NACC2_MOUSE
ID NACC2_MOUSE Reviewed; 586 AA.
AC Q9DCM7; Q3TZD3; Q8VDF8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nucleus accumbens-associated protein 2;
DE Short=NAC-2;
DE AltName: Full=BTB/POZ domain-containing protein 14A;
GN Name=Nacc2; Synonyms=Btbd14a;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: Functions as a transcriptional repressor through its
CC association with the NuRD complex. Recruits the NuRD complex to the
CC promoter of MDM2, leading to the repression of MDM2 transcription and
CC subsequent stability of p53/TP53 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; mediated by the BTB domain. Interacts with the
CC NuRD complex. Interacts (via C-terminal part) with HDAC2. Interacts
CC (via BTB domain) with MTA1, MTA2 and MTA3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Predominantly associated with
CC chromatin. {ECO:0000250}.
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DR EMBL; AK002651; BAB22259.1; -; mRNA.
DR EMBL; AK147293; BAE27827.1; -; mRNA.
DR EMBL; AK147310; BAE27838.1; -; mRNA.
DR EMBL; AK157946; BAE34276.1; -; mRNA.
DR EMBL; BC022103; AAH22103.1; -; mRNA.
DR CCDS; CCDS15796.1; -.
DR RefSeq; NP_001032175.1; NM_001037098.1.
DR RefSeq; NP_080771.3; NM_026495.3.
DR AlphaFoldDB; Q9DCM7; -.
DR SMR; Q9DCM7; -.
DR BioGRID; 212585; 1.
DR STRING; 10090.ENSMUSP00000109796; -.
DR iPTMnet; Q9DCM7; -.
DR PhosphoSitePlus; Q9DCM7; -.
DR MaxQB; Q9DCM7; -.
DR PaxDb; Q9DCM7; -.
DR PeptideAtlas; Q9DCM7; -.
DR PRIDE; Q9DCM7; -.
DR ProteomicsDB; 287345; -.
DR TopDownProteomics; Q9DCM7; -.
DR Antibodypedia; 18675; 119 antibodies from 21 providers.
DR Ensembl; ENSMUST00000028300; ENSMUSP00000028300; ENSMUSG00000026932.
DR Ensembl; ENSMUST00000114159; ENSMUSP00000109796; ENSMUSG00000026932.
DR GeneID; 67991; -.
DR KEGG; mmu:67991; -.
DR UCSC; uc008iub.1; mouse.
DR CTD; 138151; -.
DR MGI; MGI:1915241; Nacc2.
DR VEuPathDB; HostDB:ENSMUSG00000026932; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159244; -.
DR HOGENOM; CLU_029038_1_0_1; -.
DR InParanoid; Q9DCM7; -.
DR OMA; RVSYYGM; -.
DR OrthoDB; 567120at2759; -.
DR PhylomeDB; Q9DCM7; -.
DR TreeFam; TF331184; -.
DR BioGRID-ORCS; 67991; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Nacc2; mouse.
DR PRO; PR:Q9DCM7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DCM7; protein.
DR Bgee; ENSMUSG00000026932; Expressed in cerebral cortex marginal layer and 266 other tissues.
DR ExpressionAtlas; Q9DCM7; baseline and differential.
DR Genevisible; Q9DCM7; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1900477; P:negative regulation of G1/S transition of mitotic cell cycle by negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR018379; BEN_domain.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF10523; BEN; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM01025; BEN; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS51457; BEN; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..586
FT /note="Nucleus accumbens-associated protein 2"
FT /id="PRO_0000263669"
FT DOMAIN 30..94
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 349..446
FT /note="BEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 177..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT CONFLICT 502
FT /note="A -> T (in Ref. 2; AAH22103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 63219 MW; 4E7E625E70E21788 CRC64;
MSQMLHIEIP NFGNTVLGCL NEQRLLGLYC DVSIVVKGQA FKAHRAVLAA SSLYFRDLFS
GNSKSAFELP GTVPPACFQQ ILSFCYTGKL TMAASEQLVV MYTAGFLQIQ HIVERGTDLM
FKVSSPHCDS QTAMIEDASS EPQSPCNQLQ PATAAYVTSP SVPIPLLTRV KHEAMEMPPA
SGPGLASKRP LETGPRDGVA VATGAAGTPG TAPLKLPRVS YYGVPSLATL IPSIQQVPYP
PGERTSPGAS SLPTTDSPTS YHNEEDEEDD EAYDTMVEEQ YGQMYIKATG NYAVQEKPEP
VPLESRSCVL IRRDLVALPA SLISQIGYRC HPKLYSEGDP GEKLELVAGS GVYITRGQLM
NCHLCAGVKH KVLLRRLLAT FFDRNTLANS CGTGIRSSTS DPSRKPLDSR VLNAVKLYCQ
NFAPSFKESE MNVIAADMCT NARRVRKRWL PKIKSMLPEG VEMYRSVMGA SAASLPLDPE
FPSAAPQVFE QRIYAERRSD AATIVALRTD AVNVDLSTSA NPAFEANEEV DGGGSVIQEV
AAPEQLPADG QSSPQAFEQG NTSSSRPQTP VATATRRPEG TYAGTL
