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Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621)

 MCAF1_HUMAN             Reviewed;        1270 AA.
Q6VMQ6; F5GX74; G3V1U0; Q4G0T9; Q6P3T3; Q86XW5; Q9NVJ9; Q9NWC2;
Q9Y4X8;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
25-OCT-2017, entry version 135.
RecName: Full=Activating transcription factor 7-interacting protein 1;
AltName: Full=ATF-interacting protein;
Short=ATF-IP;
AltName: Full=ATF7-interacting protein;
AltName: Full=ATFa-associated modulator;
Short=hAM;
AltName: Full=MBD1-containing chromatin-associated factor 1;
AltName: Full=P621;
Name=ATF7IP; Synonyms=MCAF, MCAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, INTERACTION WITH SETDB1, AND VARIANT ARG-530.
PubMed=14536086; DOI=10.1016/j.molcel.2003.08.007;
Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B.,
Tempst P., Roeder R.G., Zhang Y.;
"mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9
of histone H3 to cause transcriptional repression.";
Mol. Cell 12:475-487(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
MBD1, AND VARIANT ILE-348.
PubMed=12665582; DOI=10.1128/MCB.23.8.2834-2843.2003;
Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H.,
Nakao M.;
"MCAF mediates MBD1-dependent transcriptional repression.";
Mol. Cell. Biol. 23:2834-2843(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-513, AND VARIANT ARG-530.
TISSUE=Brain, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 479-1270 AND 479-1270
(ISOFORM 1), AND VARIANT ARG-530.
TISSUE=Embryo, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 545-1058 (ISOFORM 1), AND INTERACTION
WITH SP1.
TISSUE=Colon;
PubMed=10976766; DOI=10.1023/A:1007177623283;
Gunther M., Laithier M., Brison O.;
"A set of proteins interacting with transcription factor Sp1
identified in a two-hybrid screening.";
Mol. Cell. Biochem. 210:131-142(2000).
[8]
INTERACTION WITH ZHX1.
PubMed=12659632; DOI=10.1042/BJ20021866;
Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T.,
Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.;
"Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins:
molecular cloning and characterization of a member of the ZHX family,
ZHX3.";
Biochem. J. 373:167-178(2003).
[9]
INTERACTION WITH SETDB1; MBD1 AND SP1, AND MUTAGENESIS OF LEU-1224.
PubMed=15691849; DOI=10.1074/jbc.M413654200;
Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.;
"Transcriptional repression and heterochromatin formation by MBD1 and
MCAF/AM family proteins.";
J. Biol. Chem. 280:13928-13935(2005).
[10]
INTERACTION WITH EBV VIRUS BRLF1.
PubMed=16314315; DOI=10.1093/nar/gki956;
Chang L.-K., Chung J.-Y., Hong Y.-R., Ichimura T., Nakao M.,
Liu S.-T.;
"Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus
via an interaction with MCAF1.";
Nucleic Acids Res. 33:6528-6539(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-673, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
INTERACTION WITH SUMO AND MBD1, AND MUTAGENESIS OF ASP-968 AND
LEU-969.
PubMed=16757475; DOI=10.1074/jbc.M602280200;
Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S.,
Nakao M., Saitoh H.;
"Involvement of SUMO modification in MBD1- and MCAF1-mediated
heterochromatin formation.";
J. Biol. Chem. 281:23180-23190(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-118; SER-473
AND SER-899, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
FUNCTION, INTERACTION WITH ERCC2; ERCC3; GTF2E1; GTF2E2; POLR2A AND
SP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-496; SER-559
AND SER-673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-445; SER-474;
SER-477 AND SER-899, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-496; SER-559
AND SER-673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-558; LYS-910 AND
LYS-938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
STRUCTURE BY NMR OF 938-981 IN COMPLEX WITH SUMO3.
PubMed=18842587; DOI=10.1074/jbc.M802528200;
Sekiyama N., Ikegami T., Yamane T., Ikeguchi M., Uchimura Y., Baba D.,
Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.;
"Structure of the small ubiquitin-like modifier (SUMO)-interacting
motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-
3.";
J. Biol. Chem. 283:35966-35975(2008).
-!- FUNCTION: Recruiter that couples transcriptional factors to
general transcription apparatus and thereby modulates
transcription regulation and chromatin formation. Can both act as
an activator or a repressor depending on the context. Mediates
MBD1-dependent transcriptional repression, probably by recruiting
complexes containing SETDB1. Required to stimulate histone
methyltransferase activity of SETDB1 and facilitate the conversion
of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex
formed with MBD1 and SETDB1 represses transcription and couples
DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3).
Facilitates telomerase TERT and TERC gene expression by SP1 in
cancer cells. {ECO:0000269|PubMed:12665582,
ECO:0000269|PubMed:14536086, ECO:0000269|PubMed:19106100}.
-!- SUBUNIT: Interacts with MBD1; the interaction is enhanced when
MBD1 is sumoylated. Probably forms a complex with SETDB1 and MBD1.
Interacts with SUMO ubiquitin-like proteins (SUMO1, SUNO2 and
SUMO3), with a preference for SUMO2 and SUMO3. Interacts with SP1,
ATF7 and ZHX1. Interacts with the general transcription machinery,
including ERCC2, ERCC3, GTF2E1, GTF2E2 and POLR2A. Interacts with
Epstein-Barr virus BRLF1/Rta protein, leading to promote and
regulate host genes in Epstein-Barr virus-infected cells.
{ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:12659632,
ECO:0000269|PubMed:12665582, ECO:0000269|PubMed:14536086,
ECO:0000269|PubMed:15691849, ECO:0000269|PubMed:16314315,
ECO:0000269|PubMed:16757475, ECO:0000269|PubMed:18842587,
ECO:0000269|PubMed:19106100}.
-!- INTERACTION:
Q9NRI5:DISC1; NbExp=3; IntAct=EBI-928732, EBI-529989;
Q9UHL9:GTF2IRD1; NbExp=3; IntAct=EBI-928732, EBI-372530;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19106100}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6VMQ6-1; Sequence=Displayed;
Name=2;
IsoId=Q6VMQ6-2; Sequence=VSP_024035, VSP_024038, VSP_024039;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6VMQ6-4; Sequence=VSP_055912;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=4;
IsoId=Q6VMQ6-5; Sequence=VSP_024035;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Detected at low levels in breast, lung and
stomach; highly up-regulated in the corresponding cancerous
tissues (at protein level). {ECO:0000269|PubMed:19106100}.
-!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37312.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AK001001; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AK001001; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAA91751.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY337596; AAQ92978.1; -; mRNA.
EMBL; AF425650; AAO91864.1; -; mRNA.
EMBL; AC007782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96320.1; -; Genomic_DNA.
EMBL; BC037312; AAH37312.1; ALT_SEQ; mRNA.
EMBL; BC063855; AAH63855.1; -; mRNA.
EMBL; AK001001; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK001550; BAA91751.1; ALT_INIT; mRNA.
EMBL; AJ242978; CAB45135.1; -; mRNA.
CCDS; CCDS66326.1; -. [Q6VMQ6-4]
CCDS; CCDS66327.1; -. [Q6VMQ6-5]
CCDS; CCDS73449.1; -. [Q6VMQ6-2]
CCDS; CCDS8663.1; -. [Q6VMQ6-1]
RefSeq; NP_001273443.1; NM_001286514.1. [Q6VMQ6-5]
RefSeq; NP_001273444.1; NM_001286515.1. [Q6VMQ6-2]
RefSeq; NP_060649.3; NM_018179.4. [Q6VMQ6-1]
RefSeq; NP_851997.1; NM_181352.1. [Q6VMQ6-4]
RefSeq; XP_006719171.1; XM_006719108.3. [Q6VMQ6-1]
RefSeq; XP_006719172.1; XM_006719109.3. [Q6VMQ6-1]
RefSeq; XP_011519056.1; XM_011520754.2. [Q6VMQ6-1]
RefSeq; XP_011519057.1; XM_011520755.2. [Q6VMQ6-1]
RefSeq; XP_016875127.1; XM_017019638.1. [Q6VMQ6-1]
RefSeq; XP_016875128.1; XM_017019639.1. [Q6VMQ6-5]
UniGene; Hs.504856; -.
UniGene; Hs.591151; -.
PDB; 2RPQ; NMR; -; B=938-981.
PDBsum; 2RPQ; -.
ProteinModelPortal; Q6VMQ6; -.
SMR; Q6VMQ6; -.
BioGrid; 120849; 38.
CORUM; Q6VMQ6; -.
IntAct; Q6VMQ6; 59.
MINT; MINT-1179935; -.
STRING; 9606.ENSP00000261168; -.
iPTMnet; Q6VMQ6; -.
PhosphoSitePlus; Q6VMQ6; -.
BioMuta; ATF7IP; -.
DMDM; 317373420; -.
EPD; Q6VMQ6; -.
MaxQB; Q6VMQ6; -.
PaxDb; Q6VMQ6; -.
PeptideAtlas; Q6VMQ6; -.
PRIDE; Q6VMQ6; -.
Ensembl; ENST00000261168; ENSP00000261168; ENSG00000171681. [Q6VMQ6-1]
Ensembl; ENST00000536444; ENSP00000445955; ENSG00000171681. [Q6VMQ6-5]
Ensembl; ENST00000540793; ENSP00000444589; ENSG00000171681. [Q6VMQ6-1]
Ensembl; ENST00000543189; ENSP00000443179; ENSG00000171681. [Q6VMQ6-2]
Ensembl; ENST00000544627; ENSP00000440440; ENSG00000171681. [Q6VMQ6-4]
GeneID; 55729; -.
KEGG; hsa:55729; -.
UCSC; uc001rbv.3; human. [Q6VMQ6-1]
CTD; 55729; -.
DisGeNET; 55729; -.
EuPathDB; HostDB:ENSG00000171681.12; -.
GeneCards; ATF7IP; -.
H-InvDB; HIX0010453; -.
HGNC; HGNC:20092; ATF7IP.
HPA; HPA016578; -.
HPA; HPA023505; -.
MIM; 613644; gene.
neXtProt; NX_Q6VMQ6; -.
OpenTargets; ENSG00000171681; -.
eggNOG; ENOG410IJ5P; Eukaryota.
eggNOG; ENOG410XUWA; LUCA.
GeneTree; ENSGT00530000063707; -.
HOVERGEN; HBG087180; -.
InParanoid; Q6VMQ6; -.
OMA; VRQVNPQ; -.
OrthoDB; EOG091G058O; -.
PhylomeDB; Q6VMQ6; -.
TreeFam; TF329427; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
ChiTaRS; ATF7IP; human.
EvolutionaryTrace; Q6VMQ6; -.
GeneWiki; ATF7IP; -.
GenomeRNAi; 55729; -.
PRO; PR:Q6VMQ6; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000171681; -.
CleanEx; HS_ATF7IP; -.
ExpressionAtlas; Q6VMQ6; baseline and differential.
Genevisible; Q6VMQ6; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0016887; F:ATPase activity; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045898; P:regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR026085; ATF7-int.
InterPro; IPR031870; ATF7IP_BD.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
PANTHER; PTHR23210; PTHR23210; 1.
Pfam; PF16788; ATF7IP_BD; 1.
Pfam; PF16794; fn3_4; 1.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Coiled coil; Complete proteome; Host-virus interaction;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 1270 Activating transcription factor 7-
interacting protein 1.
/FTId=PRO_0000281780.
DOMAIN 1160 1270 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 562 817 Interaction with SETDB1.
REGION 965 975 Interaction with SUMO.
{ECO:0000269|PubMed:16757475}.
REGION 1154 1270 Interaction with MBD1.
COILED 617 665 {ECO:0000255}.
MOTIF 553 571 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 349 580 Glu-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 118 118 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TT18}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 899 899 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 910 910 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 938 938 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MHQDQRFRM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_055912.
VAR_SEQ 520 520 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024035.
VAR_SEQ 1095 1106 VTVRVPQTTTYV -> KRFFLYMAPRYM (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_024038.
VAR_SEQ 1107 1270 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024039.
VARIANT 278 278 E -> K (in dbSNP:rs2231908).
/FTId=VAR_031283.
VARIANT 348 348 N -> I (in dbSNP:rs2231909).
{ECO:0000269|PubMed:12665582}.
/FTId=VAR_031284.
VARIANT 530 530 K -> R (in dbSNP:rs3213764).
{ECO:0000269|PubMed:14536086,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_031285.
MUTAGEN 968 968 D->A: Abolishes the interaction with
SUMO. {ECO:0000269|PubMed:16757475}.
MUTAGEN 969 969 L->A: Abolishes the interaction with
SUMO. {ECO:0000269|PubMed:16757475}.
MUTAGEN 1224 1224 L->R: Abolishes interaction with MBD1 and
subsequent transcriptional repression.
{ECO:0000269|PubMed:15691849}.
CONFLICT 457 457 L -> V (in Ref. 5; AAH37312).
{ECO:0000305}.
CONFLICT 1182 1182 S -> G (in Ref. 1; AAQ92978 and 6;
BAA91751). {ECO:0000305}.
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


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