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Reviewed, UniProtKB/Swiss-Prot P06400 (RB_HUMAN)

Last modified February 9, 2010. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Retinoblastoma-associated protein
Alternative name(s):
    pRb
      Short name=Rb
    pp110
    p105-Rb
Gene names
Name: RB1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Key regulator of entry into cell division that acts as a tumor suppressor. 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.

Subunit structure

Interacts with ATAD5 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 AATF, DNMT1, LIN9, LMNA, SUV420H1, SUV420H2, PELP1 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. Ref.13 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 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.50 Ref.52

Subcellular location

Nucleus.

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 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. Ref.50 Ref.17 Ref.41 Ref.42 Ref.44 Ref.45

Involvement in disease

Defects in RB1 are the cause of childhood cancer retinoblastoma (RB) [MIM:180200]. RB is a 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. Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65

Defects in RB1 are a cause of bladder cancer [MIM:109800].

Defects in RB1 are a cause of osteogenic sarcoma [MIM:259500].

Sequence similarities

Belongs to the retinoblastoma protein (RB) family.

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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
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processG1 phase

Traceable author statement. Source: UniProtKB

M phase

Non-traceable author statement. Source: UniProtKB

Ras protein signal transduction

Inferred from expression pattern. Source: UniProtKB

androgen receptor signaling pathway

Non-traceable author statement. Source: UniProtKB

cell cycle arrest

Traceable author statement. Source: UniProtKB

cell cycle checkpoint

Traceable author statement. Source: ProtInc

chromatin remodeling

Traceable author statement. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

myoblast differentiation

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of S phase of mitotic cell cycle

Traceable author statement. Source: UniProtKB

negative regulation of cell growth

Traceable author statement. Source: UniProtKB

negative regulation of protein kinase activity Ref.24

Inferred from physical interaction. Source: UniProtKB

regulation of lipid kinase activity

Inferred from direct assay. Source: UniProtKB

regulation of transcription involved in G1/S-phase of mitotic cell cycle

Traceable author statement. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentPML body

Inferred from direct assay. Source: UniProtKB

Rb-E2F complex

Traceable author statement. Source: UniProtKB

SWI/SNF complex

Traceable author statement. Source: UniProtKB

chromatin Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionandrogen receptor binding

Non-traceable author statement. Source: UniProtKB

kinase binding

Inferred from direct assay. Source: UniProtKB

phosphoprotein binding Ref.50

Inferred from physical interaction. Source: UniProtKB

transcription coactivator activity

Non-traceable author statement. Source: UniProtKB

transcription factor activity Ref.1

Traceable author statement. Source: ProtInc

transcription repressor activity

Traceable author statement. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928Retinoblastoma-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 residue371Phosphoserine Ref.42 Ref.45
Modified residue2491Phosphoserine; by CDC2 Ref.17 Ref.41 Ref.42 Ref.44 Ref.45
Modified residue2521Phosphothreonine; by CDC2 Ref.17 Ref.41 Ref.42 Ref.45
Modified residue3561Phosphothreonine Ref.41
Modified residue3731Phosphothreonine; by CDC2 Ref.17 Ref.41 Ref.45
Modified residue5481N6-acetyllysine Ref.46
Modified residue7951Phosphoserine By similarity
Modified residue8071Phosphoserine; by CDC2 Ref.17 Ref.42 Ref.45
Modified residue8111Phosphoserine; by CDC2 Ref.17 Ref.42 Ref.45
Modified residue8211Phosphothreonine Ref.50 Ref.44 Ref.45
Modified residue8231Phosphothreonine Ref.42 Ref.44 Ref.45
Modified residue8261Phosphothreonine Ref.50 Ref.42 Ref.45
Modified residue8411Phosphothreonine Ref.45
Modified residue8551Phosphoserine Ref.42
Modified residue8821Phosphoserine Ref.45
Modified residue8961N6-acetyllysine Ref.46

Natural variations

Natural variant721E → Q in RB. Ref.58
VAR_005572
Natural variant1331N → H: dbSNP rs3092900.
VAR_051909
Natural variant1371E → D in RB; unilateral form. Ref.61
VAR_005573
Natural variant1851I → T in RB. Ref.59
VAR_005574
Natural variant3101G → E in RB; could be a polymorphism. Ref.64
VAR_010045
Natural variant3581R → G in RB. Ref.60
VAR_010046
Natural variant3581R → Q in RB.
VAR_005575
Natural variant4361Q → K: dbSNP rs4151534. Ref.7
VAR_019379
Natural variant4471K → Q in RB. Ref.62
VAR_010048
Natural variant4571M → R in RB. Ref.55
VAR_005576
Natural variant4801Missing in RB; mild form.
VAR_005577
Natural variant5001R → G in RB. Ref.65
VAR_011580
Natural variant5251A → G: dbSNP rs4151539. Ref.7
VAR_019380
Natural variant5301K → R in RB. Ref.56
VAR_010049
Natural variant5491H → Y in RB. Ref.58
VAR_005578
Natural variant5671S → L in RB. Ref.53 Ref.63
VAR_005579
Natural variant5691L → F: dbSNP rs3092895.
VAR_051910
Natural variant6161K → E in RB. Ref.65
VAR_011581
Natural variant6351A → P in RB. Ref.59
VAR_005580
Natural variant6541V → E in RB. Ref.59
VAR_005581
Natural variant6571L → P in RB. Ref.60
VAR_010050
Natural variant6611R → W in RB; mild form. Ref.54 Ref.57 Ref.60 Ref.61
VAR_005582
Natural variant6621L → P in RB. Ref.63
VAR_005583
Natural variant6731H → P in RB.
VAR_005584
Natural variant6851Q → P in RB. Ref.59
VAR_005585
Natural variant6971D → E: dbSNP rs3092903.
VAR_051911
Natural variant7061C → Y in RB.
VAR_005586
Natural variant7121C → R in RB. Ref.63
VAR_005587
Natural variant7461E → G: dbSNP rs3092905.
VAR_034442
Natural variant8031N → K in RB. Ref.58
VAR_005588

Experimental info

Mutagenesis8211T → A: Abolishes interaction with Pocket domain; when associated with A-826. Ref.50
Mutagenesis8261T → A: Abolishes interaction with Pocket domain; when associated with A-821. Ref.50
Sequence conflict500 – 5012RS → SN in AAN64133. Ref.7

Secondary structure

1 ........................................................................................... 928
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P06400-1 [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

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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: 3657987] [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: 3823889] [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: 3480530] [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: 2701949] [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: 1352398] [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: 7902321] [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: 14702039] [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: 15057823] [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: 15489334] [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: 2717184] [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: 1316611] [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: 7881418] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-65, INVOLVEMENT IN RETINOBLASTOMA.
[15]"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: 2839300] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[16]"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: 3413073] [Abstract]
Cited for: INVOLVEMENT IN RETINOBLASTOMA.
[17]"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: 1756735] [Abstract]
Cited for: PHOSPHORYLATION AT SER-249; THR-252; THR-373; SER-807 AND SER-811.
[18]"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: 8414517] [Abstract]
Cited for: INTERACTION WITH KDM5A AND ARID4A.
[19]"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: 7525595] [Abstract]
Cited for: INTERACTION WITH THOC1.
[20]"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: 7935440] [Abstract]
Cited for: INTERACTION WITH KDM5A.
[21]"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: 10446990] [Abstract]
Cited for: INTERACTION WITH ARID3B.
[22]"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: 10409732] [Abstract]
Cited for: INTERACTION WITH NDC80.
[23]"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: 10779342] [Abstract]
Cited for: INTERACTION WITH NDC80.
[24]"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: 9858607] [Abstract]
Cited for: INTERACTION WITH TAF1.
[25]"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: 10869426] [Abstract]
Cited for: INTERACTION WITH E4F1.
[26]"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: 11223246] [Abstract]
Cited for: INTERACTION WITH EID1.
[27]"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: 10888886] [Abstract]
Cited for: INTERACTION WITH DNMT1.
[28]"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: 11484059] [Abstract]
Cited for: INTERACTION WITH SUV39H1.
[29]"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: 12450794] [Abstract]
Cited for: INTERACTION WITH AATF.
[30]"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: 12475961] [Abstract]
Cited for: INTERACTION WITH TMPO-ALPHA AND LMNA.
[31]"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: 12682072] [Abstract]
Cited for: INTERACTION WITH PELP1.
[32]"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: 15538385] [Abstract]
Cited for: INTERACTION WITH LIN9.
[33]"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: 15542589] [Abstract]
Cited for: INTERACTION WITH LIMD1.
[34]"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: 15927959] [Abstract]
Cited for: INTERACTION WITH KDM4A.
[35]"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: 15803180] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[36]"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: 15949438] [Abstract]
Cited for: INTERACTION WITH KDM5A.
[37]"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: 16337594] [Abstract]
Cited for: INTERACTION WITH PSMA3.
[38]"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: 16214886] [Abstract]
Cited for: INTERACTION WITH ZUBR1.
[39]"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: 16645588] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[40]"Revisiting retinoblastoma protein phosphorylation during the mammalian cell cycle."
Cooper S., Shayman J.A.
Cell. Mol. Life Sci. 58:580-595(2001) [PubMed: 11361093] [Abstract]
Cited for: REVIEW.
[41]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-252; THR-356 AND THR-373, MASS SPECTROMETRY.
[42]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-252; SER-807; SER-811; THR-823; THR-826 AND SER-855, MASS SPECTROMETRY.
[43]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[44]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; THR-821 AND THR-823, MASS SPECTROMETRY.
[45]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-249; THR-252; THR-373; SER-807; SER-811; THR-821; THR-823; THR-826; THR-841 AND SER-882, MASS SPECTROMETRY.
Tissue: T-cell.
[46]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-548 AND LYS-896, MASS SPECTROMETRY.
[47]"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: 9145110] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 378-562.
[48]"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: 9495340] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 380-785.
[49]"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: 12695505] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 860-876 IN COMPLEX WITH KPNA2.
[50]"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: 16360038] [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.
[51]"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: 17974914] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 380-787 IN COMPLEX WITH HUMAN ADENOVIRUS E1A PROTEIN.
[52]"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: 17996702] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-355, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, INTERACTION WITH THOC1 AND GRIP1, INTERACTION OF THE UNPHOSPHORYLATED PROTEIN WITH EID1.
[53]"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: 2594029] [Abstract]
Cited for: VARIANT RB LEU-567.
[54]"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: 1352883] [Abstract]
Cited for: VARIANT RB TRP-661.
[55]"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: 8346255] [Abstract]
Cited for: VARIANT RB ARG-457.
[56]"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: 7704558] [Abstract]
Cited for: VARIANT RB ARG-530.
[57]"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: 7927327] [Abstract]
Cited for: VARIANTS RB ASN-480 DEL AND TRP-661.
[58]"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: 8605116] [Abstract]
Cited for: VARIANTS RB GLN-72; TYR-549 AND LYS-803.
[59]"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: 7795591] [Abstract]
Cited for: VARIANTS RB THR-185; PRO-635; GLU-654 AND PRO-685.
[60]"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: 8776589] [Abstract]
Cited for: VARIANTS RB GLY-358; PRO-657 AND TRP-661.
[61]"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: 9311732] [Abstract]
Cited for: VARIANTS RB ASP-137 AND TRP-661.
[62]"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: 9140452] [Abstract]
Cited for: VARIANT RB GLN-447.
[63]"Twelve novel RB1 gene mutations in patients with hereditary retinoblastoma."
Yilmaz S., Horsthemke B., Lohmann D.R.
Hum. Mutat. 12:434-434(1998) [PubMed: 10671068] [Abstract]
Cited for: VARIANTS RB LEU-567; PRO-662 AND ARG-712.
[64]"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: 9973307] [Abstract]
Cited for: VARIANT RB GLU-310.
[65]"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: 11524739] [Abstract]
Cited for: VARIANTS RB GLY-500 AND GLU-616.
+Additional computationally mapped references.

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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.
IPIIPI00302829.
PIRRBHU. JS0276.
RefSeqNP_000312.2.
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/B380-586[»]
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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-582N.
IntActP06400. 27 interactions.
STRINGP06400.

PTM databases

PhosphoSiteP06400.

Proteomic databases

PeptideAtlasP06400.
PRIDEP06400.

Genome annotation databases

EnsemblENST00000267163; ENSP00000267163; ENSG00000139687; Homo sapiens. [Genome view]
GeneID5925.
KEGGhsa:5925.
UCSCuc001vcb.1. human.

Organism-specific databases

CTD5925.
GeneCardsGC13P047775.
H-InvDBHIX0026565.
HGNCHGNC:9884. RB1.
HPACAB000095.
CAB016687.
MIM109800. phenotype.
180200. gene+phenotype.
259500. phenotype.
Orphanet668. Osteosarcoma.
790. Retinoblastoma.
PharmGKBPA24556.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06134.
HOVERGENP06400.
InParanoidP06400.
OMAKLERTCE.
OrthoDBEOG9THZCK.
PhylomeDBP06400.

Enzyme and pathway databases

Pathway_Interaction_DBfoxm1pathway. FOXM1 transcription factor network.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP06400.
BgeeP06400.
CleanExHS_RB1.
GenevestigatorP06400.
GermOnlineENSG00000139687. Homo sapiens.

Family and domain databases

InterProIPR006670. Cyclin.
IPR011028. Cyclin-like.
IPR013763. Cyclin_related.
IPR002720. RB_A.
IPR015652. Rb_associated.
IPR002719. RB_B.
[Graphical view]
Gene3DG3DSA:1.10.472.10. Cyclin_related. 2 hits.
PANTHERPTHR13742:SF10. Rb_associated. 1 hit.
PfamPF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view]
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.
NextBio23076.
PMAP-CutDBP06400.
SOURCESearch...

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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: February 9, 2010
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Index of human polymorphisms and disease mutations

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents