NP1L4_MOUSE
ID NP1L4_MOUSE Reviewed; 375 AA.
AC Q78ZA7; O88701;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
GN Name=Nap1l4;
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=C57BL/6J;
RX PubMed=9618174; DOI=10.1093/hmg/7.7.1149;
RA Paulsen M., Davies K.R., Bowden L.M., Villar A.J., Franck O., Fuermann M.,
RA Dean W.L., Moore T.F., Rodrigues N., Davies K.E., Hu R.-J., Feinberg A.P.,
RA Maher E.R., Reik W., Walter J.;
RT "Syntenic organization of the mouse distal chromosome 7 imprinting cluster
RT and the Beckwith-Wiedemann syndrome region in chromosome 11p15.5.";
RL Hum. Mol. Genet. 7:1149-1159(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R., Lane N.,
RA Reik W., Walter J.;
RT "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT implications for a novel imprinting centre and extended imprinting.";
RL Hum. Mol. Genet. 9:2691-2706(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-51; SER-53; SER-54;
RP SER-125 AND SER-304, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, 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 [8]
RP FUNCTION.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
CC -!- FUNCTION: Acts as histone chaperone in nucleosome assembly
CC (PubMed:28366643). In condensing spermatids, mediates the loading of
CC the heterodimer composed of histones H2AB1 and H2BC1/TH2B onto the
CC nucleosomes, thereby promoting the replacement of histones to protamine
CC in male germ cells (PubMed:28366643). {ECO:0000269|PubMed:28366643}.
CC -!- SUBUNIT: Interacts with core (H2A, H2B, H3, H4) and linker (H1)
CC histones. {ECO:0000250|UniProtKB:Q99733}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99733}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99733}. Note=Present in the cytoplasm and
CC excluded from the nucleus during G0/G1 phase, then relocates to the
CC nucleus by the time cells are in S phase. Phosphorylated form localizes
CC in the cytoplasm during the G0/G1 transition, whereas dephosphorylation
CC leads to relocalization into the nucleus at the G1/S-boundary.
CC {ECO:0000250|UniProtKB:Q99733}.
CC -!- PTM: Polyglutamylated and polyglycylated. These 2 modifications occur
CC exclusively on glutamate residues and result in either polyglutamate or
CC polyglycine chains on the gamma-carboxyl group. Both modifications can
CC coexist on the same protein on adjacent residues, and lowering
CC polyglycylation levels increases polyglutamylation, and reciprocally.
CC Polyglutamylated by TTLL4. {ECO:0000269|PubMed:17499049}.
CC -!- PTM: Phosphorylated at the G0/G1 boundary but it is not phosphorylated
CC in S-phase. Phosphorylated protein remains in the cytoplasm in a
CC complex with histones during the G0/G1 transition, whereas
CC dephosphorylation triggers its transport into the nucleus at the G1/S-
CC boundary. {ECO:0000250|UniProtKB:Q99733}.
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; AJ002198; CAA05245.1; -; mRNA.
DR EMBL; AJ276505; CAC16399.1; -; Genomic_DNA.
DR CCDS; CCDS40197.1; -.
DR RefSeq; NP_001272418.1; NM_001285489.1.
DR RefSeq; NP_001272419.1; NM_001285490.1.
DR RefSeq; NP_032698.1; NM_008672.3.
DR AlphaFoldDB; Q78ZA7; -.
DR SMR; Q78ZA7; -.
DR BioGRID; 201692; 6.
DR IntAct; Q78ZA7; 3.
DR STRING; 10090.ENSMUSP00000072510; -.
DR iPTMnet; Q78ZA7; -.
DR PhosphoSitePlus; Q78ZA7; -.
DR CPTAC; non-CPTAC-3850; -.
DR EPD; Q78ZA7; -.
DR jPOST; Q78ZA7; -.
DR MaxQB; Q78ZA7; -.
DR PaxDb; Q78ZA7; -.
DR PRIDE; Q78ZA7; -.
DR ProteomicsDB; 293681; -.
DR Antibodypedia; 23223; 80 antibodies from 22 providers.
DR DNASU; 17955; -.
DR Ensembl; ENSMUST00000072727; ENSMUSP00000072510; ENSMUSG00000059119.
DR GeneID; 17955; -.
DR KEGG; mmu:17955; -.
DR UCSC; uc009kpl.2; mouse.
DR CTD; 4676; -.
DR MGI; MGI:1316687; Nap1l4.
DR VEuPathDB; HostDB:ENSMUSG00000059119; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000153362; -.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; Q78ZA7; -.
DR OMA; VSPITWK; -.
DR OrthoDB; 1216172at2759; -.
DR PhylomeDB; Q78ZA7; -.
DR TreeFam; TF314349; -.
DR BioGRID-ORCS; 17955; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Nap1l4; mouse.
DR PRO; PR:Q78ZA7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q78ZA7; protein.
DR Bgee; ENSMUSG00000059119; Expressed in saccule of membranous labyrinth and 258 other tissues.
DR ExpressionAtlas; Q78ZA7; baseline and differential.
DR Genevisible; Q78ZA7; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA: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; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT CHAIN 2..375
FT /note="Nucleosome assembly protein 1-like 4"
FT /id="PRO_0000236213"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..271
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 340..368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 375 AA; 42679 MW; A249E440F09072A6 CRC64;
MAENSLSDGG PADSVEAAKN ASNTEKLTDQ VMQNPQVLAA LQERLDNVSH TPSSYIETLP
KAVKRRINAL KQLQVRCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE
SAWHSENEEE DKLAGDMKNK VVIAEKEAAT VEELNPKGIP EFWFTIFRNV DMLSELVQEY
DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPNDYFTNPV LTKTYKMKSE PDKADPFSFE
GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNESFF NFFSPLKASG
DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD
EEGEDEDDAD VNPKV
