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P28749

- RBL1_HUMAN

UniProt

P28749 - RBL1_HUMAN

Protein

Retinoblastoma-like protein 1

Gene

RBL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. gene expression Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    6. regulation of cell cycle Source: InterPro
    7. regulation of lipid kinase activity Source: UniProtKB
    8. transcription, DNA-templated Source: Reactome
    9. transcription initiation from RNA polymerase II promoter Source: Reactome
    10. transforming growth factor beta receptor signaling pathway Source: Reactome
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinoblastoma-like protein 1
    Alternative name(s):
    107 kDa retinoblastoma-associated protein
    Short name:
    p107
    pRb1
    Gene namesi
    Name:RBL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9893. RBL1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: HPA
    3. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi640 – 6401S → A: Strongly reduces phosphorylation by CDK2 and CDK4. 1 Publication
    Mutagenesisi643 – 6431S → R: No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated with 657-A--A-660. 1 Publication
    Mutagenesisi650 – 6501S → A: No effect on phosphorylation by CDK2. 1 Publication
    Mutagenesisi657 – 6604KRRL → AAAA: Reduces S-640 phosphorylation by CDK2 and CDK4.

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34257.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10681068Retinoblastoma-like protein 1PRO_0000167839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei332 – 3321Phosphothreonine; by CDK21 Publication
    Modified residuei369 – 3691Phosphothreonine; by CDK42 Publications
    Modified residuei385 – 3851Phosphothreonine; by CDK22 Publications
    Modified residuei640 – 6401Phosphoserine; by CDK2 and CDK41 Publication
    Modified residuei650 – 6501Phosphoserine1 Publication
    Modified residuei749 – 7491Phosphoserine1 Publication
    Modified residuei762 – 7621Phosphoserine; by CDK22 Publications
    Modified residuei964 – 9641Phosphoserine; by CDK2 and CDK41 Publication
    Modified residuei975 – 9751Phosphoserine; by CDK2 and CDK41 Publication
    Modified residuei988 – 9881Phosphoserine; by CDK21 Publication
    Modified residuei997 – 9971Phosphothreonine; by CDK21 Publication
    Modified residuei1009 – 10091Phosphoserine; by CDK21 Publication
    Modified residuei1041 – 10411PhosphoserineBy similarity

    Post-translational modificationi

    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 CDK4.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP28749.
    PaxDbiP28749.
    PRIDEiP28749.

    PTM databases

    PhosphoSiteiP28749.

    Expressioni

    Gene expression databases

    ArrayExpressiP28749.
    BgeeiP28749.
    CleanExiHS_RBL1.
    GenevestigatoriP28749.

    Organism-specific databases

    HPAiHPA054962.
    HPA056525.

    Interactioni

    Subunit structurei

    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.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032553EBI-971402,EBI-2603114From a different organism.
    BEGAINQ9BUH82EBI-971402,EBI-742722
    CDK4P118022EBI-971402,EBI-295644
    DGKZQ13574-22EBI-971402,EBI-715527
    DHX30Q7L2E34EBI-971402,EBI-1211456
    DYRK1AQ136273EBI-971402,EBI-1053596
    DYRK1BQ9Y4633EBI-971402,EBI-634187
    IRF3Q146532EBI-971402,EBI-2650369
    NR2E3Q9Y5X42EBI-971402,EBI-7216962
    Pax3P246103EBI-971402,EBI-1208116From a different organism.
    PPP2CAP677752EBI-971402,EBI-712311
    Sirt1Q923E42EBI-971402,EBI-1802585From a different organism.

    Protein-protein interaction databases

    BioGridi111868. 70 interactions.
    DIPiDIP-148N.
    IntActiP28749. 35 interactions.
    MINTiMINT-1353484.
    STRINGi9606.ENSP00000362768.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H28X-ray2.80E/F653-663[»]
    ProteinModelPortaliP28749.
    SMRiP28749. Positions 86-587, 782-969.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28749.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni385 – 949565Pocket; binds T and E1AAdd
    BLAST
    Regioni385 – 584200Domain AAdd
    BLAST
    Regioni585 – 780196SpacerAdd
    BLAST
    Regioni781 – 949169Domain BAdd
    BLAST

    Sequence similaritiesi

    Belongs to the retinoblastoma protein (RB) family.Curated

    Phylogenomic databases

    eggNOGiNOG296920.
    HOGENOMiHOG000273892.
    HOVERGENiHBG017710.
    InParanoidiP28749.
    KOiK04681.
    OMAiRRDMQPL.
    OrthoDBiEOG7P5T04.
    PhylomeDBiP28749.
    TreeFamiTF105568.

    Family and domain databases

    Gene3Di1.10.472.10. 3 hits.
    InterProiIPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    IPR028310. RBL1.
    [Graphical view]
    PANTHERiPTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF20. PTHR13742:SF20. 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.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28749-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MFEDKPHAEG AAVVAAAGEA LQALCQELNL DEGSAAEALD DFTAIRGNYS     50
    LEGEVTHWLA CSLYVACRKS IIPTVGKGIM EGNCVSLTRI LRSAKLSLIQ 100
    FFSKMKKWMD MSNLPQEFRE RIERLERNFE VSTVIFKKYE PIFLDIFQNP 150
    YEEPPKLPRS RKQRRIPCSV KDLFNFCWTL FVYTKGNFRM IGDDLVNSYH 200
    LLLCCLDLIF ANAIMCPNRQ DLLNPSFKGL PSDFHTADFT ASEEPPCIIA 250
    VLCELHDGLL VEAKGIKEHY FKPYISKLFD RKILKGECLL DLSSFTDNSK 300
    AVNKEYEEYV LTVGDFDERI FLGADAEEEI GTPRKFTRDT PLGKLTAQAN 350
    VEYNLQQHFE KKRSFAPSTP LTGRRYLREK EAVITPVASA TQSVSRLQSI 400
    VAGLKNAPSD QLINIFESCV RNPVENIMKI LKGIGETFCQ HYTQSTDEQP 450
    GSHIDFAVNR LKLAEILYYK ILETVMVQET RRLHGMDMSV LLEQDIFHRS 500
    LMACCLEIVL FAYSSPRTFP WIIEVLNLQP FYFYKVIEVV IRSEEGLSRD 550
    MVKHLNSIEE QILESLAWSH DSALWEALQV SANKVPTCEE VIFPNNFETG 600
    NGGNVQGHLP LMPMSPLMHP RVKEVRTDSG SLRRDMQPLS PISVHERYSS 650
    PTAGSAKRRL FGEDPPKEML MDKIITEGTK LKIAPSSSIT AENVSILPGQ 700
    TLLTMATAPV TGTTGHKVTI PLHGVANDAG EITLIPLSMN TNQESKVKSP 750
    VSLTAHSLIG ASPKQTNLTK AQEVHSTGIN RPKRTGSLAL FYRKVYHLAS 800
    VRLRDLCLKL DVSNELRRKI WTCFEFTLVH CPDLMKDRHL DQLLLCAFYI 850
    MAKVTKEERT FQEIMKSYRN QPQANSHVYR SVLLKSIPRE VVAYNKNIND 900
    DFEMIDCDLE DATKTPDCSS GPVKEERGDL IKFYNTIYVG RVKSFALKYD 950
    LANQDHMMDA PPLSPFPHIK QQPGSPRRIS QQHSIYISPH KNGSGLTPRS 1000
    ALLYKFNGSP SKSLKDINNM IRQGEQRTKK RVIAIDSDAE SPAKRVCQEN 1050
    DDVLLKRLQD VVSERANH 1068
    Length:1,068
    Mass (Da):120,847
    Last modified:March 7, 2006 - v3
    Checksum:i2BC4876EA04BDB31
    GO
    Isoform 2 (identifier: P28749-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,014
    Mass (Da):114,688
    Checksum:iCE1D47DBF365C4CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261Missing AA sequence (PubMed:11884610)Curated
    Sequence conflicti928 – 9281G → S(PubMed:8319904)Curated
    Sequence conflicti928 – 9281G → S(PubMed:1833063)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1035 – 10351I → M.
    Corresponds to variant rs8114297 [ dbSNP | Ensembl ].
    VAR_034443

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1013 – 106856SLKDI…ERANH → VR in isoform 2. 1 PublicationVSP_017496Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13289.1. [P28749-1]
    CCDS13290.1. [P28749-2]
    PIRiA47319. A40265.
    RefSeqiNP_002886.2. NM_002895.3. [P28749-1]
    NP_899662.1. NM_183404.2. [P28749-2]
    UniGeneiHs.207745.

    Genome annotation databases

    EnsembliENST00000344359; ENSP00000343646; ENSG00000080839. [P28749-2]
    ENST00000373664; ENSP00000362768; ENSG00000080839. [P28749-1]
    GeneIDi5933.
    KEGGihsa:5933.
    UCSCiuc002xgi.3. human. [P28749-1]
    uc002xgj.1. human. [P28749-2]

    Polymorphism databases

    DMDMi90103515.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13289.1. [P28749-1 ]
    CCDS13290.1. [P28749-2 ]
    PIRi A47319. A40265.
    RefSeqi NP_002886.2. NM_002895.3. [P28749-1 ]
    NP_899662.1. NM_183404.2. [P28749-2 ]
    UniGenei Hs.207745.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H28 X-ray 2.80 E/F 653-663 [» ]
    ProteinModelPortali P28749.
    SMRi P28749. Positions 86-587, 782-969.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111868. 70 interactions.
    DIPi DIP-148N.
    IntActi P28749. 35 interactions.
    MINTi MINT-1353484.
    STRINGi 9606.ENSP00000362768.

    PTM databases

    PhosphoSitei P28749.

    Polymorphism databases

    DMDMi 90103515.

    Proteomic databases

    MaxQBi P28749.
    PaxDbi P28749.
    PRIDEi P28749.

    Protocols and materials databases

    DNASUi 5933.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344359 ; ENSP00000343646 ; ENSG00000080839 . [P28749-2 ]
    ENST00000373664 ; ENSP00000362768 ; ENSG00000080839 . [P28749-1 ]
    GeneIDi 5933.
    KEGGi hsa:5933.
    UCSCi uc002xgi.3. human. [P28749-1 ]
    uc002xgj.1. human. [P28749-2 ]

    Organism-specific databases

    CTDi 5933.
    GeneCardsi GC20M035624.
    H-InvDB HIX0040570.
    HGNCi HGNC:9893. RBL1.
    HPAi HPA054962.
    HPA056525.
    MIMi 116957. gene.
    neXtProti NX_P28749.
    PharmGKBi PA34257.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296920.
    HOGENOMi HOG000273892.
    HOVERGENi HBG017710.
    InParanoidi P28749.
    KOi K04681.
    OMAi RRDMQPL.
    OrthoDBi EOG7P5T04.
    PhylomeDBi P28749.
    TreeFami TF105568.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.

    Miscellaneous databases

    EvolutionaryTracei P28749.
    GeneWikii Retinoblastoma-like_protein_1.
    GenomeRNAii 5933.
    NextBioi 23126.
    PROi P28749.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28749.
    Bgeei P28749.
    CleanExi HS_RBL1.
    Genevestigatori P28749.

    Family and domain databases

    Gene3Di 1.10.472.10. 3 hits.
    InterProi IPR013763. Cyclin-like.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR015030. RB_C.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    IPR028310. RBL1.
    [Graphical view ]
    PANTHERi PTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF20. PTHR13742:SF20. 1 hit.
    Pfami PF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    PF08934. Rb_C. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 3 hits.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiRBL1_HUMAN
    AccessioniPrimary (citable) accession number: P28749
    Secondary accession number(s): A8K2W5
    , Q4VXA0, Q8N5K6, Q9H1L5, Q9H1M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3