ID AN32B_HUMAN Reviewed; 251 AA. AC Q92688; B2R9C7; O00655; P78458; P78459; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 200. DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B {ECO:0000303|PubMed:33045004}; DE AltName: Full=Acidic protein rich in leucines; DE AltName: Full=Putative HLA-DR-associated protein I-2; DE Short=PHAPI2; DE AltName: Full=Silver-stainable protein SSP29; GN Name=ANP32B; Synonyms=APRIL, PHAPI2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhu L., Henning D., Valdez B.C.; RT "Molecular cloning and partial characterization of a new silver-stainable RT protein."; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RC TISSUE=Pancreas; RX PubMed=9473664; DOI=10.1016/s0167-4781(97)00165-6; RA Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.; RT "Expression analysis and chromosomal mapping of a novel human gene, APRIL, RT encoding an acidic protein rich in leucines."; RL Biochim. Biophys. Acta 1395:176-180(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle, and Testis; 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP FUNCTION, PHOSPHORYLATION AT THR-244, SUBCELLULAR LOCATION, AND NUCLEAR RP LOCALIZATION SIGNAL. RX PubMed=17178712; DOI=10.1074/jbc.m608849200; RA Fries B., Heukeshoven J., Hauber I., Gruettner C., Stocking C., RA Kehlenbach R.H., Hauber J., Chemnitz J.; RT "Analysis of nucleocytoplasmic trafficking of the HuR ligand APRIL and its RT influence on CD83 expression."; RL J. Biol. Chem. 282:4504-4515(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [13] RP FUNCTION, AND INTERACTION WITH KLF5. RX PubMed=18039846; DOI=10.1128/mcb.01396-07; RA Munemasa Y., Suzuki T., Aizawa K., Miyamoto S., Imai Y., Matsumura T., RA Horikoshi M., Nagai R.; RT "Promoter region-specific histone incorporation by the novel histone RT chaperone ANP32B and DNA-binding factor KLF5."; RL Mol. Cell. Biol. 28:1171-1181(2008). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-163. RX PubMed=20015864; DOI=10.1093/carcin/bgp320; RA Shen S.M., Yu Y., Wu Y.L., Cheng J.K., Wang L.S., Chen G.Q.; RT "Downregulation of ANP32B, a novel substrate of caspase-3, enhances RT caspase-3 activation and apoptosis induction in myeloid leukemic cells."; RL Carcinogenesis 31:419-426(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=21159877; DOI=10.1128/jvi.01518-10; RA Bodem J., Schied T., Gabriel R., Rammling M., Rethwilm A.; RT "Foamy virus nuclear RNA export is distinct from that of other RT retroviruses."; RL J. Virol. 85:2333-2341(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP INTERACTION WITH HENDRA VIRUS PROTEIN M (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=24823948; DOI=10.1371/journal.pone.0097233; RA Bauer A., Neumann S., Karger A., Henning A.K., Maisner A., Lamp B., RA Dietzel E., Kwasnitschka L., Balkema-Buschmann A., Keil G.M., Finke S.; RT "ANP32B is a nuclear target of henipavirus M proteins."; RL PLoS ONE 9:e97233-e97233(2014). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [24] RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=31217244; DOI=10.1128/jvi.00217-19; RA Staller E., Sheppard C.M., Neasham P.J., Mistry B., Peacock T.P., RA Goldhill D.H., Long J.S., Barclay W.S.; RT "ANP32 Proteins Are Essential for Influenza Virus Replication in Human RT Cells."; RL J. Virol. 93:0-0(2019). RN [25] RP INTERACTION WITH SENDAI VIRUS PROTEIN M AND MEASLES VIRUS PROTEIN M RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=31793855; DOI=10.1099/jgv.0.001362; RA Guenther M., Bauer A., Mueller M., Zaeck L., Finke S.; RT "Interaction of host cellular factor ANP32B with matrix proteins of RT different paramyxoviruses."; RL J. Gen. Virol. 101:44-58(2020). RN [26] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH INFLUENZA VIRUS B RP PROTEIN PB2 (MICROBIAL INFECTION). RX PubMed=33045004; DOI=10.1371/journal.ppat.1008989; RA Zhang Z., Zhang H., Xu L., Guo X., Wang W., Ji Y., Lin C., Wang Y., RA Wang X.; RT "Selective usage of ANP32 proteins by influenza B virus polymerase: RT Implications in determination of host range."; RL PLoS Pathog. 16:e1008989-e1008989(2020). RN [27] RP STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH HISTONES H3 RP AND H4, AND LEUCINE-RICH REPEATS. RX PubMed=20538007; DOI=10.1016/j.jmb.2010.06.005; RA Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K., RA Koshiba S., Kigawa T., Nagai R., Yokoyama S.; RT "Solution structure of histone chaperone ANP32B: interaction with core RT histones H3-H4 through its acidic concave domain."; RL J. Mol. Biol. 401:97-114(2010). 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:20015864, PubMed:18039846). CC Regulates the proliferation of neuronal stem cells, differentiation of CC leukemic cells and progression from G1 to S phase of the cell cycle. As CC negative regulator of caspase-3-dependent apoptosis, may act as an CC antagonist of ANP32A in regulating tissue homeostasis CC (PubMed:20015864). Exhibits histone chaperone properties, able to CC recruit histones to certain promoters, thus regulating the CC transcription of specific genes (PubMed:20538007, PubMed:18039846). CC Also plays an essential role in the nucleocytoplasmic transport of CC specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1 CC (PubMed:17178712). Participates in the regulation of adequate adaptive CC immune responses by acting on mRNA expression and cell proliferation CC (By similarity). {ECO:0000250|UniProtKB:Q9EST5, CC ECO:0000269|PubMed:17178712, ECO:0000269|PubMed:18039846, CC ECO:0000269|PubMed:20015864, ECO:0000269|PubMed:20538007}. CC -!- FUNCTION: (Microbial infection) Plays an essential role in influenza A CC and B viral genome replication (PubMed:33045004, PubMed:31217244). Also CC plays a role in foamy virus mRNA export from the nucleus to the CC cytoplasm (PubMed:21159877). {ECO:0000269|PubMed:21159877, CC ECO:0000269|PubMed:31217244, ECO:0000269|PubMed:33045004}. CC -!- SUBUNIT: Interacts with histones H3 and H4 (PubMed:20538007). Interacts CC with KLF5; this interaction induces promoter region-specific histone CC incorporation and inhibition of histone acetylation by ANP32B CC (PubMed:18039846). {ECO:0000269|PubMed:18039846, CC ECO:0000269|PubMed:20538007}. CC -!- SUBUNIT: (Microbial infection) Interacts with Sendai virus protein M. CC {ECO:0000269|PubMed:31793855}. CC -!- SUBUNIT: (Microbial infection) Interacts with Measles virus protein M. CC {ECO:0000269|PubMed:31793855}. CC -!- SUBUNIT: (Microbial infection) Interacts with Hendra virus protein M; CC this interaction promotes nuclear localization of M. CC {ECO:0000269|PubMed:24823948}. CC -!- SUBUNIT: (Microbial infection) Interacts with influenza virus B protein CC PB2; this interaction strongly supports influenza B virus replication. CC {ECO:0000269|PubMed:33045004}. CC -!- INTERACTION: CC Q92688; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-762428, EBI-10181188; CC Q92688; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-762428, EBI-2795449; CC Q92688; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-762428, EBI-19153639; CC Q92688; P04792: HSPB1; NbExp=3; IntAct=EBI-762428, EBI-352682; CC Q92688; O60333-2: KIF1B; NbExp=3; IntAct=EBI-762428, EBI-10975473; CC Q92688; P52294: KPNA1; NbExp=8; IntAct=EBI-762428, EBI-358383; CC Q92688; O15131: KPNA5; NbExp=7; IntAct=EBI-762428, EBI-540602; CC Q92688; O60684: KPNA6; NbExp=3; IntAct=EBI-762428, EBI-359923; CC Q92688; P50222: MEOX2; NbExp=3; IntAct=EBI-762428, EBI-748397; CC Q92688; Q9NPC7: MYNN; NbExp=3; IntAct=EBI-762428, EBI-3446748; CC Q92688; O00560: SDCBP; NbExp=6; IntAct=EBI-762428, EBI-727004; CC Q92688; O76024: WFS1; NbExp=3; IntAct=EBI-762428, EBI-720609; CC Q92688; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-762428, EBI-12111538; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000269|PubMed:17178712, ECO:0000269|PubMed:24823948, CC ECO:0000269|PubMed:31217244}. Cytoplasm {ECO:0000269|PubMed:17178712}. CC Note=Accumulates in the nuclei at the S phase. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Lacks a nuclear CC localization signal. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Anp32b1, PHAPI2b; CC IsoId=Q92688-1; Sequence=Displayed; CC Name=2; Synonyms=Anp32b2, PHAPI2b; CC IsoId=Q92688-2; Sequence=VSP_019304; CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, pancreas, prostate and in CC spleen, thymus and placenta. {ECO:0000269|PubMed:9473664}. CC -!- DOMAIN: Histone binding is mediated by the concave surface of the LRR CC region. 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 (By similarity). {ECO:0000250}. CC -!- PTM: Directly cleaved by caspase-3/CASP3. CC {ECO:0000269|PubMed:20015864}. CC -!- MISCELLANEOUS: [Isoform 2]: No canonical donor splice site. CC {ECO:0000305}. 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; Y07569; CAA68855.1; -; mRNA. DR EMBL; U70439; AAB37579.1; -; mRNA. DR EMBL; Y07969; CAA69265.1; -; mRNA. DR EMBL; Y07570; CAA68856.1; -; mRNA. DR EMBL; AK313733; BAG36474.1; -; mRNA. DR EMBL; AL354726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW58865.1; -; Genomic_DNA. DR EMBL; BC013003; AAH13003.1; -; mRNA. DR EMBL; BC019658; AAH19658.1; -; mRNA. DR CCDS; CCDS6732.1; -. [Q92688-1] DR RefSeq; NP_006392.1; NM_006401.2. [Q92688-1] DR PDB; 2ELL; NMR; -; A=1-161. DR PDB; 2RR6; NMR; -; A=1-161. DR PDBsum; 2ELL; -. DR PDBsum; 2RR6; -. DR AlphaFoldDB; Q92688; -. DR BMRB; Q92688; -. DR SMR; Q92688; -. DR BioGRID; 115795; 151. DR CORUM; Q92688; -. DR IntAct; Q92688; 61. DR MINT; Q92688; -. DR STRING; 9606.ENSP00000345848; -. DR ChEMBL; CHEMBL4295917; -. DR CarbonylDB; Q92688; -. DR GlyGen; Q92688; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92688; -. DR MetOSite; Q92688; -. DR PhosphoSitePlus; Q92688; -. DR SwissPalm; Q92688; -. DR BioMuta; ANP32B; -. DR DMDM; 26390818; -. DR CPTAC; CPTAC-1595; -. DR EPD; Q92688; -. DR jPOST; Q92688; -. DR MassIVE; Q92688; -. DR MaxQB; Q92688; -. DR PaxDb; 9606-ENSP00000345848; -. DR PeptideAtlas; Q92688; -. DR ProteomicsDB; 75409; -. [Q92688-1] DR ProteomicsDB; 75410; -. [Q92688-2] DR Pumba; Q92688; -. DR TopDownProteomics; Q92688-1; -. [Q92688-1] DR TopDownProteomics; Q92688-2; -. [Q92688-2] DR Antibodypedia; 28919; 316 antibodies from 31 providers. DR DNASU; 10541; -. DR Ensembl; ENST00000339399.5; ENSP00000345848.4; ENSG00000136938.9. [Q92688-1] DR GeneID; 10541; -. DR KEGG; hsa:10541; -. DR MANE-Select; ENST00000339399.5; ENSP00000345848.4; NM_006401.3; NP_006392.1. DR UCSC; uc004aya.4; human. [Q92688-1] DR AGR; HGNC:16677; -. DR CTD; 10541; -. DR DisGeNET; 10541; -. DR GeneCards; ANP32B; -. DR HGNC; HGNC:16677; ANP32B. DR HPA; ENSG00000136938; Low tissue specificity. DR MIM; 619823; gene. DR neXtProt; NX_Q92688; -. DR OpenTargets; ENSG00000136938; -. DR PharmGKB; PA24812; -. DR VEuPathDB; HostDB:ENSG00000136938; -. DR eggNOG; KOG2739; Eukaryota. DR GeneTree; ENSGT00950000182907; -. DR HOGENOM; CLU_063314_1_1_1; -. DR InParanoid; Q92688; -. DR OMA; DEVSGEX; -. DR OrthoDB; 1386993at2759; -. DR PhylomeDB; Q92688; -. DR TreeFam; TF317206; -. DR PathwayCommons; Q92688; -. DR SignaLink; Q92688; -. DR SIGNOR; Q92688; -. DR BioGRID-ORCS; 10541; 54 hits in 1133 CRISPR screens. DR ChiTaRS; ANP32B; human. DR EvolutionaryTrace; Q92688; -. DR GeneWiki; ANP32B; -. DR GenomeRNAi; 10541; -. DR Pharos; Q92688; Tbio. DR PRO; PR:Q92688; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q92688; Protein. DR Bgee; ENSG00000136938; Expressed in tendon of biceps brachii and 218 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0048839; P:inner ear development; IEA:Ensembl. DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. DR GO; GO:0001944; P:vasculature development; IEA:Ensembl. DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32; 1. DR PANTHER; PTHR11375:SF2; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER B; 1. DR Pfam; PF14580; LRR_9; 1. DR SMART; SM00446; LRRcap; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 4. DR Genevisible; Q92688; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm; KW Host-virus interaction; Leucine-rich repeat; Nucleus; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..251 FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family FT member B" FT /id="PRO_0000137595" FT REPEAT 16..40 FT /note="LRR 1" FT /evidence="ECO:0000269|PubMed:20538007" FT REPEAT 43..64 FT /note="LRR 2" FT /evidence="ECO:0000269|PubMed:20538007" FT REPEAT 65..84 FT /note="LRR 3" FT /evidence="ECO:0000269|PubMed:20538007" FT REPEAT 89..110 FT /note="LRR 4" FT /evidence="ECO:0000269|PubMed:20538007" FT DOMAIN 123..161 FT /note="LRRCT" FT REGION 149..251 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 239..242 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:17178712" FT COMPBIAS 152..233 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 86 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EST6" FT MOD_RES 244 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:17178712, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 196..251 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9473664" FT /id="VSP_019304" FT MUTAGEN 163 FT /note="D->A: Complete loss of cleavage by CASP3." FT /evidence="ECO:0000269|PubMed:20015864" FT CONFLICT 1..2 FT /note="Missing (in Ref. 3; CAA69265)" FT /evidence="ECO:0000305" FT HELIX 3..11 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:2RR6" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 39..43 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 104..109 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:2ELL" FT HELIX 131..136 FT /evidence="ECO:0007829|PDB:2ELL" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:2ELL" SQ SEQUENCE 251 AA; 28788 MW; 93A1AADF8EDE7D53 CRC64; MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE DDEDGEEEEF DEEDDEDEDV EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR KRETDDEGED D //