Reviewed, UniProtKB/Swiss-Prot P06400 (RB_HUMAN)

Names and origin

Protein names

Recommended name:
    Retinoblastoma-associated protein
Alternative name(s):
    pRb
      Short name=Rb
    pp110
    p105-Rb

Gene names

Name:

RB1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	928 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. 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 adenovirus E1A protein, HPV E7 protein and SV40 large T antigen.
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. Ref.17 Ref.40 Ref.41 Ref.47
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.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 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.

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 Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	G1 phase Traceable author statement. Source: UniProtKB M phase Non-traceable author statement. 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 component	PML 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 function	androgen receptor binding Non-traceable author statement. Source: UniProtKB kinase binding Inferred from direct assay. Source: UniProtKB phosphoprotein binding Ref.47 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK2	P24941	1	EBI-491274,EBI-375096
Cdk4	P30285	2	EBI-491274,EBI-847225	From a different organism.
DGKZ	Q13574-2	5	EBI-491274,EBI-715527
E2F1	Q01094	1	EBI-491274,EBI-448924
E7	P06465	1	EBI-491274,EBI-963841	From a different organism.
HDAC1	Q13547	1	EBI-491274,EBI-301834
Hmga2	P52927	4	EBI-491274,EBI-912574	From a different organism.
MORF4L2	Q15014	1	EBI-491274,EBI-399257
NCOA6	Q14686	2	EBI-491274,EBI-78670
PA2G4	Q9UQ80	2	EBI-491274,EBI-924893
PPP1CA	P62136	2	EBI-491274,EBI-357253
Ppp1cb	P62142	1	EBI-491274,EBI-352326	From a different organism.
PRMT2	P55345	3	EBI-491274,EBI-78458
PSMD10	O75832	1	EBI-491274,EBI-752185
Smarca4	Q3TUD7	1	EBI-491274,EBI-1210244	From a different organism.
TAF1	P21675	1	EBI-491274,EBI-491289

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 928

928

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

37

1

Phosphoserine Ref.41

Modified residue

249

1

Phosphoserine; by CDC2 Ref.17 Ref.40 Ref.41

Modified residue

252

1

Phosphothreonine; by CDC2 Ref.17 Ref.40 Ref.41

Modified residue

356

1

Phosphothreonine Ref.40

Modified residue

373

1

Phosphothreonine; by CDC2 Ref.17 Ref.40

Modified residue

548

1

N6-acetyllysine Ref.43

Modified residue

807

1

Phosphoserine; by CDC2 Ref.17 Ref.41

Modified residue

811

1

Phosphoserine; by CDC2 Ref.17 Ref.41

Modified residue

821

1

Phosphothreonine Ref.47

Modified residue

823

1

Phosphothreonine Ref.41

Modified residue

826

1

Phosphothreonine Ref.41 Ref.47

Modified residue

855

1

Phosphoserine Ref.41

Modified residue

896

1

N6-acetyllysine Ref.43

Natural variations

Natural variant

72

1

E → Q in RB. Ref.55

VAR_005572

Natural variant

133

1

N → H: dbSNP rs3092900.

VAR_051909

Natural variant

137

1

E → D in RB; unilateral form. Ref.58

VAR_005573

Natural variant

185

1

I → T in RB. Ref.56

VAR_005574

Natural variant

310

1

G → E in RB; could be a polymorphism. Ref.61

VAR_010045

Natural variant

358

1

R → G in RB. Ref.57

VAR_010046

Natural variant

358

1

R → Q in RB.

VAR_005575

Natural variant

436

1

Q → K: dbSNP rs4151534. Ref.7

VAR_019379

Natural variant

447

1

K → Q in RB. Ref.59

VAR_010048

Natural variant

457

1

M → R in RB. Ref.52

VAR_005576

Natural variant

480

1

Missing in RB; mild form.

VAR_005577

Natural variant

500

1

R → G in RB. Ref.62

VAR_011580

Natural variant

525

1

A → G: dbSNP rs4151539. Ref.7

VAR_019380

Natural variant

530

1

K → R in RB. Ref.53

VAR_010049

Natural variant

549

1

H → Y in RB. Ref.55

VAR_005578

Natural variant

567

1

S → L in RB. Ref.50 Ref.60

VAR_005579

Natural variant

569

1

L → F: dbSNP rs3092895.

VAR_051910

Natural variant

616

1

K → E in RB. Ref.62

VAR_011581

Natural variant

635

1

A → P in RB. Ref.56

VAR_005580

Natural variant

654

1

V → E in RB. Ref.56

VAR_005581

Natural variant

657

1

L → P in RB. Ref.57

VAR_010050

Natural variant

661

1

R → W in RB; mild form. Ref.51 Ref.54 Ref.57 Ref.58

VAR_005582

Natural variant

662

1

L → P in RB. Ref.60

VAR_005583

Natural variant

673

1

H → P in RB.

VAR_005584

Natural variant

685

1

Q → P in RB. Ref.56

VAR_005585

Natural variant

697

1

D → E: dbSNP rs3092903.

VAR_051911

Natural variant

706

1

C → Y in RB.

VAR_005586

Natural variant

712

1

C → R in RB. Ref.60

VAR_005587

Natural variant

746

1

E → G: dbSNP rs3092905.

VAR_034442

Natural variant

803

1

N → K in RB. Ref.55

VAR_005588

Experimental info

Mutagenesis

821

1

T → A: Abolishes interaction with Pocket domain; when associated with A-826. Ref.47

Mutagenesis

826

1

T → A: Abolishes interaction with Pocket domain; when associated with A-821. Ref.47

Sequence conflict

500 – 501

2

RS → SN in AAN64133. Ref.7

Secondary structure

1

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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

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

314 – 328

15

Helix

333 – 338

6

Helix

341 – 343

3

Helix

347 – 353

7

Helix

384 – 390

7

Helix

398 – 405

8

Beta strand

407 – 409

3

Helix

412 – 434

23

Helix

439 – 468

30

Helix

474 – 477

4

Helix

480 – 497

18

Turn

498 – 500

3

Beta strand

504 – 506

3

Helix

516 – 521

6

Helix

525 – 538

14

Helix

544 – 559

16

Helix

568 – 576

9

Helix

646 – 669

24

Helix

676 – 690

15

Helix

692 – 694

3

Helix

700 – 714

15

Helix

721 – 728

8

Helix

737 – 740

4

Beta strand

741 – 743

3

Beta strand

745 – 747

3

Helix

752 – 758

7

Helix

760 – 769

10

Helix

770 – 772

3

Beta strand

773 – 775

3

Beta strand

830 – 836

7

Turn

838 – 840

3

Helix

841 – 853

13

Beta strand

860 – 867

8

Sequences

	Sequence		Length	Mass (Da)
	P06400-1 [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: 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. , 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. , 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. , 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: COMPLEX 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]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
[62]	"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.

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

EMBLGenBankDDBJ

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.

UniGene

Hs.408528

3D structure databases

PDBPDBe

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	380-586	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:582N.

IntAct

P06400. 25 interactions.

STRING

P06400.

PTM databases

PhosphoSite

P06400.

Proteomic databases

PeptideAtlas

P06400.

PRIDE

P06400.

Genome annotation databases

Ensembl

ENST00000267163; ENSP00000267163; ENSG00000139687; Homo sapiens. [Genome view]

GeneID

5925.

KEGG

hsa:5925.

UCSC

uc001vcb.1. human.

Organism-specific databases

CTD

5925.

GeneCards

GC13P047775.

H-InvDB

HIX0026565.

HGNC

HGNC:9884. RB1.

HPA

CAB000095.
CAB016687.

MIM

109800. phenotype.
180200. gene+phenotype.
259500. phenotype.

Orphanet

668. Osteosarcoma.
790. Retinoblastoma.

PharmGKB

PA24556.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P06400.

OMA

RTCELIY.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

P06400.

Bgee

P06400.

CleanEx

HS_RB1.

Genevestigator

P06400.

GermOnline

ENSG00000139687. Homo sapiens.

Family and domain databases

InterPro

IPR006670. Cyclin.
IPR013763. Cyclin_related.
IPR002720. RB_A.
IPR015652. Rb_associated.
IPR002719. RB_B.
IPR015030. Rb_C.
[Graphical view]

Gene3D

G3DSA:1.10.472.10. Cyclin_related. 2 hits.

PANTHER

PTHR13742:SF10. Rb_associated. 1 hit.

Pfam

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

SMART

SM00385. CYCLIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

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

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:	November 3, 2009
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.