TYY1_HUMAN
ID TYY1_HUMAN Reviewed; 414 AA.
AC P25490; Q14935;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Transcriptional repressor protein YY1;
DE AltName: Full=Delta transcription factor;
DE AltName: Full=INO80 complex subunit S;
DE AltName: Full=NF-E1;
DE AltName: Full=Yin and yang 1;
DE Short=YY-1;
GN Name=YY1; Synonyms=INO80S;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1655281; DOI=10.1016/0092-8674(91)90189-6;
RA Shi Y., Seto E., Chang L.-S., Shenk T.;
RT "Transcriptional repression by YY1, a human GLI-Kruppel-related protein,
RT and relief of repression by adenovirus E1A protein.";
RL Cell 67:377-388(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Foreskin;
RX PubMed=1946405; DOI=10.1073/pnas.88.21.9804;
RA Park K., Atchison M.;
RT "Isolation of a candidate repressor/activator, NF-E1 (YY-1, delta), that
RT binds to the immunoglobulin kappa 3' enhancer and the immunoglobulin heavy-
RT chain mu E1 site.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9804-9808(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Whitson R.H., Huang T., Dang J., Itakura K.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lymph;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9493912;
RX DOI=10.1002/(sici)1097-4644(19980315)68:4<500::aid-jcb9>3.0.co;2-u;
RA McNeil S., Guo B., Stein J.L., Lian J.B., Bushmeyer S., Seto E.,
RA Atchison M.L., Penman S., van Wijnen A.J., Stein G.S.;
RT "Targeting of the YY1 transcription factor to the nucleolus and the nuclear
RT matrix in situ: the C-terminus is a principal determinant for nuclear
RT trafficking.";
RL J. Cell. Biochem. 68:500-510(1998).
RN [6]
RP INTERACTION WITH YAF2.
RX PubMed=9016636; DOI=10.1093/nar/25.4.843;
RA Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C.;
RT "Yeast two-hybrid cloning of a novel zinc finger protein that interacts
RT with the multifunctional transcription factor YY1.";
RL Nucleic Acids Res. 25:843-849(1997).
RN [7]
RP POLY-ADP-RIBOSYLATION BY PARP1.
RX PubMed=11437367; DOI=10.1006/bbrc.2001.5115;
RA Oei S.L., Shi Y.;
RT "Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions
RT of DNA damage.";
RL Biochem. Biophys. Res. Commun. 285:27-31(2001).
RN [8]
RP INTERACTION WITH EZH2 AND EZH2.
RX PubMed=11158321; DOI=10.1128/mcb.21.4.1360-1369.2001;
RA Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.;
RT "The polycomb group protein EED interacts with YY1, and both proteins
RT induce neural tissue in Xenopus embryos.";
RL Mol. Cell. Biol. 21:1360-1369(2001).
RN [9]
RP DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH SMAD1 AND SMAD4, AND
RP FUNCTION.
RX PubMed=15329343; DOI=10.1242/dev.01344;
RA Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
RT "SMAD-mediated modulation of YY1 activity regulates the BMP response and
RT cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
RT enhancer.";
RL Development 131:4709-4723(2004).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=16314846; DOI=10.1038/sj.onc.1209080;
RA Gordon S., Akopyan G., Garban H., Bonavida B.;
RT "Transcription factor YY1: structure, function, and therapeutic
RT implications in cancer biology.";
RL Oncogene 25:1125-1142(2006).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=17721549; DOI=10.1038/nsmb1276;
RA Cai Y., Jin J., Yao T., Gottschalk A.J., Swanson S.K., Wu S., Shi Y.,
RA Washburn M.P., Florens L., Conaway R.C., Conaway J.W.;
RT "YY1 functions with INO80 to activate transcription.";
RL Nat. Struct. Mol. Biol. 14:872-874(2007).
RN [12]
RP FUNCTION IN DNA REPAIR, SUBCELLULAR LOCATION, DNA-BINDING, PROTEIN
RP INTERACTION, AND IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND THR-378, AND
RP IDENTIFICATION BY 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 [16]
RP DNA-BINDING MOTIF.
RX PubMed=18950698; DOI=10.1016/j.ygeno.2008.09.013;
RA Kim J., Kim J.;
RT "YY1's longer DNA-binding motifs.";
RL Genomics 93:152-158(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, 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 [18]
RP UBIQUITINATION.
RX PubMed=20596523; DOI=10.1371/journal.pone.0011332;
RA Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
RA Spruck C.;
RT "Development and validation of a method for profiling post-translational
RT modification activities using protein microarrays.";
RL PLoS ONE 5:E11332-E11332(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, 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 [20]
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 [21]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP 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 [23]
RP INTERACTION WITH SFMBT2, AND SUBCELLULAR LOCATION.
RX PubMed=23385818; DOI=10.1007/s12038-012-9283-6;
RA Lee K., Na W., Maeng J.H., Wu H., Ju B.G.;
RT "Regulation of DU145 prostate cancer cell growth by Scm-like with four mbt
RT domains 2.";
RL J. Biosci. 38:105-112(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-187 AND SER-247, AND
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-183; LYS-286 AND LYS-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182; LYS-183; LYS-208; LYS-230;
RP LYS-286; LYS-288; LYS-409 AND LYS-411, 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 [30]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 304-414.
RX PubMed=8942976; DOI=10.1073/pnas.93.24.13577;
RA Houbaviy H.B., Usheva A., Shenk T., Burley S.K.;
RT "Cocrystal structure of YY1 bound to the adeno-associated virus P5
RT initiator.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13577-13582(1996).
RN [31]
RP STRUCTURE BY NMR OF 353-379.
RX PubMed=9642075; DOI=10.1006/jmbi.1998.1764;
RA Viles J.H., Patel S.U., Mitchell J.B.O., Moody C.M., Justice D.E.,
RA Uppenbrink J., Doyle P.M., Harris C.J., Sadler P.J., Thornton J.M.;
RT "Design, synthesis and structure of a zinc finger with an artificial beta-
RT turn.";
RL J. Mol. Biol. 279:973-986(1998).
RN [32]
RP VARIANT GADEVS TYR-380.
RX PubMed=21076407; DOI=10.1038/ng.712;
RA Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M.,
RA de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M.,
RA van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.;
RT "A de novo paradigm for mental retardation.";
RL Nat. Genet. 42:1109-1112(2010).
RN [33]
RP VARIANT ARG-372, CHARACTERIZATION OF VARIANT ARG-372, AND FUNCTION.
RX PubMed=24326773; DOI=10.1038/ncomms3810;
RA Cao Y., Gao Z., Li L., Jiang X., Shan A., Cai J., Peng Y., Li Y., Jiang X.,
RA Huang X., Wang J., Wei Q., Qin G., Zhao J., Jin X., Liu L., Li Y., Wang W.,
RA Wang J., Ning G.;
RT "Whole exome sequencing of insulinoma reveals recurrent T372R mutations in
RT YY1.";
RL Nat. Commun. 4:2810-2810(2013).
RN [34]
RP VARIANT ARG-372, CHARACTERIZATION OF VARIANT ARG-372, AND FUNCTION.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
RN [35]
RP VARIANTS GADEVS 179-LYS--GLN-414 DEL; TYR-320; GLN-339; 344-GLN--GLN-414
RP DEL; PRO-366; VAL-366; TYR-380 AND LYS-393 DEL, CHARACTERIZATION OF
RP VARIANTS GADEVS PRO-366 AND TYR-380, AND FUNCTION.
RX PubMed=28575647; DOI=10.1016/j.ajhg.2017.05.006;
RA Gabriele M., Vulto-van Silfhout A.T., Germain P.L., Vitriolo A., Kumar R.,
RA Douglas E., Haan E., Kosaki K., Takenouchi T., Rauch A., Steindl K.,
RA Frengen E., Misceo D., Pedurupillay C.R.J., Stromme P., Rosenfeld J.A.,
RA Shao Y., Craigen W.J., Schaaf C.P., Rodriguez-Buritica D., Farach L.,
RA Friedman J., Thulin P., McLean S.D., Nugent K.M., Morton J., Nicholl J.,
RA Andrieux J., Stray-Pedersen A., Chambon P., Patrier S., Lynch S.A.,
RA Kjaergaard S., Toerring P.M., Brasch-Andersen C., Ronan A.,
RA van Haeringen A., Anderson P.J., Powis Z., Brunner H.G., Pfundt R.,
RA Schuurs-Hoeijmakers J.H.M., van Bon B.W.M., Lelieveld S., Gilissen C.,
RA Nillesen W.M., Vissers L.E.L.M., Gecz J., Koolen D.A., Testa G.,
RA de Vries B.B.A.;
RT "YY1 haploinsufficiency causes an intellectual disability syndrome
RT featuring transcriptional and chromatin dysfunction.";
RL Am. J. Hum. Genet. 100:907-925(2017).
CC -!- FUNCTION: Multifunctional transcription factor that exhibits positive
CC and negative control on a large number of cellular and viral genes by
CC binding to sites overlapping the transcription start site. Binds to the
CC consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to
CC contain a longer binding motif allowing enhanced binding; the initial
CC CG dinucleotide can be methylated greatly reducing the binding
CC affinity. The effect on transcription regulation is depending upon the
CC context in which it binds and diverse mechanisms of action include
CC direct activation or repression, indirect activation or repression via
CC cofactor recruitment, or activation or repression by disruption of
CC binding sites or conformational DNA changes. Its activity is regulated
CC by transcription factors and cytoplasmic proteins that have been shown
CC to abrogate or completely inhibit YY1-mediated activation or
CC repression. For example, it acts as a repressor in absence of
CC adenovirus E1A protein but as an activator in its presence. Acts
CC synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein
CC (BMP)-mediated cardiac-specific gene expression (PubMed:15329343).
CC Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP
CC response element (BMPRE) of cardiac activating regions. May play an
CC important role in development and differentiation. Proposed to recruit
CC the PRC2/EED-EZH2 complex to target genes that are transcriptional
CC repressed. Involved in DNA repair. In vitro, binds to DNA recombination
CC intermediate structures (Holliday junctions). Plays a role in
CC regulating enhancer activation (PubMed:28575647).
CC {ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:24326773,
CC ECO:0000269|PubMed:25787250, ECO:0000269|PubMed:28575647}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair; proposed to target the INO80
CC complex to YY1-responsive elements. {ECO:0000269|PubMed:17721549,
CC ECO:0000269|PubMed:18026119}.
CC -!- SUBUNIT: Interacts with YAF2 through the region encompassing the first
CC and second zinc fingers (PubMed:9016636). Component of the chromatin
CC remodeling INO80 complex; specifically part of a complex module
CC associated with the DBINO domain of INO80 (PubMed:17721549,
CC PubMed:18026119, PubMed:18922472, PubMed:21303910). Interacts with EED
CC and EZH2; the interactions are indicative for an association with the
CC PRC2/EED-EZH2 complex (PubMed:11158321). Interacts with SFMBT2
CC (PubMed:23385818). Found in a complex with SMAD1 and SMAD4
CC (PubMed:15329343). Found in a complex with YY1, SIN3A and HDAC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q00899,
CC ECO:0000269|PubMed:11158321, ECO:0000269|PubMed:15329343,
CC ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:23385818, ECO:0000269|PubMed:9016636}.
CC -!- INTERACTION:
CC P25490; O96019: ACTL6A; NbExp=7; IntAct=EBI-765538, EBI-355018;
CC P25490; Q9BYJ1: ALOXE3; NbExp=3; IntAct=EBI-765538, EBI-6925949;
CC P25490; P49407: ARRB1; NbExp=4; IntAct=EBI-765538, EBI-743313;
CC P25490; P45973: CBX5; NbExp=3; IntAct=EBI-765538, EBI-78219;
CC P25490; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-765538, EBI-742887;
CC P25490; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-765538, EBI-3867333;
CC P25490; G5E9A7: DMWD; NbExp=3; IntAct=EBI-765538, EBI-10976677;
CC P25490; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-765538, EBI-12260294;
CC P25490; Q14192: FHL2; NbExp=5; IntAct=EBI-765538, EBI-701903;
CC P25490; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-765538, EBI-2548508;
CC P25490; O15354: GPR37; NbExp=3; IntAct=EBI-765538, EBI-15639515;
CC P25490; P28799: GRN; NbExp=4; IntAct=EBI-765538, EBI-747754;
CC P25490; P28799-2: GRN; NbExp=3; IntAct=EBI-765538, EBI-25860013;
CC P25490; P22301: IL10; NbExp=3; IntAct=EBI-765538, EBI-1031632;
CC P25490; Q9ULG1: INO80; NbExp=9; IntAct=EBI-765538, EBI-769345;
CC P25490; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-765538, EBI-11749135;
CC P25490; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-765538, EBI-11741292;
CC P25490; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-765538, EBI-10172150;
CC P25490; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-765538, EBI-10171774;
CC P25490; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-765538, EBI-10172052;
CC P25490; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-765538, EBI-10176379;
CC P25490; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-765538, EBI-11953334;
CC P25490; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-765538, EBI-11988175;
CC P25490; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-765538, EBI-14065470;
CC P25490; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-765538, EBI-10172511;
CC P25490; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-765538, EBI-11993254;
CC P25490; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-765538, EBI-10250562;
CC P25490; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-765538, EBI-1043191;
CC P25490; Q9BYQ0: KRTAP9-8; NbExp=5; IntAct=EBI-765538, EBI-11958364;
CC P25490; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-765538, EBI-12039345;
CC P25490; Q969G2: LHX4; NbExp=4; IntAct=EBI-765538, EBI-2865388;
CC P25490; Q99750: MDFI; NbExp=3; IntAct=EBI-765538, EBI-724076;
CC P25490; Q9H944: MED20; NbExp=3; IntAct=EBI-765538, EBI-394644;
CC P25490; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-765538, EBI-742388;
CC P25490; P78527: PRKDC; NbExp=2; IntAct=EBI-765538, EBI-352053;
CC P25490; P54725: RAD23A; NbExp=3; IntAct=EBI-765538, EBI-746453;
CC P25490; Q9Y265: RUVBL1; NbExp=6; IntAct=EBI-765538, EBI-353675;
CC P25490; Q9Y230: RUVBL2; NbExp=8; IntAct=EBI-765538, EBI-352939;
CC P25490; P50454: SERPINH1; NbExp=3; IntAct=EBI-765538, EBI-350723;
CC P25490; Q15428: SF3A2; NbExp=5; IntAct=EBI-765538, EBI-2462271;
CC P25490; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-765538, EBI-5235340;
CC P25490; P37173: TGFBR2; NbExp=3; IntAct=EBI-765538, EBI-296151;
CC P25490; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-765538, EBI-5235829;
CC P25490; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-765538, EBI-11957238;
CC P25490; O76024: WFS1; NbExp=3; IntAct=EBI-765538, EBI-720609;
CC P25490; Q9HD64: XAGE1B; NbExp=3; IntAct=EBI-765538, EBI-2340004;
CC P25490; Q9H869: YY1AP1; NbExp=5; IntAct=EBI-765538, EBI-946122;
CC P25490; Q9H869-2: YY1AP1; NbExp=4; IntAct=EBI-765538, EBI-12150045;
CC P25490; Q49A12: ZNF85; NbExp=3; IntAct=EBI-765538, EBI-18141506;
CC P25490; Q8JSK4: E1A; Xeno; NbExp=4; IntAct=EBI-765538, EBI-7453955;
CC P25490; Q8CCI5: Rybp; Xeno; NbExp=2; IntAct=EBI-765538, EBI-929290;
CC P25490; P03259; Xeno; NbExp=3; IntAct=EBI-765538, EBI-6947456;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:23385818, ECO:0000269|PubMed:9493912}.
CC Note=Associated with the nuclear matrix.
CC -!- PTM: Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with
CC the effect of decreasing affinity of YY1 to its cognate DNA binding
CC sites.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
CC -!- DISEASE: Gabriele-de Vries syndrome (GADEVS) [MIM:617557]: An autosomal
CC dominant neurodevelopmental disorder characterized by delayed
CC psychomotor development and intellectual disability. Most patients have
CC behavioral and feeding problems, movement abnormalities, mild distal
CC skeletal anomalies, and dysmorphic facial features.
CC {ECO:0000269|PubMed:21076407, ECO:0000269|PubMed:28575647}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the YY transcription factor family.
CC {ECO:0000305}.
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DR EMBL; M77698; AAA59467.1; -; mRNA.
DR EMBL; M76541; AAA59926.1; -; mRNA.
DR EMBL; Z14077; CAA78455.1; -; mRNA.
DR EMBL; BC037308; AAH37308.1; -; mRNA.
DR EMBL; BC065366; AAH65366.1; -; mRNA.
DR CCDS; CCDS9957.1; -.
DR PIR; A40350; A40350.
DR RefSeq; NP_003394.1; NM_003403.4.
DR PDB; 1UBD; X-ray; 2.50 A; C=291-414.
DR PDB; 1ZNM; NMR; -; A=352-379.
DR PDB; 4C5I; X-ray; 2.59 A; C=199-228.
DR PDBsum; 1UBD; -.
DR PDBsum; 1ZNM; -.
DR PDBsum; 4C5I; -.
DR AlphaFoldDB; P25490; -.
DR SMR; P25490; -.
DR BioGRID; 113360; 447.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; P25490; -.
DR DIP; DIP-150N; -.
DR IntAct; P25490; 264.
DR MINT; P25490; -.
DR STRING; 9606.ENSP00000262238; -.
DR GlyGen; P25490; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P25490; -.
DR PhosphoSitePlus; P25490; -.
DR BioMuta; YY1; -.
DR DMDM; 3915889; -.
DR EPD; P25490; -.
DR jPOST; P25490; -.
DR MassIVE; P25490; -.
DR MaxQB; P25490; -.
DR PaxDb; P25490; -.
DR PeptideAtlas; P25490; -.
DR PRIDE; P25490; -.
DR ProteomicsDB; 54279; -.
DR Antibodypedia; 9; 598 antibodies from 42 providers.
DR DNASU; 7528; -.
DR Ensembl; ENST00000262238.10; ENSP00000262238.4; ENSG00000100811.14.
DR GeneID; 7528; -.
DR KEGG; hsa:7528; -.
DR MANE-Select; ENST00000262238.10; ENSP00000262238.4; NM_003403.5; NP_003394.1.
DR UCSC; uc001ygy.3; human.
DR CTD; 7528; -.
DR DisGeNET; 7528; -.
DR GeneCards; YY1; -.
DR GeneReviews; YY1; -.
DR HGNC; HGNC:12856; YY1.
DR HPA; ENSG00000100811; Low tissue specificity.
DR MalaCards; YY1; -.
DR MIM; 600013; gene.
DR MIM; 617557; phenotype.
DR neXtProt; NX_P25490; -.
DR OpenTargets; ENSG00000100811; -.
DR Orphanet; 506358; Gabriele-de Vries syndrome.
DR Orphanet; 97279; Insulinoma.
DR PharmGKB; PA37445; -.
DR VEuPathDB; HostDB:ENSG00000100811; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154763; -.
DR InParanoid; P25490; -.
DR OMA; DAGGRKW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P25490; -.
DR TreeFam; TF106493; -.
DR PathwayCommons; P25490; -.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P25490; -.
DR SIGNOR; P25490; -.
DR BioGRID-ORCS; 7528; 602 hits in 1118 CRISPR screens.
DR ChiTaRS; YY1; human.
DR EvolutionaryTrace; P25490; -.
DR GeneWiki; YY1; -.
DR GenomeRNAi; 7528; -.
DR Pharos; P25490; Tbio.
DR PRO; PR:P25490; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P25490; protein.
DR Bgee; ENSG00000100811; Expressed in ventricular zone and 181 other tissues.
DR ExpressionAtlas; P25490; baseline and differential.
DR Genevisible; P25490; HS.
DR GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; TAS:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0046332; F:SMAD binding; IMP:AgBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IEA:Ensembl.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:UniProtKB.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034696; P:response to prostaglandin F; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
DR GO; GO:0006403; P:RNA localization; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR IDEAL; IID00234; -.
DR InterPro; IPR017114; YY1-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR PIRSF; PIRSF037113; TF_Yin_yang; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ADP-ribosylation; Differentiation;
KW Direct protein sequencing; Disease variant; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Intellectual disability; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Spermatogenesis; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..414
FT /note="Transcriptional repressor protein YY1"
FT /id="PRO_0000047190"
FT ZN_FING 296..320
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..377
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..407
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..170
FT /note="Interaction with the SMAD1/SMAD4 complex"
FT REGION 33..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..341
FT /note="Involved in nuclear matrix association"
FT REGION 295..414
FT /note="Binding to DNA"
FT REGION 333..371
FT /note="Involved in repression of activated transcription"
FT REGION 371..397
FT /note="Involved in masking transactivation domain"
FT COMPBIAS 39..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 179..414
FT /note="Missing (in GADEVS)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079202"
FT VARIANT 320
FT /note="H -> Y (in GADEVS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079203"
FT VARIANT 339
FT /note="K -> Q (in GADEVS; unknown pathological
FT significance; dbSNP:rs1555370868)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079204"
FT VARIANT 344..414
FT /note="Missing (in GADEVS)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079205"
FT VARIANT 366
FT /note="L -> P (in GADEVS; reduced DNA-binding; reduced
FT transcription regulator activity; dbSNP:rs1131692163)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079206"
FT VARIANT 366
FT /note="L -> V (in GADEVS; unknown pathological
FT significance; dbSNP:rs1131692044)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079207"
FT VARIANT 372
FT /note="T -> R (found in patients with late onset
FT insulinomas; alters DNA-binding motif; increases
FT transactivation activity; produces a constitutive
FT activation of cAMP and Ca2+ signaling pathways involved in
FT insulin secretion; dbSNP:rs386834266)"
FT /evidence="ECO:0000269|PubMed:24326773,
FT ECO:0000269|PubMed:25787250"
FT /id="VAR_074172"
FT VARIANT 380
FT /note="D -> Y (in GADEVS; reduced DNA-binding; reduced
FT transcription regulator activity; dbSNP:rs1131692043)"
FT /evidence="ECO:0000269|PubMed:21076407,
FT ECO:0000269|PubMed:28575647"
FT /id="VAR_065086"
FT VARIANT 393
FT /note="Missing (in GADEVS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28575647"
FT /id="VAR_079208"
FT CONFLICT 65
FT /note="H -> R (in Ref. 2; AAA59926)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="G -> R (in Ref. 1; AAA59467)"
FT /evidence="ECO:0000305"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4C5I"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4C5I"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1UBD"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1UBD"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1UBD"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1ZNM"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:1UBD"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:1UBD"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:1UBD"
SQ SEQUENCE 414 AA; 44713 MW; 058C05A0AD2D04E6 CRC64;
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD DEDGGGGDHG
GGGGHGHAGH HHHHHHHHHH PPMIALQPLV TDDPTQVHHH QEVILVQTRE EVVGGDDSDG
LRAEDGFEDQ ILIPVPAPAG GDDDYIEQTL VTVAAAGKSG GGGSSSSGGG RVKKGGGKKS
GKKSYLSGGA GAAGGGGADP GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE
QIIGENSPPD YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH
KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE KPFQCTFEGC
GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL KSHILTHAKA KNNQ
