RYBP_HUMAN
ID RYBP_HUMAN Reviewed; 228 AA.
AC Q8N488; Q9P2W5; Q9UMW4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RING1 and YY1-binding protein;
DE AltName: Full=Apoptin-associating protein 1;
DE Short=APAP-1;
DE AltName: Full=Death effector domain-associated factor;
DE Short=DED-associated factor;
DE AltName: Full=YY1 and E4TF1-associated factor 1;
GN Name=RYBP; Synonyms=DEDAF, YEAF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH DEDD; FADD; CASP8 AND CASP10.
RX PubMed=11395500; DOI=10.1074/jbc.m102799200;
RA Zheng L., Schickling O., Peter M.E., Lenardo M.J.;
RT "The death effector domain-associated factor plays distinct regulatory
RT roles in the nucleus and cytoplasm.";
RL J. Biol. Chem. 276:31945-31952(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH YY1 AND GABPB1, AND REGION.
RX PubMed=11953439; DOI=10.1074/jbc.m203060200;
RA Sawa C., Yoshikawa T., Matsuda-Suzuki F., Delehouzee S., Goto M.,
RA Watanabe H., Sawada J., Kataoka K., Handa H.;
RT "YEAF1/RYBP and YAF-2 are functionally distinct members of a cofactor
RT family for the YY1 and E4TF1/hGABP transcription factors.";
RL J. Biol. Chem. 277:22484-22490(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH APOPTIN.
RX PubMed=14765135; DOI=10.1038/sj.cdd.4401391;
RA Danen-van Oorschot A.A.M.M., Voskamp P., Seelen M.C.M.J.,
RA van Miltenburg M.H.A.M., Bolk M.W., Tait S.W., Boesen-de Cock J.G.R.,
RA Rohn J.L., Borst J., Noteborn M.H.M.;
RT "Human death effector domain-associated factor interacts with the viral
RT apoptosis agonist Apoptin and exerts tumor-preferential cell killing.";
RL Cell Death Differ. 11:564-573(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng C.M., Yuo C.Y.;
RT "The chicken anemia virus protein apoptin is associated with a human
RT apoptotic protein, APAP1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH BCOR; PCGF1; RING1 AND RNF2.
RX PubMed=16943429; DOI=10.1128/mcb.00630-06;
RA Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
RT "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex
RT that is recruited to BCL6 targets.";
RL Mol. Cell. Biol. 26:6880-6889(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, INTERACTION WITH MDM2, AND IDENTIFICATION IN A COMPLEX WITH MDM2
RP AND TP53.
RX PubMed=19098711; DOI=10.1038/embor.2008.231;
RA Chen D., Zhang J., Li M., Rayburn E.R., Wang H., Zhang R.;
RT "RYBP stabilizes p53 by modulating MDM2.";
RL EMBO Rep. 10:166-172(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-227, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-123; SER-127 AND
RP SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH PCGF5; AUTS2; CSNK2B AND RYBP, AND
RP FUNCTION.
RX PubMed=25519132; DOI=10.1038/nature13921;
RA Gao Z., Lee P., Stafford J.M., von Schimmelmann M., Schaefer A.,
RA Reinberg D.;
RT "An AUTS2-polycomb complex activates gene expression in the CNS.";
RL Nature 516:349-354(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1.
RX PubMed=26687479; DOI=10.1038/srep18388;
RA Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V.,
RA Bracken A.P., Cagney G.;
RT "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a
RT pluripotency sub-network that includes DPPA4, a regulator of
RT embryogenesis.";
RL Sci. Rep. 5:18388-18388(2015).
RN [17]
RP FUNCTION, INTERACTION WITH FANK1, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=27060496; DOI=10.1016/j.cellsig.2016.03.012;
RA Ma W., Zhang X., Li M., Ma X., Huang B., Chen H., Chen D.;
RT "Proapoptotic RYBP interacts with FANK1 and induces tumor cell apoptosis
RT through the AP-1 signaling pathway.";
RL Cell. Signal. 28:779-787(2016).
RN [18]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27748911; DOI=10.3892/ijo.2016.3718;
RA Zhou H., Li J., Zhang Z., Ye R., Shao N., Cheang T., Wang S.;
RT "RING1 and YY1 binding protein suppresses breast cancer growth and
RT metastasis.";
RL Int. J. Oncol. 49:2442-2452(2016).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-77, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 145-179 IN COMPLEX WITH
RP RNF2/RING1B, AND INTERACTION WITH RNF2.
RX PubMed=20696397; DOI=10.1016/j.str.2010.04.013;
RA Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U.,
RA Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P.,
RA McEwen D.G., Kim C.A.;
RT "Polycomb group targeting through different binding partners of RING1B C-
RT terminal domain.";
RL Structure 18:966-975(2010).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1-like complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility
CC (PubMed:25519132). Component of a PRC1-like complex that mediates
CC monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is
CC required for normal silencing of one copy of the X chromosome in XX
CC females. May stimulate ubiquitination of histone H2A 'Lys-119' by
CC recruiting the complex to target sites (By similarity). Inhibits
CC ubiquitination and subsequent degradation of TP53, and thereby plays a
CC role in regulating transcription of TP53 target genes
CC (PubMed:19098711). May also regulate the ubiquitin-mediated proteasomal
CC degradation of other proteins like FANK1 to regulate apoptosis
CC (PubMed:14765135, PubMed:27060496). May be implicated in the regulation
CC of the transcription as a repressor of the transcriptional activity of
CC E4TF1 (PubMed:11953439). May bind to DNA (By similarity). May play a
CC role in the repression of tumor growth and metastasis in breast cancer
CC by down-regulating SRRM3 (PubMed:27748911).
CC {ECO:0000250|UniProtKB:Q8CCI5, ECO:0000269|PubMed:11953439,
CC ECO:0000269|PubMed:14765135, ECO:0000269|PubMed:19098711,
CC ECO:0000269|PubMed:27060496, ECO:0000269|PubMed:27748911}.
CC -!- SUBUNIT: Monomer. Component of repressive BCOR complex containing
CC Polycomb group subcomplex at least composed of BCOR, PCGF1, RING1 and
CC RNF2/RING2 (PubMed:16943429). Component of PCR1-like complexes
CC (PubMed:26687479, PubMed:20696397). Interacts with PCGF1
CC (PubMed:26687479). Part of a PCR1-like complex that contains AUTS2,
CC PCGF5, RNF2, CSNK2B AND RYBP (PubMed:25519132). Interacts with RNF2;
CC the interaction is direct (PubMed:20696397). Interacts with CBX2, YAF2,
CC RING1 and RNF2 (By similarity). Interacts with ubiquitin and
CC ubiquitinated proteins (By similarity). Interacts with ubiquitinated
CC histone H2A (By similarity). Interacts with apoptin, DEDD, FADD, CASP8,
CC CASP10, YY1 and GABPB1 (PubMed:11395500, PubMed:11953439,
CC PubMed:14765135). Together with GABPB1 and YY1, it forms a ternary
CC complex, probably being the bridge factor between these two
CC transcription factors (PubMed:11953439). Interacts with MDM2, and
CC thereby inhibits ubiquitination of TP53 (PubMed:19098711). Identified
CC in a ternary complex containing MDM2, TP53 and RYBP (PubMed:19098711).
CC Interacts with FANK1; may prevent the ubiquitin-mediated proteasomal
CC degradation of FANK1 (PubMed:27060496). Interacts with IFT57 (By
CC similarity). {ECO:0000250|UniProtKB:Q8CCI5,
CC ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:11953439,
CC ECO:0000269|PubMed:14765135, ECO:0000269|PubMed:16943429,
CC ECO:0000269|PubMed:19098711, ECO:0000269|PubMed:20696397,
CC ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:26687479,
CC ECO:0000269|PubMed:27060496}.
CC -!- INTERACTION:
CC Q8N488; P54253: ATXN1; NbExp=6; IntAct=EBI-752324, EBI-930964;
CC Q8N488; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-752324, EBI-11524452;
CC Q8N488; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-752324, EBI-2837444;
CC Q8N488; P21964-2: COMT; NbExp=3; IntAct=EBI-752324, EBI-10200977;
CC Q8N488; P02489: CRYAA; NbExp=3; IntAct=EBI-752324, EBI-6875961;
CC Q8N488; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-752324, EBI-25840379;
CC Q8N488; G5E9A7: DMWD; NbExp=3; IntAct=EBI-752324, EBI-10976677;
CC Q8N488; Q01658: DR1; NbExp=3; IntAct=EBI-752324, EBI-750300;
CC Q8N488; Q96JC9: EAF1; NbExp=3; IntAct=EBI-752324, EBI-769261;
CC Q8N488; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-752324, EBI-21603100;
CC Q8N488; P00451-2: F8; NbExp=3; IntAct=EBI-752324, EBI-25852704;
CC Q8N488; P21333-2: FLNA; NbExp=3; IntAct=EBI-752324, EBI-9641086;
CC Q8N488; P35637: FUS; NbExp=4; IntAct=EBI-752324, EBI-400434;
CC Q8N488; P14136: GFAP; NbExp=3; IntAct=EBI-752324, EBI-744302;
CC Q8N488; O14908-2: GIPC1; NbExp=3; IntAct=EBI-752324, EBI-25913156;
CC Q8N488; P78333: GPC5; NbExp=3; IntAct=EBI-752324, EBI-2558325;
CC Q8N488; P28799: GRN; NbExp=3; IntAct=EBI-752324, EBI-747754;
CC Q8N488; Q00403: GTF2B; NbExp=3; IntAct=EBI-752324, EBI-389564;
CC Q8N488; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-752324, EBI-1054873;
CC Q8N488; O43464: HTRA2; NbExp=3; IntAct=EBI-752324, EBI-517086;
CC Q8N488; P42858: HTT; NbExp=9; IntAct=EBI-752324, EBI-466029;
CC Q8N488; O60333-2: KIF1B; NbExp=3; IntAct=EBI-752324, EBI-10975473;
CC Q8N488; P02545: LMNA; NbExp=3; IntAct=EBI-752324, EBI-351935;
CC Q8N488; P31153: MAT2A; NbExp=3; IntAct=EBI-752324, EBI-1050743;
CC Q8N488; Q00987: MDM2; NbExp=11; IntAct=EBI-752324, EBI-389668;
CC Q8N488; Q92597: NDRG1; NbExp=3; IntAct=EBI-752324, EBI-716486;
CC Q8N488; P07196: NEFL; NbExp=3; IntAct=EBI-752324, EBI-475646;
CC Q8N488; P35240-4: NF2; NbExp=3; IntAct=EBI-752324, EBI-1014514;
CC Q8N488; O43933: PEX1; NbExp=3; IntAct=EBI-752324, EBI-988601;
CC Q8N488; P14618: PKM; NbExp=3; IntAct=EBI-752324, EBI-353408;
CC Q8N488; O60260-5: PRKN; NbExp=6; IntAct=EBI-752324, EBI-21251460;
CC Q8N488; P49768-2: PSEN1; NbExp=6; IntAct=EBI-752324, EBI-11047108;
CC Q8N488; P49810: PSEN2; NbExp=3; IntAct=EBI-752324, EBI-2010251;
CC Q8N488; P20618: PSMB1; NbExp=3; IntAct=EBI-752324, EBI-372273;
CC Q8N488; Q06587: RING1; NbExp=20; IntAct=EBI-752324, EBI-752313;
CC Q8N488; Q06587-2: RING1; NbExp=3; IntAct=EBI-752324, EBI-7065222;
CC Q8N488; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-752324, EBI-396669;
CC Q8N488; Q99496: RNF2; NbExp=20; IntAct=EBI-752324, EBI-722416;
CC Q8N488; Q99719: SEPTIN5; NbExp=3; IntAct=EBI-752324, EBI-373345;
CC Q8N488; P37840: SNCA; NbExp=3; IntAct=EBI-752324, EBI-985879;
CC Q8N488; Q16143: SNCB; NbExp=3; IntAct=EBI-752324, EBI-727106;
CC Q8N488; P00441: SOD1; NbExp=3; IntAct=EBI-752324, EBI-990792;
CC Q8N488; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-752324, EBI-5235340;
CC Q8N488; P49458: SRP9; NbExp=3; IntAct=EBI-752324, EBI-350743;
CC Q8N488; Q13148: TARDBP; NbExp=6; IntAct=EBI-752324, EBI-372899;
CC Q8N488; Q9NUW8: TDP1; NbExp=3; IntAct=EBI-752324, EBI-2902553;
CC Q8N488; P21980-2: TGM2; NbExp=3; IntAct=EBI-752324, EBI-25842075;
CC Q8N488; P04637: TP53; NbExp=4; IntAct=EBI-752324, EBI-366083;
CC Q8N488; P0CG47: UBB; NbExp=3; IntAct=EBI-752324, EBI-413034;
CC Q8N488; P0CG48: UBC; NbExp=3; IntAct=EBI-752324, EBI-3390054;
CC Q8N488; Q9HD64: XAGE1B; NbExp=3; IntAct=EBI-752324, EBI-2340004;
CC Q8N488; Q9P1N4; NbExp=3; IntAct=EBI-752324, EBI-25878161;
CC Q8N488; PRO_0000037319 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-752324, EBI-25487926;
CC Q8N488; Q923J1: Trpm7; Xeno; NbExp=3; IntAct=EBI-752324, EBI-8010314;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11395500,
CC ECO:0000269|PubMed:11953439, ECO:0000269|PubMed:14765135,
CC ECO:0000269|PubMed:27060496}. Cytoplasm {ECO:0000269|PubMed:11395500,
CC ECO:0000269|PubMed:14765135}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8CCI5}. Note=Primarily found in the nucleus.
CC Detected in a punctate pattern likely to represent Polycomb group (PcG)
CC bodies (By similarity). {ECO:0000250|UniProtKB:Q8CCI5}.
CC -!- TISSUE SPECIFICITY: Down-regulated in breast cancer tissues and in
CC several breast cancer cell lines (at protein level) (PubMed:27748911).
CC Widely expressed with highest levels in lymphoid tissues and placenta.
CC {ECO:0000269|PubMed:11395500, ECO:0000269|PubMed:11953439,
CC ECO:0000269|PubMed:14765135, ECO:0000269|PubMed:27748911}.
CC -!- DOMAIN: Intrinsically unstructured in the absence of binding partners.
CC Folds upon binding to DNA or RNF2 (By similarity). {ECO:0000250}.
CC -!- PTM: Monoubiquitinated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK63197.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO73587.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA89486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF179286; AAD51858.1; -; mRNA.
DR EMBL; AB029551; BAA89486.1; ALT_INIT; mRNA.
DR EMBL; AY228125; AAO73587.1; ALT_INIT; mRNA.
DR EMBL; AF227959; AAK63197.1; ALT_INIT; mRNA.
DR EMBL; BC014959; AAH14959.1; -; mRNA.
DR EMBL; BC036459; AAH36459.1; -; mRNA.
DR RefSeq; NP_036366.3; NM_012234.6.
DR PDB; 3IXS; X-ray; 1.70 A; B/D/F/H/J/L=145-179.
DR PDBsum; 3IXS; -.
DR AlphaFoldDB; Q8N488; -.
DR SMR; Q8N488; -.
DR BioGRID; 116997; 131.
DR CORUM; Q8N488; -.
DR DIP; DIP-41435N; -.
DR IntAct; Q8N488; 619.
DR MINT; Q8N488; -.
DR STRING; 9606.ENSP00000419494; -.
DR iPTMnet; Q8N488; -.
DR PhosphoSitePlus; Q8N488; -.
DR BioMuta; RYBP; -.
DR DMDM; 78102506; -.
DR EPD; Q8N488; -.
DR jPOST; Q8N488; -.
DR MassIVE; Q8N488; -.
DR MaxQB; Q8N488; -.
DR PaxDb; Q8N488; -.
DR PeptideAtlas; Q8N488; -.
DR PRIDE; Q8N488; -.
DR ProteomicsDB; 71895; -.
DR Antibodypedia; 7772; 491 antibodies from 37 providers.
DR DNASU; 23429; -.
DR Ensembl; ENST00000477973.5; ENSP00000419494.4; ENSG00000163602.12.
DR GeneID; 23429; -.
DR KEGG; hsa:23429; -.
DR UCSC; uc003dpe.4; human.
DR CTD; 23429; -.
DR DisGeNET; 23429; -.
DR GeneCards; RYBP; -.
DR HGNC; HGNC:10480; RYBP.
DR HPA; ENSG00000163602; Low tissue specificity.
DR MIM; 607535; gene.
DR neXtProt; NX_Q8N488; -.
DR PharmGKB; PA34893; -.
DR VEuPathDB; HostDB:ENSG00000163602; -.
DR eggNOG; KOG4477; Eukaryota.
DR HOGENOM; CLU_095374_0_0_1; -.
DR InParanoid; Q8N488; -.
DR OrthoDB; 1634090at2759; -.
DR PhylomeDB; Q8N488; -.
DR TreeFam; TF350501; -.
DR PathwayCommons; Q8N488; -.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q8N488; -.
DR SIGNOR; Q8N488; -.
DR BioGRID-ORCS; 23429; 11 hits in 191 CRISPR screens.
DR ChiTaRS; RYBP; human.
DR EvolutionaryTrace; Q8N488; -.
DR GeneWiki; RYBP; -.
DR GenomeRNAi; 23429; -.
DR Pharos; Q8N488; Tbio.
DR PRO; PR:Q8N488; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N488; protein.
DR Bgee; ENSG00000163602; Expressed in lower lobe of lung and 214 other tissues.
DR Genevisible; Q8N488; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR DisProt; DP00694; -.
DR InterPro; IPR039958; RYBP/YAF2.
DR InterPro; IPR033774; YAF2_RYBP.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12920; PTHR12920; 1.
DR Pfam; PF17219; YAF2_RYBP; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..228
FT /note="RING1 and YY1-binding protein"
FT /id="PRO_0000097550"
FT ZN_FING 21..50
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..226
FT /note="Interaction with GABPB1 and FANK1"
FT /evidence="ECO:0000269|PubMed:11953439,
FT ECO:0000269|PubMed:27060496"
FT REGION 172..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 20
FT /note="A -> T (in Ref. 5; AAH36459)"
FT /evidence="ECO:0000305"
FT STRAND 149..163
FT /evidence="ECO:0007829|PDB:3IXS"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:3IXS"
SQ SEQUENCE 228 AA; 24822 MW; EB9593460A3F0F4C CRC64;
MTMGDKKSPT RPKRQAKPAA DEGFWDCSVC TFRNSAEAFK CSICDVRKGT STRKPRINSQ
LVAQQVAQQY ATPPPPKKEK KEKVEKQDKE KPEKDKEISP SVTKKNTNKK TKPKSDILKD
PPSEANSIQS ANATTKTSET NHTSRPRLKN VDRSTAQQLA VTVGNVTVII TDFKEKTRSS
STSSSTVTSS AGSEQQNQSS SGSESTDKGS SRSSTPKGDM SAVNDESF
