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 24-JAN-2024, entry version 185. 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; 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 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; 200. DR ComplexPortal; CPX-2260; Non-canonical polycomb repressive complex 1.2, RING1-YAF2 variant. DR ComplexPortal; CPX-2272; Non-canonical polycomb repressive complex 1.1, RING2-PCGF1-YAF2 variant. DR ComplexPortal; CPX-2274; Non-canonical polycomb repressive complex 1.4, RING1-YAF2 variant. DR ComplexPortal; CPX-2280; Non-canonical polycomb repressive complex 1.2, RNF2-YAF2 variant. DR ComplexPortal; CPX-2282; Non-canonical polycomb repressive complex 1.4, RNF2-YAF2 variant. DR ComplexPortal; CPX-2288; Non-canonical polycomb repressive complex 1.3, RING1-YAF2-CKIIA2 variant. DR ComplexPortal; CPX-2289; Non-canonical polycomb repressive complex 1.3, RING1-YAF2-CKIIA1-A2 variant. DR ComplexPortal; CPX-2290; Non-canonical polycomb repressive complex 1.3, RING1-YAF2-CKIIA1 variant. DR ComplexPortal; CPX-2296; Non-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA2 variant. DR ComplexPortal; CPX-2297; Non-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA1-A2 variant. DR ComplexPortal; CPX-2298; Non-canonical polycomb repressive complex 1.3, RING2-YAF2-CKIIA1 variant. DR ComplexPortal; CPX-2550; Non-canonical polycomb repressive complex 1.6, RING1-YAF2 variant. DR ComplexPortal; CPX-2557; Non-canonical polycomb repressive complex 1.6, RING2-YAF2 variant. DR ComplexPortal; CPX-7561; Non-canonical polycomb repressive complex 1.1, RING1-PCGF1-YAF2 variant. DR ComplexPortal; CPX-7584; Non-canonical polycomb repressive complex 1.5, RING1-YAF2-CKIIA2 variant. DR ComplexPortal; CPX-7585; Non-canonical polycomb repressive complex 1.5, RING1-YAF2-CKIIA1-A2 variant. DR ComplexPortal; CPX-7586; Non-canonical polycomb repressive complex 1.5, RING1-YAF2-CKIIA1 variant. DR ComplexPortal; CPX-7590; Non-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA2 variant. DR ComplexPortal; CPX-7591; Non-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA1-A2 variant. DR ComplexPortal; CPX-7592; Non-canonical polycomb repressive complex 1.5, RING2-YAF2-CKIIA1 variant. DR CORUM; Q8IY57; -. DR DIP; DIP-44919N; -. DR IntAct; Q8IY57; 95. DR MINT; Q8IY57; -. DR STRING; 9606.ENSP00000328004; -. DR GlyCosmos; Q8IY57; 2 sites, 1 glycan. 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 ProteomicsDB; 71112; -. [Q8IY57-1] DR ProteomicsDB; 71114; -. [Q8IY57-3] DR Pumba; Q8IY57; -. DR Antibodypedia; 13166; 169 antibodies from 27 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 AGR; HGNC:17363; -. 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; TMKKKSY; -. DR OrthoDB; 2968533at2759; -. 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 1162 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 128 other cell types or tissues. DR ExpressionAtlas; Q8IY57; baseline and differential. 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 DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1. DR InterPro; IPR039958; RYBP/YAF2. DR InterPro; IPR033774; YAF2_RYBP. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR PANTHER; PTHR12920; RYBP AND YAF2-RELATED; 1. DR PANTHER; PTHR12920:SF2; YY1-ASSOCIATED FACTOR 2; 1. DR Pfam; PF17219; YAF2_RYBP; 1. DR Pfam; PF00641; zf-RanBP; 1. DR SMART; SM00547; ZnF_RBZ; 1. DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1. DR PROSITE; PS01358; ZF_RANBP2_1; 1. DR PROSITE; PS50199; ZF_RANBP2_2; 1. DR Genevisible; Q8IY57; HS. 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 //