NPAT_HUMAN
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 03-AUG-2022, entry version 139.
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};
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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; 59.
DR DIP; DIP-59961N; -.
DR ELM; Q14207; -.
DR IntAct; Q14207; 23.
DR STRING; 9606.ENSP00000278612; -.
DR GlyGen; Q14207; 1 site, 1 O-linked glycan (1 site).
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; Q14207; -.
DR PeptideAtlas; Q14207; -.
DR PRIDE; Q14207; -.
DR ProteomicsDB; 59930; -.
DR Antibodypedia; 45544; 42 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 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; NAECNPH; -.
DR OrthoDB; 80675at2759; -.
DR PhylomeDB; Q14207; -.
DR TreeFam; TF332825; -.
DR PathwayCommons; Q14207; -.
DR SignaLink; Q14207; -.
DR SIGNOR; Q14207; -.
DR BioGRID-ORCS; 4863; 717 hits in 1087 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 194 other tissues.
DR ExpressionAtlas; Q14207; baseline and differential.
DR Genevisible; Q14207; HS.
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:0008022; F:protein C-terminus binding; IPI: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:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR031442; NPAT_C.
DR Pfam; PF15712; NPAT_C; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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
