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Q64700 (RBL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoblastoma-like protein 2
Alternative name(s):
130 kDa retinoblastoma-associated protein
Short name=p130
Retinoblastoma-related protein 2
Short name=RBR-2
pRb2
Gene names
Name:Rbl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1135 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.6

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. Interacts with USP4 By similarity. Interacts with SUV420H1, SUV420H2 and USP4. Interacts with PML By similarity. Ref.5 Ref.6

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CenpfQ155P73EBI-2271232,EBI-2211248

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11351135Retinoblastoma-like protein 2
PRO_0000167842

Regions

Region414 – 1021608Pocket; binds E1A
Region414 – 613200Domain A
Region614 – 824211Spacer
Region825 – 1021197Domain B
Compositional bias9 – 135Poly-Pro
Compositional bias14 – 174Poly-Ala
Compositional bias20 – 245Poly-Glu
Compositional bias992 – 9954Poly-Glu

Amino acid modifications

Modified residue6361Phosphoserine Ref.7
Modified residue6391Phosphothreonine Ref.7
Modified residue6591Phosphoserine By similarity
Modified residue6691Phosphoserine By similarity
Modified residue9421Phosphoserine Ref.7
Modified residue9461Phosphoserine By similarity
Modified residue9601Phosphoserine By similarity
Modified residue9761Phosphoserine By similarity
Modified residue9801Phosphothreonine By similarity
Modified residue10311Phosphoserine By similarity

Experimental info

Sequence conflict209 – 25143Missing in AAC52555. Ref.3
Sequence conflict3411A → P in AAB48991. Ref.1
Sequence conflict3421A → P in AAC52555. Ref.3
Sequence conflict3811R → T in AAC52598. Ref.2
Sequence conflict4281T → S in AAC52598. Ref.2
Sequence conflict4311S → T in AAC52598. Ref.2
Sequence conflict4431R → Q in AAC52598. Ref.2
Sequence conflict483 – 49210Missing in AAB48991. Ref.1
Sequence conflict7681A → R in AAC52598. Ref.2
Sequence conflict8261P → A in AAC52555. Ref.3
Sequence conflict947 – 9482PT → RA in AAC52555. Ref.3
Sequence conflict10231A → S in AAC52598. Ref.2
Sequence conflict10441V → I in AAC52598. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64700 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: F509E68A156929B2

FASTA1,135127,485
        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 LERILRSCSR 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 
ANAQTDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHNNE AMPSPREKIF YYFSNSPSKR 

      1090       1100       1110       1120       1130 
LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[5]"Association of UNP, a ubiquitin-specific protease, with the pocket proteins pRb, p107 and p130."
Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.
Oncogene 20:5533-5537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP4.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636; THR-639 AND SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36799 mRNA. Translation: AAB48991.1.
U50850 mRNA. Translation: AAC52598.1.
U47333 mRNA. Translation: AAC52555.1.
AK160027 mRNA. Translation: BAE35570.1.
CCDSCCDS22518.1.
RefSeqNP_001268929.1. NM_001282000.1.
NP_001268930.1. NM_001282001.1.
NP_035380.3. NM_011250.4.
UniGeneMm.235580.

3D structure databases

ProteinModelPortalQ64700.
SMRQ64700. Positions 425-612, 828-935.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202820. 5 interactions.
IntActQ64700. 4 interactions.
MINTMINT-5181879.
STRING10090.ENSMUSP00000034091.

PTM databases

PhosphoSiteQ64700.

Proteomic databases

PaxDbQ64700.
PRIDEQ64700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034091; ENSMUSP00000034091; ENSMUSG00000031666.
GeneID19651.
KEGGmmu:19651.
UCSCuc012gid.1. mouse.

Organism-specific databases

CTD5934.
MGIMGI:105085. Rbl2.

Phylogenomic databases

eggNOGNOG296920.
GeneTreeENSGT00530000063235.
HOGENOMHOG000273892.
HOVERGENHBG017710.
InParanoidQ3TVP8.
KOK16332.
OMAPPGNFPF.
OrthoDBEOG7P5T04.
TreeFamTF105568.

Gene expression databases

ArrayExpressQ64700.
BgeeQ64700.
CleanExMM_RBL2.
GenevestigatorQ64700.

Family and domain databases

Gene3D1.10.472.10. 3 hits.
InterProIPR013763. Cyclin-like.
IPR028308. RB2.
IPR002720. RB_A.
IPR002719. RB_B.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF8. PTHR13742:SF8. 1 hit.
PfamPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
[Graphical view]
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

NextBio296912.
PROQ64700.
SOURCESearch...

Entry information

Entry nameRBL2_MOUSE
AccessionPrimary (citable) accession number: Q64700
Secondary accession number(s): Q3TVP8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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