ID H0ZPQ2_TAEGU Unreviewed; 931 AA.
AC H0ZPQ2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=RB transcriptional corepressor 1 {ECO:0000313|Ensembl:ENSTGUP00000012584.2};
GN Name=RB1 {ECO:0000313|Ensembl:ENSTGUP00000012584.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000012584.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000012584.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000012584.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000256|ARBA:ARBA00009475}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H0ZPQ2; -.
DR STRING; 59729.ENSTGUP00000012584; -.
DR Ensembl; ENSTGUT00000012723.2; ENSTGUP00000012584.2; ENSTGUG00000012205.2.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_015754_0_0_1; -.
DR InParanoid; H0ZPQ2; -.
DR OMA; VKDIGCI; -.
DR TreeFam; TF105568; -.
DR Proteomes; UP000007754; Chromosome 1.
DR GO; GO:0061793; C:chromatin lock complex; IEA:Ensembl.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0035189; C:Rb-E2F complex; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061676; F:importin-alpha family protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:Ensembl.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IEA:Ensembl.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IEA:Ensembl.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0031134; P:sister chromatid biorientation; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd20599; CYCLIN_RB; 1.
DR Gene3D; 1.10.472.140; -; 1.
DR Gene3D; 6.10.140.1380; -; 1.
DR Gene3D; 6.10.250.530; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR Pfam; PF08934; Rb_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 62..214
FT /note="Retinoblastoma-associated protein N-terminal"
FT /evidence="ECO:0000259|SMART:SM01367"
FT DOMAIN 360..562
FT /note="Retinoblastoma-associated protein A-box"
FT /evidence="ECO:0000259|SMART:SM01368"
FT DOMAIN 649..750
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 757..918
FT /note="Retinoblastoma-associated protein C-terminal"
FT /evidence="ECO:0000259|SMART:SM01369"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 106113 MW; EE5A19E9E905D7FB CRC64;
MPPKPPRRAG AARTQRPSPD GGSAPPAAPR VEVGEADFVV LCDALKVSES VRERAWKTYE
SLSAADGALA CNTKKKETWG VCIFIVAIDL DEVTFTFTEL LKSINMSVCT FFQFLKEVDV
NMDTVSTKVD STVSRLKKKY DVLFALYHKF ERTCGLIYLE QPSSEISAEL SSILVLKNYW
ITFLLAKGKV LQVEDDLVIS FQLLLCVLDY FIKLSPPAML KEPYKSSVSA VTVNGSARTP
RRGQNRSSRT AKQLDTDTKI IEILCKEHDC NLDEVKNVYF TSFIPFLNSA SILASNGLPE
VEVILKQYDE LYVKNKDIDA RLFLNHDETL QPDVRACSQL ERTPVKNNPD EEINIILPQT
PVRAAMNNIQ QLIMILNSAT DKPSDTLIKY FNNCTVNPKD SILKRVESFG HIFKKKFAEA
VGQGWAETGS QRYKLGVRLY YRVMESMLKS EEERLSVQNF SKLLNDNIFH TSLLACALEV
VMATYGRNAS QSDNTSAETD LSFPWILNVF DLKAFDFYKV IESFIRAEPS LTREMIKHLE
HCEHRIMESL AWQSGSPLFD RIKESKEREG QTDQPEPTST PNMPFQHNHT AADLYLSPVK
SPKKKASGPP LSATSPPDAQ PAVTPQTQKV QKSTSLSLFY KKVYLLAYRR LHTLFLHLLS
EHPELEPLIW TLFQHTLQNE YELMRDRHLD QIMMCSMYGI CKVKNVDLQF KMIVSAYKEL
CNTNQETFKR VLIREEKYDS IIVFYNLVFM QKLKTNILQY ASSRPPTLSP IPHIPRSPYQ
FSNSPRRVPA GNNIYISPLK SPYKFSDGFQ SPTKMTPRSR ILVSIGESFG TYEKFQKINQ
MMCNSEYQLK RCAEAGAAAP KPLKRLRFDI EGTDEADGSK HLPQESKFQQ KLAEMTSTRT
RMQKQKLNDG NDTSASEENF IERMYVNTRV H
//
