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NACC2_RAT
ID   NACC2_RAT               Reviewed;         585 AA.
AC   Q562B4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 93.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-585.
RC   TISSUE=Ovary;
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; AABR03030473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC092608; AAH92608.1; -; mRNA.
DR   RefSeq; NP_001094003.1; NM_001100533.1.
DR   AlphaFoldDB; Q562B4; -.
DR   SMR; Q562B4; -.
DR   STRING; 10116.ENSRNOP00000024786; -.
DR   PhosphoSitePlus; Q562B4; -.
DR   PaxDb; Q562B4; -.
DR   PRIDE; Q562B4; -.
DR   GeneID; 296583; -.
DR   KEGG; rno:296583; -.
DR   UCSC; RGD:1309292; rat.
DR   CTD; 138151; -.
DR   RGD; 1309292; Nacc2.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q562B4; -.
DR   PhylomeDB; Q562B4; -.
DR   PRO; PR:Q562B4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
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:RGD.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
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:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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:RGD.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR   GO; GO:0031503; P:protein-containing complex localization; ISO:RGD.
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..585
FT                   /note="Nucleus accumbens-associated protein 2"
FT                   /id="PRO_0000263670"
FT   DOMAIN          30..94
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          348..445
FT                   /note="BEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT   REGION          238..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..574
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        296
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT   CROSSLNK        426
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BF6"
FT   CROSSLNK        453
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BF6"
SQ   SEQUENCE   585 AA;  63100 MW;  E5DA8753AF7E3340 CRC64;
     MSQMLHIEIP NFGNTVLGCL NEQRLLGLYC DVSIVVKGQA FKAHRAVLAA SSLYFRDLFS
     GNSKSAFELP GTVPPACFQQ ILSFCYTGKL TMAASEQLVV MYTAGFLQIQ HIVERGTDLM
     FKVSSPHCDS QTAMIEDASS EPQSPCNQLQ PATAAYATSP SVPIPLLTRV KHEAMEMPPA
     TGPGLASKRP LDTGPRDGVA VATGAAGTPG TAPLKLPRVS YYGVPSLATL IPSIQQVPYP
     QGERTSPGAS SLPTTDSSTS YHNEDEDDDE AYDTMVEEQY GQMYIKATGN YAVQEKPEPV
     PLESRSCVLI RRDLVALPAS LISQIGYRCH PKLYSEGDPG EKLELVAGSG VYITRGQLMN
     CHLCAGVKHK VLLRRLLATF FDRNTLANSC GTGIRSSTSD PSRKPLDSRV LNAVKLYCQN
     FAPSFKESEM NVIAADMCTN ARRVRKRWLP KIKSMLPEGV EMYRSVMGAS AASLPLDPEF
     PSAASQVFEQ RIYAERRNDA ATIVALRTDA VNVDLSTSAN PAFEANEEVD GAGSVIQEVA
     APEQLPADGQ SSPQAFEQGN TSSSRPQTPV ATATRRPEGT YAGTL
 
 
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