CITE4_MOUSE
ID CITE4_MOUSE Reviewed; 182 AA.
AC Q9WUL8; Q66JX0; Q8R176; Q9CZV4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cbp/p300-interacting transactivator 4;
DE AltName: Full=MSG1-related protein 2;
DE Short=MRG-2;
GN Name=Cited4 {ECO:0000312|MGI:MGI:1861694};
GN Synonyms=Mrg2 {ECO:0000312|EMBL:AAD37357.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD37357.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CREBBP;
RP EP300 AND TFAP2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAD37357.1};
RX PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S.,
RA Shioda T.;
RT "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding
RT transcriptional coactivators: induced expression in mammary epithelial
RT cells.";
RL Genomics 80:601-613(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE32327.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28054.1}, and
RC NOD {ECO:0000312|EMBL:BAE32327.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB28054.1}, and
RC Thymus {ECO:0000312|EMBL:BAE32327.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH25116.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=NMRI {ECO:0000312|EMBL:AAH80723.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH25116.1};
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 FUNCTION.
RX PubMed=11581164; DOI=10.1101/gad.906301;
RA Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S.,
RA Isselbacher K.J., Brown M., Shioda T.;
RT "Selective coactivation of estrogen-dependent transcription by CITED1
RT CBP/p300-binding protein.";
RL Genes Dev. 15:2598-2612(2001).
CC -!- FUNCTION: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances
CC estrogen-dependent transactivation mediated by estrogen receptors. May
CC function as an inhibitor of transactivation by HIF1A by disrupting
CC HIF1A interaction with CREBBP. May be involved in regulation of gene
CC expression during development and differentiation of blood cells,
CC endothelial cells and mammary epithelial cells.
CC {ECO:0000269|PubMed:11581164, ECO:0000269|PubMed:12504852}.
CC -!- SUBUNIT: Interacts via its C-terminal region with the CH1 domain of
CC CREBBP and EP300. Interacts with all TFAP2/AP-2 isoforms.
CC {ECO:0000250|UniProtKB:Q96RK1, ECO:0000269|PubMed:12504852}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96RK1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12504852};
CC IsoId=Q9WUL8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9WUL8-2; Sequence=VSP_052035;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9WUL8-3; Sequence=VSP_052036;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, spleen and testis, and
CC weakly in liver and kidney. {ECO:0000269|PubMed:12504852}.
CC -!- DEVELOPMENTAL STAGE: Undetectable in nulliparous mammary glands but
CC strongly expressed in 11.5 dpc pregnant mammary glands. Strong
CC expression continued until the end of the lactacting stage and then
CC rapidly diminished during the weaning stage.
CC {ECO:0000269|PubMed:12504852}.
CC -!- SIMILARITY: Belongs to the CITED family. {ECO:0000255}.
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DR EMBL; AF143369; AAD37357.1; -; mRNA.
DR EMBL; AK012136; BAB28054.1; -; mRNA.
DR EMBL; AK154030; BAE32327.1; -; mRNA.
DR EMBL; BC025116; AAH25116.1; -; mRNA.
DR EMBL; BC080723; AAH80723.1; -; mRNA.
DR CCDS; CCDS18592.1; -. [Q9WUL8-1]
DR RefSeq; NP_062509.1; NM_019563.2. [Q9WUL8-1]
DR AlphaFoldDB; Q9WUL8; -.
DR BioGRID; 207856; 15.
DR IntAct; Q9WUL8; 14.
DR STRING; 10090.ENSMUSP00000092408; -.
DR PaxDb; Q9WUL8; -.
DR PRIDE; Q9WUL8; -.
DR Antibodypedia; 32148; 144 antibodies from 24 providers.
DR DNASU; 56222; -.
DR Ensembl; ENSMUST00000094814; ENSMUSP00000092408; ENSMUSG00000070803. [Q9WUL8-1]
DR GeneID; 56222; -.
DR KEGG; mmu:56222; -.
DR UCSC; uc008unl.1; mouse. [Q9WUL8-1]
DR CTD; 163732; -.
DR MGI; MGI:1861694; Cited4.
DR VEuPathDB; HostDB:ENSMUSG00000070803; -.
DR eggNOG; ENOG502QQEE; Eukaryota.
DR GeneTree; ENSGT00530000063624; -.
DR HOGENOM; CLU_128809_0_0_1; -.
DR InParanoid; Q9WUL8; -.
DR OMA; GPHALWT; -.
DR PhylomeDB; Q9WUL8; -.
DR TreeFam; TF331915; -.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR BioGRID-ORCS; 56222; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Cited4; mouse.
DR PRO; PR:Q9WUL8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WUL8; protein.
DR Bgee; ENSMUSG00000070803; Expressed in parotid gland and 107 other tissues.
DR ExpressionAtlas; Q9WUL8; baseline and differential.
DR Genevisible; Q9WUL8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR InterPro; IPR007576; CITED.
DR PANTHER; PTHR17045; PTHR17045; 1.
DR Pfam; PF04487; CITED; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..182
FT /note="Cbp/p300-interacting transactivator 4"
FT /id="PRO_0000233310"
FT REGION 22..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052036"
FT VAR_SEQ 17..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052035"
FT CONFLICT 117
FT /note="S -> W (in Ref. 2; BAB28054)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="P -> R (in Ref. 2; BAB28054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 18398 MW; C819C70AFD82043C CRC64;
MADHLMLAEG YCLLQVPPHT HGPHAPRTLQ PYAGPGMDSG LRPRGAPLGP PPPPGTLAYG
SFGSPVSFQP FPVSQSPGAG STHLQSAATP SPGRIPAPPA AAGGPSPLQP APGAAASLPP
PPPPPALGCM DTELIDEEAL TSLELELGLH RVRELPELFL GQSEFDCFSD LGSAPAAGSV
SC
