ID Q99L86_MOUSE Unreviewed; 490 AA. AC Q99L86; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 03-MAY-2023, entry version 126. DE RecName: Full=Protein Mdm4 {ECO:0000256|PIRNR:PIRNR006748}; GN Name=Mdm4 {ECO:0000313|EMBL:AAH03750.1, ECO:0000313|MGI:MGI:107934}; 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 {ECO:0000313|EMBL:AAH03750.1}; RN [1] {ECO:0000313|EMBL:AAH03750.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH03750.1}; RC TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old RC virgin mouse. Taken by biopsy. {ECO:0000313|EMBL:AAH03750.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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). CC -!- FUNCTION: Inhibits p53- and p73-mediated cell cycle arrest and CC apoptosis by binding its transcriptional activation domain. CC {ECO:0000256|PIRNR:PIRNR006748}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PIRNR:PIRNR006748}. CC -!- SIMILARITY: Belongs to the MDM2/MDM4 family. CC {ECO:0000256|ARBA:ARBA00005803, ECO:0000256|PIRNR:PIRNR006748}. 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; BC003750; AAH03750.1; -; mRNA. DR AlphaFoldDB; Q99L86; -. DR AGR; MGI:107934; -. DR MGI; MGI:107934; Mdm4. DR ChiTaRS; Mdm4; mouse. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro. DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt. DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro. DR CDD; cd17673; MDM4; 1. DR CDD; cd16784; mRING-HC-C2H2C4_MDM4; 1. DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1. DR InterPro; IPR015458; MDM4. DR InterPro; IPR016495; p53_neg-reg_MDM_2/4. DR InterPro; IPR036885; SWIB_MDM2_dom_sf. DR InterPro; IPR003121; SWIB_MDM2_domain. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12183; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1. DR PANTHER; PTHR12183:SF37; PROTEIN MDM4; 1. DR Pfam; PF02201; SWIB; 1. DR Pfam; PF13920; zf-C3HC4_3; 1. DR Pfam; PF00641; zf-RanBP; 1. DR PIRSF; PIRSF500699; MDM4; 1. DR PIRSF; PIRSF006748; p53_MDM_2/4; 1. DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1. DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1. DR PROSITE; PS51925; SWIB_MDM2; 1. DR PROSITE; PS01358; ZF_RANBP2_1; 1. DR PROSITE; PS50199; ZF_RANBP2_2; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR006748}; Nucleus {ECO:0000256|PIRNR:PIRNR006748}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006748}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00322}. FT DOMAIN 23..109 FT /note="DM2" FT /evidence="ECO:0000259|PROSITE:PS51925" FT DOMAIN 300..329 FT /note="RanBP2-type" FT /evidence="ECO:0000259|PROSITE:PS50199" FT DOMAIN 437..478 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 132..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 490 AA; 55120 MW; 58B171C5B8C37577 CRC64; MTSHSTSAQC SASDSACRIS SEQISQQVRP KLQLLKILHA AGAQGEVFTM KEVMHYLGQY IMVKQLYDQQ EQHMVYCGGD LLGDLLGCQS FSVKDPSPLY DMLRKNLVTS ASNNTDAAQT LALAQDHTMD FPSQDRLKHG ATEYSNPRKR TEEEDTHTLP TSRHKCRDSR ADEDLIEHLS QDETSRLDLD FEEWDVAGLP WWFLGNLRNN CIPKSNGSTD LQTNQDIGTA IVSDTTDDLW FLNETVSEQL GVGIKVEAAN SEQTSEVGKT SNKKTVEVGK DDDLEDSRSL SDDTDVELTS EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSNITAIP EKKDNEGIDV PDCRRTISAP VVRPKDGYLK EEKPRFDPCN SVGFLDLAHS SESQEIISSA REQTDIFSEQ KAETESMEDF QNVLKPCSLC EKRPRDGNII HGKTSHLTTC FHCARRLKKS GASCPVCKKE IQLVIKVFIA //