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Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4) (Ubiquitous nuclear protein homolog)

 UBP4_HUMAN              Reviewed;         963 AA.
Q13107; A8K6Y0; C9IY91; O43452; O43453; Q08AK8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
25-OCT-2017, entry version 169.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 4;
AltName: Full=Ubiquitin thioesterase 4;
AltName: Full=Ubiquitin-specific-processing protease 4;
AltName: Full=Ubiquitous nuclear protein homolog;
Name=USP4; Synonyms=UNP, UNPH;
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 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Brain cortex;
PubMed=7784062;
Gray D.A., Inazawa J., Gupta K., Wong A., Ueda R., Takahashi T.;
"Elevated expression of Unph, a proto-oncogene at 3p21.3, in human
lung tumors.";
Oncogene 10:2179-2183(1995).
[2]
SEQUENCE REVISION.
Gray D.A.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE
SPLICING.
TISSUE=B-cell, and T-cell;
PubMed=9464533; DOI=10.1038/sj.onc.1201537;
Frederick A., Rolfe M., Chiu M.I.;
"The human UNP locus at 3p21.31 encodes two tissue-selective,
cytoplasmic isoforms with deubiquitinating activity that have reduced
expression in small cell lung carcinoma cell lines.";
Oncogene 16:153-165(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Leukocyte;
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]
INTERACTION WITH RB1, AND MUTAGENESIS OF GLU-463 AND 459-LEU--GLU-463.
PubMed=11571652; DOI=10.1038/sj.onc.1204824;
DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T.,
Pagano M., Loda M.;
"The de-ubiquitinating enzyme Unp interacts with the retinoblastoma
protein.";
Oncogene 20:5538-5542(2001).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-311.
PubMed=16316627; DOI=10.1016/j.bbrc.2005.11.076;
Wada K., Tanji K., Kamitani T.;
"Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase
activity.";
Biochem. Biophys. Res. Commun. 339:731-736(2006).
[9]
FUNCTION, AUTODEUBIQUITINATION, UBIQUITINATION BY TRIM21, AND
MUTAGENESIS OF CYS-311.
PubMed=16472766; DOI=10.1016/j.bbrc.2006.01.144;
Wada K., Kamitani T.;
"UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself.";
Biochem. Biophys. Res. Commun. 342:253-258(2006).
[10]
FUNCTION, INTERACTION WITH ADORA2A, AND TISSUE SPECIFICITY.
PubMed=16339847; DOI=10.1124/mol.105.015818;
Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M.,
Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.;
"The ubiquitin-specific protease Usp4 regulates the cell surface level
of the A2A receptor.";
Mol. Pharmacol. 69:1083-1094(2006).
[11]
FUNCTION, INTERACTION WITH SART3, AND SUBCELLULAR LOCATION.
PubMed=20595234; DOI=10.1101/gad.1925010;
Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
"The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
reversible ubiquitination at the spliceosome.";
Genes Dev. 24:1434-1447(2010).
[12]
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).
[13]
DEUBIQUITINATION OF PDPK1.
PubMed=22347420; DOI=10.1371/journal.pone.0031003;
Uras I.Z., List T., Nijman S.M.;
"Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the
master growth factor signaling kinase PDK1.";
PLoS ONE 7:E31003-E31003(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 296-932, DOMAINS
UBIQUITIN-LIKE, AND ZINC-BINDING SITES.
PubMed=21415856; DOI=10.1038/embor.2011.33;
Luna-Vargas M.P., Faesen A.C., van Dijk W.J., Rape M., Fish A.,
Sixma T.K.;
"Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like
domain.";
EMBO Rep. 12:365-372(2011).
-!- FUNCTION: Hydrolase that deubiquitinates target proteins such as
the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of
ADORA2A increases the amount of functional receptor at the cell
surface. May regulate mRNA splicing through deubiquitination of
the U4 spliceosomal protein PRPF3. This may prevent its
recognition by the U5 component PRPF8 thereby destabilizing
interactions within the U4/U6.U5 snRNP. May also play a role in
the regulation of quality control in the ER.
{ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:16339847,
ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:20595234,
ECO:0000269|PubMed:7784062}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Interacts with RB1 (both dephosphorylated and
hypophosphorylated forms). Interacts with RBL1 and RBL2. Interacts
with ADORA2A (via cytoplasmic C-terminus); the interaction is
direct. Interacts with SART3; recruits USP4 to its substrate
PRPF3. {ECO:0000250|UniProtKB:P35123, ECO:0000269|PubMed:11571652,
ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:20595234}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-723290, EBI-723290;
P29274:ADORA2A; NbExp=4; IntAct=EBI-723290, EBI-2902702;
Q7Z6Z7:HUWE1; NbExp=4; IntAct=EBI-723290, EBI-625934;
Q13546:RIPK1; NbExp=4; IntAct=EBI-723290, EBI-358507;
P19474:TRIM21; NbExp=3; IntAct=EBI-723305, EBI-81290;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16316627,
ECO:0000269|PubMed:20595234}. Nucleus
{ECO:0000269|PubMed:16316627, ECO:0000269|PubMed:20595234}.
Note=Shuttles between the nucleus and cytoplasm. Exported to the
cytoplasm in a CRM1-dependent manner and recycled back to the
nucleus via the importin alpha/beta heterodimeric import receptor.
The relative amounts found in the nucleus and cytoplasm vary
according to the cell type. {ECO:0000269|PubMed:16316627,
ECO:0000269|PubMed:20595234}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=UnpEL;
IsoId=Q13107-1; Sequence=Displayed;
Name=2; Synonyms=UnpES;
IsoId=Q13107-2; Sequence=VSP_005258;
Name=3;
IsoId=Q13107-3; Sequence=VSP_044814, VSP_044815;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Overexpressed in small cell tumors and
adenocarcinomas of the lung compared to wild-type lung (at protein
level). Expressed in the hippocampal neurons.
{ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:7784062}.
-!- DOMAIN: The Ubiquitin-like domain 2 inserts into the catalytic
domain and competes with the ubiquitin substrate, partially
inhibiting DUB activity. {ECO:0000269|PubMed:21415856}.
-!- PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to
its proteasomal degradation. Autodeubiquitinated.
{ECO:0000269|PubMed:16472766, ECO:0000269|PubMed:22347420}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
{ECO:0000305}.
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EMBL; U20657; AAB72237.1; -; mRNA.
EMBL; AF017305; AAC27355.1; -; mRNA.
EMBL; AF017306; AAC27356.1; -; mRNA.
EMBL; AK291795; BAF84484.1; -; mRNA.
EMBL; AC121247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC068017; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC125130; AAI25131.1; -; mRNA.
CCDS; CCDS2793.1; -. [Q13107-1]
CCDS; CCDS2794.1; -. [Q13107-2]
CCDS; CCDS58832.1; -. [Q13107-3]
PIR; T09478; T09478.
RefSeq; NP_001238806.1; NM_001251877.1. [Q13107-3]
RefSeq; NP_003354.2; NM_003363.3. [Q13107-1]
RefSeq; NP_955475.1; NM_199443.2. [Q13107-2]
UniGene; Hs.403828; -.
UniGene; Hs.77500; -.
PDB; 2Y6E; X-ray; 2.40 A; A/B/C/D/E/F=296-490, A/B/C/D/E/F=765-932.
PDB; 5CTR; X-ray; 3.01 A; C/D=1-230.
PDBsum; 2Y6E; -.
PDBsum; 5CTR; -.
ProteinModelPortal; Q13107; -.
SMR; Q13107; -.
BioGrid; 113221; 114.
IntAct; Q13107; 32.
MINT; MINT-3027027; -.
STRING; 9606.ENSP00000265560; -.
BindingDB; Q13107; -.
ChEMBL; CHEMBL2406900; -.
MEROPS; C19.010; -.
iPTMnet; Q13107; -.
PhosphoSitePlus; Q13107; -.
BioMuta; USP4; -.
DMDM; 116242839; -.
EPD; Q13107; -.
MaxQB; Q13107; -.
PaxDb; Q13107; -.
PeptideAtlas; Q13107; -.
PRIDE; Q13107; -.
Ensembl; ENST00000265560; ENSP00000265560; ENSG00000114316. [Q13107-1]
Ensembl; ENST00000351842; ENSP00000341028; ENSG00000114316. [Q13107-2]
Ensembl; ENST00000416417; ENSP00000400623; ENSG00000114316. [Q13107-3]
GeneID; 7375; -.
KEGG; hsa:7375; -.
UCSC; uc003cwq.3; human. [Q13107-1]
CTD; 7375; -.
DisGeNET; 7375; -.
EuPathDB; HostDB:ENSG00000114316.12; -.
GeneCards; USP4; -.
HGNC; HGNC:12627; USP4.
HPA; HPA018499; -.
MIM; 603486; gene.
neXtProt; NX_Q13107; -.
OpenTargets; ENSG00000114316; -.
PharmGKB; PA37252; -.
eggNOG; KOG1870; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00670000097750; -.
HOGENOM; HOG000152636; -.
HOVERGEN; HBG000864; -.
InParanoid; Q13107; -.
KO; K11835; -.
OMA; HVSMLQP; -.
OrthoDB; EOG091G0157; -.
PhylomeDB; Q13107; -.
TreeFam; TF106276; -.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP4; human.
EvolutionaryTrace; Q13107; -.
GeneWiki; USP4; -.
GenomeRNAi; 7375; -.
PRO; PR:Q13107; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114316; -.
CleanEx; HS_USP4; -.
ExpressionAtlas; Q13107; baseline and differential.
Genevisible; Q13107; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031685; F:adenosine receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.2230.10; -; 1.
InterPro; IPR035927; DUSP-like_sf.
InterPro; IPR006615; Pept_C19_DUSP.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR028135; Ub_USP-typ.
InterPro; IPR028134; USP4.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
PANTHER; PTHR43913; PTHR43913; 1.
Pfam; PF06337; DUSP; 1.
Pfam; PF14836; Ubiquitin_3; 1.
Pfam; PF00443; UCH; 1.
SMART; SM00695; DUSP; 1.
SUPFAM; SSF143791; SSF143791; 1.
PROSITE; PS51283; DUSP; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Protease; Proto-oncogene; Reference proteome; Repeat; Thiol protease;
Ubl conjugation; Ubl conjugation pathway; Zinc.
CHAIN 1 963 Ubiquitin carboxyl-terminal hydrolase 4.
/FTId=PRO_0000080621.
DOMAIN 11 122 DUSP. {ECO:0000255|PROSITE-
ProRule:PRU00613}.
DOMAIN 142 226 Ubiquitin-like 1.
DOMAIN 302 923 USP.
DOMAIN 483 571 Ubiquitin-like 2.
REGION 27 216 Necessary for interaction with SART3.
{ECO:0000269|PubMed:20595234}.
REGION 405 407 Necessary for interaction with RBL2.
{ECO:0000250}.
REGION 459 463 Necessary for interaction with RB1 and
RBL2. {ECO:0000250}.
MOTIF 133 141 Nuclear export signal. {ECO:0000250}.
MOTIF 767 772 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 311 311 Nucleophile.
ACT_SITE 881 881 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
METAL 461 461 Zinc.
METAL 464 464 Zinc.
METAL 799 799 Zinc.
METAL 802 802 Zinc.
MOD_RES 655 655 Phosphoserine.
{ECO:0000250|UniProtKB:B2GUZ1}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:P35123}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000250|UniProtKB:P35123}.
VAR_SEQ 232 279 KSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMH
SSGVSRG -> N (in isoform 2).
{ECO:0000303|PubMed:9464533}.
/FTId=VSP_005258.
VAR_SEQ 233 313 SSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHS
SGVSRGGSGFSASYNCQEPPSSHIQPGLCGLGNLGNTCFM
-> VSFFLPRLECNGAILAHCNFCLPGSSNSPASASRVAPS
HLANFFFFEMESHSVTKLECGGAVSAYSRVQVMLLPQPPEW
LG (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044814.
VAR_SEQ 314 963 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044815.
VARIANT 620 620 Y -> C (in dbSNP:rs9311440).
/FTId=VAR_028180.
MUTAGEN 311 311 C->A: Loss of activity. Its
ubiquitination by TRIM21 is enhanced.
{ECO:0000269|PubMed:16316627,
ECO:0000269|PubMed:16472766}.
MUTAGEN 459 463 LVCPE->AVRPH: Reduces the interaction
with RB1. {ECO:0000269|PubMed:11571652}.
MUTAGEN 463 463 E->Q: Reduces the interaction with RB1.
{ECO:0000269|PubMed:11571652}.
CONFLICT 373 373 R -> S (in Ref. 1; AAB72237).
{ECO:0000305}.
CONFLICT 744 744 S -> R (in Ref. 1; AAB72237).
{ECO:0000305}.
HELIX 13 20 {ECO:0000244|PDB:5CTR}.
HELIX 21 23 {ECO:0000244|PDB:5CTR}.
STRAND 32 38 {ECO:0000244|PDB:5CTR}.
HELIX 39 48 {ECO:0000244|PDB:5CTR}.
HELIX 62 64 {ECO:0000244|PDB:5CTR}.
TURN 72 74 {ECO:0000244|PDB:5CTR}.
STRAND 75 77 {ECO:0000244|PDB:5CTR}.
TURN 78 81 {ECO:0000244|PDB:5CTR}.
TURN 89 92 {ECO:0000244|PDB:5CTR}.
STRAND 93 97 {ECO:0000244|PDB:5CTR}.
HELIX 98 108 {ECO:0000244|PDB:5CTR}.
STRAND 118 124 {ECO:0000244|PDB:5CTR}.
STRAND 126 128 {ECO:0000244|PDB:5CTR}.
STRAND 130 133 {ECO:0000244|PDB:5CTR}.
STRAND 140 143 {ECO:0000244|PDB:5CTR}.
STRAND 151 154 {ECO:0000244|PDB:5CTR}.
STRAND 158 161 {ECO:0000244|PDB:5CTR}.
HELIX 162 172 {ECO:0000244|PDB:5CTR}.
STRAND 177 179 {ECO:0000244|PDB:5CTR}.
STRAND 183 185 {ECO:0000244|PDB:5CTR}.
STRAND 187 191 {ECO:0000244|PDB:5CTR}.
STRAND 198 202 {ECO:0000244|PDB:5CTR}.
TURN 203 206 {ECO:0000244|PDB:5CTR}.
HELIX 311 321 {ECO:0000244|PDB:2Y6E}.
HELIX 324 331 {ECO:0000244|PDB:2Y6E}.
HELIX 335 338 {ECO:0000244|PDB:2Y6E}.
HELIX 350 362 {ECO:0000244|PDB:2Y6E}.
STRAND 364 366 {ECO:0000244|PDB:2Y6E}.
STRAND 368 370 {ECO:0000244|PDB:2Y6E}.
HELIX 373 382 {ECO:0000244|PDB:2Y6E}.
HELIX 384 386 {ECO:0000244|PDB:2Y6E}.
STRAND 388 390 {ECO:0000244|PDB:2Y6E}.
HELIX 394 408 {ECO:0000244|PDB:2Y6E}.
HELIX 428 442 {ECO:0000244|PDB:2Y6E}.
HELIX 446 451 {ECO:0000244|PDB:2Y6E}.
STRAND 453 460 {ECO:0000244|PDB:2Y6E}.
TURN 462 464 {ECO:0000244|PDB:2Y6E}.
STRAND 467 480 {ECO:0000244|PDB:2Y6E}.
HELIX 778 785 {ECO:0000244|PDB:2Y6E}.
STRAND 797 799 {ECO:0000244|PDB:2Y6E}.
TURN 800 803 {ECO:0000244|PDB:2Y6E}.
STRAND 804 806 {ECO:0000244|PDB:2Y6E}.
STRAND 809 816 {ECO:0000244|PDB:2Y6E}.
STRAND 819 826 {ECO:0000244|PDB:2Y6E}.
STRAND 828 830 {ECO:0000244|PDB:2Y6E}.
STRAND 835 837 {ECO:0000244|PDB:2Y6E}.
HELIX 852 854 {ECO:0000244|PDB:2Y6E}.
STRAND 858 860 {ECO:0000244|PDB:2Y6E}.
STRAND 864 874 {ECO:0000244|PDB:2Y6E}.
STRAND 876 879 {ECO:0000244|PDB:2Y6E}.
STRAND 881 887 {ECO:0000244|PDB:2Y6E}.
TURN 889 891 {ECO:0000244|PDB:2Y6E}.
STRAND 894 898 {ECO:0000244|PDB:2Y6E}.
STRAND 901 904 {ECO:0000244|PDB:2Y6E}.
HELIX 907 909 {ECO:0000244|PDB:2Y6E}.
STRAND 915 922 {ECO:0000244|PDB:2Y6E}.
HELIX 926 928 {ECO:0000244|PDB:2Y6E}.
SEQUENCE 963 AA; 108565 MW; 63055C9ADFE36713 CRC64;
MAEGGGCRER PDAETQKSEL GPLMRTTLQR GAQWYLIDSR WFKQWKKYVG FDSWDMYNVG
EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA WNKLLNWYGC VEGQQPIVRK
VVEHGLFVKH CKVEVYLLEL KLCENSDPTN VLSCHFSKAD TIATIEKEMR KLFNIPAERE
TRLWNKYMSN TYEQLSKLDN TVQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN
FTTSPKSSAS PYSSVSASLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG
LCGLGNLGNT CFMNSALQCL SNTAPLTDYF LKDEYEAEIN RDNPLGMKGE IAEAYAELIK
QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF LLDGLHEDLN RVKKKPYLEL
KDANGRPDAV VAKEAWENHR LRNDSVIVDT FHGLFKSTLV CPECAKVSVT FDPFCYLTLP
LPLKKDRVME VFLVPADPHC RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN
HRFHKIFQMD EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL
YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN GSRNSCEGED
EEEMEHQEEG KEQLSETEGS GEDEPGNDPS ETTQKKIKGQ PCPKRLFTFS LVNSYGTADI
NSLAADGKLL KLNSRSTLAM DWDSETRRLY YDEQESEAYE KHVSMLQPQK KKKTTVALRD
CIELFTTMET LGEHDPWYCP NCKKHQQATK KFDLWSLPKI LVVHLKRFSY NRYWRDKLDT
VVEFPIRGLN MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS
NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ GFGDDEACSM
DTN


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