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Retinoblastoma-associated protein (pRb) (Rb) (pp105)

 RB_RAT                  Reviewed;         920 AA.
P33568; Q63527;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 3.
25-OCT-2017, entry version 160.
RecName: Full=Retinoblastoma-associated protein;
AltName: Full=pRb;
Short=Rb;
AltName: Full=pp105;
Name=Rb1; Synonyms=Rb-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-920.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7665085; DOI=10.1016/0378-1119(95)00154-X;
Esumi M., Idutsu T., Kinugasa S., Ohno M., Nakabayashi H., Ikeda T.,
Shikata T.;
"Isolation and sequence polymorphism of a rat retinoblastoma (RB)
cDNA.";
Gene 161:231-235(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 806-920.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=8441612; DOI=10.1093/nar/21.1.170;
Roy N.K., Ballesteros A., Garte S.J.;
"Cloning and sequence of the rat retinoblastoma (Rb) gene cDNA.";
Nucleic Acids Res. 21:170-170(1993).
[4]
PHOSPHORYLATION BY CDK1 AND CDK2, AND INTERACTION WITH CDK1 AND CDK2.
PubMed=10542199; DOI=10.1074/jbc.274.45.31775;
Choi K.S., Eom Y.W., Kang Y., Ha M.J., Rhee H., Yoon J.-W., Kim S.-J.;
"Cdc2 and Cdk2 kinase activated by transforming growth factor-beta1
trigger apoptosis through the phosphorylation of retinoblastoma
protein in FaO hepatoma cells.";
J. Biol. Chem. 274:31775-31783(1999).
[5]
INTERACTION WITH DNMT1.
PubMed=10888886; DOI=10.1038/77124;
Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
Wolffe A.P.;
"DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses
transcription from E2F-responsive promoters.";
Nat. Genet. 25:338-342(2000).
[6]
FUNCTION, INTERACTION WITH SMARCA4 AND HDAC1, PHOSPHORYLATION AT
SER-787, DEPHOSPHORYLATION, AND MUTAGENESIS OF SER-772; SER-780 AND
SER-787.
PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
Qiu Z., Ghosh A.;
"A calcium-dependent switch in a CREST-BRG1 complex regulates
activity-dependent gene expression.";
Neuron 60:775-787(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-363; THR-366 AND
SER-799, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Key regulator of entry into cell division that acts as a
tumor suppressor. Promotes G0-G1 transition when phosphorylated by
CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target
genes. The underphosphorylated, active form of RB1 interacts with
E2F1 and represses its transcription activity, leading to cell
cycle arrest. 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
SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional
repression. Controls histone H4 'Lys-20' trimethylation. Inhibits
the intrinsic kinase activity of TAF1. Mediates transcriptional
repression by SMARCA4/BRG1 by recruiting a histone deacetylase
(HDAC) complex to the c-FOS promoter. In resting neurons,
transcription of the c-FOS promoter is inhibited by BRG1-dependent
recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium
influx, RB1 is dephosphorylated by calcineurin, which leads to
release of the repressor complex. {ECO:0000269|PubMed:19081374}.
-!- SUBUNIT: The hypophosphorylated form interacts with and sequesters
the E2F1 transcription factor. Interacts with heterodimeric E2F/DP
transcription factor complexes containing TFDP1 and either E2F1,
E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form
interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and
THOC1. Interacts with the N-terminal domain of TAF1. Interacts
with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, KMT5B, KMT5C, PELP1,
UHRF2 and TMPO-alpha. May interact with NDC80. Interacts with
GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with
E4F1, LIMD1 and USP4. Interacts with PRMT2. Interacts (when
methylated at Lys-852) with L3MBTL. Interacts with CHEK2;
phosphorylates RB1 (By similarity). Interacts with SMARCA4/BRG1
and HDAC1. Binds to CDK1 and CDK2. P-TEFB complex interacts with
RB1; promotes phosphorylation of RB1 (By similarity).
{ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P13405,
ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:10888886,
ECO:0000269|PubMed:19081374}.
-!- INTERACTION:
O09139:E2f1; NbExp=2; IntAct=EBI-1162932, EBI-1211101;
O88350:Rbbp9; NbExp=4; IntAct=EBI-1162932, EBI-1211014;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at
Ser-560 in G1, thereby releasing E2F1 which is then able to
activate cell growth. Dephosphorylated at the late M phase.
Phosphorylation of threonine residues in domain C promotes
interaction between the C-terminal domain C and the Pocket domain,
and thereby inhibits interactions with heterodimeric E2F/DP
transcription factor complexes. CDK3/cyclin-C-mediated
phosphorylation at Ser-799 and Ser-803 is required for G0-G1
transition (By similarity). Dephosphorylated at Ser-787 by
calcineruin upon calcium stimulation. {ECO:0000250,
ECO:0000269|PubMed:10542199, ECO:0000269|PubMed:19081374}.
-!- PTM: N-terminus is methylated by METTL11A/NTM1. Monomethylation at
Lys-802 by SMYD2 enhances phosphorylation at Ser-799 and Ser-803,
and promotes cell cycle progression. Monomethylation at Lys-852 by
SMYD2 promotes interaction with L3MBTL1 (By similarity).
{ECO:0000250}.
-!- PTM: Acetylation at Lys-865 and Lys-866 regulates subcellular
localization, at least during keratinocytes differentiation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
{ECO:0000305}.
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EMBL; D25233; BAA04958.1; -; mRNA.
EMBL; L07126; AAA42090.1; -; mRNA.
PIR; S35544; S35544.
RefSeq; NP_058741.1; NM_017045.1.
UniGene; Rn.55115; -.
SMR; P33568; -.
BioGrid; 246837; 5.
IntAct; P33568; 3.
STRING; 10116.ENSRNOP00000021752; -.
iPTMnet; P33568; -.
PhosphoSitePlus; P33568; -.
PaxDb; P33568; -.
PRIDE; P33568; -.
GeneID; 24708; -.
KEGG; rno:24708; -.
UCSC; RGD:3540; rat.
CTD; 5925; -.
RGD; 3540; Rb1.
eggNOG; KOG1010; Eukaryota.
eggNOG; ENOG410XQF7; LUCA.
HOGENOM; HOG000136539; -.
HOVERGEN; HBG008967; -.
InParanoid; P33568; -.
KO; K06618; -.
PhylomeDB; P33568; -.
TreeFam; TF105568; -.
PRO; PR:P33568; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0035189; C:Rb-E2F complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:InterPro.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:InterPro.
GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IMP:RGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00043; CYCLIN; 1.
Gene3D; 1.10.472.10; -; 3.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR033057; RB1.
InterPro; IPR002720; RB_A.
InterPro; IPR002719; RB_B.
InterPro; IPR015030; RB_C.
InterPro; IPR028309; RB_fam.
InterPro; IPR024599; RB_N.
PANTHER; PTHR13742; PTHR13742; 1.
PANTHER; PTHR13742:SF17; PTHR13742:SF17; 1.
Pfam; PF11934; DUF3452; 1.
Pfam; PF01858; RB_A; 1.
Pfam; PF01857; RB_B; 1.
Pfam; PF08934; Rb_C; 1.
SMART; SM00385; CYCLIN; 1.
SMART; SM01367; DUF3452; 1.
SMART; SM01368; RB_A; 1.
SMART; SM01369; Rb_C; 1.
SUPFAM; SSF47954; SSF47954; 2.
1: Evidence at protein level;
Acetylation; Cell cycle; Chromatin regulator; Complete proteome;
DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P13405}.
CHAIN 2 920 Retinoblastoma-associated protein.
/FTId=PRO_0000167838.
REGION 366 763 Pocket; binds T and E1A. {ECO:0000250}.
REGION 366 572 Domain A. {ECO:0000250}.
REGION 573 631 Spacer. {ECO:0000250}.
REGION 632 763 Domain B. {ECO:0000250}.
REGION 755 920 Interaction with LIMD1. {ECO:0000250}.
REGION 763 920 Domain C; mediates interaction with E4F1.
{ECO:0000250}.
MOTIF 862 868 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 2 2 N,N-dimethylproline.
{ECO:0000250|UniProtKB:P13405}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 242 242 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 245 245 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 349 349 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 363 363 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 366 366 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 560 560 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000250|UniProtKB:P13405}.
MOD_RES 604 604 Phosphoserine; by CHEK2 and CHEK1.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000250|UniProtKB:P06400,
ECO:0000255}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000250|UniProtKB:P06400,
ECO:0000255}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000269|PubMed:19081374}.
MOD_RES 799 799 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 802 802 N6-methyllysine; by SMYD2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 803 803 Phosphoserine; by CDK1 and CDK3.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 813 813 Phosphothreonine; by CDK6.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 815 815 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 818 818 Phosphothreonine; by CDK4.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 833 833 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 847 847 Phosphoserine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 852 852 N6-methyllysine; by SMYD2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 865 865 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 866 866 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P06400}.
MUTAGEN 772 772 S->A: Decreased association with HDAC1;
when associated with A-780 and A-787.
{ECO:0000269|PubMed:19081374}.
MUTAGEN 780 780 S->A: Decreased association with HDAC1;
when associated with A-772 and A-787.
{ECO:0000269|PubMed:19081374}.
MUTAGEN 787 787 S->A: Decreased association with HDAC1;
when associated with A-772 and A-780.
{ECO:0000269|PubMed:19081374}.
CONFLICT 668 668 L -> P (in Ref. 2; BAA04958).
{ECO:0000305}.
CONFLICT 798 798 I -> M (in Ref. 2; BAA04958).
{ECO:0000305}.
CONFLICT 866 867 KL -> TW (in Ref. 3; AAA42090).
{ECO:0000305}.
SEQUENCE 920 AA; 105025 MW; 3BA735EA59927301 CRC64;
MPPKAPRRTA AAEPPPPPPP PPEDDPAQDS DPEELPLIRL EFEKIEEPEF IALCQKLKVP
DHVRERAWLT WEKVSSVDGI LEGYIQKKKE LWGICIFIAA VDLDEMPFTF TELQKSIETS
VYKFFDLLKE IDTSTKVDNA VSRLLKKYNV LCALYSKLER TCGLIYLTQP SSGLSTEINS
MLVLKVSWIT FLLAKGEVVQ MEDDLVISFQ LMLCVLDYFI KLSPPALLRE PYKTAATPIN
GSPRTPRRGQ NRSARIAKQL ESDTRTIEVL CKEHECNVDE VKNVYFKNFI PFISSLGIVS
SNGLPELESL SKRYEEVYLK SKDLDARLFL DHDKTLQTDT IDSFETERTP RKSNPDEEAN
MVTPHTPVRT VMNTIQQLMV ILNSASDQPS ENLISYFSNC TVNPKENILK RVKDVGHIFK
EKFASAVGQG CIDIGAQRYK LGVRLYYRVM ESMLKSEEER LSIQNFSKLL NDNIFHMSLL
ACALEVVMAT YSRSMLQNLD SGTDLSFPWI LNVLNLKAFD FYKVIESFIK VEANLTREMI
KHLERCEHRI MESLAWLSDS PLFDLIKQSK DGEGPDHLES ACSLSLPLQS NHTAADMYLS
PIRSPKKRTS TTRVNSAANT ETQAASAFHT QKPLKSTSLS LFYKKVYRLA YLRLNTLCAR
LLSDHPELEH IIWTLFQHTL ENEYELMKDR HLDQIMMCSM YGICKVKNID LKFKIIVTAY
KDLPHAAQET FKRVLIREEE FDSIIVFYNS VFMQRLKTNI LQYASTRPPT LSPIPHIPRS
PYKFSSSPLR IPGGNIYISP LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI
NQMVCNSDRV LKRSAEGGNP PKPLKKLRFD IEGSDEADGS KHLPAESKFQ QKLAEMTSTR
TRMQKQKLND SMEISNKEEK


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MCA2104 RAT ANTI RETINOBLASTOMA GENE PROTEIN (pThr356), Product Type Monoclonal Antibody, Specificity RETINOBLASTOMA , Target Species Synthetic Peptide, Host Rat, Format Purified, Isotypes IgG2a, Applic 0.1 mg


 

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