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Q08999

- RBL2_HUMAN

UniProt

Q08999 - RBL2_HUMAN

Protein

Retinoblastoma-like protein 2

Gene

RBL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (17 Oct 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, 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.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. mitotic cell cycle Source: Reactome
    3. regulation of cell cycle Source: InterPro
    4. regulation of lipid kinase activity Source: UniProtKB
    5. regulation of transcription from RNA polymerase II promoter Source: InterPro
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_821. Cyclin D associated events in G1.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RBL2
    Synonyms:RB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9894. RBL2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nucleolus Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA34258.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11391139Retinoblastoma-like protein 2PRO_0000167841Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei639 – 6391Phosphoserine1 Publication
    Modified residuei642 – 6421PhosphothreonineBy similarity
    Modified residuei662 – 6621Phosphoserine1 Publication
    Modified residuei672 – 6721Phosphoserine2 Publications
    Modified residuei948 – 9481PhosphoserineBy similarity
    Modified residuei952 – 9521Phosphoserine1 Publication
    Modified residuei966 – 9661Phosphoserine1 Publication
    Modified residuei971 – 9711Phosphoserine1 Publication
    Modified residuei972 – 9721Phosphoserine1 Publication
    Modified residuei973 – 9731Phosphoserine1 Publication
    Modified residuei974 – 9741Phosphothreonine1 Publication
    Modified residuei981 – 9811Phosphoserine1 Publication
    Modified residuei982 – 9821Phosphoserine1 Publication
    Modified residuei986 – 9861Phosphothreonine1 Publication
    Modified residuei1035 – 10351Phosphoserine1 Publication

    Post-translational modificationi

    During G0 and early G1 phase of the cell cycle, phosphorylated on Ser-639 and on 5 sites within the domain B. Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent proteolysis.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ08999.
    PaxDbiQ08999.
    PRIDEiQ08999.

    PTM databases

    PhosphoSiteiQ08999.

    Expressioni

    Developmental stagei

    G0-restricted expression.

    Gene expression databases

    ArrayExpressiQ08999.
    BgeeiQ08999.
    CleanExiHS_RBL2.
    GenevestigatoriQ08999.

    Organism-specific databases

    HPAiCAB016547.
    HPA019703.

    Interactioni

    Subunit structurei

    Interacts with AATF. 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 RINT1. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5).By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032552EBI-971439,EBI-2603114From a different organism.
    DGKZQ13574-22EBI-971439,EBI-715527
    LIN54Q6MZP710EBI-971439,EBI-1389411
    Pax3P246103EBI-971439,EBI-1208116From a different organism.
    PPP2CAP677752EBI-971439,EBI-712311
    Sirt1Q923E42EBI-971439,EBI-1802585From a different organism.
    Vsx2Q614124EBI-971439,EBI-1208174From a different organism.

    Protein-protein interaction databases

    BioGridi111869. 59 interactions.
    DIPiDIP-425N.
    IntActiQ08999. 33 interactions.
    MINTiMINT-102310.
    STRINGi9606.ENSP00000262133.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08999.
    SMRiQ08999. Positions 49-618, 832-933.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni417 – 1024608Pocket; binds E1AAdd
    BLAST
    Regioni417 – 616200Domain AAdd
    BLAST
    Regioni617 – 827211SpacerAdd
    BLAST
    Regioni828 – 1024197Domain BAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 168Poly-Pro
    Compositional biasi17 – 204Poly-Ala
    Compositional biasi23 – 264Poly-Glu
    Compositional biasi998 – 10014Poly-Glu

    Sequence similaritiesi

    Belongs to the retinoblastoma protein (RB) family.Curated

    Phylogenomic databases

    eggNOGiNOG296920.
    HOGENOMiHOG000273892.
    HOVERGENiHBG017710.
    InParanoidiQ08999.
    KOiK16332.
    OMAiPPGNFPF.
    OrthoDBiEOG7P5T04.
    PhylomeDBiQ08999.
    TreeFamiTF105568.

    Family and domain databases

    Gene3Di1.10.472.10. 3 hits.
    InterProiIPR013763. Cyclin-like.
    IPR028308. RB2.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view]
    PANTHERiPTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF8. PTHR13742:SF8. 1 hit.
    PfamiPF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    [Graphical view]
    SMARTiSM00385. CYCLIN. 2 hits.
    [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: Q08999-1) [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

    MPSGGDQSPP PPPPPPAAAA SDEEEEDDGE AEDAAPPAES PTPQIQQRFD     50
    ELCSRLNMDE AARAEAWDSY RSMSESYTLE GNDLHWLACA LYVACRKSVP 100
    TVSKGTVEGN YVSLTRILKC SEQSLIEFFN KMKKWEDMAN LPPHFRERTE 150
    RLERNFTVSA VIFKKYEPIF QDIFKYPQEE QPRQQRGRKQ RRQPCTVSEI 200
    FHFCWVLFIY AKGNFPMISD DLVNSYHLLL CALDLVYGNA LQCSNRKELV 250
    NPNFKGLSED FHAKDSKPSS DPPCIIEKLC SLHDGLVLEA KGIKEHFWKP 300
    YIRKLYEKKL LKGKEENLTG FLEPGNFGES FKAINKAYEE YVLSVGNLDE 350
    RIFLGEDAEE EIGTLSRCLN AGSGTETAER VQMKNILQQH FDKSKALRIS 400
    TPLTGVRYIK ENSPCVTPVS TATHSLSRLH TMLTGLRNAP SEKLEQILRT 450
    CSRDPTQAIA NRLKEMFEIY SQHFQPDEDF SNCAKEIASK HFRFAEMLYY 500
    KVLESVIEQE QKRLGDMDLS GILEQDAFHR SLLACCLEVV TFSYKPPGNF 550
    PFITEIFDVP LYHFYKVIEV FIRAEDGLCR EVVKHLNQIE EQILDHLAWK 600
    PESPLWEKIR DNENRVPTCE EVMPPQNLER ADEICIAGSP LTPRRVTEVR 650
    ADTGGLGRSI TSPTTLYDRY SSPPASTTRR RLFVENDSPS DGGTPGRMPP 700
    QPLVNAVPVQ NVSGETVSVT PVPGQTLVTM ATATVTANNG QTVTIPVQGI 750
    ANENGGITFF PVQVNVGGQA QAVTGSIQPL SAQALAGSLS SQQVTGTTLQ 800
    VPGQVAIQQI SPGGQQQKQG QSVTSSSNRP RKTSSLSLFF RKVYHLAAVR 850
    LRDLCAKLDI SDELRKKIWT CFEFSIIQCP ELMMDRHLDQ LLMCAIYVMA 900
    KVTKEDKSFQ NIMRCYRTQP QARSQVYRSV LIKGKRKRRN SGSSDSRSHQ 950
    NSPTELNKDR TSRDSSPVMR SSSTLPVPQP SSAPPTPTRL TGANSDMEEE 1000
    ERGDLIQFYN NIYIKQIKTF AMKYSQANMD APPLSPYPFV RTGSPRRIQL 1050
    SQNHPVYISP HKNETMLSPR EKIFYYFSNS PSKRLREINS MIRTGETPTK 1100
    KRGILLEDGS ESPAKRICPE NHSALLRRLQ DVANDRGSH 1139
    Length:1,139
    Mass (Da):128,367
    Last modified:October 17, 2006 - v3
    Checksum:iD129032FB1F383D4
    GO
    Isoform 2 (identifier: Q08999-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-216: Missing.
         638-1042: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:518
    Mass (Da):59,349
    Checksum:i12F3758A5A3AD0D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371P → S in CAA53661. (PubMed:8253383)Curated
    Sequence conflicti37 – 371P → S in AAC50479. (PubMed:8643454)Curated
    Sequence conflicti64 – 641A → P(PubMed:8253383)Curated
    Sequence conflicti64 – 641A → P(PubMed:8643454)Curated
    Sequence conflicti206 – 2061V → M in CAA52671. (PubMed:8361765)Curated
    Sequence conflicti1093 – 10931R → H in AAH34490. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991V → F.1 Publication
    VAR_069377
    Natural varianti210 – 2101Y → C.
    Corresponds to variant rs17800727 [ dbSNP | Ensembl ].
    VAR_028437

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 216216Missing in isoform 2. 1 PublicationVSP_054328Add
    BLAST
    Alternative sequencei638 – 1042405Missing in isoform 2. 1 PublicationVSP_054329Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76061 mRNA. Translation: CAA53661.1.
    S67171 mRNA. Translation: AAB29227.1.
    AK304283 mRNA. Translation: BAH14149.1.
    AC007342 Genomic DNA. No translation available.
    BC034490 mRNA. Translation: AAH34490.1.
    X74594 mRNA. Translation: CAA52671.1.
    U53220 Genomic DNA. Translation: AAC50479.1.
    CCDSiCCDS10748.1. [Q08999-1]
    PIRiA49370.
    RefSeqiNP_005602.3. NM_005611.3. [Q08999-1]
    UniGeneiHs.513609.

    Genome annotation databases

    EnsembliENST00000262133; ENSP00000262133; ENSG00000103479. [Q08999-1]
    ENST00000544545; ENSP00000444685; ENSG00000103479. [Q08999-2]
    GeneIDi5934.
    KEGGihsa:5934.
    UCSCiuc002ehi.4. human. [Q08999-1]

    Polymorphism databases

    DMDMi116242746.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76061 mRNA. Translation: CAA53661.1 .
    S67171 mRNA. Translation: AAB29227.1 .
    AK304283 mRNA. Translation: BAH14149.1 .
    AC007342 Genomic DNA. No translation available.
    BC034490 mRNA. Translation: AAH34490.1 .
    X74594 mRNA. Translation: CAA52671.1 .
    U53220 Genomic DNA. Translation: AAC50479.1 .
    CCDSi CCDS10748.1. [Q08999-1 ]
    PIRi A49370.
    RefSeqi NP_005602.3. NM_005611.3. [Q08999-1 ]
    UniGenei Hs.513609.

    3D structure databases

    ProteinModelPortali Q08999.
    SMRi Q08999. Positions 49-618, 832-933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111869. 59 interactions.
    DIPi DIP-425N.
    IntActi Q08999. 33 interactions.
    MINTi MINT-102310.
    STRINGi 9606.ENSP00000262133.

    PTM databases

    PhosphoSitei Q08999.

    Polymorphism databases

    DMDMi 116242746.

    Proteomic databases

    MaxQBi Q08999.
    PaxDbi Q08999.
    PRIDEi Q08999.

    Protocols and materials databases

    DNASUi 5934.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262133 ; ENSP00000262133 ; ENSG00000103479 . [Q08999-1 ]
    ENST00000544545 ; ENSP00000444685 ; ENSG00000103479 . [Q08999-2 ]
    GeneIDi 5934.
    KEGGi hsa:5934.
    UCSCi uc002ehi.4. human. [Q08999-1 ]

    Organism-specific databases

    CTDi 5934.
    GeneCardsi GC16P053467.
    HGNCi HGNC:9894. RBL2.
    HPAi CAB016547.
    HPA019703.
    MIMi 180203. gene.
    neXtProti NX_Q08999.
    PharmGKBi PA34258.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296920.
    HOGENOMi HOG000273892.
    HOVERGENi HBG017710.
    InParanoidi Q08999.
    KOi K16332.
    OMAi PPGNFPF.
    OrthoDBi EOG7P5T04.
    PhylomeDBi Q08999.
    TreeFami TF105568.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_821. Cyclin D associated events in G1.

    Miscellaneous databases

    ChiTaRSi RBL2. human.
    GeneWikii Retinoblastoma-like_protein_2.
    GenomeRNAii 5934.
    NextBioi 23132.
    PROi Q08999.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08999.
    Bgeei Q08999.
    CleanExi HS_RBL2.
    Genevestigatori Q08999.

    Family and domain databases

    Gene3Di 1.10.472.10. 3 hits.
    InterProi IPR013763. Cyclin-like.
    IPR028308. RB2.
    IPR002720. RB_A.
    IPR002719. RB_B.
    IPR028309. RB_fam.
    IPR024599. RB_N.
    [Graphical view ]
    PANTHERi PTHR13742. PTHR13742. 1 hit.
    PTHR13742:SF8. PTHR13742:SF8. 1 hit.
    Pfami PF11934. DUF3452. 1 hit.
    PF01858. RB_A. 1 hit.
    PF01857. RB_B. 1 hit.
    [Graphical view ]
    SMARTi SM00385. CYCLIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The adenovirus E1A-associated 130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E."
      Li Y., Graham C., Lacy S., Duncan A.M.V., Whyte P.
      Genes Dev. 7:2366-2377(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta and Spleen.
    2. "Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins."
      Hannon G.J., Demetrick D., Beach D.
      Genes Dev. 7:2378-2391(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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 2).
      Tissue: Trachea.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      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 1).
      Tissue: Testis.
    6. "Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain."
      Mayol X., Grana X., Baldi A., Sang N., Hu Q., Giordano A.
      Oncogene 8:2561-2566(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-1139 (ISOFORM 1).
    7. "Genomic structure of the human retinoblastoma-related Rb2/p130 gene."
      Baldi A., Boccia V., Claudio P.P., de Luca A., Giordano A.
      Proc. Natl. Acad. Sci. U.S.A. 93:4629-4632(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
      Tissue: Placenta.
    8. "Phosphorylation of the retinoblastoma-related protein p130 in growth-arrested cells."
      Canhoto A.J., Chestukhin A., Litovchick L., DeCaprio J.A.
      Oncogene 19:5116-5122(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-639; SER-952; SER-966; SER-971; SER-972; SER-973; THR-974; SER-981; SER-982 AND THR-986, IDENTIFICATION BY MASS SPECTROMETRY.
    9. Cited for: INTERACTION WITH AATF.
    10. "The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)."
      Tedesco D., Lukas J., Reed S.I.
      Genes Dev. 16:2946-2957(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-672.
    11. "The Rb-related p130 protein controls telomere lengthening through an interaction with a Rad50-interacting protein, RINT-1."
      Kong L.-J., Meloni A.R., Nevins J.R.
      Mol. Cell 22:63-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RINT1.
    12. "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.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 SER-662; SER-672 AND SER-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence."
      Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M., Dejean A., Bischof O.
      EMBO J. 31:95-109(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML.
    17. Cited for: VARIANT PHE-99.

    Entry informationi

    Entry nameiRBL2_HUMAN
    AccessioniPrimary (citable) accession number: Q08999
    Secondary accession number(s): B7Z913
    , Q15073, Q16084, Q8NE70, Q92812
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 144 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3