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E3 ubiquitin-protein ligase BRE1B (BRE1-B) (EC 2.3.2.27) (95 kDa retinoblastoma-associated protein) (RBP95) (RING finger protein 40) (RING-type E3 ubiquitin transferase BRE1B)

 BRE1B_HUMAN             Reviewed;        1001 AA.
O75150; Q6AHZ6; Q6N005; Q7L3T6; Q8N615; Q96T18; Q9BSV9; Q9HC82;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 4.
25-OCT-2017, entry version 152.
RecName: Full=E3 ubiquitin-protein ligase BRE1B;
Short=BRE1-B;
EC=2.3.2.27 {ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543};
AltName: Full=95 kDa retinoblastoma-associated protein;
Short=RBP95;
AltName: Full=RING finger protein 40;
AltName: Full=RING-type E3 ubiquitin transferase BRE1B {ECO:0000305};
Name=RNF40; Synonyms=BRE1B, KIAA0661;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, SUBUNIT, INTERACTION WITH RB1, MUTAGENESIS OF LEU-109;
CYS-111 AND GLU-113, AND VARIANT ARG-615.
TISSUE=Fetal brain;
PubMed=10944455; DOI=10.1006/bbrc.2000.3242;
Wen H., Ao S.;
"RBP95, a novel leucine zipper protein, binds to the retinoblastoma
protein.";
Biochem. Biophys. Res. Commun. 275:141-148(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-615.
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
ARG-615.
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-615.
TISSUE=Cervix, and Rectum tumor;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-615.
TISSUE=Brain, Mammary gland, Skin, and Uterus;
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).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND IDENTIFICATION IN A COMPLEX
WITH RNF20 AND UBE2E1.
PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and
their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=19410543; DOI=10.1016/j.cell.2009.02.027;
Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A.,
Shilatifard A., Muir T.W., Roeder R.G.;
"RAD6-mediated transcription-coupled H2B ubiquitylation directly
stimulates H3K4 methylation in human cells.";
Cell 137:459-471(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH WAC.
PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
Zhang F., Yu X.;
"WAC, a functional partner of RNF20/40, regulates histone H2B
ubiquitination and gene transcription.";
Mol. Cell 41:384-397(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-578 AND LYS-579, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase
complex that mediates monoubiquitination of 'Lys-120' of histone
H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
transcriptional activation and is also prerequisite for histone H3
'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me,
respectively). It thereby plays a central role in histone code and
gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase
complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports
about the cooperation with UBE2E1/UBCH are contradictory. Required
for transcriptional activation of Hox genes.
{ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:16307923,
ECO:0000269|PubMed:19410543}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the RNF20/40 complex (also known as BRE1
complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies
of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1
and WAC. {ECO:0000269|PubMed:10944455,
ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19410543,
ECO:0000269|PubMed:21329877}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-744408, EBI-10187270;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-744408, EBI-10247802;
P42858:HTT; NbExp=3; IntAct=EBI-744408, EBI-466029;
Q09161:NCBP1; NbExp=3; IntAct=EBI-744408, EBI-464743;
P06400:RB1; NbExp=3; IntAct=EBI-744408, EBI-491274;
Q5VTR2:RNF20; NbExp=10; IntAct=EBI-744408, EBI-2372238;
Q86XK3:SFR1; NbExp=3; IntAct=EBI-744408, EBI-1104535;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-744408, EBI-10180829;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10944455}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75150-1; Sequence=Displayed;
Name=3;
IsoId=O75150-3; Sequence=VSP_016682, VSP_016683;
Note=No experimental confirmation available.;
Name=4;
IsoId=O75150-4; Sequence=VSP_016681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher
level in testis, heart and pancreas, while it is only weakly
expressed in lung, skeletal muscle and small intestine.
{ECO:0000269|PubMed:10944455}.
-!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31636.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAE45869.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; AF122819; AAG13723.1; -; mRNA.
EMBL; AB014561; BAA31636.2; ALT_INIT; mRNA.
EMBL; AK027406; BAB55092.1; -; mRNA.
EMBL; BX640763; CAE45869.1; ALT_SEQ; mRNA.
EMBL; CR627431; CAH10518.1; -; mRNA.
EMBL; AC106886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004527; AAH04527.2; -; mRNA.
EMBL; BC006133; AAH06133.1; -; mRNA.
EMBL; BC011769; AAH11769.1; -; mRNA.
EMBL; BC018647; AAH18647.1; -; mRNA.
EMBL; BC030802; AAH30802.2; -; mRNA.
CCDS; CCDS10691.1; -. [O75150-1]
CCDS; CCDS55994.1; -. [O75150-4]
PIR; JC7363; JC7363.
RefSeq; NP_001193962.1; NM_001207033.1.
RefSeq; NP_001193963.1; NM_001207034.1.
RefSeq; NP_001273501.1; NM_001286572.2.
RefSeq; NP_055586.1; NM_014771.3.
UniGene; Hs.65238; -.
ProteinModelPortal; O75150; -.
SMR; O75150; -.
BioGrid; 115149; 90.
CORUM; O75150; -.
IntAct; O75150; 33.
MINT; MINT-1466706; -.
STRING; 9606.ENSP00000325677; -.
iPTMnet; O75150; -.
PhosphoSitePlus; O75150; -.
BioMuta; RNF40; -.
EPD; O75150; -.
MaxQB; O75150; -.
PaxDb; O75150; -.
PeptideAtlas; O75150; -.
PRIDE; O75150; -.
DNASU; 9810; -.
Ensembl; ENST00000324685; ENSP00000325677; ENSG00000103549.
Ensembl; ENST00000357890; ENSP00000350563; ENSG00000103549.
GeneID; 9810; -.
KEGG; hsa:9810; -.
UCSC; uc002dzq.4; human. [O75150-1]
CTD; 9810; -.
DisGeNET; 9810; -.
EuPathDB; HostDB:ENSG00000103549.21; -.
GeneCards; RNF40; -.
HGNC; HGNC:16867; RNF40.
HPA; HPA041330; -.
HPA; HPA054227; -.
MIM; 607700; gene.
neXtProt; NX_O75150; -.
PharmGKB; PA34440; -.
eggNOG; KOG0978; Eukaryota.
eggNOG; ENOG410Y5C6; LUCA.
HOVERGEN; HBG080312; -.
InParanoid; O75150; -.
KO; K10696; -.
OrthoDB; EOG091G01SA; -.
PhylomeDB; O75150; -.
TreeFam; TF323183; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SIGNOR; O75150; -.
UniPathway; UPA00143; -.
ChiTaRS; RNF40; human.
GeneWiki; RNF40; -.
GenomeRNAi; 9810; -.
PRO; PR:O75150; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103549; -.
CleanEx; HS_RNF40; -.
ExpressionAtlas; O75150; baseline and differential.
Genevisible; O75150; HS.
GO; GO:0043679; C:axon terminus; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
GO; GO:0033503; C:HULC complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IMP:UniProtKB.
GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; IMP:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1001 E3 ubiquitin-protein ligase BRE1B.
/FTId=PRO_0000055839.
ZN_FING 948 987 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 44 91 {ECO:0000255}.
COILED 189 377 {ECO:0000255}.
COILED 437 525 {ECO:0000255}.
COILED 627 946 {ECO:0000255}.
MOD_RES 20 20 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U319}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:Q5VTR2}.
MOD_RES 355 355 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q5VTR2}.
MOD_RES 517 517 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3U319}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000250|UniProtKB:Q5VTR2}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000250|UniProtKB:Q3U319}.
CROSSLNK 578 578 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 579 579 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 332 431 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016681.
VAR_SEQ 822 838 DAQLLTVQKLEEKERAL -> WPPPACRLELERWGSWP
(in isoform 3).
{ECO:0000303|PubMed:10944455}.
/FTId=VSP_016682.
VAR_SEQ 839 1001 Missing (in isoform 3).
{ECO:0000303|PubMed:10944455}.
/FTId=VSP_016683.
VARIANT 463 463 R -> H (in dbSNP:rs11556801).
/FTId=VAR_055021.
VARIANT 615 615 Q -> R (in dbSNP:rs7195142).
{ECO:0000269|PubMed:10944455,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:9734811}.
/FTId=VAR_055022.
MUTAGEN 109 109 L->S: Abolishes interaction with RB1.
{ECO:0000269|PubMed:10944455}.
MUTAGEN 111 111 C->M: Abolishes interaction with RB1.
{ECO:0000269|PubMed:10944455}.
MUTAGEN 113 113 E->Q: Abolishes interaction with RB1.
{ECO:0000269|PubMed:10944455}.
CONFLICT 56 56 N -> D (in Ref. 3; BAB55092).
{ECO:0000305}.
CONFLICT 96 96 R -> L (in Ref. 1; AAG13723).
{ECO:0000305}.
CONFLICT 108 108 L -> P (in Ref. 3; BAB55092).
{ECO:0000305}.
CONFLICT 172 172 S -> G (in Ref. 3; BAB55092).
{ECO:0000305}.
CONFLICT 387 387 E -> K (in Ref. 4; CAH10518).
{ECO:0000305}.
CONFLICT 562 562 K -> E (in Ref. 4; CAE45869).
{ECO:0000305}.
CONFLICT 600 600 S -> F (in Ref. 4; CAE45869).
{ECO:0000305}.
CONFLICT 714 714 D -> N (in Ref. 3; BAB55092).
{ECO:0000305}.
SEQUENCE 1001 AA; 113650 MW; 82D7CD183EDD5EFC CRC64;
MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS
APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE
LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL
QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL
QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK
NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN
REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV
SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS
SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE LLKGLRAELK
KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK
IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR
EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG
SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK
ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC CNTRKKDAVL
TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI S


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