Retinoblastoma-like protein 2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q64700 (RBL2_MOUSE)

Last modified July 7, 2009. Version 73. History...

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

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Names and origin

Protein names

Recommended name:
    Retinoblastoma-like protein 2
      Short name=RBR-2
Alternative name(s):
    PRB2
    130 kDa retinoblastoma-associated protein
    p130

Gene names

Name:

Rbl2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	1135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Key regulator of entry into cell division. 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 SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation, associates preferentially with E2F5. Binds to cyclins A and E. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. May act as a tumor suppressor. Ref.4
Subunit structure	Interacts with AATF and RINT1. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 By similarity. Interacts with SUV420H1 and SUV420H2.
Subcellular location	Nucleus.
Post-translational modification	During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-636 and on 5 sites within the domain B. Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent proteolysis By similarity.
Sequence similarities	Belongs to the retinoblastoma protein (RB) family.

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Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Disease	Tumor suppressor
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cenpf	Q155P7	2	EBI-2271232,EBI-2211248

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1135

1135

Retinoblastoma-like protein 2

PRO_0000167842

Regions

Region

414 – 1021

608

Pocket; binds E1A

Region

414 – 613

200

Domain A

Region

614 – 824

211

Spacer

Region

825 – 1021

197

Domain B

Compositional bias

9 – 13

Poly-Pro

Compositional bias

14 – 17

Poly-Ala

Compositional bias

20 – 24

Poly-Glu

Compositional bias

992 – 995

Poly-Glu

Amino acid modifications

Modified residue

410

Phosphoserine Ref.5

Modified residue

414

Phosphothreonine Ref.5

Modified residue

636

Phosphoserine Ref.5

Modified residue

639

Phosphothreonine Ref.5

Modified residue

669

Phosphoserine By similarity

Modified residue

942

Phosphoserine Ref.5

Modified residue

946

Phosphoserine By similarity

Modified residue

960

Phosphoserine By similarity

Modified residue

965

Phosphoserine By similarity

Modified residue

967

Phosphoserine By similarity

Modified residue

968

Phosphothreonine By similarity

Modified residue

975

Phosphoserine By similarity

Modified residue

976

Phosphoserine By similarity

Modified residue

980

Phosphothreonine By similarity

Modified residue

1027

Phosphothreonine Ref.5

Experimental info

Sequence conflict

211 – 253

Missing Ref.3

Sequence conflict

341

A → P in AAB48991. Ref.2

Sequence conflict

342

A → P in AAC52555. Ref.3

Sequence conflict

381

R → T in AAC52598. Ref.1

Sequence conflict

428

T → S in AAC52598. Ref.1

Sequence conflict

431

S → T in AAC52598. Ref.1

Sequence conflict

443

Q → R Ref.2

Sequence conflict

443

Q → R Ref.3

Sequence conflict

484 – 493

Missing Ref.2

Sequence conflict

768

A → R in AAC52598. Ref.1

Sequence conflict

826

P → A in AAC52555. Ref.3

Sequence conflict

947 – 948

PT → RA in AAC52555. Ref.3

Sequence conflict

1023

S → A Ref.2

Sequence conflict

1023

S → A Ref.3

Sequence conflict

1044

V → I in AAC52598. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q64700-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 0565E4F998ACCA0D
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FASTA

1,135

127,473

        10         20         30         40         50         60 
MASGGNQSPP PPPAAAASSE EEEEDGDAAD RAQPAGSPSH QIQQRFEELC SRLNMDEAAR 

        70         80         90        100        110        120 
AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS KGTAEGNYVS LTRILRCSEQ 

       130        140        150        160        170        180 
SLIEFFNKMK KWEDMANLPP HFRERTERLE RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR 

       190        200        210        220        230        240 
QQRGRKQRRQ PCTTSEIFHF CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC 

       250        260        270        280        290        300 
SNRKELVNPN FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR 

       310        320        330        340        350        360 
KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF LGEDAEEEVG 

       370        380        390        400        410        420 
TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL TGVRYVQENS PCVTPVSTAA 

       430        440        450        460        470        480 
HSLSRLHTML SGLRNAPSEK LEQILRSCSR DPTQAIADRL KEMYEIYSQH FQPDENFSNC 

       490        500        510        520        530        540 
AKEIANKHFR FAEMLYYKVL ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS 

       550        560        570        580        590        600 
HKPPGNFPFI AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS 

       610        620        630        640        650        660 
PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA GGLGRSITSP 

       670        680        690        700        710        720 
TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV NAVPVQNVPG ETVSVTPVPG 

       730        740        750        760        770        780 
QTLVTMATAT VTANNGQTVT IPVQGIANEN GGITFFPVQV NVGGQAQAVA GSIQPLSAQA 

       790        800        810        820        830        840 
LAGSLSSQQV TGTTLQVPGP VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY 

       850        860        870        880        890        900 
YLAGVRLRDL CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK 

       910        920        930        940        950        960 
EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL NTDRASRDSS 

       970        980        990       1000       1010       1020 
PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI QFYNNIYRKQ IQAFAMKYSQ 

      1030       1040       1050       1060       1070       1080 
ANSQTDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHNNE AMPSPREKIF YYFSNSPSKR 

      1090       1100       1110       1120       1130 
LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and developmental expression of mouse p130, a member of the retinoblastoma gene family." Chen G., Guy C.T., Chen H.W., Hu N., Lee E.Y.H.P., Lee W.H. J. Biol. Chem. 271:9567-9572(1996) [PubMed: 8621630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning, expression, and developmental characterization of the murine retinoblastoma-related gene Rb2/p130." Pertile P., Baldi A., de Luca A., Virgilio L., Pisano M.M., Giordano A. Cell Growth Differ. 6:1659-1664(1995) [PubMed: 9019172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning and expression of the Rb-related mouse p130 mRNA." Lecouter J.E., Whyte P.F.M., Rudnicki M.A. Oncogene 12:1433-1440(1996) [PubMed: 8622859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin." Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A. Nat. Cell Biol. 7:420-428(2005) [PubMed: 15750587] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; THR-414; SER-636; THR-639; SER-942 AND THR-1027, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U36799 mRNA. Translation: AAB48991.1. U50850 mRNA. Translation: AAC52598.1. U47333 mRNA. Translation: AAC52555.1.
IPI	IPI00317271.
UniGene	Mm.235580
3D structure databases
HSSP	HSSP built from PDB template 1O9K based on UniProtKB P06400.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64700. 1 interaction.
PTM databases
PhosphoSite	Q64700.
Proteomic databases
PRIDE	Q64700.
Genome annotation databases
Ensembl	ENSMUSG00000031666. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:105085. Rbl2.
Phylogenomic databases
HOGENOM	Q64700.
HOVERGEN	Q64700.
Gene expression databases
ArrayExpress	Q64700.
Bgee	Q64700.
CleanEx	MM_RBL2.
GermOnline	ENSMUSG00000031666. Mus musculus.
Family and domain databases
InterPro	IPR006670. Cyclin. IPR013763. Cyclin_related. IPR002720. RB_A. IPR002719. RB_B. [Graphical view]
Gene3D	G3DSA:1.10.472.10. Cyclin_related. 2 hits.
Pfam	PF01858. RB_A. 1 hit. PF01857. RB_B. 1 hit. [Graphical view]
SMART	SM00385. CYCLIN. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

RBL2_MOUSE

Accession

Primary (citable) accession number: Q64700

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	July 7, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents