NP1L4_HUMAN
ID NP1L4_HUMAN Reviewed; 375 AA.
AC Q99733; B2R6J4; F5HFY4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
DE AltName: Full=Nucleosome assembly protein 2 {ECO:0000303|PubMed:8923002};
DE Short=NAP-2 {ECO:0000303|PubMed:8923002};
GN Name=NAP1L4 {ECO:0000312|HGNC:HGNC:7640};
GN Synonyms=NAP2 {ECO:0000303|PubMed:8923002};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8923002; DOI=10.1093/hmg/5.11.1743;
RA Hu R.-J., Lee M.P., Johnson L.A., Feinberg A.P.;
RT "A novel human homologue of yeast nucleosome assembly protein, 65 kb
RT centromeric to the p57KIP2 gene, is biallelically expressed in fetal and
RT adult tissues.";
RL Hum. Mol. Genet. 5:1743-1748(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Okuwaki M., Kato K., Nagata K.;
RT "human nucleosome assembly protein 1-like 4b.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9325046; DOI=10.1006/geno.1997.4868;
RA Rodriguez P., Munroe D., Prawitt D., Chu L.L., Bric E., Kim J., Reid L.H.,
RA Davies C., Nakagama H., Loebbert R., Winterpacht A., Petruzzi M.J.,
RA Higgins M.J., Nowak N., Evans G., Shows T., Weissman B.E., Zabel B.,
RA Housman D.E., Pelletier J.;
RT "Functional characterization of human nucleosome assembly protein-2
RT (NAP1L4) suggests a role as a histone chaperone.";
RL Genomics 44:253-265(1997).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10764593; DOI=10.1006/jmbi.2000.3674;
RA Rodriguez P., Pelletier J., Price G.B., Zannis-Hadjopoulos M.;
RT "NAP-2: histone chaperone function and phosphorylation state through the
RT cell cycle.";
RL J. Mol. Biol. 298:225-238(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND SER-125, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-304, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5; SER-7; SER-12; THR-51; SER-54 AND SER-125, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5; SER-7; SER-12 AND SER-125, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-7; SER-12; THR-51;
RP THR-58 AND SER-125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=29899097; DOI=10.1128/jvi.00838-18;
RA Meshram C.D., Agback P., Shiliaev N., Urakova N., Mobley J.A., Agback T.,
RA Frolova E.I., Frolov I.;
RT "Multiple Host Factors Interact with the Hypervariable Domain of
RT Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific
RT Mode.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Acts as histone chaperone in nucleosome assembly.
CC {ECO:0000269|PubMed:9325046}.
CC -!- SUBUNIT: Interacts with core (H2A, CD2APH2B, H3, H4) and linker (H1)
CC histones. {ECO:0000269|PubMed:9325046}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Chikungunya virus non-
CC structural protein 3 (via C-terminus). {ECO:0000269|PubMed:29899097}.
CC -!- INTERACTION:
CC Q99733; P55209: NAP1L1; NbExp=2; IntAct=EBI-2255116, EBI-356392;
CC Q99733; P04608: tat; Xeno; NbExp=3; IntAct=EBI-2255116, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10764593,
CC ECO:0000269|PubMed:9325046}. Cytoplasm {ECO:0000269|PubMed:10764593,
CC ECO:0000269|PubMed:9325046}. Note=Present in the cytoplasm and excluded
CC from the nucleus during G0/G1 phase, then relocates to the nucleus by
CC the time cells are in S phase (PubMed:9325046). Phosphorylated form
CC localizes in the cytoplasm during the G0/G1 transition, whereas
CC dephosphorylation leads to relocalization into the nucleus at the G1/S-
CC boundary (PubMed:10764593). {ECO:0000269|PubMed:10764593,
CC ECO:0000269|PubMed:9325046}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99733-1; Sequence=Displayed;
CC Name=2; Synonyms=NAP1L4b {ECO:0000303|Ref.2};
CC IsoId=Q99733-2; Sequence=VSP_053910;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Biallelically expressed in fetal and
CC adult tissues. Highest levels in testis. {ECO:0000269|PubMed:8923002}.
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:0000269|PubMed:10764593}.
CC -!- PTM: Polyglutamylated by TTLL4, a modification that occurs exclusively
CC on glutamate residues and results in polyglutamate chains on the gamma-
CC carboxyl group. Some residues may also be monoglycylated but not
CC polyglycylated due to the absence of functional TTLL10 in human (By
CC similarity). {ECO:0000250|UniProtKB:Q78ZA7, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; U77456; AAC50870.1; -; mRNA.
DR EMBL; AB500094; BAH95827.1; -; mRNA.
DR EMBL; AK312599; BAG35491.1; -; mRNA.
DR EMBL; AC131971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022090; AAH22090.1; -; mRNA.
DR CCDS; CCDS41599.1; -. [Q99733-1]
DR RefSeq; NP_005960.1; NM_005969.3. [Q99733-1]
DR AlphaFoldDB; Q99733; -.
DR SMR; Q99733; -.
DR BioGRID; 110757; 164.
DR IntAct; Q99733; 68.
DR MINT; Q99733; -.
DR STRING; 9606.ENSP00000369915; -.
DR ChEMBL; CHEMBL3886061; -.
DR GlyGen; Q99733; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99733; -.
DR MetOSite; Q99733; -.
DR PhosphoSitePlus; Q99733; -.
DR SwissPalm; Q99733; -.
DR BioMuta; NAP1L4; -.
DR DMDM; 2498672; -.
DR EPD; Q99733; -.
DR jPOST; Q99733; -.
DR MassIVE; Q99733; -.
DR MaxQB; Q99733; -.
DR PaxDb; Q99733; -.
DR PeptideAtlas; Q99733; -.
DR PRIDE; Q99733; -.
DR ProteomicsDB; 27835; -.
DR ProteomicsDB; 78450; -. [Q99733-1]
DR Antibodypedia; 23223; 80 antibodies from 22 providers.
DR DNASU; 4676; -.
DR Ensembl; ENST00000380542.9; ENSP00000369915.4; ENSG00000205531.13. [Q99733-1]
DR Ensembl; ENST00000526115.5; ENSP00000436397.1; ENSG00000205531.13. [Q99733-2]
DR Ensembl; ENST00000616696.1; ENSP00000478654.1; ENSG00000273562.4. [Q99733-2]
DR Ensembl; ENST00000619695.4; ENSP00000483728.1; ENSG00000273562.4. [Q99733-1]
DR Ensembl; ENST00000620138.4; ENSP00000481412.1; ENSG00000205531.13. [Q99733-2]
DR Ensembl; ENST00000632791.1; ENSP00000487984.1; ENSG00000273562.4. [Q99733-2]
DR GeneID; 4676; -.
DR KEGG; hsa:4676; -.
DR MANE-Select; ENST00000380542.9; ENSP00000369915.4; NM_005969.4; NP_005960.1.
DR UCSC; uc001lxc.4; human. [Q99733-1]
DR CTD; 4676; -.
DR DisGeNET; 4676; -.
DR GeneCards; NAP1L4; -.
DR HGNC; HGNC:7640; NAP1L4.
DR HPA; ENSG00000205531; Tissue enhanced (brain).
DR MIM; 601651; gene.
DR neXtProt; NX_Q99733; -.
DR OpenTargets; ENSG00000205531; -.
DR PharmGKB; PA31442; -.
DR VEuPathDB; HostDB:ENSG00000205531; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000153362; -.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; Q99733; -.
DR OMA; VSPITWK; -.
DR PhylomeDB; Q99733; -.
DR TreeFam; TF314349; -.
DR PathwayCommons; Q99733; -.
DR SignaLink; Q99733; -.
DR BioGRID-ORCS; 4676; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; NAP1L4; human.
DR GeneWiki; NAP1L4; -.
DR GenomeRNAi; 4676; -.
DR Pharos; Q99733; Tbio.
DR PRO; PR:Q99733; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q99733; protein.
DR Bgee; ENSG00000205531; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; Q99733; baseline and differential.
DR Genevisible; Q99733; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
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; Alternative splicing; Chaperone; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..375
FT /note="Nucleosome assembly protein 1-like 4"
FT /id="PRO_0000185658"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..137
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 16..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 375
FT /note="V -> KEPSQPAECKQQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053910"
FT CONFLICT 107
FT /note="R -> K (in Ref. 3; BAG35491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42823 MW; 788E1F9F5BC8FD45 CRC64;
MADHSFSDGV PSDSVEAAKN ASNTEKLTDQ VMQNPRVLAA LQERLDNVPH TPSSYIETLP
KAVKRRINAL KQLQVRCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE
SEWHSENEEE EKLAGDMKSK VVVTEKAAAT AEEPDPKGIP EFWFTIFRNV DMLSELVQEY
DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPNDYFTNSV LTKTYKMKSE PDKADPFSFE
GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNESFF NFFNPLKASG
DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD
EEGEDEDDAE INPKV
