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Protein

Retinoblastoma-associated protein

Gene

RB1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. 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, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Also acts as a transcription repressor of E2F target genes by recruiting chromatin-modifying enzymes to promoters (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-associated protein
Alternative name(s):
p104
pRb
Short name:
Rb
Gene namesi
Name:RB1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 921921Retinoblastoma-associated proteinPRO_0000331619Add
BLAST

Post-translational modificationi

Phosphorylated in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ90600.
PRIDEiQ90600.

Interactioni

Subunit structurei

Interacts with and sequesters the E2F1 transcription factor. Interacts with SUV39H1, KMT5B and KMT5C (By similarity). Interacts with, and is inhibited by fowl adenovirus 1 protein GAM-1.By similarity1 Publication

Protein-protein interaction databases

STRINGi9031.ENSGALP00000035706.

Structurei

3D structure databases

ProteinModelPortaliQ90600.
SMRiQ90600. Positions 37-345, 370-575, 629-777, 822-865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi863 – 8697Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 794Poly-Lys

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
HOGENOMiHOG000136539.
HOVERGENiHBG008967.
InParanoidiQ90600.
KOiK06618.
PhylomeDBiQ90600.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR033057. RB1.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF21. PTHR13742:SF21. 1 hit.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
SM01367. DUF3452. 1 hit.
SM01368. RB_A. 1 hit.
SM01369. Rb_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequencei

Sequence statusi: Complete.

Q90600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKPLRRAG AARSQRTSPE GGAGTASPPG GTRLEVGEAE FVALCDALKA
60 70 80 90 100
PDSVREKAWM TYQSLAAADG ASAYNKKKKE TWGVCIFIVA IDLDEMTFTF
110 120 130 140 150
TELLKSLSIS VCTFFQFLKE VDVNMDTVST KVDSTVSRLK KKYDVLLALY
160 170 180 190 200
HKFERTCGLI YLEQPSSEIS AELSSVLVLK NYWITFLLAK GKVLQMEDDL
210 220 230 240 250
VISFQLLLCV LDYFIKLSPP AMLKEPYKSA VTALTVNGST RTPRRGQNRN
260 270 280 290 300
ARASKQIDTD TKVIEILCKE HDCNLDEVKN VYFTSFIPFL NSLGVVASNG
310 320 330 340 350
LPEVDVLSKQ YDELYLKNKD IDARLFLDHD ETLQPDVIAC SQLERTPRKN
360 370 380 390 400
NPDEEVNHVL PQTPVRAAMN TIQQLMMILN SATDKPSDTL IAYFNNCTVN
410 420 430 440 450
PEDSILKRVE SLGHIFKKKF AEAVGQGCAE IGSQRYQLGV RLYYRVMESM
460 470 480 490 500
LKSEEERLSV HNFSKLLNDN IFHTSLLACA LEIVMATYGR TASQSDGTSA
510 520 530 540 550
ETDLSFPWIL NVFDLKAFDF YKVIESFIKV EPSLTRDMIK HLERCEHRIM
560 570 580 590 600
ESLAWQSDSP LFDLIKQSKE REGQTDQPEP TSTLNLPLQH NHTAADLYLS
610 620 630 640 650
PVRSPKKKAS GHPQSGTSNP DAQPSATSQT QKPQKSTSLS LFYKKVFRLA
660 670 680 690 700
YLRLHTLFFR LLSEHPDLEP LIWTLFQHTL QNESELMRDR HLDQIMMCSM
710 720 730 740 750
YGICKVKNVD LRFKTIVSAY KELPNTNQET FKRVLIREEQ YDSIIVFYNL
760 770 780 790 800
VFMQKLKTNI LQYASNRPPT LSPIPHIPRS PYQFSNSPRR VPAGNNIYIS
810 820 830 840 850
PLKSPYKFSD GFHSPTKMTP RSRILVSIGE TFGTSEKFQK INQMVCNSES
860 870 880 890 900
HVKRSAEPSD APKPLKRLRF DIEGQDEADG GKHLPQESKF QQKLAEMTST
910 920
RTRMQKQKLN DGNDTSANEE K
Length:921
Mass (Da):104,436
Last modified:November 1, 1996 - v1
Checksum:i8527B7B4ACB12F36
GO

Sequence cautioni

The sequence AAA19644 differs from that shown. Reason: Frameshift at position 13. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631Q → E in AAA19644 (PubMed:8193168).Curated
Sequence conflicti163 – 1631E → S in AAA19644 (PubMed:8193168).Curated
Sequence conflicti411 – 4111S → C in AAA19644 (PubMed:8193168).Curated
Sequence conflicti619 – 6191N → G in AAA19644 (PubMed:8193168).Curated
Sequence conflicti791 – 7922VP → A in AAA19644 (PubMed:8193168).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72218 mRNA. Translation: CAA51019.1.
U00113 mRNA. Translation: AAA19644.1. Frameshift.
X72217 Genomic DNA. Translation: CAA51018.1.
PIRiS45298.
RefSeqiNP_989750.1. NM_204419.1.
UniGeneiGga.2986.

Genome annotation databases

GeneIDi386582.
KEGGigga:386582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72218 mRNA. Translation: CAA51019.1.
U00113 mRNA. Translation: AAA19644.1. Frameshift.
X72217 Genomic DNA. Translation: CAA51018.1.
PIRiS45298.
RefSeqiNP_989750.1. NM_204419.1.
UniGeneiGga.2986.

3D structure databases

ProteinModelPortaliQ90600.
SMRiQ90600. Positions 37-345, 370-575, 629-777, 822-865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000035706.

Proteomic databases

PaxDbiQ90600.
PRIDEiQ90600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi386582.
KEGGigga:386582.

Organism-specific databases

CTDi5925.

Phylogenomic databases

eggNOGiKOG1010. Eukaryota.
ENOG410XQF7. LUCA.
HOGENOMiHOG000136539.
HOVERGENiHBG008967.
InParanoidiQ90600.
KOiK06618.
PhylomeDBiQ90600.

Miscellaneous databases

PROiQ90600.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR033057. RB1.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF21. PTHR13742:SF21. 1 hit.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
SM01367. DUF3452. 1 hit.
SM01368. RB_A. 1 hit.
SM01369. Rb_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRB_CHICK
AccessioniPrimary (citable) accession number: Q90600
Secondary accession number(s): Q788Q6, Q90599, Q91016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.