NP1L1_MOUSE
ID NP1L1_MOUSE Reviewed; 391 AA.
AC P28656; Q3UL14;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Nucleosome assembly protein 1-like 1;
DE AltName: Full=Brain protein DN38;
DE AltName: Full=NAP-1-related protein;
DE Flags: Precursor;
GN Name=Nap1l1; Synonyms=Nrp;
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].
RA Okuda A.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-391.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA Kato K.;
RT "A collection of cDNA clones with specific expression patterns in mouse
RT brain.";
RL Eur. J. Neurosci. 2:704-711(1990).
RN [5]
RP PROTEIN SEQUENCE OF 267-275, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP GLUTAMYLATION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT "A targeted multienzyme mechanism for selective microtubule
RT polyglutamylation.";
RL Mol. Cell 26:437-448(2007).
RN [8]
RP GLYCYLATION AT GLU-359 AND GLU-360, AND MUTAGENESIS OF GLU-359 AND GLU-360.
RX PubMed=18331838; DOI=10.1016/j.febslet.2008.02.079;
RA Ikegami K., Horigome D., Mukai M., Livnat I., MacGregor G.R., Setou M.;
RT "TTLL10 is a protein polyglycylase that can modify nucleosome assembly
RT protein 1.";
RL FEBS Lett. 582:1129-1134(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62; THR-64 AND SER-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH SETD1A.
RX PubMed=29490266; DOI=10.1016/j.celrep.2018.02.019;
RA Qiao H., Li Y., Feng C., Duo S., Ji F., Jiao J.;
RT "Nap1l1 controls embryonic neural progenitor cell proliferation and
RT differentiation in the developing brain.";
RL Cell Rep. 22:2279-2293(2018).
CC -!- FUNCTION: Histone chaperone that plays a role in the nuclear import of
CC H2A-H2B and nucleosome assembly. Participates also in several important
CC DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin
CC remodeling which is essential for transcription-coupled nucleotide
CC excision DNA repair. Stimulates also homologous recombination (HR) by
CC RAD51 and RAD54 which is essential in mitotic DNA double strand break
CC (DSB) repair (By similarity). Plays a key role in the regulation of
CC embryonic neurogenesis (PubMed:29490266). Promotes the proliferation of
CC neural progenitors and inhibits neuronal differentiation during
CC cortical development (PubMed:29490266). Regulates neurogenesis via the
CC modulation of RASSF10; regulates RASSF10 expression by promoting
CC SETD1A-mediated H3K4 methylation at the RASSF10 promoter
CC (PubMed:29490266). {ECO:0000250|UniProtKB:P55209,
CC ECO:0000269|PubMed:29490266}.
CC -!- SUBUNIT: Homodimer. The dimer binds strongly and sequentially to single
CC and double H2A-H2B heterodimers. Interacts with ERCC6; this interaction
CC increases ERCC6 processivity. Interacts with RAD54 (By similarity).
CC Interacts with SETD1A (PubMed:29490266). {ECO:0000250|UniProtKB:P55209,
CC ECO:0000269|PubMed:29490266}.
CC -!- INTERACTION:
CC P28656; Q9WVS7: Map2k5; NbExp=20; IntAct=EBI-645055, EBI-446144;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29490266}. Cytoplasm
CC {ECO:0000269|PubMed:29490266}. Melanosome
CC {ECO:0000250|UniProtKB:P55209}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain (at protein level)
CC (PubMed:29490266). High expression in cerebral cortex, not in
CC cerebellar cortex. {ECO:0000269|PubMed:29490266}.
CC -!- DEVELOPMENTAL STAGE: During brain development, expression decreases
CC from 12 dpc to P0. Expressed predominantly but not restricted in the
CC ventricular zone (VZ)/subventricular zone (SVZ), and peak expression is
CC observed at 12.5 dpc, in which the cerebral cortex consists primarily
CC of neural progenitor cells (NPCs). At 15.5 dpc, the expression
CC decreases in the cerebral cortical plate. At 18.5 dpc, when the
CC embryonic neurogenesis period nears its end, the expression throughout
CC the cerebral cortex is lower than that at 12.5 dpc (at protein level).
CC {ECO:0000269|PubMed:29490266}.
CC -!- DOMAIN: The acidic domains are probably involved in the interaction
CC with histones.
CC -!- PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in
CC polyglycine chains on the gamma-carboxyl group. Both polyglutamylation
CC and polyglycylation modifications can coexist on the same protein on
CC adjacent residues, and lowering polyglycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000269|PubMed:18331838}.
CC -!- PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in
CC polyglutamate chains on the gamma-carboxyl group. Both
CC polyglutamylation and polyglycylation modifications can coexist on the
CC same protein on adjacent residues, and lowering polyglycylation levels
CC increases polyglutamylation, and reciprocally.
CC {ECO:0000269|PubMed:17499049}.
CC -!- DISRUPTION PHENOTYPE: Mice show abnormal embryonic neurogenesis.
CC {ECO:0000269|PubMed:29490266}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {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; D12618; BAA02142.1; -; mRNA.
DR EMBL; AK050375; BAC34219.1; -; mRNA.
DR EMBL; AK136161; BAE22850.1; -; mRNA.
DR EMBL; AK145766; BAE26637.1; -; mRNA.
DR EMBL; BC076591; AAH76591.1; -; mRNA.
DR EMBL; X61449; CAA43689.1; -; mRNA.
DR CCDS; CCDS36058.1; -.
DR PIR; JS0707; JS0707.
DR RefSeq; NP_056596.1; NM_015781.4.
DR AlphaFoldDB; P28656; -.
DR SMR; P28656; -.
DR BioGRID; 207325; 13.
DR IntAct; P28656; 6.
DR MINT; P28656; -.
DR STRING; 10090.ENSMUSP00000126850; -.
DR iPTMnet; P28656; -.
DR PhosphoSitePlus; P28656; -.
DR SwissPalm; P28656; -.
DR EPD; P28656; -.
DR jPOST; P28656; -.
DR MaxQB; P28656; -.
DR PaxDb; P28656; -.
DR PeptideAtlas; P28656; -.
DR PRIDE; P28656; -.
DR ProteomicsDB; 293710; -.
DR Antibodypedia; 29629; 206 antibodies from 29 providers.
DR DNASU; 53605; -.
DR Ensembl; ENSMUST00000065917; ENSMUSP00000070068; ENSMUSG00000058799.
DR Ensembl; ENSMUST00000217908; ENSMUSP00000151750; ENSMUSG00000058799.
DR Ensembl; ENSMUST00000218828; ENSMUSP00000151972; ENSMUSG00000058799.
DR GeneID; 53605; -.
DR KEGG; mmu:53605; -.
DR UCSC; uc007hac.2; mouse.
DR CTD; 4673; -.
DR MGI; MGI:1855693; Nap1l1.
DR VEuPathDB; HostDB:ENSMUSG00000058799; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000153362; -.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; P28656; -.
DR OMA; NSAYNDE; -.
DR PhylomeDB; P28656; -.
DR BioGRID-ORCS; 53605; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Nap1l1; mouse.
DR PRO; PR:P28656; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P28656; protein.
DR Bgee; ENSMUSG00000058799; Expressed in embryonic post-anal tail and 270 other tissues.
DR ExpressionAtlas; P28656; baseline and differential.
DR Genevisible; P28656; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
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 Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Lipoprotein; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
KW Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT CHAIN 2..388
FT /note="Nucleosome assembly protein 1-like 1"
FT /id="PRO_0000185653"
FT PROPEP 389..391
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT /id="PRO_0000396686"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..279
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 359
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000269|PubMed:18331838"
FT MOD_RES 360
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000269|PubMed:18331838"
FT MOD_RES 388
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 388
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MUTAGEN 359
FT /note="E->D: Reduced polyglycylation."
FT /evidence="ECO:0000269|PubMed:18331838"
FT MUTAGEN 360
FT /note="E->D: Reduced polyglycylation."
FT /evidence="ECO:0000269|PubMed:18331838"
FT CONFLICT 377..390
FT /note="YDPKKDQNPAECKQ -> MTQRRIRTQPSASSSE (in Ref. 4;
FT CAA43689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 45345 MW; 48F17F3A44D9A597 CRC64;
MADIDNKEQS ELDQDLEDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA ALQERLDGLV
DTPTGYIESL PKVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI
INAIYEPTEE ECEWKPDEED EVSEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL
LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NDYFTNEVLT KTYRMRSEPD
DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF
FAPPEVPENG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE
ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q
