YAF2_HUMAN
ID YAF2_HUMAN Reviewed; 180 AA.
AC Q8IY57; A8K5P0; B4DFU3; G3V465; Q99710;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=YY1-associated factor 2;
GN Name=YAF2;
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] (ISOFORM 1), FUNCTION, AND INTERACTION WITH YY1.
RC TISSUE=Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Amygdala, Brain, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYCN.
RX PubMed=11593398; DOI=10.1038/sj.onc.1204747;
RA Bannasch D., Maedge B., Schwab M.;
RT "Functional interaction of Yaf2 with the central region of MycN.";
RL Oncogene 20:5913-5919(2001).
RN [7]
RP IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3;
RP RING1; RNF2; MBLR; L3MBTL2 AND BAT8.
RX PubMed=12004135; DOI=10.1126/science.1069861;
RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT genes in G0 cells.";
RL Science 296:1132-1136(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH MYC.
RX PubMed=12706874; DOI=10.1016/s0304-3835(02)00696-1;
RA Maedge B., Geisen C., Moeroey T., Schwab M.;
RT "Yaf2 inhibits Myc biological function.";
RL Cancer Lett. 193:171-176(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP STRUCTURE BY NMR OF 17-58.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-RANBP domain of YY1-associated factor 2.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Binds to MYC and inhibits MYC-mediated transactivation. Also
CC binds to MYCN and enhances MYCN-dependent transcriptional activation.
CC Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of
CC the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of
CC histone H3, suggesting that it is involved in chromatin-remodeling.
CC {ECO:0000269|PubMed:11593398, ECO:0000269|PubMed:12706874,
CC ECO:0000269|PubMed:9016636}.
CC -!- SUBUNIT: Interacts with MYC, MYCN, RNF2/RING1B and YY1. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2.
CC {ECO:0000269|PubMed:11593398, ECO:0000269|PubMed:12004135,
CC ECO:0000269|PubMed:12706874, ECO:0000269|PubMed:9016636}.
CC -!- INTERACTION:
CC Q8IY57; Q06587: RING1; NbExp=7; IntAct=EBI-2842031, EBI-752313;
CC Q8IY57; Q9Y6X0: SETBP1; NbExp=3; IntAct=EBI-2842031, EBI-2548259;
CC Q8IY57; Q9HD64: XAGE1B; NbExp=3; IntAct=EBI-2842031, EBI-2340004;
CC Q8IY57-5; Q92688: ANP32B; NbExp=3; IntAct=EBI-12111538, EBI-762428;
CC Q8IY57-5; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-12111538, EBI-2559016;
CC Q8IY57-5; Q8TDQ1-4: CD300LF; NbExp=3; IntAct=EBI-12111538, EBI-17784261;
CC Q8IY57-5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12111538, EBI-10976677;
CC Q8IY57-5; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-12111538, EBI-10239299;
CC Q8IY57-5; Q96JC9: EAF1; NbExp=5; IntAct=EBI-12111538, EBI-769261;
CC Q8IY57-5; P28799: GRN; NbExp=3; IntAct=EBI-12111538, EBI-747754;
CC Q8IY57-5; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-12111538, EBI-725672;
CC Q8IY57-5; Q9C086: INO80B; NbExp=3; IntAct=EBI-12111538, EBI-715611;
CC Q8IY57-5; P47929: LGALS7B; NbExp=3; IntAct=EBI-12111538, EBI-357504;
CC Q8IY57-5; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-12111538, EBI-726739;
CC Q8IY57-5; Q9P0L2: MARK1; NbExp=3; IntAct=EBI-12111538, EBI-968587;
CC Q8IY57-5; P61970: NUTF2; NbExp=3; IntAct=EBI-12111538, EBI-591778;
CC Q8IY57-5; O14917: PCDH17; NbExp=3; IntAct=EBI-12111538, EBI-947061;
CC Q8IY57-5; Q9BT43: POLR3GL; NbExp=3; IntAct=EBI-12111538, EBI-2855862;
CC Q8IY57-5; O60927: PPP1R11; NbExp=3; IntAct=EBI-12111538, EBI-1048104;
CC Q8IY57-5; Q06587: RING1; NbExp=8; IntAct=EBI-12111538, EBI-752313;
CC Q8IY57-5; Q99496: RNF2; NbExp=5; IntAct=EBI-12111538, EBI-722416;
CC Q8IY57-5; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-12111538, EBI-12023934;
CC Q8IY57-5; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-12111538, EBI-12037215;
CC Q8IY57-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12111538, EBI-5235340;
CC Q8IY57-5; Q9UKI8: TLK1; NbExp=3; IntAct=EBI-12111538, EBI-740492;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11593398}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8IY57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY57-5; Sequence=VSP_055659;
CC Name=3;
CC IsoId=Q8IY57-3; Sequence=VSP_043415;
CC Name=4;
CC IsoId=Q8IY57-4; Sequence=VSP_044598, VSP_044599;
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DR EMBL; U72209; AAC51116.1; -; mRNA.
DR EMBL; AK127531; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291355; BAF84044.1; -; mRNA.
DR EMBL; AK294260; BAG57554.1; -; mRNA.
DR EMBL; AC020629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW57839.1; -; Genomic_DNA.
DR EMBL; BC037777; AAH37777.1; -; mRNA.
DR CCDS; CCDS31775.1; -. [Q8IY57-1]
DR CCDS; CCDS53778.1; -. [Q8IY57-3]
DR CCDS; CCDS53779.1; -. [Q8IY57-5]
DR CCDS; CCDS53780.1; -. [Q8IY57-4]
DR RefSeq; NP_001177906.1; NM_001190977.2. [Q8IY57-3]
DR RefSeq; NP_001177908.1; NM_001190979.2. [Q8IY57-5]
DR RefSeq; NP_001177909.1; NM_001190980.2. [Q8IY57-4]
DR RefSeq; NP_005739.2; NM_005748.5. [Q8IY57-1]
DR PDB; 2D9G; NMR; -; A=19-58.
DR PDBsum; 2D9G; -.
DR AlphaFoldDB; Q8IY57; -.
DR SMR; Q8IY57; -.
DR BioGRID; 115441; 194.
DR CORUM; Q8IY57; -.
DR DIP; DIP-44919N; -.
DR IntAct; Q8IY57; 95.
DR MINT; Q8IY57; -.
DR GlyGen; Q8IY57; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8IY57; -.
DR PhosphoSitePlus; Q8IY57; -.
DR BioMuta; YAF2; -.
DR DMDM; 215274199; -.
DR EPD; Q8IY57; -.
DR jPOST; Q8IY57; -.
DR MassIVE; Q8IY57; -.
DR MaxQB; Q8IY57; -.
DR PeptideAtlas; Q8IY57; -.
DR PRIDE; Q8IY57; -.
DR ProteomicsDB; 71112; -. [Q8IY57-1]
DR ProteomicsDB; 71114; -. [Q8IY57-3]
DR Antibodypedia; 13166; 158 antibodies from 26 providers.
DR DNASU; 10138; -.
DR Ensembl; ENST00000327791.8; ENSP00000328004.5; ENSG00000015153.15. [Q8IY57-5]
DR Ensembl; ENST00000380790.4; ENSP00000370167.4; ENSG00000015153.15. [Q8IY57-3]
DR Ensembl; ENST00000534854.7; ENSP00000439256.2; ENSG00000015153.15. [Q8IY57-1]
DR Ensembl; ENST00000555248.2; ENSP00000451626.2; ENSG00000015153.15. [Q8IY57-4]
DR GeneID; 10138; -.
DR KEGG; hsa:10138; -.
DR MANE-Select; ENST00000534854.7; ENSP00000439256.2; NM_005748.6; NP_005739.2.
DR UCSC; uc001rmv.4; human. [Q8IY57-1]
DR CTD; 10138; -.
DR DisGeNET; 10138; -.
DR GeneCards; YAF2; -.
DR HGNC; HGNC:17363; YAF2.
DR HPA; ENSG00000015153; Low tissue specificity.
DR MIM; 607534; gene.
DR neXtProt; NX_Q8IY57; -.
DR OpenTargets; ENSG00000015153; -.
DR PharmGKB; PA38236; -.
DR VEuPathDB; HostDB:ENSG00000015153; -.
DR GeneTree; ENSGT00390000013995; -.
DR HOGENOM; CLU_095374_0_0_1; -.
DR InParanoid; Q8IY57; -.
DR OMA; VCTFRNG; -.
DR OrthoDB; 1634090at2759; -.
DR PhylomeDB; Q8IY57; -.
DR TreeFam; TF350501; -.
DR PathwayCommons; Q8IY57; -.
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; Q8IY57; -.
DR BioGRID-ORCS; 10138; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; YAF2; human.
DR EvolutionaryTrace; Q8IY57; -.
DR GeneWiki; YAF2; -.
DR GenomeRNAi; 10138; -.
DR Pharos; Q8IY57; Tbio.
DR PRO; PR:Q8IY57; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IY57; protein.
DR Bgee; ENSG00000015153; Expressed in right atrium auricular region and 126 other tissues.
DR ExpressionAtlas; Q8IY57; baseline and differential.
DR Genevisible; Q8IY57; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR039958; RYBP/YAF2.
DR InterPro; IPR038039; YAF2.
DR InterPro; IPR033774; YAF2_RYBP.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR12920; PTHR12920; 1.
DR PANTHER; PTHR12920:SF2; PTHR12920:SF2; 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; Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..180
FT /note="YY1-associated factor 2"
FT /id="PRO_0000066113"
FT ZN_FING 19..48
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 8..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043415"
FT VAR_SEQ 50
FT /note="T -> TRSTLFEVIVSASRTKEPLKFPISG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055659"
FT VAR_SEQ 52..117
FT /note="KPRPVSQLVAQQVTQQFVPPTQSKKEKKDKVEKEKSEKETTSKKNSHKKTRP
FT RLKNVDRSSAQHLE -> DSKEGGKLVSYSTASLGVRGTLRNRVGGGSSEEKKQAEYLA
FT PGRRRNIVHRGVGPGQRSGPSLKEA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044598"
FT VAR_SEQ 118..180
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044599"
FT CONFLICT 13..14
FT /note="QP -> HA (in Ref. 1; AAC51116)"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2D9G"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2D9G"
SQ SEQUENCE 180 AA; 19901 MW; 199A56EE06BB4FBE CRC64;
MGDKKSPTRP KRQPKPSSDE GYWDCSVCTF RNSAEAFKCM MCDVRKGTST RKPRPVSQLV
AQQVTQQFVP PTQSKKEKKD KVEKEKSEKE TTSKKNSHKK TRPRLKNVDR SSAQHLEVTV
GDLTVIITDF KEKTKSPPAS SAASADQHSQ SGSSSDNTER GMSRSSSPRG EASSLNGESH
