sequencing."
      Hogg A., Onadim Z., Baird P.N., Cowell J.K.
      Oncogene 7:1445-1451(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Carcinoma.
    6. "Complete genomic sequence of the human retinoblastoma susceptibility gene."
      Toguchida J., McGee T.L., Paterson J.C., Eagle J.R., Tucker S., Yandell D.W., Dryja T.P.
      Genomics 17:535-543(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. NIEHS SNPs program
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-436 AND GLY-525.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix and Testis.
    12. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
    13. "Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma gene product."
      Chellappan S., Kraus V.B., Kroger B., Munger K., Howley P.M., Phelps W.C., Nevins J.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:4549-4553(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN AND HPV E7 PROTEIN.
    14. "Spectrum of small length germline mutations in the RB1 gene."
      Lohmann D.R., Brandt B., Hopping W., Passarge E., Horsthemke B.
      Hum. Mol. Genet. 3:2187-2193(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 47-65, INVOLVEMENT IN RETINOBLASTOMA.
    15. "Identification of G1 kinase activity for cdk6, a novel cyclin D partner."
      Meyerson M., Harlow E.
      Mol. Cell. Biol. 14:2077-2086(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDK6.
    16. "SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene."
      Decaprio J.A., Ludlow J.W., Figge J., Shew J.-Y., Huang C.-M., Lee W.-H., Marsilio E., Paucha E., Livingston D.M.
      Cell 54:275-283(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
    17. "Molecular mechanism of retinoblastoma gene inactivation in retinoblastoma cell line Y79."
      Lee E.Y.-H.P., Bookstein R., Young L.-J., Lin C.-J., Rosenfeld M.G., Lee W.-H.
      Proc. Natl. Acad. Sci. U.S.A. 85:6017-6021(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RETINOBLASTOMA.
    18. "The retinoblastoma protein is phosphorylated on multiple sites by human cdc2."
      Lees J.A., Buchkovich K.J., Marshak D.R., Anderson C.W., Harlow E.
      EMBO J. 10:4279-4290(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-249; THR-252; THR-373; SER-807 AND SER-811.
    19. "Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
      Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
      Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5A AND ARID4A.
    20. "The amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing."
      Durfee T., Mancini M.A., Jones D., Elledge S.J., Lee W.H.
      J. Cell Biol. 127:609-622(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THOC1.
    21. "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein."
      Kim Y.W., Otterson G.A., Kratzke R.A., Coxon A.B., Kaye F.J.
      Mol. Cell. Biol. 14:7256-7264(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5A.
    22. "The human cytomegalovirus IE1-72 protein interacts with the cellular p107 protein and relieves p107-mediated transcriptional repression of an E2F-responsive promoter."
      Poma E.E., Kowalik T.F., Zhu L., Sinclair J.H., Huang E.S.
      J. Virol. 70:7867-7877(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
    23. "Bdp, a new member of a family of DNA-binding proteins, associates with the retinoblastoma gene product."
      Numata S., Claudio P.P., Dean C., Giordano A., Croce C.M.
      Cancer Res. 59:3741-3747(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARID3B.
    24. "Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1."
      Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.
      Cell 98:859-869(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-567 BY CDK2, PHOSPHORYLATION BY CDK4 AND CDK6.
    25. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
      Zheng L., Chen Y., Lee W.-H.
      Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    26. "Retinoblastoma protein enhances the fidelity of chromosome segregation mediated by hsHec1p."
      Zheng L., Chen Y., Riley D.J., Chen P.-L., Lee W.-H.
      Mol. Cell. Biol. 20:3529-3537(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    27. "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250."
      Siegert J.L., Robbins P.D.
      Mol. Cell. Biol. 19:846-854(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAF1.
    28. "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F."
      Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., Medema R., Vignais M.-L., Sardet C.
      Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E4F1.
    29. "Identification and characterization of a novel human cDNA encoding a 21 kDa pRb-associated protein."
      Wen H., Ao S.
      Gene 263:85-92(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EID1.
    30. "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters."
      Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.
      Nat. Genet. 25:338-342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT1.
    31. Cited for: INTERACTION WITH SUV39H1.
    32. "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein."
      DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T., Pagano M., Loda M.
      Oncogene 20:5538-5542(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP4.
    33. Cited for: INTERACTION WITH AATF.
    34. "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein."
      Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.
      Mol. Biol. Cell 13:4401-4413(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMPO-ALPHA AND LMNA.
    35. "Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity."
      Prathapam T., Kuhne C., Banks L.
      Nucleic Acids Res. 30:5261-5268(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNW1.
    36. "Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein."
      Balasenthil S., Vadlamudi R.K.
      J. Biol. Chem. 278:22119-22127(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELP1.
    37. "Cyclin C/cdk3 promotes Rb-dependent G0 exit."
      Ren S., Rollins B.J.
      Cell 117:239-251(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G0-G1 TRANSITION, PHOSPHORYLATION AT SER-807 AND SER-811 BY CDK3.
    38. "Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein."
      Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R., Gaubatz S.
      EMBO J. 23:4627-4638(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIN9.
    39. "LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription."
      Sharp T.V., Munoz F., Bourboulia D., Presneau N., Darai E., Wang H.-W., Cannon M., Butcher D.N., Nicholson A.G., Klein G., Imreh S., Boshoff C.
      Proc. Natl. Acad. Sci. U.S.A. 101:16531-16536(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIMD1.
    40. "Preferences for phosphorylation sites in the retinoblastoma protein of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro."
      Takaki T., Fukasawa K., Suzuki-Takahashi I., Semba K., Kitagawa M., Taya Y., Hirai H.
      J. Biochem. 137:381-386(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-821 AND THR-826.
    41. "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
      Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
      J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM4A.
    42. "Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas."
      Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T.
      Mod. Pathol. 18:1249-1257(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5B.
    43. "Binding of pRB to the PHD protein RBP2 promotes cellular differentiation."
      Benevolenskaya E.V., Murray H.L., Branton P., Young R.A., Kaelin W.G. Jr.
      Mol. Cell 18:623-635(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5A.
    44. "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein."
      Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X.
      Mol. Cell 20:699-708(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMA3.
    45. Cited for: INTERACTION WITH ZUBR1.
    46. "Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells."
      Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M., Vogt T.
      J. Invest. Dermatol. 126:1850-1859(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDM5B.
    47. "Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB and E2F-1 after DNA damage."
      Inoue Y., Kitagawa M., Taya Y.
      EMBO J. 26:2083-2093(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-612 BY CHEK2, INTERACTION WITH CHEK2.
    48. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252 AND THR-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    49. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-252; SER-612; SER-807; SER-811; THR-823 AND THR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    50. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    51. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-373; SER-807 AND THR-841, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    52. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    53. Cited for: METHYLATION AT LYS-860, INTERACTION WITH L3MBTL1, MUTAGENESIS OF LYS-860; LYS-870 AND 873-LYS-LYS-874.
    54. "Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation."
      Pickard A., Wong P.P., McCance D.J.
      J. Cell Sci. 123:3718-3726(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-873 AND LYS-874, SUBCELLULAR LOCATION, MUTAGENESIS OF 873-LYS--LYS-874.
    55. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-821 AND THR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    56. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    57. "NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
      Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
      Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UHRF2.
    58. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    59. "RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation."
      Cho H.S., Hayami S., Toyokawa G., Maejima K., Yamane Y., Suzuki T., Dohmae N., Kogure M., Kang D., Neal D.E., Ponder B.A., Yamaue H., Nakamura Y., Hamamoto R.
      Neoplasia 14:476-486(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-810 BY SMYD2.
    60. "Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box."
      Kim H.Y., Cho Y.
      Nat. Struct. Biol. 4:390-395(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 378-562.
    61. "Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7."
      Lee J.O., Russo A.A., Pavletich N.P.
      Nature 391:859-865(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 380-785.
    62. "Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha."
      Fontes M.R.M., Teh T., Jans D., Brinkworth R.I., Kobe B.
      J. Biol. Chem. 278:27981-27987(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 860-876 IN COMPLEX WITH KPNA2.
    63. "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release."
      Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.
      Cell 123:1093-1106(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 829-874 IN COMPLEX WITH E2F1 AND TFDP1, INTERACTION WITH HETERODIMERIC COMPLEXES CONTAINING TFDP1 AND EITHER E2F1; E2F3; E2F4 OR E2F5, MUTAGENESIS OF THR-821 AND THR-826, PHOSPHORYLATION AT THR-821 AND THR-826.
    64. "Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor."
      Liu X., Marmorstein R.
      Genes Dev. 21:2711-2716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 380-787 IN COMPLEX WITH HUMAN ADENOVIRUS E1A PROTEIN.
    65. "Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture."
      Hassler M., Singh S., Yue W.W., Luczynski M., Lakbir R., Sanchez-Sanchez F., Bader T., Pearl L.H., Mittnacht S.
      Mol. Cell 28:371-385(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-355, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THOC1 AND GRIP1, INTERACTION OF THE UNPHOSPHORYLATED PROTEIN WITH EID1.
    66. "Oncogenic point mutations in the human retinoblastoma gene: their application to genetic counseling."
      Yandell D.W., Campbell T.A., Dayton S.H., Petersen R., Walton D., Little J.B., McConkie-Rosell A., Buckley E., Dryja T.P.
      N. Engl. J. Med. 321:1689-1695(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RB LEU-567.
    67. "Oncogenic point mutations in exon 20 of the RB1 gene in families showing incomplete penetrance and mild expression of the retinoblastoma phenotype."
      Onadim Z., Hogg A., Baird P.N., Cowell J.K.
      Proc. Natl. Acad. Sci. U.S.A. 89:6177-6181(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RB TRP-661.
    68. "Molecular mechanisms of oncogenic mutations in tumors from patients with bilateral and unilateral retinoblastoma."
      Hogg A., Bia B., Onadim Z., Cowell J.K.
      Proc. Natl. Acad. Sci. U.S.A. 90:7351-7355(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RB ARG-457.
    69. "Frequent constitutional C to T mutations in CGA-arginine codons in the RB1 gene produce premature stop codons in patients with bilateral (hereditary) retinoblastoma."
      Cowell J.K., Smith T., Bia B.
      Eur. J. Hum. Genet. 2:281-290(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RB ARG-530.
    70. "Distinct RB1 gene mutations with low penetrance in hereditary retinoblastoma."
      Lohmann D.R., Brandt B., Hoepping W., Passarge E., Horsthemke B.
      Hum. Genet. 94:349-354(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB ASN-480 DEL AND TRP-661.
    71. "Germline mutations in the RB1 gene in patients with hereditary retinoblastoma."
      Liu Z., Song Y., Bia B., Cowell J.K.
      Genes Chromosomes Cancer 14:277-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB GLN-72; TYR-549 AND LYS-803.
    72. "Spectrum of germline mutations in the RB1 gene: a study of 232 patients with hereditary and non hereditary retinoblastoma."
      Blanquet V., Turleau C., Gross-Morand M.S., Senamaud-Beaufort C., Doz F., Besmond C.
      Hum. Mol. Genet. 4:383-388(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB THR-185; PRO-635; GLU-654 AND PRO-685.
    73. "Mutational scanning of large genes by extensive PCR multiplexing and two-dimensional electrophoresis: application to the RB1 gene."
      Van Orsouw N.J., Li D., van der Vlies P., Scheffer H., Eng C., Buys C.H.C.M., Li F.P., Vijg J.
      Hum. Mol. Genet. 5:755-761(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB GLY-358; PRO-657 AND TRP-661.
    74. "Constitutional RB1-gene mutations in patients with isolated unilateral retinoblastoma."
      Lohmann D.R., Gerick M., Brandt B., Oelschlaeger U., Lorenz B., Passarge E., Horsthemke B.
      Am. J. Hum. Genet. 61:282-294(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB ASP-137 AND TRP-661.
    75. Cited for: VARIANT RB GLN-447.
    76. "Twelve novel RB1 gene mutations in patients with hereditary retinoblastoma."
      Yilmaz S., Horsthemke B., Lohmann D.R.
      Hum. Mutat. 12:434-434(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB LEU-567; PRO-662 AND ARG-712.
    77. "RB1 gene mutations in peripheral blood DNA of patients with isolated unilateral retinoblastoma."
      Klutz M., Horsthemke B., Lohmann D.R.
      Am. J. Hum. Genet. 64:667-668(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RB GLU-310.
    78. "Identification of four novel RB1 germline mutations in Korean retinoblastoma patients."
      Yu Y.S., Kim I.-J., Ku J.-L., Park J.-G.
      Hum. Mutat. 18:252-252(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS RB GLY-500 AND GLU-616.
    79. Cited for: VARIANT HIS-173.

    Entry informationi

    Entry nameiRB_HUMAN
    AccessioniPrimary (citable) accession number: P06400
    Secondary accession number(s): A8K5E3
    , P78499, Q5VW46, Q8IZL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 199 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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