ID MCAF1_HUMAN Reviewed; 1270 AA. AC Q6VMQ6; F5GX74; G3V1U0; Q4G0T9; Q6P3T3; Q86XW5; Q9NVJ9; Q9NWC2; Q9Y4X8; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 175. DE RecName: Full=Activating transcription factor 7-interacting protein 1 {ECO:0000305}; DE AltName: Full=ATF-interacting protein; DE Short=ATF-IP; DE AltName: Full=ATF7-interacting protein; DE AltName: Full=ATFa-associated modulator; DE Short=hAM; DE AltName: Full=MBD1-containing chromatin-associated factor 1; DE AltName: Full=P621; GN Name=ATF7IP {ECO:0000312|HGNC:HGNC:20092}; Synonyms=MCAF, MCAF1; 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), IDENTIFICATION BY MASS RP SPECTROMETRY, FUNCTION, INTERACTION WITH SETDB1, AND VARIANT ARG-530. RX PubMed=14536086; DOI=10.1016/j.molcel.2003.08.007; RA Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B., RA Tempst P., Roeder R.G., Zhang Y.; RT "mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of RT histone H3 to cause transcriptional repression."; RL Mol. Cell 12:475-487(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD1, RP AND VARIANT ILE-348. RX PubMed=12665582; DOI=10.1128/mcb.23.8.2834-2843.2003; RA Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H., RA Nakao M.; RT "MCAF mediates MBD1-dependent transcriptional repression."; RL Mol. Cell. Biol. 23:2834-2843(2003). 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), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-513, AND VARIANT ARG-530. RC TISSUE=Brain, and PNS; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 479-1270 AND 479-1270 (ISOFORM RP 1), AND VARIANT ARG-530. RC TISSUE=Embryo, and Teratocarcinoma; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 545-1058 (ISOFORM 1), AND INTERACTION WITH RP SP1. RC TISSUE=Colon; RX PubMed=10976766; DOI=10.1023/a:1007177623283; RA Gunther M., Laithier M., Brison O.; RT "A set of proteins interacting with transcription factor Sp1 identified in RT a two-hybrid screening."; RL Mol. Cell. Biochem. 210:131-142(2000). RN [8] RP INTERACTION WITH ZHX1. RX PubMed=12659632; DOI=10.1042/bj20021866; RA Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T., RA Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.; RT "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: RT molecular cloning and characterization of a member of the ZHX family, RT ZHX3."; RL Biochem. J. 373:167-178(2003). RN [9] RP INTERACTION WITH SETDB1; MBD1 AND SP1, AND MUTAGENESIS OF LEU-1224. RX PubMed=15691849; DOI=10.1074/jbc.m413654200; RA Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.; RT "Transcriptional repression and heterochromatin formation by MBD1 and RT MCAF/AM family proteins."; RL J. Biol. Chem. 280:13928-13935(2005). RN [10] RP INTERACTION WITH EPSTEIN-BARR VIRUS/EBV PROTEIN BRLF1 (MICROBIAL RP INFECTION). RX PubMed=16314315; DOI=10.1093/nar/gki956; RA Chang L.-K., Chung J.-Y., Hong Y.-R., Ichimura T., Nakao M., Liu S.-T.; RT "Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via RT an interaction with MCAF1."; RL Nucleic Acids Res. 33:6528-6539(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-673, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP INTERACTION WITH SUMO AND MBD1, AND MUTAGENESIS OF ASP-968 AND LEU-969. RX PubMed=16757475; DOI=10.1074/jbc.m602280200; RA Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M., RA Saitoh H.; RT "Involvement of SUMO modification in MBD1- and MCAF1-mediated RT heterochromatin formation."; RL J. Biol. Chem. 281:23180-23190(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-118; SER-473 AND RP SER-899, AND 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 [15] 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 [16] RP FUNCTION, INTERACTION WITH ERCC2; ERCC3; GTF2E1; GTF2E2; POLR2A AND SP1, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19106100; DOI=10.1074/jbc.m807098200; RA Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., RA Watanabe S., Saitoh N., Ito T., Nakao M.; RT "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated RT telomerase activity."; RL J. Biol. Chem. 284:5165-5174(2009). RN [17] 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 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-496; SER-559 AND RP SER-673, AND 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-445; SER-474; SER-477 RP AND SER-899, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-496; SER-559 AND RP SER-673, AND 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 [23] RP FUNCTION, INTERACTION WITH SETDB1, AND SUBCELLULAR LOCATION. RX PubMed=27732843; DOI=10.1016/j.celrep.2016.09.050; RA Timms R.T., Tchasovnikarova I.A., Antrobus R., Dougan G., Lehner P.J.; RT "ATF7IP-Mediated Stabilization of the Histone Methyltransferase SETDB1 Is RT Essential for Heterochromatin Formation by the HUSH Complex."; RL Cell Rep. 17:653-659(2016). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-558; LYS-910 AND LYS-938, RP AND IDENTIFICATION BY MASS 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 [25] RP STRUCTURE BY NMR OF 938-981 IN COMPLEX WITH SUMO3. RX PubMed=18842587; DOI=10.1074/jbc.m802528200; RA Sekiyama N., Ikegami T., Yamane T., Ikeguchi M., Uchimura Y., Baba D., RA Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.; RT "Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of RT MBD1-containing chromatin-associated factor 1 bound to SUMO-3."; RL J. Biol. Chem. 283:35966-35975(2008). CC -!- FUNCTION: Recruiter that couples transcriptional factors to general CC transcription apparatus and thereby modulates transcription regulation CC and chromatin formation. Can both act as an activator or a repressor CC depending on the context. Required for HUSH-mediated heterochromatin CC formation and gene silencing (PubMed:27732843). Mediates MBD1-dependent CC transcriptional repression, probably by recruiting complexes containing CC SETDB1 (PubMed:12665582). Stabilizes SETDB1, is required to stimulate CC histone methyltransferase activity of SETDB1 and facilitates the CC conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The CC complex formed with MBD1 and SETDB1 represses transcription and couples CC DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3) CC (PubMed:14536086, PubMed:27732843). Facilitates telomerase TERT and CC TERC gene expression by SP1 in cancer cells (PubMed:19106100). CC {ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, CC ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:27732843}. CC -!- SUBUNIT: Interacts with MBD1; the interaction is enhanced when MBD1 is CC sumoylated (PubMed:12665582, PubMed:16757475). Interacts with SETDB1; CC the interaction protects SETDB1 from proteasomal degradation and is CC required to stimulate histone methyltransferase activity and facilitate CC the conversion of dimethylated to trimethylated H3 'Lys-9' CC (PubMed:14536086, PubMed:15691849, PubMed:27732843). Interacts with CC SUMO ubiquitin-like proteins (SUMO1, SUNO2 and SUMO3), with a CC preference for SUMO2 and SUMO3 (PubMed:16757475, PubMed:18842587). CC Interacts with SP1, ATF7 and ZHX1 (PubMed:10976766, PubMed:12659632, CC PubMed:19106100). Interacts with the general transcription machinery, CC including ERCC2, ERCC3, GTF2E1, GTF2E2 and POLR2A (PubMed:19106100). CC {ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:12659632, CC ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086, CC ECO:0000269|PubMed:15691849, ECO:0000269|PubMed:16757475, CC ECO:0000269|PubMed:18842587, ECO:0000269|PubMed:19106100, CC ECO:0000269|PubMed:27732843}. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus CC BRLF1/Rta protein, leading to the regulation of host genes in Epstein- CC Barr virus-infected cells. {ECO:0000269|PubMed:16314315}. CC -!- INTERACTION: CC Q6VMQ6; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-928732, EBI-529989; CC Q6VMQ6; Q9UHL9: GTF2IRD1; NbExp=3; IntAct=EBI-928732, EBI-372530; CC Q6VMQ6-2; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-12070560, EBI-744366; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19106100, CC ECO:0000269|PubMed:27732843}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6VMQ6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6VMQ6-2; Sequence=VSP_024035, VSP_024038, VSP_024039; CC Name=3; CC IsoId=Q6VMQ6-4; Sequence=VSP_055912; CC Name=4; CC IsoId=Q6VMQ6-5; Sequence=VSP_024035; CC -!- TISSUE SPECIFICITY: Detected at low levels in breast, lung and stomach; CC highly up-regulated in the corresponding cancerous tissues (at protein CC level). {ECO:0000269|PubMed:19106100}. CC -!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37312.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AK001001; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AK001001; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=BAA91751.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AY337596; AAQ92978.1; -; mRNA. DR EMBL; AF425650; AAO91864.1; -; mRNA. DR EMBL; AC007782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008814; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC124892; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471094; EAW96320.1; -; Genomic_DNA. DR EMBL; BC037312; AAH37312.1; ALT_SEQ; mRNA. DR EMBL; BC063855; AAH63855.1; -; mRNA. DR EMBL; AK001001; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK001550; BAA91751.1; ALT_INIT; mRNA. DR EMBL; AJ242978; CAB45135.1; -; mRNA. DR CCDS; CCDS66326.1; -. [Q6VMQ6-4] DR CCDS; CCDS66327.1; -. [Q6VMQ6-5] DR CCDS; CCDS73449.1; -. [Q6VMQ6-2] DR CCDS; CCDS8663.1; -. [Q6VMQ6-1] DR RefSeq; NP_001273443.1; NM_001286514.1. [Q6VMQ6-5] DR RefSeq; NP_001273444.1; NM_001286515.1. [Q6VMQ6-2] DR RefSeq; NP_060649.3; NM_018179.4. [Q6VMQ6-1] DR RefSeq; NP_851997.1; NM_181352.1. [Q6VMQ6-4] DR RefSeq; XP_006719171.1; XM_006719108.3. DR RefSeq; XP_006719172.1; XM_006719109.3. DR RefSeq; XP_011519056.1; XM_011520754.2. DR RefSeq; XP_011519057.1; XM_011520755.2. DR RefSeq; XP_016875127.1; XM_017019638.1. DR RefSeq; XP_016875128.1; XM_017019639.1. DR PDB; 2RPQ; NMR; -; B=938-981. DR PDBsum; 2RPQ; -. DR AlphaFoldDB; Q6VMQ6; -. DR SMR; Q6VMQ6; -. DR BioGRID; 120849; 79. DR CORUM; Q6VMQ6; -. DR IntAct; Q6VMQ6; 82. DR MINT; Q6VMQ6; -. DR STRING; 9606.ENSP00000440440; -. DR GlyCosmos; Q6VMQ6; 18 sites, 2 glycans. DR GlyGen; Q6VMQ6; 36 sites, 2 O-linked glycans (36 sites). DR iPTMnet; Q6VMQ6; -. DR PhosphoSitePlus; Q6VMQ6; -. DR BioMuta; ATF7IP; -. DR DMDM; 317373420; -. DR EPD; Q6VMQ6; -. DR jPOST; Q6VMQ6; -. DR MassIVE; Q6VMQ6; -. DR MaxQB; Q6VMQ6; -. DR PaxDb; 9606-ENSP00000440440; -. DR PeptideAtlas; Q6VMQ6; -. DR ProteomicsDB; 24334; -. DR ProteomicsDB; 32440; -. DR ProteomicsDB; 67728; -. [Q6VMQ6-1] DR ProteomicsDB; 67729; -. [Q6VMQ6-2] DR Pumba; Q6VMQ6; -. DR Antibodypedia; 12020; 112 antibodies from 20 providers. DR DNASU; 55729; -. DR Ensembl; ENST00000261168.9; ENSP00000261168.4; ENSG00000171681.13. [Q6VMQ6-1] DR Ensembl; ENST00000536444.5; ENSP00000445955.1; ENSG00000171681.13. [Q6VMQ6-5] DR Ensembl; ENST00000540793.5; ENSP00000444589.1; ENSG00000171681.13. [Q6VMQ6-1] DR Ensembl; ENST00000543189.5; ENSP00000443179.1; ENSG00000171681.13. [Q6VMQ6-2] DR Ensembl; ENST00000544627.5; ENSP00000440440.1; ENSG00000171681.13. [Q6VMQ6-4] DR GeneID; 55729; -. DR KEGG; hsa:55729; -. DR MANE-Select; ENST00000261168.9; ENSP00000261168.4; NM_018179.5; NP_060649.3. DR UCSC; uc001rbv.3; human. [Q6VMQ6-1] DR AGR; HGNC:20092; -. DR CTD; 55729; -. DR DisGeNET; 55729; -. DR GeneCards; ATF7IP; -. DR HGNC; HGNC:20092; ATF7IP. DR HPA; ENSG00000171681; Low tissue specificity. DR MIM; 613644; gene. DR neXtProt; NX_Q6VMQ6; -. DR OpenTargets; ENSG00000171681; -. DR VEuPathDB; HostDB:ENSG00000171681; -. DR eggNOG; ENOG502QSM2; Eukaryota. DR GeneTree; ENSGT00530000063707; -. DR HOGENOM; CLU_009529_0_0_1; -. DR InParanoid; Q6VMQ6; -. DR OMA; QETIHEP; -. DR OrthoDB; 4053704at2759; -. DR PhylomeDB; Q6VMQ6; -. DR TreeFam; TF329427; -. DR PathwayCommons; Q6VMQ6; -. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR SignaLink; Q6VMQ6; -. DR BioGRID-ORCS; 55729; 36 hits in 1175 CRISPR screens. DR ChiTaRS; ATF7IP; human. DR EvolutionaryTrace; Q6VMQ6; -. DR GeneWiki; ATF7IP; -. DR GenomeRNAi; 55729; -. DR Pharos; Q6VMQ6; Tbio. DR PRO; PR:Q6VMQ6; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q6VMQ6; Protein. DR Bgee; ENSG00000171681; Expressed in buccal mucosa cell and 208 other cell types or tissues. DR ExpressionAtlas; Q6VMQ6; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0006306; P:DNA methylation; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB. DR GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:UniProtKB. DR DisProt; DP01277; -. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR IDEAL; IID00216; -. DR InterPro; IPR026085; ATF7-int. DR InterPro; IPR031870; ATF7IP_BD. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23210; ACTIVATING TRANSCRIPTION FACTOR 7 INTERACTING PROTEIN; 1. DR PANTHER; PTHR23210:SF22; ACTIVATING TRANSCRIPTION FACTOR 7-INTERACTING PROTEIN 1; 1. DR Pfam; PF16788; ATF7IP_BD; 1. DR Pfam; PF16794; fn3_4; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR PROSITE; PS50853; FN3; 1. DR Genevisible; Q6VMQ6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil; KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..1270 FT /note="Activating transcription factor 7-interacting FT protein 1" FT /id="PRO_0000281780" FT DOMAIN 1160..1270 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 104..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 235..402 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 455..570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 562..817 FT /note="Interaction with SETDB1" FT REGION 658..685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 822..862 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 886..906 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 918..1026 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 965..975 FT /note="Interaction with SUMO" FT /evidence="ECO:0000269|PubMed:16757475" FT REGION 1115..1160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1154..1270 FT /note="Interaction with MBD1" FT COILED 617..665 FT /evidence="ECO:0000255" FT MOTIF 553..571 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 149..174 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 253..267 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 307..347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..377 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 541..570 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 822..836 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 918..966 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 982..1002 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1003..1017 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1132..1150 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 57 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569" FT MOD_RES 118 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 474 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 477 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 479 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TT18" FT MOD_RES 496 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 559 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 673 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 33 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 558 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 910 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 938 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MHQDQRFRM (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_055912" FT VAR_SEQ 520 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024035" FT VAR_SEQ 1095..1106 FT /note="VTVRVPQTTTYV -> KRFFLYMAPRYM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024038" FT VAR_SEQ 1107..1270 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024039" FT VARIANT 278 FT /note="E -> K (in dbSNP:rs2231908)" FT /id="VAR_031283" FT VARIANT 348 FT /note="N -> I (in dbSNP:rs2231909)" FT /evidence="ECO:0000269|PubMed:12665582" FT /id="VAR_031284" FT VARIANT 530 FT /note="K -> R (in dbSNP:rs3213764)" FT /evidence="ECO:0000269|PubMed:14536086, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_031285" FT MUTAGEN 968 FT /note="D->A: Abolishes the interaction with SUMO." FT /evidence="ECO:0000269|PubMed:16757475" FT MUTAGEN 969 FT /note="L->A: Abolishes the interaction with SUMO." FT /evidence="ECO:0000269|PubMed:16757475" FT MUTAGEN 1224 FT /note="L->R: Abolishes interaction with MBD1 and subsequent FT transcriptional repression." FT /evidence="ECO:0000269|PubMed:15691849" FT CONFLICT 457 FT /note="L -> V (in Ref. 5; AAH37312)" FT /evidence="ECO:0000305" FT CONFLICT 1182 FT /note="S -> G (in Ref. 1; AAQ92978 and 6; BAA91751)" FT /evidence="ECO:0000305" SQ SEQUENCE 1270 AA; 136394 MW; 96F6E4FBA1D79385 CRC64; MDSLEEPQKK VFKARKTMRV SDRQQLEAVY KVKEELLKTD VKLLNGNHEN GDLDPTSPLE NMDYIKDKEE VNGIEEICFD PEGSKAEWKE TPCILSVNVK NKQDDDLNCE PLSPHNITPE PVSKLPAEPV SGDPAPGDLD AGDPASGVLA SGDSTSGDPT SSEPSSSDAA SGDATSGDAP SGDVSPGDAT SGDATADDLS SGDPTSSDPI PGEPVPVEPI SGDCAADDIA SSEITSVDLA SGAPASTDPA SDDLASGDLS SSELASDDLA TGELASDELT SESTFDRTFE PKSVPVCEPV PEIDNIEPSS NKDDDFLEKN GADEKLEQIQ SKDSLDEKNK ADNNIDANEE TLETDDTTIC SDRPPENEKK VEEDIITELA LGEDAISSSM EIDQGEKNED ETSADLVETI NENVIEDNKS ENILENTDSM ETDEIIPILE KLAPSEDELT CFSKTSLLPI DETNPDLEEK MESSFGSPSK QESSESLPKE AFLVLSDEED ISGEKDESEV ISQNETCSPA EVESNEKDNK PEEEEQVIHE DDERPSEKNE FSRRKRSKSE DMDNVQSKRR RYMEEEYEAE FQVKITAKGD INQKLQKVIQ WLLEEKLCAL QCAVFDKTLA ELKTRVEKIE CNKRHKTVLT ELQAKIARLT KRFEAAKEDL KKRHEHPPNP PVSPGKTVND VNSNNNMSYR NAGTVRQMLE SKRNVSESAP PSFQTPVNTV SSTNLVTPPA VVSSQPKLQT PVTSGSLTAT SVLPAPNTAT VVATTQVPSG NPQPTISLQP LPVILHVPVA VSSQPQLLQS HPGTLVTNQP SGNVEFISVQ SPPTVSGLTK NPVSLPSLPN PTKPNNVPSV PSPSIQRNPT ASAAPLGTTL AVQAVPTAHS IVQATRTSLP TVGPSGLYSP STNRGPIQMK IPISAFSTSS AAEQNSNTTP RIENQTNKTI DASVSKKAAD STSQCGKATG SDSSGVIDLT MDDEESGASQ DPKKLNHTPV STMSSSQPVS RPLQPIQPAP PLQPSGVPTS GPSQTTIHLL PTAPTTVNVT HRPVTQVTTR LPVPRAPANH QVVYTTLPAP PAQAPLRGTV MQAPAVRQVN PQNSVTVRVP QTTTYVVNNG LTLGSTGPQL TVHHRPPQVH TEPPRPVHPA PLPEAPQPQR LPPEAASTSL PQKPHLKLAR VQSQNGIVLS WSVLEVDRSC ATVDSYHLYA YHEEPSATVP SQWKKIGEVK ALPLPMACTL TQFVSGSKYY FAVRAKDIYG RFGPFCDPQS TDVISSTQSS //