Reviewed, UniProtKB/Swiss-Prot Q64701 (RBL1_MOUSE)

Names and origin

Protein names

Recommended name:
    Retinoblastoma-like protein 1
Alternative name(s):
    PRB1
    107 kDa retinoblastoma-associated protein
    p107

Gene names

Name:

Rbl1

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

Protein attributes

Sequence length	1063 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. 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. Forms a complex with adenovirus E1A and with SV40 large T antigen. May bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. May act as a tumor suppressor. Ref.4
Subunit structure	Interacts with AATF. Interacts with KDM5A. 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 Potential.
Tissue specificity	Highly expressed in fetal heart and liver. Expressed at low levels in all other fetal tissues except skeletal muscle. High levels in neonatal spleen and thymus with low levels in other tissues. In adult, highly expressed in testis. Barely detectable in other tissues.
Developmental stage	Highly expressed in fetal tissues. Expression markedly decreased in adult.
Post-translational modification	Phosphorylated. SV40 large T antigen binds only to the unphosphorylated form, whereas the adenovirus E1A binds to both forms. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-959 and Ser-970 by CDK4 By similarity.
Sequence similarities	Belongs to the retinoblastoma protein (RB) family.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
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 negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P12534	1	EBI-1213109,EBI-1213075	From a different organism.
Cenpf	Q155P7	2	EBI-1213109,EBI-2211248

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q64701-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: Q64701-2)

The sequence of this isoform differs from the canonical sequence as follows:
     592-594: IFP → SQG
     595-1063: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1063	1063	Retinoblastoma-like protein 1		PRO_0000167840
Regions
	Region	383 – 944	562	Pocket; binds T and E1A
	Region	383 – 584	202	Domain A
	Region	585 – 779	195	Spacer
	Region	780 – 944	165	Domain B
Amino acid modifications
	Modified residue	332	1	Phosphothreonine By similarity
	Modified residue	369	1	Phosphothreonine By similarity
	Modified residue	385	1	Phosphothreonine By similarity
	Modified residue	640	1	Phosphoserine By similarity
	Modified residue	650	1	Phosphoserine By similarity
	Modified residue	761	1	Phosphoserine By similarity
	Modified residue	959	1	Phosphoserine By similarity
	Modified residue	970	1	Phosphoserine By similarity
	Modified residue	983	1	Phosphoserine By similarity
	Modified residue	992	1	Phosphothreonine By similarity
	Modified residue	1004	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	592 – 594	3	IFP → SQG in isoform Short.		VSP_005537
	Alternative sequence	595 – 1063	469	Missing in isoform Short.		VSP_005538

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified May 1, 1997. Version 2. Checksum: 7805034B1BF56773	FASTA	1,063	119,499
	10 20 30 40 50 60 MFEDEPHAEG AAAVAAAREA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVIHWLA 70 80 90 100 110 120 CSLYVACRKS IIPTVGKGVM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 130 140 150 160 170 180 RIERLERNFE VSTVIFKKFE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 190 200 210 220 230 240 FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRR DLLNPSFKGL PSDFHAPDFK 250 260 270 280 290 300 AAEEPPCIIA VLCDLHDGLL VEAKGIKEHY FKPYISKLFD KKILKGECLL DLSSFTDNSK 310 320 330 340 350 360 AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTADT PFGKLTSQAS VECNLQQHFE 370 380 390 400 410 420 KKRSFAPSTP LTGRRYLQEK EAVTTPVASA TQSVSRLQSI VAGLKSAPSE QLLNIFESCM 430 440 450 460 470 480 RNPMGNIIKI VKGIGETFCQ HYTQSTDKQP GSHIDFAVNR LKLAEILYYK ILETIMVQET 490 500 510 520 530 540 RRLHGMDMSV LLEQDIFHKS LMACCLEIVL FAYSSPRTFP WIIEVLDLQP FYFYKVIEVV 550 560 570 580 590 600 IRSEEGLSRD MVKHLNSIEE QILESLAWTN NSALWEALHA SANRVPSCEE VIFPNNFEIG 610 620 630 640 650 660 NGGNVQGHLP MMPMSPIIHP RVKEVRTDSG SLRQDMQPLS PISVHERYSS PAAGSAKRRL 670 680 690 700 710 720 FGDDPPKDTL MDKIMAEGTK LKIAPSSVTA ESLSISPGQA LLTMATTTVT GTTGRKVTVP 730 740 750 760 770 780 LHGIANDAGE ITLVPISMNP TQESTAESPV SLTAQSLIGT SPKQTHLTKA QDAHLTGVSK 790 800 810 820 830 840 PKRTGSLALF YRKVYHLASV RLRDLCLKLD VSNELRRKIW TCFEFTLVHC PDLMKDRHLD 850 860 870 880 890 900 QLLLCAFYIM AKVTKEERTF QERMKSYRNQ PQANSHVYRS VLLKSIPGGV VVYNGDCEMT 910 920 930 940 950 960 DGDIEDATKT PNCSSEPVKE ERGDLIKFYN TVYVGRVKSF ALKYDLSNQD HIMDAPPLSP 970 980 990 1000 1010 1020 FPHIKQQPGS PRRISQQHSL YVSPHKNGAG LTPRSALLYK FNGSPSKSLK DINNMIRQGE 1030 1040 1050 1060 QKTKKRVIAI SGDADSPAKR LCQENDDVLL KRLQDVVSER ANH
	Isoform Short. Checksum: 264EAF692D791D03	FASTA	594	67,497
	10 20 30 40 50 60 MFEDEPHAEG AAAVAAAREA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVIHWLA 70 80 90 100 110 120 CSLYVACRKS IIPTVGKGVM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 130 140 150 160 170 180 RIERLERNFE VSTVIFKKFE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 190 200 210 220 230 240 FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRR DLLNPSFKGL PSDFHAPDFK 250 260 270 280 290 300 AAEEPPCIIA VLCDLHDGLL VEAKGIKEHY FKPYISKLFD KKILKGECLL DLSSFTDNSK 310 320 330 340 350 360 AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTADT PFGKLTSQAS VECNLQQHFE 370 380 390 400 410 420 KKRSFAPSTP LTGRRYLQEK EAVTTPVASA TQSVSRLQSI VAGLKSAPSE QLLNIFESCM 430 440 450 460 470 480 RNPMGNIIKI VKGIGETFCQ HYTQSTDKQP GSHIDFAVNR LKLAEILYYK ILETIMVQET 490 500 510 520 530 540 RRLHGMDMSV LLEQDIFHKS LMACCLEIVL FAYSSPRTFP WIIEVLDLQP FYFYKVIEVV 550 560 570 580 590 IRSEEGLSRD MVKHLNSIEE QILESLAWTN NSALWEALHA SANRVPSCEE VSQG

References

[1]	"Molecular cloning, chromosomal mapping, and expression of the mouse p107 gene." Huppi K., Siwarski D., Mock B.A., Dosik J., Hamel P.A. Mamm. Genome 7:353-355(1996) [PubMed: 8661722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Developmental expression of p107 mRNA and evidence for alternative splicing of the p107 (RBL1) gene product." Kim K.K., Soonpaa M.H., Wang H., Field L.J. Genomics 28:520-529(1995) [PubMed: 7490090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[3]	Kim K.K., Soonpaa M.H., Wang H., Field L.J. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U33320 mRNA. Translation: AAB18279.1. U27177 mRNA. Translation: AAB53235.1. U27178 mRNA. Translation: AAB53236.1.
IPI	IPI00137864. IPI00352179.
PIR	I49328.
UniGene	Mm.244671
3D structure databases
HSSP	HSSP built from PDB template 1GUX based on UniProtKB P06400.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64701. 2 interactions.
PTM databases
PhosphoSite	Q64701.
Proteomic databases
PRIDE	Q64701.
Genome annotation databases
Ensembl	ENSMUSG00000027641. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:103300. Rbl1.
Phylogenomic databases
HOGENOM	Q64701.
HOVERGEN	Q64701.
Gene expression databases
ArrayExpress	Q64701.
Bgee	Q64701.
CleanEx	MM_RBL1.
GermOnline	ENSMUSG00000027641. 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. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	296908.
SOURCE	Search...

Entry information

Entry name

RBL1_MOUSE

Accession

Primary (citable) accession number: Q64701

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	July 7, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)