ID   NPAT_MOUSE              Reviewed;        1420 AA.
AC   Q8BMA5; Q8BWA9; Q8BY06;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Protein NPAT;
GN   Name=Npat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=9199343; DOI=10.1128/mcb.17.7.4080;
RA   Di Fruscio M., Weiher H., Vanderhyden B.C., Imai T., Shiomi T., Hori T.,
RA   Jaenisch R., Gray D.A.;
RT   "Proviral inactivation of the Npat gene of Mpv 20 mice results in early
RT   embryonic arrest.";
RL   Mol. Cell. Biol. 17:4080-4086(1997).
RN   [4]
RP   DEVELOPMENTAL STAGE.
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   [5]
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598 AND SER-1249, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). Required for
CC       early embryonic development. {ECO:0000250, ECO:0000269|PubMed:9199343}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17003125}.
CC       Note=Concentrates in Cajal bodies tethered to histone gene clusters.
CC       {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expression peaks at the G1/S phase boundary.
CC       {ECO:0000269|PubMed:12665581}.
CC   -!- DOMAIN: The LisH domain is required for the activation of histone gene
CC       transcription. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-771, Ser-773, Ser-1096, Thr-1264 and Thr-
CC       1343 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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NPAT family. {ECO:0000305}.
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DR   EMBL; AK033012; BAC28125.1; -; mRNA.
DR   EMBL; AK042624; BAC31308.1; -; mRNA.
DR   EMBL; AK053074; BAC35255.1; -; mRNA.
DR   EMBL; AC156640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS40637.1; -.
DR   RefSeq; NP_001074621.1; NM_001081152.1.
DR   AlphaFoldDB; Q8BMA5; -.
DR   SMR; Q8BMA5; -.
DR   BioGRID; 232697; 3.
DR   STRING; 10090.ENSMUSP00000048709; -.
DR   iPTMnet; Q8BMA5; -.
DR   PhosphoSitePlus; Q8BMA5; -.
DR   EPD; Q8BMA5; -.
DR   jPOST; Q8BMA5; -.
DR   MaxQB; Q8BMA5; -.
DR   PaxDb; 10090-ENSMUSP00000048709; -.
DR   PeptideAtlas; Q8BMA5; -.
DR   ProteomicsDB; 293946; -.
DR   Pumba; Q8BMA5; -.
DR   Antibodypedia; 45544; 51 antibodies from 12 providers.
DR   Ensembl; ENSMUST00000035850.8; ENSMUSP00000048709.8; ENSMUSG00000033054.8.
DR   GeneID; 244879; -.
DR   KEGG; mmu:244879; -.
DR   UCSC; uc009pmf.1; mouse.
DR   AGR; MGI:107605; -.
DR   CTD; 4863; -.
DR   MGI; MGI:107605; Npat.
DR   VEuPathDB; HostDB:ENSMUSG00000033054; -.
DR   eggNOG; ENOG502QYUR; Eukaryota.
DR   GeneTree; ENSGT00390000012388; -.
DR   HOGENOM; CLU_004845_0_0_1; -.
DR   InParanoid; Q8BMA5; -.
DR   OMA; CFDNVLP; -.
DR   OrthoDB; 2917859at2759; -.
DR   PhylomeDB; Q8BMA5; -.
DR   TreeFam; TF332825; -.
DR   BioGRID-ORCS; 244879; 26 hits in 80 CRISPR screens.
DR   ChiTaRS; Npat; mouse.
DR   PRO; PR:Q8BMA5; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BMA5; Protein.
DR   Bgee; ENSMUSG00000033054; Expressed in manus and 226 other cell types or tissues.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0044843; P:cell cycle G1/S phase transition; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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; Q8BMA5; MM.
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..1420
FT                   /note="Protein NPAT"
FT                   /id="PRO_0000318164"
FT   DOMAIN          3..35
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          1..319
FT                   /note="Interaction with MIZF"
FT                   /evidence="ECO:0000250"
FT   REGION          5..25
FT                   /note="Required for activation of histone gene
FT                   transcription and interaction with MIZF"
FT                   /evidence="ECO:0000250"
FT   REGION          121..145
FT                   /note="Required for activation of histone gene
FT                   transcription and interaction with MIZF"
FT                   /evidence="ECO:0000250"
FT   REGION          179..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..339
FT                   /note="Mediates transcriptional activation"
FT                   /evidence="ECO:0000250"
FT   REGION          534..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..652
FT                   /note="Required for acceleration of G1 phase"
FT                   /evidence="ECO:0000250"
FT   REGION          696..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..847
FT                   /note="Required for acceleration of G1 phase"
FT                   /evidence="ECO:0000250"
FT   REGION          1033..1048
FT                   /note="Required for acceleration of G1 phase"
FT                   /evidence="ECO:0000250"
FT   REGION          1089..1190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1202..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1223..1247
FT                   /note="Required for acceleration of G1 phase"
FT                   /evidence="ECO:0000250"
FT   REGION          1249..1297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1342
FT                   /note="Required for acceleration of G1 phase"
FT                   /evidence="ECO:0000250"
FT   REGION          1348..1400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         598
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         771
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         773
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         1096
FT                   /note="Phosphoserine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         1146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         1223
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         1249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1264
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   MOD_RES         1343
FT                   /note="Phosphothreonine; by CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   CROSSLNK        1112
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   CROSSLNK        1144
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   CROSSLNK        1274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14207"
FT   CONFLICT        1141
FT                   /note="S -> P (in Ref. 1; BAC35255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1420 AA;  152176 MW;  1035459489343314 CRC64;
     MLLPSDVARL VLGYLQQENL TSTCQTFILE SSNLKEYAEH CTDEGFIPAC LLSLFGKNLT
     TILNEYVAMK AKETSNDVPT IMSSLWKKLD HTLSQIRSMH SSPGFAAHQR ARTRNGIAEI
     KRQRWLASQA APVSSELLVL PYASGQFTTS PLVATQAVKP TGPISTPVRS NIVVVNQSQP
     QSTVTNTAGE SLNIIPGPQE RKTQTSLMSP GRRKSESQKK SLTSSGPHSS RNFQDPNAFA
     VEKQMVIENA REKILSNKSL QEKLAENINK FLTSDSSVAQ VPKQTDSNPT EPETSIDELL
     GLPSEIHMSE EAIQDILEQT ESDPAFQALF DLFDYGKTKN NKNMPQISSQ PMETNSNIVL
     PEETNLTIKS SFETEESDGQ SGQPPFCTSY QNEDVLLNDL KSGNSHDVLP QESQENFSQI
     SSNIQKKTFK TAIPAEQKCA LDITLESVSN LSDFNQRGSS AECNEHCSEL FASQIPTEAE
     VAVGEKNSLS ADILSQSQYQ PDQPSVPVTS FVSLGGETND KNLVLSGKNS QLLSQSTPLT
     TKPSKSQLCE NSNNIIKVKT NPQASESADS SETANRKTET NTVSPAAAQP QADCQDNSPL
     QSKPPPGIGE SLGVNVTEKI EIHLEEPAPS DKQLSNDAAS VDLNPTESKT EPLQSASAQE
     PEPPSVKDGD TIFLSLSEHN SCEEVALVLG EGNPVKNNNS LSSESGGSVG VSPETQNTDG
     KTSNSTEVDA SSIVSLKIII SDDPFVSSDA ELNSAVSSIS GENLPTIILS SKSPAKNAEF
     VTCLSSEETA SAVVSVEVGD SGSMEQNLLV LKPEEPMVNN TQNEDGIAFS ANVAPCVPKD
     GGYIQLMPTT STAFGNSSNI LIATCMTDST ALGPTVSQSN VVVLPGSSAP MTAQPPQQQL
     QTPPKSNSAF AVSQAVSPNF SQGSAIIIAS PVQPVLQGMV GMIPVSVVGQ NGNTFSTPPQ
     QVLHMPLAAP VCNRSIAQLP IPQKSQKAQG LRNKLITGKQ VNNLTNLSSL SEACHTQRTE
     ASDKNIATEL GKKMEDTTIS LSGERVAPPS KPFESHRRVL CFDSTVSSVA NTQGSLYKMT
     SENKEKKEAS FSHLDSPILS STLKPPPNNA IKREREKTVP KILSKSETAS SRHTTVKEVQ
     SEKKVSPTEV ALESLHKATA NKENELCGDG ERPKNADTSK LPGGQQNGSL RNEKAIASLQ
     ELTKKQATPS NNKNATSVGG TVKDQKQEQS KPASSLIGAE ILQDVPIHSP ANRSADTDLP
     VPRTPGSGAG EKHKEEPSDS MKAPASRRCG EEGSMPRVMI PPVTADLPAC SPASETGSEN
     SVSMAAHTLM ILSRAAIART TATPLKDNTQ QFRTSSRSTT KKRKIEELDE CERNSRTSGK
     NLANSSVPMK KKKIKKKKLP SSFPAGMDVD KFLLSLHYDE
//