ID NPAT_HUMAN Reviewed; 1427 AA. AC Q14207; A8K1V5; A8K6M2; Q13632; Q14967; Q16580; Q86W55; Q8IWE9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-MAR-2024, entry version 148. DE RecName: Full=Protein NPAT; DE AltName: Full=Nuclear protein of the ataxia telangiectasia mutated locus; DE Short=Nuclear protein of the ATM locus; DE AltName: Full=p220; GN Name=NPAT; Synonyms=CAND3, E14; 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], TISSUE SPECIFICITY, AND VARIANT ILE-575. RX PubMed=8743993; DOI=10.1101/gr.6.5.439; RA Imai T., Yamauchi M., Seki N., Sugawara T., Saito T., Matsuda Y., Ito H., RA Nagase T., Nomura N., Hori T.; RT "Identification and characterization of a new gene physically linked to the RT ATM gene."; RL Genome Res. 6:439-447(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS LEU-295; RP MET-399; ILE-575; ILE-621; GLU-967; VAL-973; ALA-987 AND ARG-1191. RX PubMed=8923007; DOI=10.1093/hmg/5.11.1785; RA Byrd P.J., Cooper P.R., Stankovic T., Kullar H.S., Watts G.D.J., RA Robinson P.J., Taylor A.M.R.; RT "A gene transcribed from the bidirectional ATM promoter coding for a serine RT rich protein: amino acid sequence, structure and expression studies."; RL Hum. Mol. Genet. 5:1785-1791(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-575. RX PubMed=9205109; DOI=10.1006/geno.1997.4769; RA Imai T., Sugawara T., Nishiyama A., Shimada R., Ohki R., Seki N., RA Sagara M., Ito H., Yamauchi M., Hori T.; RT "The structure and organization of the human NPAT gene."; RL Genomics 42:388-392(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PHE-540; ILE-575 AND RP LYS-999. RC TISSUE=Hippocampus, and Placenta; 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 MRNA] OF 1-1369, AND VARIANT ILE-575. RC TISSUE=Lymph, 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1169. RX PubMed=9060412; DOI=10.1007/s003359900371; RA Chen X., Yang L., Udar N., Liang T., Uhrhammer N., Xu S., Bay J.-O., RA Wang Z., Dandakar S., Chiplunkar S., Klisak I., Telatar M., Yang H., RA Concannon P., Gatti R.A.; RT "CAND3: a ubiquitously expressed gene immediately adjacent and in opposite RT transcriptional orientation to the ATM gene at 11q23.1."; RL Mamm. Genome 8:129-133(1997). RN [7] RP FUNCTION, INTERACTION WITH CCNE1 AND CDK2, DEVELOPMENTAL STAGE, AND RP PHOSPHORYLATION. RX PubMed=9472014; DOI=10.1101/gad.12.4.456; RA Zhao J., Dynlacht B., Imai T., Hori T., Harlow E.; RT "Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase RT entry."; RL Genes Dev. 12:456-461(1998). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10995386; DOI=10.1101/gad.827700; RA Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G., RA Fletcher J.A., Harlow E.; RT "NPAT links cyclin E-Cdk2 to the regulation of replication-dependent RT histone gene transcription."; RL Genes Dev. 14:2283-2297(2000). RN [9] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CCNA1; RP CCNE1 AND CDK2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-775; SER-779; RP SER-1100; THR-1270 AND THR-1350 BY CDK2, AND MUTAGENESIS OF SER-775; RP SER-779; SER-1100; THR-1270 AND THR-1350. RX PubMed=10995387; DOI=10.1101/gad.829500; RA Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., Wang J., RA Qin J., Chow L.T., Harper J.W.; RT "Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in RT Cajal bodies promotes histone gene transcription."; RL Genes Dev. 14:2298-2313(2000). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=12032824; DOI=10.1038/sj.onc.1205485; RA Kim W.-J., Vo Q.N., Shrivastav M., Lataxes T.A., Brown K.D.; RT "Aberrant methylation of the ATM promoter correlates with increased RT radiosensitivity in a human colorectal tumor cell line."; RL Oncogene 21:3864-3871(2002). RN [11] RP INTERACTION WITH GAPDH; NME1; NME2 AND STIP1. RX PubMed=12887926; DOI=10.1016/s0092-8674(03)00552-x; RA Zheng L., Roeder R.G., Luo Y.; RT "S phase activation of the histone H2B promoter by OCA-S, a coactivator RT complex that contains GAPDH as a key component."; RL Cell 114:255-266(2003). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=12665581; DOI=10.1128/mcb.23.8.2821-2833.2003; RA Gao G., Bracken A.P., Burkard K., Pasini D., Classon M., Attwooll C., RA Sagara M., Imai T., Helin K., Zhao J.; RT "NPAT expression is regulated by E2F and is essential for cell cycle RT progression."; RL Mol. Cell. Biol. 23:2821-2833(2003). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF VAL-7; LEU-10; RP VAL-11; LEU-15; GLU-18; PHE-27 AND GLU-30. RX PubMed=12724424; DOI=10.1128/mcb.23.10.3669-3680.2003; RA Wei Y., Jin J., Harper J.W.; RT "The cyclin E/Cdk2 substrate and Cajal body component p220(NPAT) activates RT histone transcription through a novel LisH-like domain."; RL Mol. Cell. Biol. 23:3669-3680(2003). RN [14] RP FUNCTION, AND MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND RP THR-1350. RX PubMed=14585971; DOI=10.1128/mcb.23.22.8110-8123.2003; RA Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., RA Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.; RT "Identification of HiNF-P, a key activator of cell cycle-controlled histone RT H4 genes at the onset of S phase."; RL Mol. Cell. Biol. 23:8110-8123(2003). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=14612403; DOI=10.1128/mcb.23.23.8586-8600.2003; RA Ye X., Wei Y., Nalepa G., Harper J.W.; RT "The cyclin E/Cdk2 substrate p220(NPAT) is required for S-phase entry, RT histone gene expression, and Cajal body maintenance in human somatic RT cells."; RL Mol. Cell. Biol. 23:8586-8600(2003). RN [16] RP FUNCTION, INTERACTION WITH CCNE1 AND CREBBP, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND THR-1350. RX PubMed=15555599; DOI=10.1016/j.bbrc.2004.10.198; RA Wang A., Ikura T., Eto K., Ota M.S.; RT "Dynamic interaction of p220(NPAT) and CBP/p300 promotes S-phase entry."; RL Biochem. Biophys. Res. Commun. 325:1509-1516(2004). RN [17] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=14976556; DOI=10.1038/sj.emboj.7600120; RA Su C., Gao G., Schneider S., Helt C., Weiss C., O'Reilly M.A., Bohmann D., RA Zhao J.; RT "DNA damage induces downregulation of histone gene expression through the RT G1 checkpoint pathway."; RL EMBO J. 23:1133-1143(2004). RN [18] RP FUNCTION. RX PubMed=16131487; DOI=10.1074/jbc.m506995200; RA Holmes W.F., Braastad C.D., Mitra P., Hampe C., Doenecke D., Albig W., RA Stein J.L., van Wijnen A.J., Stein G.S.; RT "Coordinate control and selective expression of the full complement of RT replication-dependent histone H4 genes in normal and cancer cells."; RL J. Biol. Chem. 280:37400-37407(2005). RN [19] RP FUNCTION, INTERACTION WITH MIZF, AND SUBCELLULAR LOCATION. RX PubMed=15988025; DOI=10.1128/mcb.25.14.6140-6153.2005; RA Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., RA Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., RA Stein G.S.; RT "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 RT gene regulation at the G1/S phase cell cycle transition."; RL Mol. Cell. Biol. 25:6140-6153(2005). RN [20] RP SUBCELLULAR LOCATION. RX PubMed=17068332; DOI=10.1074/jbc.m608165200; RA Gangwani L.; RT "Deficiency of the zinc finger protein ZPR1 causes defects in transcription RT and cell cycle progression."; RL J. Biol. Chem. 281:40330-40340(2006). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=16972248; DOI=10.1002/jcp.20776; RA Becker K.A., Ghule P.N., Therrien J.A., Lian J.B., Stein J.L., RA van Wijnen A.J., Stein G.S.; RT "Self-renewal of human embryonic stem cells is supported by a shortened G1 RT cell cycle phase."; RL J. Cell. Physiol. 209:883-893(2006). RN [22] RP INTERACTION WITH CASP8AP2, AND SUBCELLULAR LOCATION. RX PubMed=17003125; DOI=10.1073/pnas.0604227103; RA Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M., RA Knight R.A., Matera A.G., Melino G., De Laurenzi V.; RT "FLASH is required for histone transcription and S-phase progression."; RL Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006). RN [23] RP FUNCTION. RX PubMed=17974976; DOI=10.1158/0008-5472.can-07-1560; RA Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., RA van Wijnen A.J., Stein J.L., Stein G.S.; RT "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone RT target genes."; RL Cancer Res. 67:10334-10342(2007). RN [24] RP FUNCTION. RX PubMed=17826007; DOI=10.1016/j.gene.2007.07.027; RA Xie R.-L., Liu L., Mitra P., Stein J.L., van Wijnen A.J., Stein G.S.; RT "Transcriptional activation of the histone nuclear factor P (HiNF-P) gene RT by HiNF-P and its cyclin E/CDK2 responsive co-factor p220NPAT defines a RT novel autoregulatory loop at the G1/S phase transition."; RL Gene 402:94-102(2007). RN [25] RP FUNCTION, AND MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND RP THR-1350. RX PubMed=17163457; DOI=10.1002/jcb.21157; RA Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.; RT "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 RT gene transcription."; RL J. Cell. Biochem. 101:181-191(2007). RN [26] RP DEVELOPMENTAL STAGE, AND INDUCTION. RX PubMed=17096384; DOI=10.1002/jcp.20903; RA Becker K.A., Stein J.L., Lian J.B., van Wijnen A.J., Stein G.S.; RT "Establishment of histone gene regulation and cell cycle checkpoint control RT in human embryonic stem cells."; RL J. Cell. Physiol. 210:517-526(2007). RN [27] RP SUBCELLULAR LOCATION. RX PubMed=17520687; DOI=10.1002/jcp.21119; RA Ghule P.N., Becker K.A., Harper J.W., Lian J.B., Stein J.L., RA van Wijnen A.J., Stein G.S.; RT "Cell cycle dependent phosphorylation and subnuclear organization of the RT histone gene regulator p220(NPAT) in human embryonic stem cells."; RL J. Cell. Physiol. 213:9-17(2007). RN [28] RP FUNCTION, INTERACTION WITH BZW1; RUVBL1; RUVBL2; TRRAP AND YY1, AND RP MUTAGENESIS OF 331-LEU--ASP-333. RX PubMed=17967892; DOI=10.1128/mcb.00607-07; RA DeRan M., Pulvino M., Greene E., Su C., Zhao J.; RT "Transcriptional activation of histone genes requires NPAT-dependent RT recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S RT phase transition."; RL Mol. Cell. Biol. 28:435-447(2008). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1228, 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 [31] RP IDENTIFICATION BY 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 [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-554; SER-1151; RP SER-1200 AND THR-1350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [33] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1116; LYS-1149 AND LYS-1280, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- FUNCTION: Required for progression through the G1 and S phases of the CC cell cycle and for S phase entry. Activates transcription of the CC histone H2A, histone H2B, histone H3 and histone H4 genes in CC conjunction with MIZF. Also positively regulates the ATM, MIZF and CC PRKDC promoters. Transcriptional activation may be accomplished at CC least in part by the recruitment of the NuA4 histone acetyltransferase CC (HAT) complex to target gene promoters. {ECO:0000269|PubMed:10995386, CC ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:12665581, CC ECO:0000269|PubMed:12724424, ECO:0000269|PubMed:14585971, CC ECO:0000269|PubMed:14612403, ECO:0000269|PubMed:15555599, CC ECO:0000269|PubMed:15988025, ECO:0000269|PubMed:16131487, CC ECO:0000269|PubMed:17163457, ECO:0000269|PubMed:17826007, CC ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:17974976, CC ECO:0000269|PubMed:9472014}. CC -!- SUBUNIT: Interacts with the cylin/CDK complexes CCNE1/CDK2 and CC CCNA1/CDK2. Interacts with BZW1, CASP8AP2, CREBBP, MIZF and YY1. CC Interacts with the RUVBL1, RUVBL2 and TRRAP subunits of the NuA4 CC complex. May also interact with GAPDH, NME1, NME2 and STIP1. CC {ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:12887926, CC ECO:0000269|PubMed:15555599, ECO:0000269|PubMed:15988025, CC ECO:0000269|PubMed:17003125, ECO:0000269|PubMed:17967892, CC ECO:0000269|PubMed:9472014}. CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, Cajal body. Note=Concentrates CC in two Cajal bodies tethered to histone gene clusters at chromosome CC 6p21 during G1, S and G2 phases. Also concentrates in two additional CC Cajal bodies tethered to histone gene clusters at chromosome 1q21 CC specifically during S and G2 phases. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:8743993, ECO:0000269|PubMed:8923007}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle. Expression CC peaks at the G1/S phase boundary and declines during S phase. CC {ECO:0000269|PubMed:17096384, ECO:0000269|PubMed:9472014}. CC -!- INDUCTION: By expression of E2F1, E2F2, E2F3 and E2F4. Expression is CC reduced in response to radiation-induced DNA damage. CC {ECO:0000269|PubMed:12665581, ECO:0000269|PubMed:17096384}. CC -!- DOMAIN: The LisH domain is required for the activation of histone gene CC transcription. {ECO:0000269|PubMed:12724424}. CC -!- PTM: Phosphorylated at Ser-775, Ser-779, Ser-1100, Thr-1270 and Thr- CC 1350 by CCNE1/CDK2 at G1-S transition and until prophase, which CC promotes association with histone gene clusters and stimulates CC activation of histone transcription. Also phosphorylated by CCNA1/CDK2 CC in vitro. {ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:14976556, CC ECO:0000269|PubMed:9472014}. CC -!- SIMILARITY: Belongs to the NPAT family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB02735.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. A chimeric cDNA originating from chromosomes 11 and 4.; Evidence={ECO:0000305}; CC Sequence=AAH40356.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAH50561.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; D83243; BAA11861.1; -; mRNA. DR EMBL; X97186; CAA65824.1; -; mRNA. DR EMBL; D89854; BAA21367.1; -; Genomic_DNA. DR EMBL; AK290020; BAF82709.1; -; mRNA. DR EMBL; AK291687; BAF84376.1; -; mRNA. DR EMBL; BC040356; AAH40356.1; ALT_SEQ; mRNA. DR EMBL; BC050561; AAH50561.1; ALT_SEQ; mRNA. DR EMBL; U58852; AAB02735.1; ALT_SEQ; mRNA. DR CCDS; CCDS41710.1; -. DR RefSeq; NP_002510.2; NM_002519.2. DR AlphaFoldDB; Q14207; -. DR SMR; Q14207; -. DR BioGRID; 110924; 68. DR DIP; DIP-59961N; -. DR ELM; Q14207; -. DR IntAct; Q14207; 21. DR STRING; 9606.ENSP00000278612; -. DR GlyGen; Q14207; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q14207; -. DR PhosphoSitePlus; Q14207; -. DR BioMuta; NPAT; -. DR DMDM; 296439285; -. DR EPD; Q14207; -. DR jPOST; Q14207; -. DR MassIVE; Q14207; -. DR MaxQB; Q14207; -. DR PaxDb; 9606-ENSP00000278612; -. DR PeptideAtlas; Q14207; -. DR ProteomicsDB; 59930; -. DR Pumba; Q14207; -. DR Antibodypedia; 45544; 51 antibodies from 12 providers. DR DNASU; 4863; -. DR Ensembl; ENST00000278612.9; ENSP00000278612.8; ENSG00000149308.17. DR GeneID; 4863; -. DR KEGG; hsa:4863; -. DR MANE-Select; ENST00000278612.9; ENSP00000278612.8; NM_002519.3; NP_002510.2. DR UCSC; uc001pjz.6; human. DR AGR; HGNC:7896; -. DR CTD; 4863; -. DR DisGeNET; 4863; -. DR GeneCards; NPAT; -. DR HGNC; HGNC:7896; NPAT. DR HPA; ENSG00000149308; Low tissue specificity. DR MIM; 601448; gene. DR neXtProt; NX_Q14207; -. DR OpenTargets; ENSG00000149308; -. DR PharmGKB; PA31697; -. DR VEuPathDB; HostDB:ENSG00000149308; -. DR eggNOG; ENOG502QYUR; Eukaryota. DR GeneTree; ENSGT00390000012388; -. DR HOGENOM; CLU_004845_0_0_1; -. DR InParanoid; Q14207; -. DR OMA; CFDNVLP; -. DR OrthoDB; 2917859at2759; -. DR PhylomeDB; Q14207; -. DR TreeFam; TF332825; -. DR PathwayCommons; Q14207; -. DR SignaLink; Q14207; -. DR SIGNOR; Q14207; -. DR BioGRID-ORCS; 4863; 738 hits in 1165 CRISPR screens. DR ChiTaRS; NPAT; human. DR GeneWiki; NPAT_(gene); -. DR GenomeRNAi; 4863; -. DR Pharos; Q14207; Tbio. DR PRO; PR:Q14207; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q14207; Protein. DR Bgee; ENSG00000149308; Expressed in secondary oocyte and 195 other cell types or tissues. DR ExpressionAtlas; Q14207; baseline and differential. DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB. DR GO; GO:0044843; P:cell cycle G1/S phase transition; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR InterPro; IPR006594; LisH. DR InterPro; IPR031442; NPAT_C. DR PANTHER; PTHR15087; PROTEIN NPAT; 1. DR PANTHER; PTHR15087:SF14; PROTEIN NPAT; 1. DR Pfam; PF15712; NPAT_C; 1. DR SMART; SM00667; LisH; 1. DR PROSITE; PS50896; LISH; 1. DR Genevisible; Q14207; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Cell cycle; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1427 FT /note="Protein NPAT" FT /id="PRO_0000318163" FT DOMAIN 3..35 FT /note="LisH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126" FT REGION 1..318 FT /note="Interaction with MIZF" FT /evidence="ECO:0000269|PubMed:15988025" FT REGION 5..25 FT /note="Required for activation of histone gene FT transcription and interaction with MIZF" FT /evidence="ECO:0000269|PubMed:15988025" FT REGION 121..145 FT /note="Required for activation of histone gene FT transcription and interaction with MIZF" FT /evidence="ECO:0000269|PubMed:15988025" FT REGION 199..231 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 262..338 FT /note="Mediates transcriptional activation" FT REGION 628..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 629..653 FT /note="Required for acceleration of G1 phase" FT REGION 683..732 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 828..853 FT /note="Required for acceleration of G1 phase" FT REGION 1039..1054 FT /note="Required for acceleration of G1 phase" FT REGION 1095..1121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1133..1152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1228..1252 FT /note="Required for acceleration of G1 phase" FT REGION 1253..1327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1325..1349 FT /note="Required for acceleration of G1 phase" FT REGION 1348..1413 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 693..732 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1095..1112 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1274..1292 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1348..1363 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1366..1384 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 554 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 599 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BMA5" FT MOD_RES 775 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:10995387" FT MOD_RES 779 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:10995387" FT MOD_RES 1100 FT /note="Phosphoserine; by CDK2" FT /evidence="ECO:0000269|PubMed:10995387" FT MOD_RES 1151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1200 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1228 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1254 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BMA5" FT MOD_RES 1270 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000269|PubMed:10995387" FT MOD_RES 1350 FT /note="Phosphothreonine; by CDK2" FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 1116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1149 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1280 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 295 FT /note="I -> L (in dbSNP:rs1131748)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038696" FT VARIANT 399 FT /note="L -> M (in dbSNP:rs1051521)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038697" FT VARIANT 447 FT /note="V -> M (in dbSNP:rs35504388)" FT /id="VAR_038698" FT VARIANT 483 FT /note="I -> L (in dbSNP:rs968207)" FT /id="VAR_038699" FT VARIANT 540 FT /note="L -> F (in dbSNP:rs4144901)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_038700" FT VARIANT 575 FT /note="V -> I (in dbSNP:rs2070661)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8743993, FT ECO:0000269|PubMed:8923007, ECO:0000269|PubMed:9205109" FT /id="VAR_038701" FT VARIANT 608 FT /note="V -> A (in dbSNP:rs35095430)" FT /id="VAR_038702" FT VARIANT 621 FT /note="V -> I (in dbSNP:rs1051522)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038703" FT VARIANT 967 FT /note="Q -> E (in dbSNP:rs1131750)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038704" FT VARIANT 973 FT /note="L -> V (in dbSNP:rs1131751)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038705" FT VARIANT 987 FT /note="V -> A (in dbSNP:rs1051524)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038706" FT VARIANT 999 FT /note="N -> K (in dbSNP:rs34052882)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_038707" FT VARIANT 1191 FT /note="Q -> R (in dbSNP:rs1051525)" FT /evidence="ECO:0000269|PubMed:8923007" FT /id="VAR_038708" FT MUTAGEN 7 FT /note="V->A: Impairs activation of histone gene FT transcription; when associated with A-10; A-11; A-15 and FT A-18." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 10 FT /note="L->A: Impairs activation of histone gene FT transcription; when associated with A-7; A-11; A-15 and FT A-18." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 11 FT /note="V->A: Impairs activation of histone gene FT transcription; when associated with A-7; A-10; A-15 and FT A-18." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 15 FT /note="L->A: Impairs activation of histone gene FT transcription; when associated with A-7; A-10; A-11 and FT A-18." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 18 FT /note="E->A: Impairs activation of histone gene FT transcription; when associated with A-7; A-10; A-11 and FT A-15." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 27 FT /note="F->A: Impairs activation of histone gene FT transcription; when associated with A-30." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 30 FT /note="E->A: Impairs activation of histone gene FT transcription; when associated with A-27." FT /evidence="ECO:0000269|PubMed:12724424" FT MUTAGEN 331..333 FT /note="LFD->AAA: Impairs activation of histone gene FT transcription. Impairs interaction with BZW1, RUVBL1, FT RUVBL2 and TRRAP." FT /evidence="ECO:0000269|PubMed:17967892" FT MUTAGEN 775 FT /note="S->A: Impairs activation of histone gene FT transcription; when associated with A-779; A-1100; A-1270 FT and A-1350." FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15555599, FT ECO:0000269|PubMed:17163457" FT MUTAGEN 779 FT /note="S->A: Impairs activation of histone gene FT transcription; when associated with A-775; A-1100; A-1270 FT and A-1350." FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15555599, FT ECO:0000269|PubMed:17163457" FT MUTAGEN 1100 FT /note="S->A: Impairs activation of histone gene FT transcription; when associated with A-775; A-779; A-1270 FT and A-1350." FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15555599, FT ECO:0000269|PubMed:17163457" FT MUTAGEN 1270 FT /note="T->A: Impairs activation of histone gene FT transcription; when associated with A-775; A-779; A-1100 FT and A-1350." FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15555599, FT ECO:0000269|PubMed:17163457" FT MUTAGEN 1350 FT /note="T->A: Impairs activation of histone gene FT transcription; when associated with A-775; A-779; A-1100 FT and A-1270." FT /evidence="ECO:0000269|PubMed:10995387, FT ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15555599, FT ECO:0000269|PubMed:17163457" FT CONFLICT 22 FT /note="S -> Y (in Ref. 6; AAB02735)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="S -> N (in Ref. 4; BAF84376)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="F -> L (in Ref. 4; BAF84376)" FT /evidence="ECO:0000305" FT CONFLICT 471 FT /note="Y -> N (in Ref. 2; CAA65824)" FT /evidence="ECO:0000305" FT CONFLICT 785 FT /note="E -> G (in Ref. 4; BAF82709)" FT /evidence="ECO:0000305" FT CONFLICT 1145 FT /note="Q -> R (in Ref. 4; BAF82709)" FT /evidence="ECO:0000305" SQ SEQUENCE 1427 AA; 154290 MW; D5C5E630A56227F9 CRC64; MLLPSDVARL VLGYLQQENL ISTCQTFILE SSDLKEYAEH CTDEGFIPAC LLSLFGKNLT TILNEYVAMK TKETSNNVPA IMSSLWKKLD HTLSQIRSMQ SSPRFAGSQR ARTRTGIAEI KRQRKLASQT APASAELLTL PYLSGQFTTP PSTGTQVTRP SGQISDPSRS YFVVVNHSQS QDTVTTGEAL NVIPGAQEKK AHASLMSPGR RKSESQRKST TLSGPHSTIR NFQDPNAFAV EKQMVIENAR EKILSNKSLQ EKLAENINKF LTSDNNIAQV PKQTDNNPTE PETSIDEFLG LPSEIHMSEE AIQDILEQTE SDPAFQALFD LFDYGKTKNN KNISQSISSQ PMESNPSIVL ADETNLAVKG SFETEESDGQ SGQPAFCTSY QNDDPLNALK NSNNHDVLRQ EDQENFSQIS TSIQKKAFKT AVPTEQKCDI DITFESVPNL NDFNQRGNSN AECNPHCAEL YTNQMSTETE MAIGIEKNSL SSNVPSESQL QPDQPDIPIT SFVSLGCEAN NENLILSGKS SQLLSQDTSL TGKPSKKSQF CENSNDTVKL KINFHGSKSS DSSEVHKSKI EINVLEPVMS QLSNCQDNSC LQSEILPVSV ESSHLNVSGQ VEIHLGDSLS STKQPSNDSA SVELNHTENE AQASKSENSQ EPSSSVKEEN TIFLSLGGNA NCEKVALTPP EGTPVENSHS LPPESVCSSV GDSHPESQNT DDKPSSNNSA EIDASNIVSL KVIISDDPFV SSDTELTSAV SSINGENLPT IILSSPTKSP TKNAELVKCL SSEETVGAVV YAEVGDSASM EQSLLTFKSE DSAVNNTQNE DGIAFSANVT PCVSKDGGYI QLMPATSTAF GNSNNILIAT CVTDPTALGT SVSQSNVVVL PGNSAPMTAQ PLPPQLQTPP RSNSVFAVNQ AVSPNFSQGS AIIIASPVQP VLQGMVGMIP VSVVGQNGNN FSTPPRQVLH MPLTAPVCNR SIPQFPVPPK SQKAQGLRNK PCIGKQVNNL VDSSGHSVGC HAQKTEVSDK SIATDLGKKS EETTVPFPEE SIVPAAKPCH RRVLCFDSTT APVANTQGPN HKMVSQNKER NAVSFPNLDS PNVSSTLKPP SNNAIKREKE KPPLPKILSK SESAISRHTT IRETQSEKKV SPTEIVLESF HKATANKENE LCSDVERQKN PENSKLSIGQ QNGGLRSEKS IASLQEMTKK QGTSSNNKNV LSVGTAVKDL KQEQTKSASS LITTEMLQDI QRHSSVSRLA DSSDLPVPRT PGSGAGEKHK EEPIDIIKAP SSRRFSEDSS TSKVMVPPVT PDLPACSPAS ETGSENSVNM AAHTLMILSR AAISRTTSAT PLKDNTQQFR ASSRSTTKKR KIEELDERER NSRPSSKNLT NSSIPMKKKK IKKKKLPSSF PAGMDVDKFL LSLHYDE //