NP1L2_MOUSE
ID NP1L2_MOUSE Reviewed; 460 AA.
AC P51860; Q8K3R9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nucleosome assembly protein 1-like 2;
DE AltName: Full=Brain-specific protein, X-linked;
GN Name=Nap1l2; Synonyms=Bpx;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8789438; DOI=10.1093/hmg/5.1.41;
RA Rougeulle C., Avner P.;
RT "Cloning and characterization of a murine brain specific gene Bpx and its
RT human homologue lying within the Xic candidate region.";
RL Hum. Mol. Genet. 5:41-49(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=12045143; DOI=10.1101/gr.152902;
RA Chureau C., Prissette M., Bourdet A., Barbe V., Cattolico L., Jones L.,
RA Eggen A., Avner P., Duret L.;
RT "Comparative sequence analysis of the X-inactivation center region in
RT mouse, human and bovine.";
RL Genome Res. 12:894-908(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Acidic protein which may be involved in interactions with
CC other proteins or DNA.
CC -!- INTERACTION:
CC P51860; Q9UHL9: GTF2IRD1; Xeno; NbExp=3; IntAct=EBI-12516895, EBI-372530;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain, specifically expressed in neurons.
CC -!- DEVELOPMENTAL STAGE: First expressed around the day 7 embryo.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; X92352; CAA63109.1; -; mRNA.
DR EMBL; AJ421480; CAD33966.1; -; Genomic_DNA.
DR EMBL; AK051439; BAC34638.1; -; mRNA.
DR EMBL; AK131621; BAE20726.1; -; mRNA.
DR EMBL; AL773526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466564; EDL14110.1; -; Genomic_DNA.
DR EMBL; BC115708; AAI15709.1; -; mRNA.
DR EMBL; BC115761; AAI15762.1; -; mRNA.
DR CCDS; CCDS53164.1; -.
DR RefSeq; NP_032697.2; NM_008671.2.
DR AlphaFoldDB; P51860; -.
DR SMR; P51860; -.
DR BioGRID; 201691; 9.
DR IntAct; P51860; 1.
DR STRING; 10090.ENSMUSP00000112677; -.
DR PhosphoSitePlus; P51860; -.
DR MaxQB; P51860; -.
DR PaxDb; P51860; -.
DR PRIDE; P51860; -.
DR ProteomicsDB; 293711; -.
DR Antibodypedia; 27991; 138 antibodies from 20 providers.
DR DNASU; 17954; -.
DR Ensembl; ENSMUST00000121720; ENSMUSP00000112677; ENSMUSG00000082229.
DR GeneID; 17954; -.
DR KEGG; mmu:17954; -.
DR UCSC; uc009tzi.2; mouse.
DR CTD; 4674; -.
DR MGI; MGI:106654; Nap1l2.
DR VEuPathDB; HostDB:ENSMUSG00000082229; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000163372; -.
DR HOGENOM; CLU_038841_3_1_1; -.
DR InParanoid; P51860; -.
DR OMA; WMAAIEE; -.
DR OrthoDB; 1216172at2759; -.
DR PhylomeDB; P51860; -.
DR TreeFam; TF314349; -.
DR BioGRID-ORCS; 17954; 2 hits in 74 CRISPR screens.
DR PRO; PR:P51860; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P51860; protein.
DR Bgee; ENSMUSG00000082229; Expressed in pontine nuclear group and 154 other tissues.
DR Genevisible; P51860; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:MGI.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:MGI.
DR GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; IDA:MGI.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome.
FT CHAIN 1..460
FT /note="Nucleosome assembly protein 1-like 2"
FT /id="PRO_0000185656"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 346..352
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 213..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 385
FT /note="D -> V (in Ref. 1; CAA63109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 52158 MW; A55AF60553862E82 CRC64;
MAESVDHKEL SESNQEELGS QVMAEGPGES QDRSEGVSIE PGDGGQHGEE TVAAGVGEEG
KGEEAAAGSG EDAGKCGGTD EDSDSDRPKG LIGYLLDTDF VESLPVKVKC RVLALKKLQT
RAAHLESKFL REFHDIERKF AEMYQPLLEK RRQIINAVYE PTEEECEYKS DCEDYFEEEM
DEEEETNGNE DGMVHEYVDE DDGYEDCYYD YDDEEEEEEE DDSAGATGGE EVNEEDPKGI
PDFWLTVLKN VEALTPMIKK YDEPILKLLT DIKVKLSDPG EPLSFTLEFH FKPNEYFKNE
LLTKTYVLKS KLACYDPHPY RGTAIEYATG CDIDWNEGKN VTLRTIKKKQ RHRVWGTVRT
VTEDFPKDSF FNFFSPHGIS LNGGDENDDF LLGHNLRTYI IPRSVLFFSG DALESQQEGV
VREVNDEIYD KIIYDDWMAA IEEVKACCKN LEALVEDIDR
