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P28749 (RBL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoblastoma-like protein 1
Alternative name(s):
107 kDa retinoblastoma-associated protein
Short name=p107
pRb1
Gene names
Name:RBL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1068 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. 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.

Subunit structure

Interacts with SUV420H1, SUV420H2 and USP4 By similarity. 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 AATF. Interacts with KDM5A. Interacts with SV40 and JC virus large T antigens. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Subcellular location

Nucleus Potential.

Post-translational modification

Exists in both phosphorylated and unphosphorylated forms, and T, but not E1A, binds only to the unphosphorylated form. Cell-cycle arrest properties are inactivated by phosphorylation on Thr-332, Ser-640, Ser-964 and Ser-975 by CDK4. Ref.8 Ref.12

Sequence similarities

Belongs to the retinoblastoma protein (RB) family.

Ontologies

Keywords
   Biological processCell cycle
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

regulation of cell cycle

Inferred from electronic annotation. Source: InterPro

regulation of lipid kinase activity

Inferred from direct assay PubMed 16286473. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16286473. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28749-1)

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 2 (identifier: P28749-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1013-1068: SLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH → VR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10681068Retinoblastoma-like protein 1
PRO_0000167839

Regions

Region385 – 949565Pocket; binds T and E1A
Region385 – 584200Domain A
Region585 – 780196Spacer
Region781 – 949169Domain B

Amino acid modifications

Modified residue3321Phosphothreonine; by CDK2 Ref.8
Modified residue3691Phosphothreonine; by CDK4 Ref.8 Ref.12
Modified residue3851Phosphothreonine; by CDK2 Ref.8 Ref.15
Modified residue6401Phosphoserine; by CDK2 and CDK4 Ref.8
Modified residue6501Phosphoserine Ref.12
Modified residue7491Phosphoserine Ref.15
Modified residue7621Phosphoserine; by CDK2 Ref.8 Ref.15
Modified residue9641Phosphoserine; by CDK2 and CDK4 Ref.8
Modified residue9751Phosphoserine; by CDK2 and CDK4 Ref.8
Modified residue9881Phosphoserine; by CDK2 Ref.8
Modified residue9971Phosphothreonine; by CDK2 Ref.8
Modified residue10091Phosphoserine; by CDK2 Ref.8
Modified residue10411Phosphoserine By similarity

Natural variations

Alternative sequence1013 – 106856SLKDI…ERANH → VR in isoform 2.
VSP_017496
Natural variant10351I → M.
Corresponds to variant rs8114297 [ dbSNP | Ensembl ].
VAR_034443

Experimental info

Mutagenesis6401S → A: Strongly reduces phosphorylation by CDK2 and CDK4. Ref.8
Mutagenesis6431S → R: No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated with 657-A--A-660. Ref.8
Mutagenesis6501S → A: No effect on phosphorylation by CDK2. Ref.8
Mutagenesis657 – 6604KRRL → AAAA: Reduces S-640 phosphorylation by CDK2 and CDK4. Ref.8
Sequence conflict3261Missing AA sequence Ref.8
Sequence conflict9281G → S Ref.1
Sequence conflict9281G → S Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 2BC4876EA04BDB31

FASTA1,068120,847
        10         20         30         40         50         60 
MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS LEGEVTHWLA 

        70         80         90        100        110        120 
CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ FFSKMKKWMD MSNLPQEFRE 

       130        140        150        160        170        180 
RIERLERNFE VSTVIFKKYE PIFLDIFQNP YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL 

       190        200        210        220        230        240 
FVYTKGNFRM IGDDLVNSYH LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT 

       250        260        270        280        290        300 
ASEEPPCIIA VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK 

       310        320        330        340        350        360 
AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN VEYNLQQHFE 

       370        380        390        400        410        420 
KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI VAGLKNAPSD QLINIFESCV 

       430        440        450        460        470        480 
RNPVENIMKI LKGIGETFCQ HYTQSTDEQP GSHIDFAVNR LKLAEILYYK ILETVMVQET 

       490        500        510        520        530        540 
RRLHGMDMSV LLEQDIFHRS LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV 

       550        560        570        580        590        600 
IRSEEGLSRD MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG 

       610        620        630        640        650        660 
NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS PTAGSAKRRL 

       670        680        690        700        710        720 
FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ TLLTMATAPV TGTTGHKVTI 

       730        740        750        760        770        780 
PLHGVANDAG EITLIPLSMN TNQESKVKSP VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN 

       790        800        810        820        830        840 
RPKRTGSLAL FYRKVYHLAS VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL 

       850        860        870        880        890        900 
DQLLLCAFYI MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND 

       910        920        930        940        950        960 
DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD LANQDHMMDA 

       970        980        990       1000       1010       1020 
PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS ALLYKFNGSP SKSLKDINNM 

      1030       1040       1050       1060 
IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN DDVLLKRLQD VVSERANH 

« Hide

Isoform 2 [UniParc].

Checksum: CE1D47DBF365C4CB
Show »

FASTA1,014114,688

References

« Hide 'large scale' references
[1]"Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein."
Zhu L., van den Heuvel S., Helin K., Fattaey A., Ewen M., Livingston D., Dyson N., Harlow E.
Genes Dev. 7:1111-1125(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Tongue.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein."
Ewen M.E., Xing Y., Lawrence J.B., Livingston D.M.
Cell 66:1155-1164(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-1068 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[7]"Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins."
Zhu L., Zhu L., Xie E., Chang L.S.
Mol. Cell. Biol. 15:3552-3562(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
[8]"Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4."
Leng X., Noble M., Adams P.D., Qin J., Harper J.W.
Mol. Cell. Biol. 22:2242-2254(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 320-334; 364-374; 635-657; 949-977 AND 1006-1012, PHOSPHORYLATION AT THR-332; THR-369; THR-385; SER-640; SER-762; SER-964; SER-975; SER-988; THR-997 AND SER-1009, MUTAGENESIS OF SER-640; SER-643; SER-650 AND 657-LYS--LEU-660, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus."
Dyson N., Buchkovich K., Whyte P., Harlow E.
Cell 58:249-255(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 AND JC VIRUS LARGE T ANTIGEN.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5A.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AATF.
[12]"Distinct phosphorylation events regulate p130- and p107-mediated repression of E2F-4."
Farkas T., Hansen K., Holm K., Lukas J., Bartek J.
J. Biol. Chem. 277:26741-26752(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-369 AND SER-650.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WITH E2F4 AND TFDP1.
[14]"LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385; SER-749 AND SER-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14812 mRNA. Translation: AAA02489.1.
AK290380 mRNA. Translation: BAF83069.1.
AL136172, AL365505, AL391114 Genomic DNA. Translation: CAI95716.1.
AL365505, AL136172, AL391114 Genomic DNA. Translation: CAI95177.1.
AL391114, AL136172, AL365505 Genomic DNA. Translation: CAI95151.1.
AL365505, AL136172, AL391114 Genomic DNA. Translation: CAI95178.1.
AL391114, AL136172, AL365505 Genomic DNA. Translation: CAI95152.1.
AL136172, AL365505, AL391114 Genomic DNA. Translation: CAI95717.1.
CH471077 Genomic DNA. Translation: EAW76088.1.
BC032247 mRNA. Translation: AAH32247.1.
M74547 mRNA. Translation: AAA36397.1.
S78664 Genomic DNA. Translation: AAD14290.1.
CCDSCCDS13289.1. [P28749-1]
CCDS13290.1. [P28749-2]
PIRA40265. A47319.
RefSeqNP_002886.2. NM_002895.3. [P28749-1]
NP_899662.1. NM_183404.2. [P28749-2]
UniGeneHs.207745.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H28X-ray2.80E/F653-663[»]
ProteinModelPortalP28749.
SMRP28749. Positions 86-587, 782-969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111868. 70 interactions.
DIPDIP-148N.
IntActP28749. 35 interactions.
MINTMINT-1353484.
STRING9606.ENSP00000362768.

PTM databases

PhosphoSiteP28749.

Polymorphism databases

DMDM90103515.

Proteomic databases

MaxQBP28749.
PaxDbP28749.
PRIDEP28749.

Protocols and materials databases

DNASU5933.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344359; ENSP00000343646; ENSG00000080839. [P28749-2]
ENST00000373664; ENSP00000362768; ENSG00000080839. [P28749-1]
GeneID5933.
KEGGhsa:5933.
UCSCuc002xgi.3. human. [P28749-1]
uc002xgj.1. human. [P28749-2]

Organism-specific databases

CTD5933.
GeneCardsGC20M035624.
H-InvDBHIX0040570.
HGNCHGNC:9893. RBL1.
HPAHPA054962.
HPA056525.
MIM116957. gene.
neXtProtNX_P28749.
PharmGKBPA34257.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296920.
HOGENOMHOG000273892.
HOVERGENHBG017710.
InParanoidP28749.
KOK04681.
OMARRDMQPL.
OrthoDBEOG7P5T04.
PhylomeDBP28749.
TreeFamTF105568.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP28749.
BgeeP28749.
CleanExHS_RBL1.
GenevestigatorP28749.

Family and domain databases

Gene3D1.10.472.10. 3 hits.
InterProIPR013763. Cyclin-like.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
IPR028310. RBL1.
[Graphical view]
PANTHERPTHR13742. PTHR13742. 1 hit.
PTHR13742:SF20. PTHR13742:SF20. 1 hit.
PfamPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMSSF47954. SSF47954. 3 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP28749.
GeneWikiRetinoblastoma-like_protein_1.
GenomeRNAi5933.
NextBio23126.
PROP28749.
SOURCESearch...

Entry information

Entry nameRBL1_HUMAN
AccessionPrimary (citable) accession number: P28749
Secondary accession number(s): A8K2W5 expand/collapse secondary AC list , Q4VXA0, Q8N5K6, Q9H1L5, Q9H1M1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM