ID AN32A_HUMAN Reviewed; 249 AA. AC P39687; B2R6T4; Q53FK4; Q5J8L8; Q7M4N6; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 02-SEP-2026, entry version 226. DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member A {ECO:0000303|PubMed:33045004, ECO:0000303|PubMed:33208942}; DE AltName: Full=Acidic nuclear phosphoprotein pp32; DE Short=pp32; DE AltName: Full=Leucine-rich acidic nuclear protein; DE Short=LANP; DE AltName: Full=Mapmodulin; DE AltName: Full=Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; DE AltName: Full=Putative HLA-DR-associated protein I; DE Short=PHAPI; GN Name=ANP32A; Synonyms=C15orf1, LANP, MAPM, PHAP1; 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], AND PROTEIN SEQUENCE OF 1-26; 29-47; 71-97 AND RP 100-161. RC TISSUE=B-cell lymphoma; RX PubMed=8192856; DOI=10.1515/bchm3.1994.375.2.113; RA Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., RA Zimmermann B., Kratzin H.D., Hilschmann N.; RT "Purification and characterization of two putative HLA class II associated RT proteins: PHAPI and PHAPII."; RL Biol. Chem. Hoppe-Seyler 375:113-126(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 7-12 AND 29-44. RC TISSUE=Kidney; RX PubMed=8679524; DOI=10.1021/bi960581y; RA Li M., Makkinje A., Damuni Z.; RT "Molecular identification of I1PP2A, a novel potent heat-stable inhibitor RT protein of protein phosphatase 2A."; RL Biochemistry 35:6998-7002(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8970164; DOI=10.1091/mbc.7.12.2045; RA Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E., Voneiff E., RA Kuhajda F.P., Pasternack G.R.; RT "Structure of pp32, an acidic nuclear protein which inhibits oncogene- RT induced formation of transformed foci."; RL Mol. Biol. Cell 7:2045-2056(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9353121; DOI=10.1038/40159; RA Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.; RT "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin- RT 1."; RL Nature 389:974-978(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=15642345; DOI=10.1016/j.febslet.2004.11.097; RA Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.; RT "Inhibitors of protein phosphatase-2A from human brain structures, RT immunocytological localization and activities towards dephosphorylation of RT the Alzheimer type hyperphosphorylated tau."; RL FEBS Lett. 579:363-372(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Synovium; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; 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 [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10400610; DOI=10.1074/jbc.274.29.20053; RA Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., Pasternack G.R.; RT "Identification of sequences required for inhibition of oncogene-mediated RT transformation by pp32."; RL J. Biol. Chem. 274:20053-20055(1999). RN [12] RP INTERACTION WITH THE INHAT COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=11163245; DOI=10.1016/s0092-8674(01)00196-9; RA Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.; RT "Regulation of histone acetylation and transcription by INHAT, a human RT cellular complex containing the Set oncoprotein."; RL Cell 104:119-130(2001). RN [13] RP INTERACTION WITH SET. RX PubMed=11555662; DOI=10.1074/jbc.m108137200; RA Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., RA Lieberman J.; RT "Granzyme A activates an endoplasmic reticulum-associated caspase- RT independent nuclease to induce single-stranded DNA nicks."; RL J. Biol. Chem. 276:43285-43293(2001). RN [14] RP FUNCTION. RX PubMed=11360199; DOI=10.1038/sj.onc.1204294; RA Bai J., Brody J.R., Kadkol S.S., Pasternack G.R.; RT "Tumor suppression and potentiation by manipulation of pp32 expression."; RL Oncogene 20:2153-2160(2001). RN [15] RP INTERACTION WITH ELAVL1, AND SUBCELLULAR LOCATION. RX PubMed=11729309; DOI=10.1126/science.1064693; RA Gallouzi I.-E., Steitz J.A.; RT "Delineation of mRNA export pathways by the use of cell-permeable RT peptides."; RL Science 294:1895-1901(2001). RN [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11830591; DOI=10.1074/jbc.m112455200; RA Seo S.B., Macfarlan T., McNamara P., Hong R., Mukai Y., Heo S., RA Chakravarti D.; RT "Regulation of histone acetylation and transcription by nuclear protein RT pp32, a subunit of the INHAT complex."; RL J. Biol. Chem. 277:14005-14010(2002). RN [17] RP IDENTIFICATION IN THE SET COMPLEX. RX PubMed=12628186; DOI=10.1016/s0092-8674(03)00150-8; RA Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.; RT "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL- RT mediated apoptosis, and the nucleosome assembly protein SET is its RT inhibitor."; RL Cell 112:659-672(2003). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=12524539; DOI=10.1038/ni885; RA Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., RA Pommier Y., Lieberman J.; RT "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by RT granzyme A."; RL Nat. Immunol. 4:145-153(2003). RN [19] RP PHOSPHORYLATION AT SER-158 AND SER-204, AND MUTAGENESIS OF SER-158 AND RP SER-204. RX PubMed=15287743; DOI=10.1021/bi0493968; RA Hong R., Macfarlan T., Kutney S.N., Seo S.B., Mukai Y., Yelin F., RA Pasternack G.R., Chakravarti D.; RT "The identification of phosphorylation sites of pp32 and biochemical RT purification of a cellular pp32-kinase."; RL Biochemistry 43:10157-10165(2004). RN [20] 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 [21] RP IDENTIFICATION IN THE SET COMPLEX. RX PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005; RA Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., RA Perrino F.W., Lieberman J.; RT "The exonuclease TREX1 is in the SET complex and acts in concert with NM23- RT H1 to degrade DNA during granzyme A-mediated cell death."; RL Mol. Cell 23:133-142(2006). RN [22] RP FUNCTION. RX PubMed=16341127; DOI=10.1038/sj.cdd.4401825; RA Fan Z., Zhang H., Zhang Q.; RT "Tumor suppressor pp32 represses cell growth through inhibition of RT transcription by blocking acetylation and phosphorylation of histone H3 and RT initiating its proapoptotic activity."; RL Cell Death Differ. 13:1485-1494(2006). RN [23] RP FUNCTION, AND INTERACTION WITH E4F1. RX PubMed=17557114; DOI=10.1038/sj.embor.7400983; RA Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., RA Opal P.; RT "The role of LANP and ataxin 1 in E4F-mediated transcriptional RT repression."; RL EMBO Rep. 8:671-677(2007). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [25] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ELAVL1. RX PubMed=18180367; DOI=10.1083/jcb.200709030; RA Mazroui R., Di Marco S., Clair E., von Roretz C., Tenenbaum S.A., RA Keene J.D., Saleh M., Gallouzi I.E.; RT "Caspase-mediated cleavage of HuR in the cytoplasm contributes to RT pp32/PHAP-I regulation of apoptosis."; RL J. Cell Biol. 180:113-127(2008). RN [26] RP FUNCTION. RX PubMed=18439902; DOI=10.1016/j.molcel.2008.03.014; RA Kim H.E., Jiang X., Du F., Wang X.; RT "PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 RT aggregation and enhancing nucleotide exchange on Apaf-1."; RL Mol. Cell 30:239-247(2008). RN [27] 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 [28] 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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, 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 [31] 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 [32] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA VIRUS A PROTEIN RP PB2 (MICROBIAL INFECTION), AND MUTAGENESIS OF GLU-189 AND GLU-196. RX PubMed=30666459; DOI=10.1007/s00705-018-04139-z; RA Wei X., Liu Z., Wang J., Yang R., Yang J., Guo Y., Tan H., Chen H., Liu Q., RA Liu L.; RT "The interaction of cellular protein ANP32A with influenza A virus RT polymerase component PB2 promotes vRNA synthesis."; RL Arch. Virol. 164:787-798(2019). RN [33] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=32694517; DOI=10.1038/s41467-020-17407-x; RA Camacho-Zarco A.R., Kalayil S., Maurin D., Salvi N., Delaforge E., RA Milles S., Jensen M.R., Hart D.J., Cusack S., Blackledge M.; RT "Molecular basis of host-adaptation interactions between influenza virus RT polymerase PB2 subunit and ANP32A."; RL Nat. Commun. 11:3656-3656(2020). RN [34] 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 [35] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH INFLUENZA C PROTEIN RP PB2 (MICROBIAL INFECTION). RX PubMed=33208942; DOI=10.1038/s41586-020-2927-z; RA Carrique L., Fan H., Walker A.P., Keown J.R., Sharps J., Staller E., RA Barclay W.S., Fodor E., Grimes J.M.; RT "Host ANP32A mediates the assembly of the influenza virus replicase."; RL Nature 587:638-643(2020). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-149, AND LEUCINE-RICH REPEATS. RX PubMed=17567741; DOI=10.1110/ps.072803507; RA Huyton T., Wolberger C.; RT "The crystal structure of the tumor suppressor protein pp32 (Anp32a): RT structural insights into Anp32 family of proteins."; RL Protein Sci. 16:1308-1315(2007). CC -!- FUNCTION: Multifunctional protein that is involved in the regulation of CC many processes including tumor suppression, apoptosis, cell cycle CC progression or transcription (PubMed:10400610, PubMed:11360199, CC PubMed:16341127, PubMed:18439902). Promotes apoptosis by favouring the CC activation of caspase-9/CASP9 and allowing apoptosome formation CC (PubMed:18439902). In addition, plays a role in the modulation of CC histone acetylation and transcription as part of the INHAT (inhibitor CC of histone acetyltransferases) complex. Inhibits the histone- CC acetyltransferase activity of EP300/CREBBP (CREB-binding protein) and CC EP300/CREBBP-associated factor by histone masking (PubMed:11830591). CC Preferentially binds to unmodified histone H3 and sterically inhibiting CC its acetylation and phosphorylation leading to cell growth inhibition CC (PubMed:16341127). Participates in other biochemical processes such as CC regulation of mRNA nuclear-to-cytoplasmic translocation and stability CC by its association with ELAVL1 (Hu-antigen R) (PubMed:18180367). Plays CC a role in E4F1-mediated transcriptional repression as well as CC inhibition of protein phosphatase 2A (PubMed:15642345, CC PubMed:17557114). {ECO:0000269|PubMed:10400610, CC ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:11830591, CC ECO:0000269|PubMed:15642345, ECO:0000269|PubMed:16341127, CC ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:18180367, CC ECO:0000269|PubMed:18439902}. CC -!- FUNCTION: (Microbial infection) Plays an essential role in influenza A, CC B and C viral genome replication (PubMed:30666459, PubMed:32694517, CC PubMed:33045004, PubMed:33208942). Mechanistically, mediates the CC assembly of the viral replicase asymmetric dimers composed of PB1, PB2 CC and PA via its N-terminal region (PubMed:33208942). Also plays an CC essential role in foamy virus mRNA export from the nucleus CC (PubMed:21159877). {ECO:0000269|PubMed:21159877, CC ECO:0000269|PubMed:30666459, ECO:0000269|PubMed:32694517, CC ECO:0000269|PubMed:33045004, ECO:0000269|PubMed:33208942}. CC -!- SUBUNIT: Component of the SET complex, composed of at least ANP32A, CC APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. CC Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1. CC Part of the INHAT (inhibitor of histone acetyltransferases) complex. CC Interacts with E4F1. {ECO:0000269|PubMed:11163245, CC ECO:0000269|PubMed:11555662, ECO:0000269|PubMed:11729309, CC ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, CC ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:18180367}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with CC influenza virus A protein PB2; this interaction promotes viral CC replication. {ECO:0000269|PubMed:30666459}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with CC influenza virus B protein PB2; this interaction promotes viral CC replication. {ECO:0000269|PubMed:33045004}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with CC influenza virus C protein PB2; this interaction promotes viral CC replication by bridging viral replicase dimers together. CC {ECO:0000269|PubMed:33208942}. CC -!- INTERACTION: CC P39687; P54253: ATXN1; NbExp=3; IntAct=EBI-359234, EBI-930964; CC P39687; O15169: AXIN1; NbExp=2; IntAct=EBI-359234, EBI-710484; CC P39687; Q66K89: E4F1; NbExp=3; IntAct=EBI-359234, EBI-1227043; CC P39687; P67775: PPP2CA; NbExp=2; IntAct=EBI-359234, EBI-712311; CC P39687; P63331: Ppp2ca; Xeno; NbExp=2; IntAct=EBI-359234, EBI-7050205; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11830591, CC ECO:0000269|PubMed:18180367}. Cytoplasm {ECO:0000269|PubMed:18180367}. CC Endoplasmic reticulum. Note=Translocates to the cytoplasm during the CC process of neuritogenesis (By similarity). Shuttles between nucleus and CC cytoplasm. {ECO:0000250, ECO:0000269|PubMed:18180367}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highly expressed CC in kidney and skeletal muscle, moderate levels of expression in brain, CC placenta and pancreas, and weakly expressed in lung. Found in all CC regions of the brain examined (amygdala, caudate nucleus, corpus CC callosum, hippocampus and thalamus), with highest levels in amygdala. CC {ECO:0000269|PubMed:15642345}. CC -!- PTM: Phosphorylated on serine residues, at least in part by casein CC kinase 2/CK2. {ECO:0000269|PubMed:15287743}. CC -!- PTM: The N-terminus is blocked. 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 -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD97000.1; Type=Erroneous initiation; Evidence={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; X75090; CAA52981.1; -; mRNA. DR EMBL; U60823; AAC50570.1; -; mRNA. DR EMBL; U73477; AAB39706.1; -; mRNA. DR EMBL; AF025684; AAB91548.1; -; mRNA. DR EMBL; AY349171; AAQ79832.1; -; mRNA. DR EMBL; BT007436; AAP36104.1; -; mRNA. DR EMBL; AK223280; BAD97000.1; ALT_INIT; mRNA. DR EMBL; AK312703; BAG35581.1; -; mRNA. DR EMBL; CH471082; EAW77824.1; -; Genomic_DNA. DR EMBL; BC007200; AAH07200.1; -; mRNA. DR CCDS; CCDS45292.1; -. DR PIR; S36375; S36375. DR PIR; S43309; S43309. DR RefSeq; NP_006296.1; NM_006305.4. DR PDB; 2JE0; X-ray; 2.40 A; A/B/C/D/E/F=1-149. DR PDB; 2JE1; X-ray; 2.69 A; A/B/C/D=1-149. DR PDB; 4XOS; X-ray; 1.56 A; A/B=1-149. DR PDB; 6XZQ; EM; 3.60 A; G=1-249. DR PDB; 8RMR; EM; 3.25 A; G=1-249. DR PDB; 8RN0; EM; 3.13 A; G=1-249. DR PDB; 8RNA; EM; 3.57 A; G=1-249. DR PDB; 8RNB; EM; 3.31 A; G=1-249. DR PDB; 8RNC; EM; 3.52 A; G=1-249. DR AlphaFoldDB; P39687; -. DR EMDB; EMD-10665; -. DR EMDB; EMD-19368; -. DR EMDB; EMD-19382; -. DR EMDB; EMD-19392; -. DR EMDB; EMD-19393; -. DR EMDB; EMD-19394; -. DR SASBDB; P39687; -. DR SMR; P39687; -. DR BioGRID; 113791; 152. DR ComplexPortal; CPX-26714; Inhibitor of acetyltransferases complex. DR ComplexPortal; CPX-26715; SET complex. DR CORUM; P39687; -. DR FunCoup; P39687; 3825. DR IntAct; P39687; 46. DR MINT; P39687; -. DR NDEx; IQUERY-CP-ANP32A; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000417864; -. DR BindingDB; P39687; -. DR ChEMBL; CHEMBL4295758; -. DR GlyGen; P39687; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P39687; -. DR PhosphoSitePlus; P39687; -. DR SwissPalm; P39687; -. DR BioMuta; ANP32A; -. DR DMDM; 730318; -. DR jPOST; P39687; -. DR MassIVE; P39687; -. DR PaxDb; 9606-ENSP00000417864; -. DR PeptideAtlas; P39687; -. DR ProteomicsDB; 55318; -. DR Pumba; P39687; -. DR TopDownProteomics; P39687; -. DR Antibodypedia; 3930; 492 antibodies from 40 providers. DR DNASU; 8125; -. DR Ensembl; ENST00000465139.6; ENSP00000417864.2; ENSG00000140350.16. DR GeneID; 8125; -. DR KEGG; hsa:8125; -. DR MANE-Select; ENST00000465139.6; ENSP00000417864.2; NM_006305.4; NP_006296.1. DR UCSC; uc002arl.4; human. DR AGR; HGNC:13233; -. DR ClinPGx; PA24811; -. DR CTD; 8125; -. DR DisGeNET; 8125; -. DR GeneCards; ANP32A; -. DR HGNC; HGNC:13233; ANP32A. DR HPA; ENSG00000140350; Low tissue specificity. DR MIM; 600832; gene. DR OpenTargets; ENSG00000140350; -. DR VEuPathDB; HostDB:ENSG00000140350; -. DR eggNOG; KOG2739; Eukaryota. DR GeneTree; ENSGT00950000182907; -. DR HOGENOM; CLU_063314_1_1_1; -. DR InParanoid; P39687; -. DR OMA; VTNENAY; -. DR OrthoDB; 2160613at2759; -. DR PAN-GO; P39687; 5 GO annotations based on evolutionary models. DR PhylomeDB; P39687; -. DR PathwayCommons; P39687; -. DR Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA. DR SignaLink; P39687; -. DR SIGNOR; P39687; -. DR Agora; ENSG00000140350; -. DR BioGRID-ORCS; 8125; 24 hits in 1162 CRISPR screens. DR ChiTaRS; ANP32A; human. DR EvolutionaryTrace; P39687; -. DR GenomeRNAi; 8125; -. DR Pharos; P39687; Tbio. DR PRO; PR:P39687; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P39687; protein. DR Bgee; ENSG00000140350; Expressed in ganglionic eminence and 210 other cell types or tissues. DR ExpressionAtlas; P39687; baseline and differential. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; NAS:ComplexPortal. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006284; P:base-excision repair; NAS:ComplexPortal. DR GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; NAS:ComplexPortal. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0051338; P:regulation of transferase activity; NAS:ComplexPortal. DR FunFam; 3.80.10.10:FF:000003; Acidic leucine-rich nuclear phosphoprotein 32 family member A; 1. 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:SF1; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER A; 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 PDBsum; 2JE0; -. DR PDBsum; 2JE1; -. DR PDBsum; 4XOS; -. DR PDBsum; 6XZQ; -. DR PDBsum; 8RMR; -. DR PDBsum; 8RN0; -. DR PDBsum; 8RNA; -. DR PDBsum; 8RNB; -. DR PDBsum; 8RNC; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; KW Host-virus interaction; Leucine-rich repeat; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..249 FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family FT member A" FT /id="PRO_0000137592" FT REPEAT 18..38 FT /note="LRR 1" FT /evidence="ECO:0000269|PubMed:17567741" FT REPEAT 43..64 FT /note="LRR 2" FT /evidence="ECO:0000269|PubMed:17567741" FT REPEAT 65..87 FT /note="LRR 3" FT /evidence="ECO:0000269|PubMed:17567741" FT REPEAT 89..110 FT /note="LRR 4" FT /evidence="ECO:0000269|PubMed:17567741" FT DOMAIN 123..161 FT /note="LRRCT" FT REGION 147..249 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 150..174 FT /note="Necessary for tumor-suppressive function" FT REGION 165..249 FT /note="Interaction with E4F1" FT /evidence="ECO:0000250" FT COMPBIAS 147..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 157..230 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 15 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 158 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15287743, FT ECO:0007744|PubMed:24275569" FT MOD_RES 204 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:15287743" FT MUTAGEN 158 FT /note="S->A: Complete loss of phosphorylation; when FT associated with A-204." FT /evidence="ECO:0000269|PubMed:15287743" FT MUTAGEN 158 FT /note="S->A: No loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:15287743" FT MUTAGEN 189 FT /note="E->A: Loss of interaction with influenza virus FT APB2." FT /evidence="ECO:0000269|PubMed:30666459" FT MUTAGEN 196 FT /note="E->A: Loss of interaction with influenza virus FT APB2." FT /evidence="ECO:0000269|PubMed:30666459" FT MUTAGEN 204 FT /note="S->A: Complete loss of phosphorylation; when FT associated with A-158." FT /evidence="ECO:0000269|PubMed:15287743" FT MUTAGEN 204 FT /note="S->A: No loss of phosphorylation." FT CONFLICT 186 FT /note="V -> A (in Ref. 8; BAD97000)" FT /evidence="ECO:0000305" FT HELIX 3..10 FT /evidence="ECO:0007829|PDB:4XOS" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:8RNB" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:8RN0" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:8RNB" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 81..86 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 107..111 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:4XOS" FT HELIX 131..138 FT /evidence="ECO:0007829|PDB:4XOS" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:8RNB" SQ SEQUENCE 249 AA; 28585 MW; CA2D1A756FBAEA04 CRC64; MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD //