位置:首页 > 蛋白库 > NACC1_MOUSE
NACC1_MOUSE
ID   NACC1_MOUSE             Reviewed;         514 AA.
AC   Q7TSZ8; Q80X97; Q9CZ72;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Nucleus accumbens-associated protein 1;
DE            Short=NAC-1;
DE   AltName: Full=BTB/POZ domain-containing protein 14B;
GN   Name=Nacc1; Synonyms=Btbd14b, Nac1;
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=Embryo;
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=C57BL/6J; TISSUE=Brain;
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   [3]
RP   TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX   PubMed=14521994; DOI=10.1016/s0306-4522(03)00376-2;
RA   Mackler S.A., Homan Y.X., Korutla L., Conti A.C., Blendy J.A.;
RT   "The mouse Nac1 gene, encoding a cocaine-regulated bric-a-brac tramtrac
RT   broad complex/pox virus and zinc finger protein, is regulated by AP1.";
RL   Neuroscience 121:355-361(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=17130457; DOI=10.1073/pnas.0604083103;
RA   Nakayama K., Nakayama N., Davidson B., Sheu J.-J.C., Jinawath N.,
RA   Santillan A., Salani R., Bristow R.E., Morin P.J., Kurman R.J., Wang T.-L.,
RA   Shih I.-M.;
RT   "A BTB/POZ protein, NAC-1, is related to tumor recurrence and is essential
RT   for tumor growth and survival.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18739-18744(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17945361; DOI=10.1016/j.bbr.2007.08.036;
RA   Mackler S., Pacchioni A., Degnan R., Homan Y., Conti A.C., Kalivas P.,
RA   Blendy J.A.;
RT   "Requirement for the POZ/BTB protein NAC1 in acute but not chronic
RT   psychomotor stimulant response.";
RL   Behav. Brain Res. 187:48-55(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-496, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Functions as a transcriptional repressor. Seems to function
CC       as a transcriptional corepressor in neuronal cells through recruitment
CC       of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell
CC       proliferation and survival. This may be mediated at least in part
CC       through repressing transcriptional activity of GADD45GIP1. Required for
CC       recruiting the proteasome from the nucleus to the cytoplasm and
CC       dendritic spines. Involved in the acute behavioral and neurological
CC       responses to cocaine and amphetamines. {ECO:0000269|PubMed:17130457,
CC       ECO:0000269|PubMed:17945361}.
CC   -!- SUBUNIT: Homooligomer; mediated by the BTB domain. Interacts with HDAC3
CC       and HDAC4. Interacts (via BTB domain) with CUL3, PSMD7 AND RCOR1 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q7TSZ8; Q8BX22: Sall4; NbExp=4; IntAct=EBI-5691985, EBI-2312582;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Distribution in the
CC       cytoplasm is dependent on phosphorylation. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC       the brain, kidney and liver, and at lower levels in heart, lung and
CC       testes. {ECO:0000269|PubMed:14521994}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable with no obvious developmental or
CC       physiological impairments. In addition, they do not display alterations
CC       in chronic responses to cocaine and amphetamine administration, but do
CC       however display significantly diminished acute behavioral and
CC       neurochemical responses to these drugs. {ECO:0000269|PubMed:17945361}.
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; AK012935; BAB28558.1; -; mRNA.
DR   EMBL; BC048157; AAH48157.1; -; mRNA.
DR   EMBL; BC052706; AAH52706.1; -; mRNA.
DR   EMBL; BC054800; AAH54800.1; -; mRNA.
DR   CCDS; CCDS22475.1; -.
DR   RefSeq; NP_080064.3; NM_025788.3.
DR   RefSeq; XP_006531355.1; XM_006531292.2.
DR   RefSeq; XP_006531356.1; XM_006531293.3.
DR   RefSeq; XP_006531357.1; XM_006531294.3.
DR   AlphaFoldDB; Q7TSZ8; -.
DR   SMR; Q7TSZ8; -.
DR   BioGRID; 211748; 20.
DR   DIP; DIP-29930N; -.
DR   IntAct; Q7TSZ8; 6.
DR   MINT; Q7TSZ8; -.
DR   STRING; 10090.ENSMUSP00000001975; -.
DR   iPTMnet; Q7TSZ8; -.
DR   PhosphoSitePlus; Q7TSZ8; -.
DR   EPD; Q7TSZ8; -.
DR   MaxQB; Q7TSZ8; -.
DR   PaxDb; Q7TSZ8; -.
DR   PeptideAtlas; Q7TSZ8; -.
DR   PRIDE; Q7TSZ8; -.
DR   ProteomicsDB; 287353; -.
DR   Antibodypedia; 13525; 319 antibodies from 38 providers.
DR   DNASU; 66830; -.
DR   Ensembl; ENSMUST00000001975; ENSMUSP00000001975; ENSMUSG00000001910.
DR   GeneID; 66830; -.
DR   KEGG; mmu:66830; -.
DR   UCSC; uc009mmu.2; mouse.
DR   CTD; 112939; -.
DR   MGI; MGI:1914080; Nacc1.
DR   VEuPathDB; HostDB:ENSMUSG00000001910; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000159327; -.
DR   HOGENOM; CLU_029038_1_0_1; -.
DR   InParanoid; Q7TSZ8; -.
DR   OMA; SSCYFRD; -.
DR   OrthoDB; 567120at2759; -.
DR   PhylomeDB; Q7TSZ8; -.
DR   TreeFam; TF331184; -.
DR   BioGRID-ORCS; 66830; 7 hits in 73 CRISPR screens.
DR   ChiTaRS; Nacc1; mouse.
DR   PRO; PR:Q7TSZ8; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q7TSZ8; protein.
DR   Bgee; ENSMUSG00000001910; Expressed in embryonic post-anal tail and 226 other tissues.
DR   ExpressionAtlas; Q7TSZ8; baseline and differential.
DR   Genevisible; Q7TSZ8; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; 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   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..514
FT                   /note="Nucleus accumbens-associated protein 1"
FT                   /id="PRO_0000274042"
FT   DOMAIN          30..94
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          360..457
FT                   /note="BEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT   REGION          183..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   MOD_RES         245
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:O35260"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        167
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        167
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        182
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        304
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        438
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        466
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CROSSLNK        485
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RE7"
FT   CONFLICT        401
FT                   /note="S -> R (in Ref. 1; BAB28558)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="G -> V (in Ref. 2; AAH48157)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  56537 MW;  C83C23891B097626 CRC64;
     MAQTLQMEIP NFGNSILECL NEQRLQGLYC DVSVVVKGHA FKAHRAVLAA SSSYFRDLFN
     SSRSAVVELP AAVQPQSFQQ ILTFCYTGRL SMNMGDQFLL IYTAGFLQIQ EIMEKGTEFF
     LKVSSPSCDS QGLHPEEAPS SEPQSPVAQT LGWPACSTPL PLVSRVKTEQ ELDSVQCTPM
     AKRLWDSSQK EAGGSGGNNG SRKMAKFSTP DLALNRMPQP LSMATATAAV AVVAVGGCVS
     GPSMSERTSP GTSSAYTSDS PSSYHNEEDE EEDAGEEGTD EQYRQICNMY TMYSMLNVGQ
     TAEKVEALPE QVVLESRSRI RVRQDLASLP AELINQIGNR CHPKLYDEGD PSEKLELVTG
     TNVYITRAQL MNCHVSAGTR HKVLLRRLLA SFFDRNTLAN SCGTGIRSST NDPRRKPLDS
     RVLHAVKYYC QNFAPNFKES EMNAIAADMC TNARRVVRKS WLPKTKPLHL VEGDNYSSFI
     SDTCKIEPDM MSMEHSFETA SHDGEAGPSA EVLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024