MCAF1_HUMAN
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 03-AUG-2022, entry version 166.
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};
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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. [Q6VMQ6-1]
DR RefSeq; XP_006719172.1; XM_006719109.3. [Q6VMQ6-1]
DR RefSeq; XP_011519056.1; XM_011520754.2. [Q6VMQ6-1]
DR RefSeq; XP_011519057.1; XM_011520755.2. [Q6VMQ6-1]
DR RefSeq; XP_016875127.1; XM_017019638.1. [Q6VMQ6-1]
DR RefSeq; XP_016875128.1; XM_017019639.1. [Q6VMQ6-5]
DR PDB; 2RPQ; NMR; -; B=938-981.
DR PDBsum; 2RPQ; -.
DR AlphaFoldDB; Q6VMQ6; -.
DR SMR; Q6VMQ6; -.
DR BioGRID; 120849; 73.
DR CORUM; Q6VMQ6; -.
DR IntAct; Q6VMQ6; 82.
DR MINT; Q6VMQ6; -.
DR STRING; 9606.ENSP00000440440; -.
DR GlyGen; Q6VMQ6; 18 sites, 2 O-linked glycans (18 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; Q6VMQ6; -.
DR PeptideAtlas; Q6VMQ6; -.
DR PRIDE; Q6VMQ6; -.
DR ProteomicsDB; 24334; -.
DR ProteomicsDB; 32440; -.
DR ProteomicsDB; 67728; -. [Q6VMQ6-1]
DR ProteomicsDB; 67729; -. [Q6VMQ6-2]
DR Antibodypedia; 12020; 96 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 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; VRASPMQ; -.
DR OrthoDB; 324622at2759; -.
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; 31 hits in 1094 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 206 other tissues.
DR ExpressionAtlas; Q6VMQ6; baseline and differential.
DR Genevisible; Q6VMQ6; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR DisProt; DP01277; -.
DR Gene3D; 2.60.40.10; -; 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; PTHR23210; 1.
DR Pfam; PF16788; ATF7IP_BD; 1.
DR Pfam; PF16794; fn3_4; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
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
