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AN32E_MOUSE
ID   AN32E_MOUSE             Reviewed;         260 AA.
AC   P97822; E9Q5H9; Q3TH89; Q3TX26; Q8BPF8; Q8C2L4; Q8C7Q8; Q9CZD2;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
DE   AltName: Full=Cerebellar postnatal development protein 1;
DE   AltName: Full=LANP-like protein;
DE            Short=LANP-L;
GN   Name=Anp32e; Synonyms=Cpd1;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=11430900; DOI=10.1016/s0006-8993(01)02351-4;
RA   Radrizzani M., Vila-Ortiz G., Cafferata E.G.A., Di Tella M.C.,
RA   Gonzalez-Guerrico A., Perandones C., Pivetta O.H., Carminatti H.,
RA   Idoyaga Vargas V.P., Santa-Coloma T.A.;
RT   "Differential expression of CPD1 during postnatal development in the mouse
RT   cerebellum.";
RL   Brain Res. 907:162-174(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH KPNA1 AND
RP   KPNA2.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=10692581; DOI=10.1016/s0014-5793(00)01218-7;
RA   Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.;
RT   "Characterization of the nuclear transport of a novel leucine-rich acidic
RT   nuclear protein-like protein.";
RL   FEBS Lett. 468:171-175(2000).
RN   [3] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, Spinal cord, and Thymus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and 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).
RN   [6]
RP   FUNCTION.
RX   PubMed=14964690; DOI=10.1080/14734220310017212;
RA   Santa-Coloma T.A.;
RT   "Anp32e (Cpd1) and related protein phosphatase 2 inhibitors.";
RL   Cerebellum 2:310-320(2003).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16420440; DOI=10.1111/j.1460-9568.2005.04555.x;
RA   Costanzo R.V., Vila-Ortiz G.J., Perandones C., Carminatti H., Matilla A.,
RA   Radrizzani M.;
RT   "Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during
RT   synaptogenesis.";
RL   Eur. J. Neurosci. 23:309-324(2006).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15895553; DOI=10.1080/14734220410019020;
RA   Matilla A., Radrizzani M.;
RT   "The Anp32 family of proteins containing leucine-rich repeats.";
RL   Cerebellum 4:7-18(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20844742; DOI=10.1371/journal.pone.0012649;
RA   Kular R.K., Gogliotti R.G., Opal P.;
RT   "Cpd-1 null mice display a subtle neurological phenotype.";
RL   PLoS ONE 5:0-0(2010).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21049064; DOI=10.1371/journal.pone.0013597;
RA   Reilly P.T., Afzal S., Wakeham A., Haight J., You-Ten A., Zaugg K.,
RA   Dembowy J., Young A., Mak T.W.;
RT   "Generation and characterization of the Anp32e-deficient mouse.";
RL   PLoS ONE 5:E13597-E13597(2010).
RN   [12]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23675506; DOI=10.1371/journal.pone.0063815;
RA   Wong P., Leo V.I., Low M., Mak T.W., Zhang X., Reilly P.T.;
RT   "Targeted ANP32E mutant mice do not demonstrate obvious movement defects.";
RL   PLoS ONE 8:E63815-E63815(2013).
RN   [13]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=24463511; DOI=10.1038/nature12922;
RA   Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA   Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA   Hamiche A.;
RT   "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL   Nature 505:648-653(2014).
CC   -!- FUNCTION: Histone chaperone that specifically mediates the genome-wide
CC       removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1
CC       from its normal sites of deposition, especially from enhancer and
CC       insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the
CC       nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus
CC       shifting the equilibrium towards dissociation and the off-chromatin
CC       state (PubMed:24463511). Inhibits activity of protein phosphatase 2A
CC       (PP2A). Does not inhibit protein phosphatase 1. May play a role in
CC       cerebellar development and synaptogenesis.
CC       {ECO:0000269|PubMed:11430900, ECO:0000269|PubMed:14964690,
CC       ECO:0000269|PubMed:16420440, ECO:0000269|PubMed:24463511}.
CC   -!- SUBUNIT: Component of a SWR1-like complex, composed of EP400,
CC       KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex
CC       does not contain SRCAP. Interacts with H2A.Z/H2AZ1 (By similarity).
CC       Interacts with the importin alpha KPNA1 and KPNA2. {ECO:0000250,
CC       ECO:0000269|PubMed:10692581}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97822-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97822-2; Sequence=VSP_007373;
CC       Name=3;
CC         IsoId=P97822-3; Sequence=VSP_059599;
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in cerebellum and
CC       spleen. In the cerebellum, expressed mainly in granule cells and, to a
CC       lesser extent, in Purkinje cells. {ECO:0000269|PubMed:11430900}.
CC   -!- DEVELOPMENTAL STAGE: Low levels are found at postnatal day 4. Levels
CC       increase from postnatal day 7 to postnatal day 17. Levels decrease and
CC       remain low in the adult. {ECO:0000269|PubMed:11430900}.
CC   -!- DOMAIN: The H2A.Z-interacting domain (ZID) mediates a direct
CC       interaction with H2A.Z/H2AZ1. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. The phosphorylation is nuclear localization signal
CC       (NLS)-dependent (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and fertile
CC       (PubMed:20844742, PubMed:21049064, PubMed:23675506). They display a
CC       subtle neurological clasping phenotype and mild motor deficits
CC       (PubMed:20844742). Motor defects were not confirmed by a subsequent
CC       analysis (PubMed:23675506). Deletion in embryonic fibroblasts results
CC       in the appearance of a significant number of new H2A.Z/H2AZ1 around the
CC       transcription start site as well as at other chromatin regions
CC       (PubMed:24463511). {ECO:0000269|PubMed:20844742,
CC       ECO:0000269|PubMed:21049064, ECO:0000269|PubMed:23675506,
CC       ECO:0000269|PubMed:24463511}.
CC   -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR   EMBL; U89345; AAB49462.2; -; mRNA.
DR   EMBL; AB037685; BAB03507.1; -; mRNA.
DR   EMBL; AC092855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK012759; BAB28449.1; -; mRNA.
DR   EMBL; AK049647; BAC33858.1; -; mRNA.
DR   EMBL; AK076049; BAC36147.1; -; mRNA.
DR   EMBL; AK088401; BAC40331.1; -; mRNA.
DR   EMBL; AK147888; BAE28205.1; -; mRNA.
DR   EMBL; AK159446; BAE35090.1; -; mRNA.
DR   EMBL; AK168380; BAE40309.1; -; mRNA.
DR   EMBL; BC005690; AAH05690.1; -; mRNA.
DR   EMBL; BC080684; AAH80684.1; -; mRNA.
DR   CCDS; CCDS17626.1; -. [P97822-1]
DR   CCDS; CCDS57238.1; -. [P97822-2]
DR   CCDS; CCDS57239.1; -. [P97822-3]
DR   RefSeq; NP_001240686.1; NM_001253757.1. [P97822-2]
DR   RefSeq; NP_001240687.1; NM_001253758.1. [P97822-3]
DR   RefSeq; NP_075699.3; NM_023210.4. [P97822-1]
DR   AlphaFoldDB; P97822; -.
DR   SMR; P97822; -.
DR   BioGRID; 211498; 1.
DR   IntAct; P97822; 3.
DR   STRING; 10090.ENSMUSP00000128483; -.
DR   iPTMnet; P97822; -.
DR   PhosphoSitePlus; P97822; -.
DR   SwissPalm; P97822; -.
DR   EPD; P97822; -.
DR   jPOST; P97822; -.
DR   MaxQB; P97822; -.
DR   PaxDb; P97822; -.
DR   PeptideAtlas; P97822; -.
DR   PRIDE; P97822; -.
DR   ProteomicsDB; 282093; -. [P97822-1]
DR   ProteomicsDB; 282094; -. [P97822-2]
DR   ProteomicsDB; 357028; -.
DR   Antibodypedia; 20276; 139 antibodies from 29 providers.
DR   DNASU; 66471; -.
DR   Ensembl; ENSMUST00000015893; ENSMUSP00000015893; ENSMUSG00000015749. [P97822-2]
DR   Ensembl; ENSMUST00000165307; ENSMUSP00000128483; ENSMUSG00000015749. [P97822-1]
DR   Ensembl; ENSMUST00000171368; ENSMUSP00000130599; ENSMUSG00000015749. [P97822-3]
DR   GeneID; 66471; -.
DR   KEGG; mmu:66471; -.
DR   UCSC; uc008qlu.2; mouse. [P97822-1]
DR   UCSC; uc008qlv.2; mouse. [P97822-2]
DR   CTD; 81611; -.
DR   MGI; MGI:1913721; Anp32e.
DR   VEuPathDB; HostDB:ENSMUSG00000015749; -.
DR   eggNOG; KOG2739; Eukaryota.
DR   GeneTree; ENSGT00950000182907; -.
DR   InParanoid; P97822; -.
DR   OMA; MPNNQVS; -.
DR   OrthoDB; 1622194at2759; -.
DR   PhylomeDB; P97822; -.
DR   TreeFam; TF317206; -.
DR   BioGRID-ORCS; 66471; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Anp32e; mouse.
DR   PRO; PR:P97822; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P97822; protein.
DR   Bgee; ENSMUSG00000015749; Expressed in embryonic post-anal tail and 263 other tissues.
DR   ExpressionAtlas; P97822; baseline and differential.
DR   Genevisible; P97822; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR   GO; GO:0019212; F:phosphatase inhibitor activity; IDA:MGI.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR045081; AN32.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR11375; PTHR11375; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chaperone; Chromatin regulator;
KW   Cytoplasm; Isopeptide bond; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..260
FT                   /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT                   member E"
FT                   /id="PRO_0000137600"
FT   REPEAT          18..38
FT                   /note="LRR 1"
FT   REPEAT          43..64
FT                   /note="LRR 2"
FT   REPEAT          65..87
FT                   /note="LRR 3"
FT   REPEAT          89..110
FT                   /note="LRR 4"
FT   DOMAIN          123..161
FT                   /note="LRRCT"
FT   REGION          149..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..260
FT                   /note="ZID domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        150..203
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..240
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTT0"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTT0"
FT   VAR_SEQ         19..141
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059599"
FT   VAR_SEQ         208..219
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007373"
FT   CONFLICT        38
FT                   /note="N -> D (in Ref. 4; BAE35090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="N -> D (in Ref. 4; BAB28449)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="S -> T (in Ref. 4; BAC33858)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  29622 MW;  7F94E46D72A04780 CRC64;
     MEMKKKINME LKNRAPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA NVELSSLARL
     PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI KDLSTVEALQ NLKNLKSLDL
     FNCEITNLED YRESIFELLQ QITYLDGFDQ EDNEAPDSEE EDDDDEDGDE DEEDEDEDEA
     GPPEGYEEEE DDDEDEAGSE VGEGEEEVGL SYLMKDEIQD EEDDDDYVDE GEEEEEEEEE
     GLRGEKRKRD AEDDGEEDDD
 
 
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