MCAF2_HUMAN
ID MCAF2_HUMAN Reviewed; 682 AA.
AC Q5U623; B2RNR2; Q53EZ7; Q658U2; Q6IS97; Q8N9X8; Q9H9L6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Activating transcription factor 7-interacting protein 2;
DE Short=ATF7-interacting protein 2;
DE AltName: Full=MBD1-containing chromatin-associated factor 2;
GN Name=ATF7IP2; Synonyms=MCAF2;
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).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 339-682 (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-398 (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 324-681 (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-488 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
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. Mediates MBD1-dependent transcriptional
CC repression, probably by recruiting complexes containing SETDB1. The
CC complex formed with MBD1 and SETDB1 represses transcription and
CC probably couples DNA methylation and histone H3 'Lys-9' trimethylation
CC (H3K9me3) activity (Probable). {ECO:0000305}.
CC -!- SUBUNIT: Interacts with MBD1, SETDB1 and SP1. Probably forms a complex
CC with SETDB1 and MBD1.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U623-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U623-2; Sequence=VSP_024042, VSP_024043;
CC -!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY560615; AAT66299.1; -; mRNA.
DR EMBL; AK022730; BAB14209.1; ALT_INIT; mRNA.
DR EMBL; AK093414; BAC04157.1; -; mRNA.
DR EMBL; BC033891; AAH33891.1; -; mRNA.
DR EMBL; BC069713; AAH69713.1; -; mRNA.
DR EMBL; BC069730; AAH69730.1; -; mRNA.
DR EMBL; BC069695; AAH69695.1; -; mRNA.
DR EMBL; BC137079; AAI37080.1; -; mRNA.
DR EMBL; AL832987; CAH56323.1; -; mRNA.
DR EMBL; AK223492; BAD97212.1; -; mRNA.
DR CCDS; CCDS10540.1; -. [Q5U623-1]
DR CCDS; CCDS58422.1; -. [Q5U623-2]
DR RefSeq; NP_001243089.1; NM_001256160.1. [Q5U623-2]
DR RefSeq; NP_079273.2; NM_024997.3. [Q5U623-1]
DR RefSeq; XP_006721016.1; XM_006720953.3. [Q5U623-1]
DR RefSeq; XP_016879194.1; XM_017023705.1. [Q5U623-1]
DR RefSeq; XP_016879195.1; XM_017023706.1. [Q5U623-2]
DR AlphaFoldDB; Q5U623; -.
DR BioGRID; 123097; 36.
DR CORUM; Q5U623; -.
DR IntAct; Q5U623; 5.
DR STRING; 9606.ENSP00000379808; -.
DR iPTMnet; Q5U623; -.
DR PhosphoSitePlus; Q5U623; -.
DR BioMuta; ATF7IP2; -.
DR DMDM; 143352739; -.
DR EPD; Q5U623; -.
DR jPOST; Q5U623; -.
DR MassIVE; Q5U623; -.
DR PaxDb; Q5U623; -.
DR PeptideAtlas; Q5U623; -.
DR PRIDE; Q5U623; -.
DR ProteomicsDB; 65237; -. [Q5U623-1]
DR ProteomicsDB; 65238; -. [Q5U623-2]
DR Antibodypedia; 52153; 88 antibodies from 17 providers.
DR DNASU; 80063; -.
DR Ensembl; ENST00000324570.9; ENSP00000322811.5; ENSG00000166669.14. [Q5U623-2]
DR Ensembl; ENST00000356427.2; ENSP00000348799.2; ENSG00000166669.14. [Q5U623-1]
DR Ensembl; ENST00000396559.5; ENSP00000379807.1; ENSG00000166669.14. [Q5U623-2]
DR Ensembl; ENST00000396560.6; ENSP00000379808.2; ENSG00000166669.14. [Q5U623-1]
DR Ensembl; ENST00000562102.6; ENSP00000457731.2; ENSG00000166669.14. [Q5U623-1]
DR GeneID; 80063; -.
DR KEGG; hsa:80063; -.
DR MANE-Select; ENST00000562102.6; ENSP00000457731.2; NM_001393719.1; NP_001380648.1.
DR UCSC; uc002czu.3; human. [Q5U623-1]
DR CTD; 80063; -.
DR DisGeNET; 80063; -.
DR GeneCards; ATF7IP2; -.
DR HGNC; HGNC:20397; ATF7IP2.
DR HPA; ENSG00000166669; Tissue enhanced (testis).
DR MIM; 613645; gene.
DR neXtProt; NX_Q5U623; -.
DR OpenTargets; ENSG00000166669; -.
DR PharmGKB; PA134988230; -.
DR VEuPathDB; HostDB:ENSG00000166669; -.
DR eggNOG; ENOG502S2DM; Eukaryota.
DR GeneTree; ENSGT00530000063707; -.
DR HOGENOM; CLU_025197_1_0_1; -.
DR InParanoid; Q5U623; -.
DR OMA; CHENPSN; -.
DR OrthoDB; 324622at2759; -.
DR PhylomeDB; Q5U623; -.
DR TreeFam; TF329427; -.
DR PathwayCommons; Q5U623; -.
DR SignaLink; Q5U623; -.
DR BioGRID-ORCS; 80063; 13 hits in 1083 CRISPR screens.
DR ChiTaRS; ATF7IP2; human.
DR GenomeRNAi; 80063; -.
DR Pharos; Q5U623; Tdark.
DR PRO; PR:Q5U623; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q5U623; protein.
DR Bgee; ENSG00000166669; Expressed in right testis and 176 other tissues.
DR ExpressionAtlas; Q5U623; baseline and differential.
DR Genevisible; Q5U623; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR026085; ATF7-int.
DR InterPro; IPR026089; ATF7-int_2.
DR InterPro; IPR031870; ATF7IP_BD.
DR InterPro; IPR003961; FN3_dom.
DR PANTHER; PTHR23210; PTHR23210; 1.
DR PANTHER; PTHR23210:SF23; PTHR23210:SF23; 1.
DR Pfam; PF16788; ATF7IP_BD; 1.
DR Pfam; PF16794; fn3_4; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..682
FT /note="Activating transcription factor 7-interacting
FT protein 2"
FT /id="PRO_0000281784"
FT DOMAIN 575..680
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 120..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..378
FT /evidence="ECO:0000255"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 495..543
FT /note="AVQKKLDSIIDLTKEGLSNCNTESPVSPLESHSKAASNSKETTPLAQNA ->
FT KVQYPPWSHIRKLLQTQRKQPHWHKMQSRFLSPLSTCHLSQNHQHHYLN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024042"
FT VAR_SEQ 544..682
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024043"
FT VARIANT 527
FT /note="S -> L (in dbSNP:rs34834862)"
FT /id="VAR_053872"
FT VARIANT 537
FT /note="T -> I (in dbSNP:rs9932051)"
FT /id="VAR_031286"
FT VARIANT 543
FT /note="A -> T (in dbSNP:rs9931441)"
FT /id="VAR_031287"
FT CONFLICT 61
FT /note="Missing (in Ref. 1; AAT66299 and 3; AAH33891)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="I -> T (in Ref. 2; BAB14209)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="P -> L (in Ref. 5; BAD97212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 75764 MW; 2FF5417BB7058E31 CRC64;
MASPDRSKRK ILKAKKTMPL SCRKQVEMLN KSRNVEALKT AIGSNVPSGN QSFSPSVITR
TTEITKCSPS ENGASSLDSN KNSISEKSKV FSQNCIKPVE EIVHSETKLE QVVCSYQKPS
RTTESPSRVF TEEAKDSLNT SENDSEHQTN VTRSLFEHEG ACSLKSSCCP PSVLSGVVQM
PESTVTSTVG DKKTDQMVFH LETNSNSESH DKRQSDNILC SEDSGFVPVE KTPNLVNSVT
SNNCADDILK TDECSRTSIS NCESADSTWQ SSLDTNNNSH YQKKRMFSEN EENVKRMKTS
EQINENICVS LERQTAFLEQ VRHLIQQEIY SINYELFDKK LKELNQRIGK TECRNKHEGI
ADKLLAKIAK LQRRIKTVLL FQRNCLKPNM LSSNGASKVA NSEAMILDKN LESVNSPIEK
SSVNYEPSNP SEKGSKKINL SSDQNKSVSE SNNDDVMLIS VESPNLTTPI TSNPTDTRKI
TSGNSSNSPN AEVMAVQKKL DSIIDLTKEG LSNCNTESPV SPLESHSKAA SNSKETTPLA
QNAVQVPESF EHLPPLPEPP APLPELVDKT RDTLPPQKPE LKVKRVFRPN GIALTWNITK
INPKCAPVES YHLFLCHENS NNKLIWKKIG EIKALPLPMA CTLSQFLASN RYYFTVQSKD
IFGRYGPFCD IKSIPGFSEN LT
