AN32B_HUMAN
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 03-AUG-2022, entry version 192.
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=4; 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}.
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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; 135.
DR CORUM; Q92688; -.
DR IntAct; Q92688; 60.
DR MINT; Q92688; -.
DR STRING; 9606.ENSP00000345848; -.
DR ChEMBL; CHEMBL4295917; -.
DR CarbonylDB; Q92688; -.
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; Q92688; -.
DR PeptideAtlas; Q92688; -.
DR PRIDE; Q92688; -.
DR ProteomicsDB; 75409; -. [Q92688-1]
DR ProteomicsDB; 75410; -. [Q92688-2]
DR TopDownProteomics; Q92688-1; -. [Q92688-1]
DR TopDownProteomics; Q92688-2; -. [Q92688-2]
DR Antibodypedia; 28919; 281 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 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; 1622194at2759; -.
DR PhylomeDB; Q92688; -.
DR TreeFam; TF317206; -.
DR PathwayCommons; Q92688; -.
DR SignaLink; Q92688; -.
DR SIGNOR; Q92688; -.
DR BioGRID-ORCS; 10541; 51 hits in 1054 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 216 other tissues.
DR Genevisible; Q92688; HS.
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; -; 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; 1.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 4.
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
