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

 RB_MOUSE                Reviewed;         921 AA.
P13405; Q4VA62;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 188.
RecName: Full=Retinoblastoma-associated protein;
AltName: Full=pRb;
Short=Rb;
AltName: Full=pp105;
Name=Rb1; Synonyms=Rb-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2671991; DOI=10.1073/pnas.86.17.6474;
Bernards R., Schackleford G.M., Gerber M.R., Horowitz J.M.,
Friend S.H., Schartl M., Bogenmann E., Rapaport J., McGee T.,
Dryja T.P., Weinberg R.A.;
"Structure and expression of the murine retinoblastoma gene and
characterization of its encoded protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:6474-6478(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Wu J., Liao J.D.;
"Sequencing of the full-length cDNA sequence of the murine
retinoblastoma gene.";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
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).
[5]
INTERACTION WITH E4F1.
PubMed=10869426; DOI=10.1073/pnas.130198397;
Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
Medema R., Vignais M.-L., Sardet C.;
"pRB binds to and modulates the transrepressing activity of the E1A-
regulated transcription factor p120E4F.";
Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
[6]
INTERACTION WITH USP4.
PubMed=11571651; DOI=10.1038/sj.onc.1204823;
Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.;
"Association of UNP, a ubiquitin-specific protease, with the pocket
proteins pRb, p107 and p130.";
Oncogene 20:5533-5537(2001).
[7]
TISSUE SPECIFICITY, AND COLOCALIZATION WITH RB1CC1.
STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
PubMed=12095676; DOI=10.1016/S0378-1119(02)00585-1;
Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A.,
Saeki Y., Okabe H.;
"Isolation, characterization and mapping of the mouse and human RB1CC1
genes.";
Gene 291:29-34(2002).
[8]
FUNCTION, AND INTERACTION WITH KMT5B AND KMT5C.
PubMed=15750587; DOI=10.1038/ncb1235;
Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
Blasco M.A.;
"Role of the RB1 family in stabilizing histone methylation at
constitutive heterochromatin.";
Nat. Cell Biol. 7:420-428(2005).
[9]
INTERACTION WITH ATAD5.
PubMed=15983387; DOI=10.1073/pnas.0504222102;
Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M.,
Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.;
"Frag1, a homolog of alternative replication factor C subunits, links
replication stress surveillance with apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
[10]
INTERACTION WITH PRMT2.
PubMed=16616919; DOI=10.1016/j.yexcr.2006.03.001;
Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T.,
Nabel E.G.;
"The arginine methyltransferase PRMT2 binds RB and regulates E2F
function.";
Exp. Cell Res. 312:2040-2053(2006).
[11]
FUNCTION, INTERACTION WITH KMT5B AND KMT5C, AND MUTAGENESIS OF
ILE-746; ASN-750 AND MET-754.
PubMed=16612004; DOI=10.1128/MCB.26.9.3659-3671.2006;
Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A.,
Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G.,
Dyson N.J., Dick F.A.;
"The retinoblastoma protein regulates pericentric heterochromatin.";
Mol. Cell. Biol. 26:3659-3671(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-243; THR-246;
THR-364; THR-367; SER-601; SER-605; SER-773; SER-800; SER-804;
THR-814; THR-819 AND SER-848, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2.
PubMed=20668449; DOI=10.1038/nature09343;
Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
-!- 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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004}.
-!- 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, TMPO-alpha and USP4. May interact with NDC80. Interacts
with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts
with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 and HDAC1.
Interacts with USP4. Interacts (when methylated at Lys-853) with
L3MBTL1. Binds to CDK1 and CDK2. Interacts with CHEK2;
phosphorylates RB1 (By similarity). Interacts with PRMT2.
Interacts with CEBPA. P-TEFB complex interacts with RB1; promotes
phosphorylation of RB1 (By similarity).
{ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P33568,
ECO:0000269|PubMed:10869426, ECO:0000269|PubMed:10888886,
ECO:0000269|PubMed:11571651, ECO:0000269|PubMed:15750587,
ECO:0000269|PubMed:15983387, ECO:0000269|PubMed:16612004,
ECO:0000269|PubMed:16616919}.
-!- INTERACTION:
Q155P7:Cenpf; NbExp=4; IntAct=EBI-971782, EBI-2211248;
Q80UP3:Dgkz; NbExp=2; IntAct=EBI-971782, EBI-971774;
P63158:Hmgb1; NbExp=2; IntAct=EBI-971782, EBI-6665811;
Q9R002:Ifi202; NbExp=7; IntAct=EBI-971782, EBI-3043899;
P24610:Pax3; NbExp=3; IntAct=EBI-971782, EBI-1208116;
P52946:Pdx1; NbExp=2; IntAct=EBI-971782, EBI-7128945;
Q3TKT4:Smarca4; NbExp=3; IntAct=EBI-971782, EBI-1210244;
Q61412:Vsx2; NbExp=2; IntAct=EBI-971782, EBI-1208174;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Expressed in the cell nuclei of renal tubules,
hepatocytes and skeletal muscles. Colocalizes with RB1CC1 in
various tissues. {ECO:0000269|PubMed:12095676}.
-!- PTM: Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at
Ser-561 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. Dephosphorylated at Ser-788 by
calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated
phosphorylation at Ser-800 and Ser-804 is required for G0-G1
transition (By similarity). Phosphorylated by CDK1 and CDK2 upon
TGFB1-mediated apoptosis (By similarity). {ECO:0000250}.
-!- PTM: Monomethylation at Lys-803 by SMYD2 enhances phosphorylation
at Ser-800 and Ser-804, and promotes cell cycle progression.
Monomethylation at Lys-853 by SMYD2 promotes interaction with
L3MBTL1 (By similarity). N-terminus is methylated by
METTL11A/NTM1. {ECO:0000250, ECO:0000269|PubMed:20668449}.
-!- PTM: Acetylation at Lys-866 and Lys-867 regulates subcellular
localization, at least during keratinocytes differentiation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinoblastoma protein entry;
URL="https://en.wikipedia.org/wiki/Retinoblastoma_protein";
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EMBL; M26391; AAA39964.1; -; mRNA.
EMBL; DQ400415; ABD72475.1; -; mRNA.
EMBL; BC096525; AAH96525.1; -; mRNA.
CCDS; CCDS27267.1; -.
PIR; A33718; A33718.
RefSeq; NP_033055.2; NM_009029.2.
UniGene; Mm.273862; -.
ProteinModelPortal; P13405; -.
SMR; P13405; -.
BioGrid; 202815; 35.
CORUM; P13405; -.
DIP; DIP-37637N; -.
IntAct; P13405; 19.
MINT; MINT-225292; -.
STRING; 10090.ENSMUSP00000022701; -.
iPTMnet; P13405; -.
PhosphoSitePlus; P13405; -.
EPD; P13405; -.
MaxQB; P13405; -.
PaxDb; P13405; -.
PeptideAtlas; P13405; -.
PRIDE; P13405; -.
Ensembl; ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105.
GeneID; 19645; -.
KEGG; mmu:19645; -.
UCSC; uc007upp.2; mouse.
CTD; 5925; -.
MGI; MGI:97874; Rb1.
eggNOG; KOG1010; Eukaryota.
eggNOG; ENOG410XQF7; LUCA.
GeneTree; ENSGT00530000063235; -.
HOGENOM; HOG000136539; -.
HOVERGEN; HBG008967; -.
InParanoid; P13405; -.
KO; K06618; -.
OMA; TNILQYA; -.
OrthoDB; EOG091G0398; -.
TreeFam; TF105568; -.
Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
Reactome; R-MMU-68949; Orc1 removal from chromatin.
Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
PRO; PR:P13405; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022105; -.
CleanEx; MM_RB1; -.
ExpressionAtlas; P13405; baseline and differential.
Genevisible; P13405; MM.
GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0035189; C:Rb-E2F complex; IDA:BHF-UCL.
GO; GO:0005819; C:spindle; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007050; P:cell cycle arrest; IMP:MGI.
GO; GO:0051301; P:cell division; IMP:MGI.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0048565; P:digestive tract development; IMP:MGI.
GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0034349; P:glial cell apoptotic process; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISO:MGI.
GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IGI:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0042551; P:neuron maturation; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IGI:MGI.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISO:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
GO; GO:0071922; P:regulation of cohesin loading; ISO:MGI.
GO; GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0031134; P:sister chromatid biorientation; ISO:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
GO; GO:0001894; P:tissue homeostasis; IGI:MGI.
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; 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:SF26; PTHR13742:SF26; 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:0000269|PubMed:20668449}.
CHAIN 2 921 Retinoblastoma-associated protein.
/FTId=PRO_0000167837.
REGION 367 764 Pocket; binds T and E1A. {ECO:0000250}.
REGION 367 573 Domain A. {ECO:0000250}.
REGION 574 632 Spacer. {ECO:0000250}.
REGION 633 764 Domain B. {ECO:0000250}.
REGION 756 921 Interaction with LIMD1. {ECO:0000250}.
REGION 764 921 Domain; mediates interaction with E4F1.
{ECO:0000250}.
MOTIF 863 869 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 9 12 Poly-Ala.
COMPBIAS 14 22 Poly-Pro.
MOD_RES 2 2 N,N-dimethylproline; by NTM1.
{ECO:0000269|PubMed:20668449}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 246 246 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 350 350 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 364 364 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 367 367 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 561 561 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 601 601 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 617 617 Phosphoserine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 800 800 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 803 803 N6-methyllysine; by SMYD2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 804 804 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 814 814 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 816 816 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 819 819 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 834 834 Phosphothreonine.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 848 848 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 853 853 N6-methyllysine; by SMYD2.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 866 866 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P06400}.
MOD_RES 867 867 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P06400}.
MUTAGEN 746 746 I->A: Abolishes the interaction with many
chromatin regulators but not that with
KMT5B and KMT5C; when associated with A-
750 and A-754.
{ECO:0000269|PubMed:16612004}.
MUTAGEN 750 750 N->A: Abolishes the interaction with many
chromatin regulators but not that with
KMT5B and KMT5C; when associated with A-
746 and A-754.
{ECO:0000269|PubMed:16612004}.
MUTAGEN 754 754 M->A: Abolishes the interaction with many
chromatin regulators but not that with
KMT5B and KMT5C; when associated with A-
746 and A-750.
{ECO:0000269|PubMed:16612004}.
CONFLICT 867 868 KL -> NV (in Ref. 1; AAA39964).
{ECO:0000305}.
SEQUENCE 921 AA; 105367 MW; AE81D35A07ADB493 CRC64;
MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE FIALCQKLKV
PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA AVDLDEMPFT FTELQKSIET
SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN VLCALYSKLE RTCELIYLTQ PSSALSTEIN
SMLVLKISWI TFLLAKGEVL QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI
NGSPRTPRRG QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV
SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT PRKNNPDEEA
NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN CTVNPKENIL KRVKDVGHIF
KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV MESMLKSEEE RLSIQNFSKL LNDNIFHMSL
LACALEVVMA TYSRSTLQHL DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM
IKHLERCEHR IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL
SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL AYLRLNTLCA
RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS MYGICKVKNI DLKFKIIVTA
YKDLPHAAQE TFKRVLIREE EFDSIIVFYN SVFMQRLKTN ILQYASTRPP TLSPIPHIPR
SPYKFSSSPL RIPGGNIYIS PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK
INQMVCNSDR VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST
RTRMQKQRMN ESKDVSNKEE K


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