P06400 (RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinoblastoma-associated protein

Alternative name(s):
p105-Rb
pRb
Short name=Rb
pp110

Gene names

Name:

RB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	928 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.52 Ref.56 Ref.62 Ref.64
Subcellular location	Nucleus Ref.53.
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.62 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.52 Ref.58 Acetylation at Lys-873 and Lys-874 regulates subcellular localization, at least during keratinocytes differentiation.
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.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 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 process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Proto-oncogene
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome Ras protein signal transduction Inferred from expression pattern PubMed 9054499. Source: BHF-UCL S phase of mitotic cell cycle Traceable author statement. Source: Reactome androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB cell cycle arrest Traceable author statement PubMed 19149898. Source: BHF-UCL cell division Inferred from electronic annotation. Source: Compara cell morphogenesis involved in neuron differentiation Inferred from electronic annotation. Source: Compara chromatin remodeling Traceable author statement PubMed 19149898. Source: BHF-UCL digestive tract development Inferred from electronic annotation. Source: Compara enucleate erythrocyte differentiation Inferred from electronic annotation. Source: Compara maintenance of mitotic sister chromatid cohesion Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL 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 S phase of mitotic cell cycle Traceable author statement PubMed 19149898. Source: BHF-UCL negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 10783144PubMed 19223331. Source: UniProtKB neuron apoptotic process Inferred from electronic annotation. Source: Compara neuron maturation Inferred from electronic annotation. Source: Compara neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of macrophage differentiation Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of transcription, DNA-dependent 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 transcription involved in G1/S phase of mitotic cell cycle Traceable author statement PubMed 19149898. Source: BHF-UCL sister chromatid biorientation Inferred from mutant phenotype PubMed 20551165. Source: BHF-UCL striated muscle cell differentiation Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML 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 spindle Inferred from electronic annotation. Source: Compara
Molecular_function	androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB core promoter binding Inferred from direct assay PubMed 15735762. Source: UniProtKB kinase binding Inferred from direct assay PubMed 16286473. 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03070	2	EBI-491274,EBI-617698	From a different organism.
CDK2	P24941	3	EBI-491274,EBI-375096
Cdk4	P30285	2	EBI-491274,EBI-847225	From a different organism.
Cenpf	Q155P7	4	EBI-491274,EBI-2211248	From a different organism.
DGKZ	Q13574-2	6	EBI-491274,EBI-715527
E2F1	Q01094	10	EBI-491274,EBI-448924
E7	P06465	2	EBI-491274,EBI-963841	From a different organism.
FRK	P42685	3	EBI-491274,EBI-1383583
HDAC1	Q13547	2	EBI-491274,EBI-301834
Hmga2	P52927	5	EBI-491274,EBI-912574	From a different organism.
Ifi202	Q9R002	5	EBI-491274,EBI-3043899	From a different organism.
IRF3	Q14653	2	EBI-491274,EBI-2650369
MAPK14	Q16539	3	EBI-491274,EBI-73946
MDM2	Q00987	3	EBI-491274,EBI-389668
NCOA6	Q14686	3	EBI-491274,EBI-78670
NEFM	P07197	2	EBI-491274,EBI-1105035
ospF	Q8VSP9	2	EBI-491274,EBI-6506625	From a different organism.
PA2G4	Q9UQ80	4	EBI-491274,EBI-924893
PPP1CA	P62136	2	EBI-491274,EBI-357253
PRMT2	P55345	3	EBI-491274,EBI-78458
PURA	Q00577	6	EBI-491274,EBI-1045860
RAF1	P04049	3	EBI-491274,EBI-365996
RNF40	O75150	3	EBI-491274,EBI-744408
Sirt1	Q923E4	4	EBI-491274,EBI-1802585	From a different organism.
Smarca4	Q3TKT4	4	EBI-491274,EBI-1210244	From a different organism.
UHRF2	Q96PU4	4	EBI-491274,EBI-625304

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 928

927

Retinoblastoma-associated protein

PRO_0000167836

Regions

Region

373 – 771

399

Pocket; binds T and E1A

Region

373 – 579

207

Domain A

Region

580 – 639

60

Spacer

Region

640 – 771

132

Domain B

Region

763 – 928

166

Interaction with LIMD1

Region

771 – 928

158

Domain C; mediates interaction with E4F1

Motif

870 – 876

7

Nuclear localization signal Probable

Compositional bias

10 – 18

9

Poly-Ala

Compositional bias

20 – 29

10

Poly-Pro

Amino acid modifications

Modified residue

2

1

N,N-dimethylproline By similarity

Modified residue

37

1

Phosphoserine Ref.49 Ref.50

Modified residue

249

1

Phosphoserine; by CDK1 Ref.18 Ref.48 Ref.49 Ref.50 Ref.57

Modified residue

252

1

Phosphothreonine; by CDK1 Ref.18 Ref.48 Ref.49

Modified residue

356

1

Phosphothreonine Ref.48

Modified residue

373

1

Phosphothreonine; by CDK1 Ref.18 Ref.50

Modified residue

567

1

Phosphoserine; by CDK2 Ref.24

Modified residue

612

1

Phosphoserine; by CHEK2 and CHEK1 Ref.47 Ref.49

Modified residue

795

1

Phosphoserine By similarity

Modified residue

807

1

Phosphoserine; by CDK1 and CDK3 Ref.18 Ref.37 Ref.49 Ref.50

Modified residue

810

1

N6-methyllysine; by SMYD2 Ref.58

Modified residue

811

1

Phosphoserine; by CDK1 and CDK3 Ref.18 Ref.37 Ref.49

Modified residue

821

1

Phosphothreonine; by CDK6 Ref.40 Ref.54 Ref.62

Modified residue

823

1

Phosphothreonine Ref.49

Modified residue

826

1

Phosphothreonine; by CDK4 Ref.40 Ref.49 Ref.54 Ref.62

Modified residue

841

1

Phosphothreonine Ref.50

Modified residue

860

1

N6-methyllysine; by SMYD2 Ref.52

Modified residue

873

1

N6-acetyllysine; by PCAF Ref.53

Modified residue

874

1

N6-acetyllysine; by PCAF Ref.53

Natural variations

Natural variant

72

1

E → Q in RB. Ref.70

VAR_005572

Natural variant

133

1

N → H.
Corresponds to variant rs3092900 [ dbSNP | Ensembl ].

VAR_051909

Natural variant

137

1

E → D in RB; unilateral form. Ref.73

VAR_005573

Natural variant

185

1

I → T in RB. Ref.71

VAR_005574

Natural variant

310

1

G → E in RB; unknown pathological significance. Ref.76

VAR_010045

Natural variant

358

1

R → G in RB. Ref.72

VAR_010046

Natural variant

358

1

R → Q in RB.

VAR_005575

Natural variant

436

1

Q → K. Ref.7
Corresponds to variant rs4151534 [ dbSNP | Ensembl ].

VAR_019379

Natural variant

447

1

K → Q in RB. Ref.74

VAR_010048

Natural variant

457

1

M → R in RB. Ref.67

VAR_005576

Natural variant

480

1

Missing in RB; mild form. Ref.69

VAR_005577

Natural variant

500

1

R → G in RB. Ref.77

VAR_011580

Natural variant

525

1

A → G. Ref.7
Corresponds to variant rs4151539 [ dbSNP | Ensembl ].

VAR_019380

Natural variant

530

1

K → R in RB. Ref.68

VAR_010049

Natural variant

549

1

H → Y in RB. Ref.70

VAR_005578

Natural variant

567

1

S → L in RB. Ref.65 Ref.75

VAR_005579

Natural variant

569

1

L → F.
Corresponds to variant rs3092895 [ dbSNP | Ensembl ].

VAR_051910

Natural variant

616

1

K → E in RB. Ref.77

VAR_011581

Natural variant

635

1

A → P in RB. Ref.71

VAR_005580

Natural variant

654

1

V → E in RB. Ref.71

VAR_005581

Natural variant

657

1

L → P in RB. Ref.72

VAR_010050

Natural variant

661

1

R → W in RB; mild form. Ref.66 Ref.69 Ref.72 Ref.73

VAR_005582

Natural variant

662

1

L → P in RB. Ref.75

VAR_005583

Natural variant

673

1

H → P in RB.

VAR_005584

Natural variant

685

1

Q → P in RB. Ref.71

VAR_005585

Natural variant

697

1

D → E.
Corresponds to variant rs3092903 [ dbSNP | Ensembl ].

VAR_051911

Natural variant

706

1

C → Y in RB.

VAR_005586

Natural variant

712

1

C → R in RB. Ref.75

VAR_005587

Natural variant

746

1

E → G.
Corresponds to variant rs3092905 [ dbSNP | Ensembl ].

VAR_034442

Natural variant

803

1

N → K in RB. Ref.70

VAR_005588

Experimental info

Mutagenesis

821

1

T → A: Abolishes interaction with Pocket domain; when associated with A-826. Ref.62

Mutagenesis

826

1

T → A: Abolishes interaction with Pocket domain; when associated with A-821. Ref.62

Mutagenesis

860

1

K → R: Abolishes monomethylation by SMYD2 and subsequent interaction with L3MBTL1. Ref.52

Mutagenesis

870

1

K → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. Ref.52

Mutagenesis

873 – 874

2

KK → R: Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874. Ref.53

Mutagenesis

873 – 874

2

KK → RR: Does not alter Rb localization in cycling cells, but mislocalizes to the cytoplasm during keratinocytes differentiation. Ref.53

Sequence conflict

500 – 501

2

RS → SN in AAN64133. Ref.7

Secondary structure

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928

Helix Strand Turn

Details...

Helix

55 – 63

9

Helix

68 – 82

15

Helix

95 – 110

16

Helix

117 – 124

8

Helix

128 – 135

8

Helix

142 – 172

31

Beta strand

180 – 182

3

Helix

188 – 204

17

Beta strand

207 – 209

3

Helix

212 – 228

17

Helix

232 – 234

3

Turn

237 – 240

4

Helix

241 – 243

3

Helix

272 – 281

10

Helix

285 – 294

10

Helix

296 – 299

4

Helix

302 – 306

5

Helix

314 – 328

15

Helix

333 – 338

6

Helix

341 – 343

3

Helix

347 – 353

7

Helix

382 – 391

10

Helix

398 – 405

8

Beta strand

407 – 409

3

Helix

412 – 434

23

Helix

436 – 438

3

Helix

439 – 468

30

Helix

474 – 477

4

Helix

480 – 501

22

Turn

504 – 506

3

Beta strand

511 – 513

3

Helix

516 – 521

6

Helix

525 – 529

5

Helix

532 – 538

7

Helix

544 – 559

16

Helix

561 – 563

3

Beta strand

564 – 566

3

Helix

569 – 577

9

Helix

602 – 607

6

Helix

645 – 669

25

Helix

676 – 690

15

Helix

692 – 695

4

Helix

700 – 714

15

Helix

721 – 728

8

Beta strand

731 – 733

3

Helix

737 – 740

4

Beta strand

741 – 743

3

Beta strand

745 – 747

3

Beta strand

748 – 750

3

Helix

752 – 758

7

Helix

760 – 770

11

Beta strand

773 – 775

3

Beta strand

830 – 836

7

Turn

838 – 840

3

Helix

841 – 853

13

Sequences

	Sequence		Length	Mass (Da)
	P06400 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: C8E746111E19CC32	FASTA	928	106,159
	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

References

	« Hide 'large scale' referencesShow '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.
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[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.
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[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.
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[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.
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[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[50]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[51]	"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].
[52]	"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.
[53]	"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.
[54]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[55]	"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].
[56]	"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.
[57]	"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, MASS SPECTROMETRY.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
[62]	"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.
[63]	"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.
[64]	"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, MASS SPECTROMETRY, INTERACTION WITH THOC1 AND GRIP1, INTERACTION OF THE UNPHOSPHORYLATED PROTEIN WITH EID1.
[65]	"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.
[66]	"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.
[67]	"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.
[68]	"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.
[69]	"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.
[70]	"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.
[71]	"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.
[72]	"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.
[73]	"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.
[74]	"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.
[75]	"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.
[76]	"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.
[77]	"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.
+	Additional computationally mapped references.

Web resources

RB1base

RB1 mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Wikipedia

Retinoblastoma protein entry

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 , 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.

IPI

IPI00302829.

PIR

RBHU. JS0276.

RefSeq

NP_000312.2. NM_000321.2.

UniGene

Hs.408528.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AD6	X-ray	2.30	A	378-562	[»]
1GH6	X-ray	3.20	B	379-772	[»]
1GUX	X-ray	1.85	A	372-589	[»]
			B	636-787	[»]
1H25	X-ray	2.50	E	868-878	[»]
1N4M	X-ray	2.20	A/B	380-785	[»]
1O9K	X-ray	2.60	A/C/E/G	372-589	[»]
			B/D/F/H	636-787	[»]
1PJM	X-ray	2.50	A	860-876	[»]
2AZE	X-ray	2.55	C	829-874	[»]
2QDJ	X-ray	2.00	A	52-355	[»]
2R7G	X-ray	1.67	A/C	380-787	[»]
3N5U	X-ray	3.20	C	870-882	[»]
3POM	X-ray	2.50	A/B	380-787	[»]
4ELJ	X-ray	2.70	A	53-787	[»]
4ELL	X-ray	1.98	A/B	380-787	[»]

ProteinModelPortal

P06400.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-582N.

IntAct

P06400. 57 interactions.

MINT

MINT-98847.

STRING

9606.ENSP00000267163.

PTM databases

PhosphoSite

P06400.

Polymorphism databases

DMDM

132164.

Proteomic databases

PaxDb

P06400.

PeptideAtlas

P06400.

PRIDE

P06400.

Protocols and materials databases

DNASU

5925.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000267163; ENSP00000267163; ENSG00000139687.

GeneID

5925.

KEGG

hsa:5925.

UCSC

uc001vcb.3. human.

Organism-specific databases

CTD

5925.

GeneCards

GC13P048877.

HGNC

HGNC:9884. RB1.

HPA

CAB000095.
CAB016687.

MIM

109800. phenotype.
180200. phenotype.
259500. phenotype.
614041. gene.

neXtProt

NX_P06400.

Orphanet

790. Retinoblastoma.

PharmGKB

PA295.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296920.

HOVERGEN

HBG008967.

InParanoid

P06400.

KO

K06618.

OMA

TNILQYA.

OrthoDB

EOG4TXBRB.

PhylomeDB

P06400.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_115566. Cell Cycle.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P06400.

Bgee

P06400.

CleanEx

HS_RB1.

Genevestigator

P06400.

GermOnline

ENSG00000139687. Homo sapiens.

Family and domain databases

Gene3D

1.10.472.10. 2 hits.

InterPro

IPR013763. Cyclin-like.
IPR024599. DUF3452_retinoblatoma-assoc.
IPR002720. RB_A.
IPR015652. Rb_associated.
IPR002719. RB_B.
IPR015030. Rb_C.
[Graphical view]

PANTHER

PTHR13742:SF10. PTHR13742:SF10. 1 hit.

Pfam

PF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]

SMART

SM00385. CYCLIN. 1 hit.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

ProtoNet

Search...

Other

BindingDB

P06400.

ChEMBL

CHEMBL5288.

ChiTaRS

RB1. human.

DrugBank

DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.

EvolutionaryTrace

P06400.

GenomeRNAi

5925.

NextBio

23076.

PMAP-CutDB

P06400.

SOURCE

Search...

Entry information

Entry name

RB_HUMAN

Accession

Primary (citable) accession number: P06400
Secondary accession number(s): A8K5E3 , P78499, Q5VW46, Q8IZL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 183 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.