NPAT_MOUSE
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 03-AUG-2022, entry version 118.
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; Q8BMA5; -.
DR PeptideAtlas; Q8BMA5; -.
DR PRIDE; Q8BMA5; -.
DR ProteomicsDB; 293946; -.
DR Antibodypedia; 45544; 42 antibodies from 12 providers.
DR Ensembl; ENSMUST00000035850; ENSMUSP00000048709; ENSMUSG00000033054.
DR GeneID; 244879; -.
DR KEGG; mmu:244879; -.
DR UCSC; uc009pmf.1; mouse.
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; NAECNPH; -.
DR OrthoDB; 80675at2759; -.
DR PhylomeDB; Q8BMA5; -.
DR TreeFam; TF332825; -.
DR BioGRID-ORCS; 244879; 26 hits in 75 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 223 other tissues.
DR Genevisible; Q8BMA5; MM.
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:0008022; F:protein C-terminus binding; 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:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO:MGI.
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..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
