AN32B_MOUSE
ID AN32B_MOUSE Reviewed; 272 AA.
AC Q9EST5; B1AVH9; Q566J4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
DE AltName: Full=Proliferation-related acidic leucine-rich protein PAL31;
GN Name=Anp32b; Synonyms=Pal31;
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).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11162633; DOI=10.1006/bbrc.2000.4244;
RA Sun W., Hattori N., Mutai H., Toyoshima Y., Kimura H., Tanaka S.,
RA Shiota K.;
RT "PAL31, a nuclear protein required for progression to the S phase.";
RL Biochem. Biophys. Res. Commun. 280:1048-1054(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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=FVB/N, and NMRI; TISSUE=Mammary tumor;
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [7]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21636789; DOI=10.1073/pnas.1106211108;
RA Reilly P.T., Afzal S., Gorrini C., Lui K., Bukhman Y.V., Wakeham A.,
RA Haight J., Ling T.W., Cheung C.C., Elia A.J., Turner P.V., Mak T.W.;
RT "Acidic nuclear phosphoprotein 32kDa (ANP32)B-deficient mouse reveals a
RT hierarchy of ANP32 importance in mammalian development.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10243-10248(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30890743; DOI=10.1038/s41598-019-41269-z;
RA Chemnitz J., Pieper D., Stich L., Schumacher U., Balabanov S., Spohn M.,
RA Grundhoff A., Steinkasserer A., Hauber J., Zinser E.;
RT "The acidic protein rich in leucines Anp32b is an immunomodulator of
RT inflammation in mice.";
RL Sci. Rep. 9:4853-4853(2019).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=32231671; DOI=10.3389/fimmu.2020.00450;
RA Beck S., Zickler M., Pinho Dos Reis V., Guenther T., Grundhoff A.,
RA Reilly P.T., Mak T.W., Stanelle-Bertram S., Gabriel G.;
RT "ANP32B Deficiency Protects Mice From Lethal Influenza A Virus Challenge by
RT Dampening the Host Immune Response.";
RL Front. Immunol. 11:450-450(2020).
CC -!- FUNCTION: Multifunctional protein that is involved in the regulation of
CC many processes including cell proliferation, apoptosis, cell cycle
CC progression or transcription (PubMed:21636789). Regulates the
CC proliferation of neuronal stem cells, differentiation of leukemic cells
CC and progression from G1 to S phase of the cell cycle. As negative
CC regulator of caspase-3-dependent apoptosis, may act as an antagonist of
CC ANP32A in regulating tissue homeostasis (By similarity). Exhibits
CC histone chaperone properties, able to recruit histones to certain
CC promoters, thus regulating the transcription of specific genes (By
CC similarity). Also plays an essential role in the nucleocytoplasmic
CC transport of specific mRNAs via the uncommon nuclear mRNA export
CC receptor XPO1/CRM1 (By similarity). Participates in the regulation of
CC adequate adaptive immune responses by acting on mRNA expression and
CC cell proliferation (PubMed:30890743). {ECO:0000250|UniProtKB:Q92688,
CC ECO:0000269|PubMed:21636789, ECO:0000269|PubMed:30890743}.
CC -!- SUBUNIT: Interacts with histones H3 and H4. Interacts with KLF5; this
CC interaction induces promoter region-specific histone incorporation and
CC inhibition of histone acetylation by ANP32B.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92688}.
CC Note=Accumulates in the nuclei at the S phase.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EST5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EST5-2; Sequence=VSP_023520, VSP_023521;
CC -!- DOMAIN: Histone binding is mediated by the concave surface of the LRR
CC region. {ECO:0000250}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group.
CC -!- PTM: Directly cleaved by caspase-3/CASP3.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display an highly penetrant
CC perinatal lethality in a mixed genetic background and a fully penetrant
CC lethality in a pure C57BL/6 background (PubMed:21636789). Mutants also
CC show enhanced clinical symptoms correlated with depletion of naive
CC effector T-cells, exhaustion of lymphocytes and enhanced prevalence of
CC follicular T-helper cells (PubMed:30890743). In addition, mice show
CC significantly reduced H3N2 or H5N1 influenza viral loads, inflammatory
CC cytokine response and reduced pathogenicity compared to WT
CC (PubMed:32231671). {ECO:0000269|PubMed:21636789,
CC ECO:0000269|PubMed:30890743, ECO:0000269|PubMed:32231671}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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; AB025582; BAB12436.1; -; mRNA.
DR EMBL; AK165807; BAE38387.1; -; mRNA.
DR EMBL; AL683884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003489; AAH03489.1; -; mRNA.
DR EMBL; BC005628; AAH05628.1; -; mRNA.
DR EMBL; BC093506; AAH93506.1; -; mRNA.
DR CCDS; CCDS18151.1; -. [Q9EST5-1]
DR RefSeq; NP_570959.1; NM_130889.3. [Q9EST5-1]
DR AlphaFoldDB; Q9EST5; -.
DR SMR; Q9EST5; -.
DR BioGRID; 212319; 14.
DR IntAct; Q9EST5; 1.
DR STRING; 10090.ENSMUSP00000099990; -.
DR iPTMnet; Q9EST5; -.
DR PhosphoSitePlus; Q9EST5; -.
DR SwissPalm; Q9EST5; -.
DR EPD; Q9EST5; -.
DR jPOST; Q9EST5; -.
DR MaxQB; Q9EST5; -.
DR PaxDb; Q9EST5; -.
DR PeptideAtlas; Q9EST5; -.
DR PRIDE; Q9EST5; -.
DR ProteomicsDB; 282091; -. [Q9EST5-1]
DR ProteomicsDB; 282092; -. [Q9EST5-2]
DR TopDownProteomics; Q9EST5-1; -. [Q9EST5-1]
DR Antibodypedia; 28919; 281 antibodies from 31 providers.
DR DNASU; 67628; -.
DR Ensembl; ENSMUST00000102926; ENSMUSP00000099990; ENSMUSG00000028333. [Q9EST5-1]
DR GeneID; 67628; -.
DR KEGG; mmu:67628; -.
DR UCSC; uc008stt.1; mouse. [Q9EST5-1]
DR UCSC; uc012dds.1; mouse. [Q9EST5-2]
DR CTD; 10541; -.
DR MGI; MGI:1914878; Anp32b.
DR VEuPathDB; HostDB:ENSMUSG00000028333; -.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; Q9EST5; -.
DR OMA; DEVSGEX; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; Q9EST5; -.
DR TreeFam; TF317206; -.
DR BioGRID-ORCS; 67628; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Anp32b; mouse.
DR PRO; PR:Q9EST5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9EST5; protein.
DR Bgee; ENSMUSG00000028333; Expressed in embryonic post-anal tail and 70 other tissues.
DR Genevisible; Q9EST5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR045081; AN32.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR11375; PTHR11375; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..272
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member B"
FT /id="PRO_0000236252"
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..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 260..263
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
FT COMPBIAS 152..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EST6"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EST6"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT VAR_SEQ 227
FT /note="E -> EVNTTVFFPICVKTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023520"
FT VAR_SEQ 269..272
FT /note="GEDD -> EEEPKNSSRDIPPSSVSPLVIHHQAWGLRPNKIVNVVRFSCKTL
FT AVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023521"
SQ SEQUENCE 272 AA; 31079 MW; BC22DC591AA6BC15 CRC64;
MDMKRRIHLE LRNRTPAAVR ELVLDNCKAM DGKIEGLTDE FVNLEFLSLI SVGLFSVSDL
PKLPKLKKLE LSENRIFGGL DRLAEELPSL THLNLSGNNL KDISTLEPLK RLDCLKSLDL
FGCEVTNRSD YRETVFRLLP QLSYLDGYDR EDQEAPDSDV EVDSVEEAPD SDGEVDGVDK
EEEDEEGEDE EEEEDEDGEE EEDEDEEDED EDEDVEGEDD EDEVSGEEEE FGHDGEVDED
EEDEDEDEDE EEEESGKGEK RKRETDDEGE DD
