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Q08999

- RBL2_HUMAN

UniProt

Q08999 - RBL2_HUMAN

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Protein
Retinoblastoma-like protein 2
Gene
RBL2, RB2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 2
PRO_0000167841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei639 – 6391Phosphoserine1 Publication
Modified residuei642 – 6421Phosphothreonine By similarity
Modified residuei662 – 6621Phosphoserine1 Publication
Modified residuei672 – 6721Phosphoserine2 Publications
Modified residuei948 – 9481Phosphoserine By similarity
Modified residuei952 – 9521Phosphoserine1 Publication
Modified residuei966 – 9661Phosphoserine1 Publication
Modified residuei971 – 9711Phosphoserine Inferred
Modified residuei972 – 9721Phosphoserine Inferred
Modified residuei973 – 9731Phosphoserine Inferred
Modified residuei974 – 9741Phosphothreonine Inferred
Modified residuei981 – 9811Phosphoserine Inferred
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.2 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).4 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni417 – 1024608Pocket; binds E1A
Add
BLAST
Regioni417 – 616200Domain A
Add
BLAST
Regioni617 – 827211Spacer
Add
BLAST
Regioni828 – 1024197Domain B
Add
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

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

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.
VSP_054328Add
BLAST
Alternative sequencei638 – 1042405Missing in isoform 2.
VSP_054329Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371P → S in CAA53661. 1 Publication
Sequence conflicti37 – 371P → S in AAC50479. 1 Publication
Sequence conflicti64 – 641A → P1 Publication
Sequence conflicti64 – 641A → P1 Publication
Sequence conflicti206 – 2061V → M in CAA52671. 1 Publication
Sequence conflicti1093 – 10931R → H in AAH34490. 1 Publication

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.
ENST00000544545; ENSP00000444685; ENSG00000103479.
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 .
ENST00000544545 ; ENSP00000444685 ; ENSG00000103479 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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