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P06400 (RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoblastoma-associated protein
Alternative name(s):
p105-Rb
pRb
Short name=Rb
pp110
Gene names
Name:RB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.37

Subunit structure

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. Ref.13 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.53 Ref.57 Ref.63 Ref.65

Subcellular location

Nucleus Ref.54.

Tissue specificity

Expressed in the retina.

Domain

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

Post-translational modification

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. Ref.15 Ref.18 Ref.24 Ref.37 Ref.40 Ref.47 Ref.63

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. Ref.53 Ref.59

Acetylation at Lys-873 and Lys-874 regulates subcellular localization, at least during keratinocytes differentiation. Ref.54

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78

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.

Sequence similarities

Belongs to the retinoblastoma protein (RB) family.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Proto-oncogene
   LigandDNA-binding
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Ras protein signal transduction

Inferred from expression pattern PubMed 9054499. Source: BHF-UCL

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cell cycle arrest

Traceable author statement PubMed 19149898. Source: BHF-UCL

cell cycle checkpoint

Traceable author statement PubMed 10825186. Source: ProtInc

cell morphogenesis involved in neuron differentiation

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Traceable author statement PubMed 19149898. Source: BHF-UCL

digestive tract development

Inferred from electronic annotation. Source: Ensembl

enucleate erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

maintenance of mitotic sister chromatid cohesion

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Traceable author statement PubMed 9529249. Source: BHF-UCL

myoblast differentiation

Inferred from mutant phenotype PubMed 15541338. Source: UniProtKB

negative regulation of G1/S transition of mitotic cell cycle

Traceable author statement PubMed 19149898. Source: BHF-UCL

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from physical interaction Ref.27. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 9529249. Source: BHF-UCL

negative regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter during mitosis

Traceable author statement PubMed 19149898. Source: BHF-UCL

negative regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10783144PubMed 19223331. Source: UniProtKB

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neuron maturation

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic metaphase/anaphase transition

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

protein localization to chromosome, centromeric region

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

regulation of centromere complex assembly

Traceable author statement PubMed 20551165. Source: BHF-UCL

regulation of cohesin localization to chromatin

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

regulation of lipid kinase activity

Inferred from direct assay PubMed 16286473. Source: UniProtKB

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

regulation of transcription involved in G1/S transition of mitotic cell cycle

Traceable author statement PubMed 19149898. Source: BHF-UCL

sister chromatid biorientation

Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay PubMed 9448006. Source: UniProtKB

Rb-E2F complex

Traceable author statement PubMed 19149898. Source: BHF-UCL

SWI/SNF complex

Traceable author statement PubMed 19149898. Source: BHF-UCL

chromatin

Traceable author statement Ref.1. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17540172. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 15735762. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.63PubMed 8288605. Source: IntAct

kinase binding

Inferred from direct assay PubMed 16286473. Source: UniProtKB

phosphoprotein binding

Inferred from physical interaction Ref.63. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.63PubMed 19223331. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 10944455. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 928927Retinoblastoma-associated protein
PRO_0000167836

Regions

Region373 – 771399Pocket; binds T and E1A
Region373 – 579207Domain A
Region580 – 63960Spacer
Region640 – 771132Domain B
Region763 – 928166Interaction with LIMD1
Region771 – 928158Domain C; mediates interaction with E4F1
Motif870 – 8767Nuclear localization signal Probable
Compositional bias10 – 189Poly-Ala
Compositional bias20 – 2910Poly-Pro

Amino acid modifications

Modified residue21N,N-dimethylproline By similarity
Modified residue371Phosphoserine Ref.49 Ref.51
Modified residue2491Phosphoserine; by CDK1 Ref.18 Ref.48 Ref.49 Ref.51 Ref.58
Modified residue2521Phosphothreonine; by CDK1 Ref.18 Ref.48 Ref.49
Modified residue3561Phosphothreonine Ref.48
Modified residue3731Phosphothreonine; by CDK1 Ref.18 Ref.51
Modified residue5671Phosphoserine; by CDK2 Ref.24
Modified residue6121Phosphoserine; by CHEK2 and CHEK1 Ref.47 Ref.49
Modified residue7951Phosphoserine By similarity
Modified residue8071Phosphoserine; by CDK1 and CDK3 Ref.18 Ref.37 Ref.49 Ref.51
Modified residue8101N6-methyllysine; by SMYD2 Ref.59
Modified residue8111Phosphoserine; by CDK1 and CDK3 Ref.18 Ref.37 Ref.49
Modified residue8211Phosphothreonine; by CDK6 Ref.40 Ref.55 Ref.63
Modified residue8231Phosphothreonine Ref.49
Modified residue8261Phosphothreonine; by CDK4 Ref.40 Ref.49 Ref.55 Ref.63
Modified residue8411Phosphothreonine Ref.51
Modified residue8601N6-methyllysine; by SMYD2 Ref.53
Modified residue8731N6-acetyllysine; by PCAF Ref.54
Modified residue8741N6-acetyllysine; by PCAF Ref.54

Natural variations

Natural variant721E → Q in RB. Ref.71
VAR_005572
Natural variant1331N → H.
Corresponds to variant rs3092900 [ dbSNP | Ensembl ].
VAR_051909
Natural variant1371E → D in RB; unilateral form. Ref.74
VAR_005573
Natural variant1731Y → H. Ref.79
VAR_069376
Natural variant1851I → T in RB. Ref.72
VAR_005574
Natural variant3101G → E in RB; unknown pathological significance. Ref.77
VAR_010045
Natural variant3581R → G in RB. Ref.73
VAR_010046
Natural variant3581R → Q in RB.
VAR_005575
Natural variant4361Q → K. Ref.7
Corresponds to variant rs4151534 [ dbSNP | Ensembl ].
VAR_019379
Natural variant4471K → Q in RB. Ref.75
VAR_010048
Natural variant4571M → R in RB. Ref.68
VAR_005576
Natural variant4801Missing in RB; mild form. Ref.70
VAR_005577
Natural variant5001R → G in RB. Ref.78
VAR_011580
Natural variant5251A → G. Ref.7
Corresponds to variant rs4151539 [ dbSNP | Ensembl ].
VAR_019380
Natural variant5301K → R in RB. Ref.69
VAR_010049
Natural variant5491H → Y in RB. Ref.71
VAR_005578
Natural variant5671S → L in RB. Ref.66 Ref.76
VAR_005579
Natural variant5691L → F.
Corresponds to variant rs3092895 [ dbSNP | Ensembl ].
VAR_051910
Natural variant6161K → E in RB. Ref.78
VAR_011581
Natural variant6351A → P in RB. Ref.72
VAR_005580
Natural variant6541V → E in RB. Ref.72
VAR_005581
Natural variant6571L → P in RB. Ref.73
VAR_010050
Natural variant6611R → W in RB; mild form. Ref.67 Ref.70 Ref.73 Ref.74
VAR_005582
Natural variant6621L → P in RB. Ref.76
VAR_005583
Natural variant6731H → P in RB.
VAR_005584
Natural variant6851Q → P in RB. Ref.72
VAR_005585
Natural variant6971D → E.
Corresponds to variant rs3092903 [ dbSNP | Ensembl ].
VAR_051911
Natural variant7061C → Y in RB.
VAR_005586
Natural variant7121C → R in RB. Ref.76
VAR_005587
Natural variant7461E → G.
Corresponds to variant rs3092905 [ dbSNP | Ensembl ].
VAR_034442
Natural variant8031N → K in RB. Ref.71
VAR_005588

Experimental info

Mutagenesis8211T → A: Abolishes interaction with Pocket domain; when associated with A-826. Ref.63
Mutagenesis8261T → A: Abolishes interaction with Pocket domain; when associated with A-821. Ref.63
Mutagenesis8601K → R: Abolishes monomethylation by SMYD2 and subsequent interaction with L3MBTL1. Ref.53
Mutagenesis8701K → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. Ref.53
Mutagenesis873 – 8742KK → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. Ref.54
Mutagenesis873 – 8742KK → RR: Does not alter Rb localization in cycling cells, but mislocalizes to the cytoplasm during keratinocytes differentiation. Ref.54
Sequence conflict500 – 5012RS → SN in AAN64133. Ref.7

Secondary structure

......................................................................................................... 928
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06400 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: C8E746111E19CC32

FASTA928106,159
        10         20         30         40         50         60 
MPPKTPRKTA ATAAAAAAEP PAPPPPPPPE EDPEQDSGPE DLPLVRLEFE ETEEPDFTAL 

        70         80         90        100        110        120 
CQKLKIPDHV RERAWLTWEK VSSVDGVLGG YIQKKKELWG ICIFIAAVDL DEMSFTFTEL 

       130        140        150        160        170        180 
QKNIEISVHK FFNLLKEIDT STKVDNAMSR LLKKYDVLFA LFSKLERTCE LIYLTQPSSS 

       190        200        210        220        230        240 
ISTEINSALV LKVSWITFLL AKGEVLQMED DLVISFQLML CVLDYFIKLS PPMLLKEPYK 

       250        260        270        280        290        300 
TAVIPINGSP RTPRRGQNRS ARIAKQLEND TRIIEVLCKE HECNIDEVKN VYFKNFIPFM 

       310        320        330        340        350        360 
NSLGLVTSNG LPEVENLSKR YEEIYLKNKD LDARLFLDHD KTLQTDSIDS FETQRTPRKS 

       370        380        390        400        410        420 
NLDEEVNVIP PHTPVRTVMN TIQQLMMILN SASDQPSENL ISYFNNCTVN PKESILKRVK 

       430        440        450        460        470        480 
DIGYIFKEKF AKAVGQGCVE IGSQRYKLGV RLYYRVMESM LKSEEERLSI QNFSKLLNDN 

       490        500        510        520        530        540 
IFHMSLLACA LEVVMATYSR STSQNLDSGT DLSFPWILNV LNLKAFDFYK VIESFIKAEG 

       550        560        570        580        590        600 
NLTREMIKHL ERCEHRIMES LAWLSDSPLF DLIKQSKDRE GPTDHLESAC PLNLPLQNNH 

       610        620        630        640        650        660 
TAADMYLSPV RSPKKKGSTT RVNSTANAET QATSAFQTQK PLKSTSLSLF YKKVYRLAYL 

       670        680        690        700        710        720 
RLNTLCERLL SEHPELEHII WTLFQHTLQN EYELMRDRHL DQIMMCSMYG ICKVKNIDLK 

       730        740        750        760        770        780 
FKIIVTAYKD LPHAVQETFK RVLIKEEEYD SIIVFYNSVF MQRLKTNILQ YASTRPPTLS 

       790        800        810        820        830        840 
PIPHIPRSPY KFPSSPLRIP GGNIYISPLK SPYKISEGLP TPTKMTPRSR ILVSIGESFG 

       850        860        870        880        890        900 
TSEKFQKINQ MVCNSDRVLK RSAEGSNPPK PLKKLRFDIE GSDEADGSKH LPGESKFQQK 

       910        920 
LAEMTSTRTR MQKQKMNDSM DTSNKEEK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Genomic organization of the human retinoblastoma gene."
T'Ang A., Wu K.J., Hashimoto T., Liu W.Y., Takahashi R., Shi X.H., Mihara K., Zhang F.H., Chen Y.Y., Du C., Qian J., Lin Y.G., Murphree A.L., Qiu W.R., Thompson T., Benedict W.F., Fung Y.K.T.
Oncogene 4:401-407(1989) [PubMed] [Europe PMC] [Abstract]
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]"Rb targets histone H3 methylation and HP1 to promoters."
Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A., O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E., Kouzarides T.
Nature 412:561-565(2001) [PubMed] [Europe PMC] [Abstract]
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]"Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb."
Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S., Floridi A., Passananti C., Fanciulli M.
Cancer Cell 2:387-399(2002) [PubMed] [Europe PMC] [Abstract]
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]"p600, a unique protein required for membrane morphogenesis and cell survival."
Nakatani Y., Konishi H., Vassilev A., Kurooka H., Ishiguro K., Sawada J., Ikura T., Korsmeyer S.J., Qin J., Herlitz A.M.
Proc. Natl. Acad. Sci. U.S.A. 102:15093-15098(2005) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Methylation of the retinoblastoma tumor suppressor by SMYD2."
Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M., Gozani O., Sage J.
J. Biol. Chem. 285:37733-37740(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Genetics of retinoblastoma: a study."
Mateu E., Sanchez F., Najera C., Beneyto M., Castell V., Hernandez M., Serra I., Prieto F.
Cancer Genet. Cytogenet. 95:40-50(1997) [PubMed] [Europe PMC] [Abstract]
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]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15400 mRNA. Translation: AAA69807.1. Sequence problems.
M28419 mRNA. Translation: AAA69808.1.
M33647 mRNA. Translation: AAA69806.1.
L41870 mRNA. Translation: AAB59465.1.
M27866 expand/collapse EMBL AC list , 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.
PIRRBHU. JS0276.
RefSeqNP_000312.2. NM_000321.2.
UniGeneHs.408528.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD6X-ray2.30A378-562[»]
1GH6X-ray3.20B379-772[»]
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-ray2.50A860-876[»]
2AZEX-ray2.55C829-874[»]
2QDJX-ray2.00A52-355[»]
2R7GX-ray1.67A/C380-787[»]
3N5UX-ray3.20C870-882[»]
3POMX-ray2.50A/B380-787[»]
4ELJX-ray2.70A53-787[»]
4ELLX-ray1.98A/B380-787[»]
ProteinModelPortalP06400.
SMRP06400. Positions 53-786, 829-872.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111860. 205 interactions.
DIPDIP-582N.
IntActP06400. 84 interactions.
MINTMINT-98847.
STRING9606.ENSP00000267163.

Chemistry

BindingDBP06400.
ChEMBLCHEMBL5288.
DrugBankDB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.

PTM databases

PhosphoSiteP06400.

Polymorphism databases

DMDM132164.

Proteomic databases

PaxDbP06400.
PeptideAtlasP06400.
PRIDEP06400.

Protocols and materials databases

DNASU5925.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267163; ENSP00000267163; ENSG00000139687.
GeneID5925.
KEGGhsa:5925.
UCSCuc001vcb.3. human.

Organism-specific databases

CTD5925.
GeneCardsGC13P048877.
HGNCHGNC:9884. RB1.
HPACAB000095.
CAB016687.
MIM109800. phenotype.
180200. phenotype.
259500. phenotype.
614041. gene.
neXtProtNX_P06400.
Orphanet357027. Familial retinoblastoma.
357034. Unilateral retinoblastoma.
PharmGKBPA295.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296920.
HOVERGENHBG008967.
InParanoidP06400.
KOK06618.
OMATNILQYA.
OrthoDBEOG7P5T04.
PhylomeDBP06400.
TreeFamTF105568.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
SignaLinkP06400.

Gene expression databases

ArrayExpressP06400.
BgeeP06400.
CleanExHS_RB1.
GenevestigatorP06400.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR015652. RB1.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF11. PTHR13742:SF11. 1 hit.
PfamPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

ChiTaRSRB1. human.
EvolutionaryTraceP06400.
GeneWikiRetinoblastoma_protein.
GenomeRNAi5925.
NextBio23076.
PMAP-CutDBP06400.
PROP06400.
SOURCESearch...

Entry information

Entry nameRB_HUMAN
AccessionPrimary (citable) accession number: P06400
Secondary accession number(s): A8K5E3 expand/collapse secondary AC list , P78499, Q5VW46, Q8IZL4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 194 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM