ID NP1L1_HUMAN Reviewed; 391 AA. AC P55209; B3KNT8; B3KV44; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 220. DE RecName: Full=Nucleosome assembly protein 1-like 1; DE AltName: Full=Histone H2A-H2B chaperone NAP1L1 {ECO:0000305}; DE AltName: Full=NAP-1-related protein; DE Short=hNRP; DE Flags: Precursor; GN Name=NAP1L1; Synonyms=NRP; 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). RC TISSUE=Thymus; RX PubMed=8297347; DOI=10.1042/bj2970389; RA Simon H.-U., Mills G.B., Kozlowski M., Hogg D., Branch D., Ishimi Y., RA Siminovitch K.A.; RT "Molecular characterization of hNRP, a cDNA encoding a human nucleosome- RT assembly-protein-I-related gene product involved in the induction of cell RT proliferation."; RL Biochem. J. 297:389-397(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Cerebellum; 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 MRNA] (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [9] RP ISOPRENYLATION AT CYS-388. RX PubMed=15308774; DOI=10.1073/pnas.0403413101; RA Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., RA Weinbaum C., Tamanoi F., Falck J., Zhao Y.; RT "A tagging-via-substrate technology for detection and proteomics of RT farnesylated proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004). RN [10] RP IDENTIFICATION BY 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 [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-62; SER-69 AND RP SER-143, AND 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 [15] RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION). RX PubMed=18226242; DOI=10.1186/1742-4690-5-8; RA Vardabasso C., Manganaro L., Lusic M., Marcello A., Giacca M.; RT "The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds RT HIV-1 Tat and promotes viral transcription."; RL Retrovirology 5:8-8(2008). RN [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND RP IDENTIFICATION BY MASS 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 [20] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONES H2A AND H2B. RX PubMed=20002496; DOI=10.1111/j.1365-2443.2009.01361.x; RA Okuwaki M., Kato K., Nagata K.; RT "Functional characterization of human nucleosome assembly protein 1-like RT proteins as histone chaperones."; RL Genes Cells 15:13-27(2010). RN [21] 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 [22] RP FUNCTION, MOTIF, AND MUTAGENESIS OF GLU-126; GLU-130 AND TRP-134. RX PubMed=21211722; DOI=10.1016/j.molcel.2010.12.008; RA Mehrotra P.V., Ahel D., Ryan D.P., Weston R., Wiechens N., Kraehenbuehl R., RA Owen-Hughes T., Ahel I.; RT "DNA repair factor APLF is a histone chaperone."; RL Mol. Cell 41:46-55(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION BY RP MASS SPECTROMETRY [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 [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=23691099; DOI=10.1371/journal.pone.0063802; RA Mansouri S., Wang S., Frappier L.; RT "A role for the nucleosome assembly proteins TAF-Ibeta and NAP1 in the RT activation of BZLF1 expression and Epstein-Barr virus reactivation."; RL PLoS ONE 8:e63802-e63802(2013). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [27] RP FUNCTION, AND INTERACTION WITH RAD54. RX PubMed=24798879; DOI=10.1038/srep04863; RA Machida S., Takaku M., Ikura M., Sun J., Suzuki H., Kobayashi W., RA Kinomura A., Osakabe A., Tachiwana H., Horikoshi Y., Fukuto A., Matsuda R., RA Ura K., Tashiro S., Ikura T., Kurumizaka H.; RT "Nap1 stimulates homologous recombination by RAD51 and RAD54 in higher- RT ordered chromatin containing histone H1."; RL Sci. Rep. 4:4863-4863(2014). RN [28] 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 [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [30] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN HERPESVIRUS 8 RP PROTEIN LANA1 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=27599637; DOI=10.1038/srep32633; RA Gupta N., Thakker S., Verma S.C.; RT "KSHV encoded LANA recruits Nucleosome Assembly Protein NAP1L1 for RT regulating viral DNA replication and transcription."; RL Sci. Rep. 6:32633-32633(2016). RN [31] RP FUNCTION, INTERACTION WITH H2A AND HA2B, AND SUBUNIT. RX PubMed=26841755; DOI=10.1111/gtc.12339; RA Ohtomo H., Akashi S., Moriwaki Y., Okuwaki M., Osakabe A., Nagata K., RA Kurumizaka H., Nishimura Y.; RT "C-terminal acidic domain of histone chaperone human NAP1 is an efficient RT binding assistant for histone H2A-H2B, but not H3-H4."; RL Genes Cells 21:252-263(2016). RN [32] RP INTERACTION WITH HEPATITIS C VIRUS PROTEIN NS5A (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=28659470; DOI=10.1128/jvi.00880-17; RA Cevik R.E., Cesarec M., Da Silva Filipe A., Licastro D., McLauchlan J., RA Marcello A.; RT "Hepatitis C Virus NS5A Targets Nucleosome Assembly Protein NAP1L1 To RT Control the Innate Cellular Response."; RL J. Virol. 91:0-0(2017). RN [33] RP FUNCTION, AND INTERACTION WITH ERCC6. RX PubMed=28369616; DOI=10.1093/nar/gkx188; RA Lee J.Y., Lake R.J., Kirk J., Bohr V.A., Fan H.Y., Hohng S.; RT "NAP1L1 accelerates activation and decreases pausing to enhance nucleosome RT remodeling by CSB."; RL Nucleic Acids Res. 45:4696-4707(2017). RN [34] 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: Histone chaperone that plays a role in the nuclear import of CC H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, CC PubMed:26841755). Also participates in several important DNA repair CC mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which CC is essential for transcription-coupled nucleotide excision DNA repair CC (PubMed:28369616). Also stimulates homologous recombination (HR) by CC RAD51 and RAD54 which is essential in mitotic DNA double strand break CC (DSB) repair (PubMed:24798879). Plays a key role in the regulation of CC embryonic neurogenesis (By similarity). Promotes the proliferation of CC neural progenitors and inhibits neuronal differentiation during CC cortical development (By similarity). Regulates neurogenesis via the CC modulation of RASSF10; regulates RASSF10 expression by promoting CC SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By CC similarity). {ECO:0000250|UniProtKB:P28656, CC ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:21211722, CC ECO:0000269|PubMed:24798879, ECO:0000269|PubMed:26841755, CC ECO:0000269|PubMed:28369616}. CC -!- FUNCTION: (Microbial infection) Positively regulates Epstein-Barr virus CC reactivation in epithelial cells through the induction of viral BZLF1 CC expression. {ECO:0000269|PubMed:23691099}. CC -!- FUNCTION: (Microbial infection) Together with human herpesvirus 8 CC protein LANA1, assists the proper assembly of the nucleosome on the CC replicated viral DNA. {ECO:0000269|PubMed:27599637}. CC -!- SUBUNIT: Homodimer (PubMed:26841755). The dimer binds strongly and CC sequentially to single and double H2A-H2B heterodimers CC (PubMed:26841755). Interacts with ERCC6; this interaction increases CC ERCC6 processivity (PubMed:28369616). Interacts with RAD54 CC (PubMed:24798879). Interacts with SETD1A (By similarity). CC {ECO:0000250|UniProtKB:P28656, ECO:0000269|PubMed:24798879, CC ECO:0000269|PubMed:26841755, ECO:0000269|PubMed:28369616}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 8 CC protein LANA1 (via N-terminus); this interaction is required for LANA1- CC dependent DNA replication. {ECO:0000269|PubMed:27599637}. CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis virus protein CC NS5A (via C-terminus); this interaction sequesters NAP1L1 in the CC cytoplasm, blocking its nuclear translocation. CC {ECO:0000269|PubMed:28659470}. CC -!- SUBUNIT: (Microbial infection) Interacts with Chikungunya virus non- CC structural protein 3 (via C-terminus). {ECO:0000269|PubMed:29899097}. CC -!- INTERACTION: CC P55209; Q92793: CREBBP; NbExp=3; IntAct=EBI-356392, EBI-81215; CC P55209; P36957: DLST; NbExp=3; IntAct=EBI-356392, EBI-351007; CC P55209; Q09472: EP300; NbExp=3; IntAct=EBI-356392, EBI-447295; CC P55209; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-356392, EBI-7960826; CC P55209; P52333: JAK3; NbExp=4; IntAct=EBI-356392, EBI-518246; CC P55209; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-356392, EBI-3911716; CC P55209; Q99733: NAP1L4; NbExp=4; IntAct=EBI-356392, EBI-2255116; CC P55209; P10588: NR2F6; NbExp=2; IntAct=EBI-356392, EBI-2681496; CC P55209; P62750: RPL23A; NbExp=3; IntAct=EBI-356392, EBI-353254; CC P55209; P54274: TERF1; NbExp=2; IntAct=EBI-356392, EBI-710997; CC P55209; Q6ZVT0: TTLL10; NbExp=5; IntAct=EBI-356392, EBI-7844656; CC P55209; P04608: tat; Xeno; NbExp=6; IntAct=EBI-356392, EBI-6164389; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:27599637}. Chromosome CC {ECO:0000250|UniProtKB:P28656}. Melanosome CC {ECO:0000269|PubMed:17081065}. Cytoplasm {ECO:0000269|PubMed:20002496, CC ECO:0000269|PubMed:28659470}. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P55209-1; Sequence=Displayed; CC Name=2; CC IsoId=P55209-2; Sequence=VSP_053909; CC Name=3; CC IsoId=P55209-3; Sequence=VSP_057357, VSP_057358; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- DOMAIN: The NAP1L motif is required for the histone chaperone activity. CC {ECO:0000269|PubMed:21211722}. CC -!- DOMAIN: The acidic domains are probably involved in the interaction CC with histones. {ECO:0000269|PubMed:26841755}. CC -!- PTM: Monoglycylated on glutamate residues. Cannot be polyglycylated due CC to the absence of functional TTLL10 in human (By similarity). CC {ECO:0000250|UniProtKB:P28656, ECO:0000305}. CC -!- PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in CC polyglutamate chains on the gamma-carboxyl group. Both CC polyglutamylation and monoglycylation modifications can coexist on the CC same protein on adjacent residues, and lowering polyglycylation levels CC increases polyglutamylation, and reciprocally. CC {ECO:0000250|UniProtKB:P28656}. 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; M86667; AAC37544.1; -; mRNA. DR EMBL; BT007023; AAP35669.1; -; mRNA. DR EMBL; AK055020; BAG51450.1; -; mRNA. DR EMBL; AK122670; BAG53656.1; -; mRNA. DR EMBL; AL162068; CAB82405.1; -; mRNA. DR EMBL; AC011611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW97318.1; -; Genomic_DNA. DR EMBL; BC002387; AAH02387.1; -; mRNA. DR CCDS; CCDS9013.1; -. [P55209-1] DR PIR; S40510; S40510. DR RefSeq; NP_001294853.1; NM_001307924.3. DR RefSeq; NP_001317160.1; NM_001330231.2. [P55209-1] DR RefSeq; NP_001317161.1; NM_001330232.2. DR RefSeq; NP_004528.1; NM_004537.7. [P55209-1] DR RefSeq; NP_631946.1; NM_139207.5. [P55209-1] DR RefSeq; XP_011536695.1; XM_011538393.3. [P55209-1] DR PDB; 7BP5; X-ray; 1.90 A; C=371-377. DR PDB; 7UN3; EM; 3.50 A; B/C=2-391. DR PDB; 7UN6; EM; 3.30 A; B/C=2-391. DR AlphaFoldDB; P55209; -. DR EMDB; EMD-26612; -. DR EMDB; EMD-26614; -. DR SMR; P55209; -. DR BioGRID; 110754; 394. DR CORUM; P55209; -. DR FunCoup; P55209; 3751. DR IntAct; P55209; 186. DR MINT; P55209; -. DR NDEx; IQUERY-CP-NAP1L1; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000477538; -. DR BindingDB; P55209; -. DR ChEMBL; CHEMBL6067393; -. DR GlyGen; P55209; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55209; -. DR MetOSite; P55209; -. DR PhosphoSitePlus; P55209; -. DR SwissPalm; P55209; -. DR BioMuta; NAP1L1; -. DR DMDM; 1709337; -. DR OGP; P55209; -. DR CPTAC; CPTAC-97; -. DR CPTAC; CPTAC-98; -. DR jPOST; P55209; -. DR MassIVE; P55209; -. DR PaxDb; 9606-ENSP00000477538; -. DR PeptideAtlas; P55209; -. DR ProteomicsDB; 3510; -. DR ProteomicsDB; 3741; -. DR ProteomicsDB; 56810; -. [P55209-1] DR Pumba; P55209; -. DR ABCD; P55209; 1 sequenced antibody. DR Antibodypedia; 29629; 217 antibodies from 33 providers. DR DNASU; 4673; -. DR Ensembl; ENST00000393263.7; ENSP00000376947.3; ENSG00000187109.16. [P55209-1] DR Ensembl; ENST00000431879.7; ENSP00000409795.3; ENSG00000187109.16. [P55209-3] DR Ensembl; ENST00000549596.5; ENSP00000447793.1; ENSG00000187109.16. [P55209-2] DR Ensembl; ENST00000618691.5; ENSP00000477538.1; ENSG00000187109.16. [P55209-1] DR Ensembl; ENST00000880560.1; ENSP00000550619.1; ENSG00000187109.16. [P55209-1] DR Ensembl; ENST00000880561.1; ENSP00000550620.1; ENSG00000187109.16. [P55209-1] DR Ensembl; ENST00000951463.1; ENSP00000621522.1; ENSG00000187109.16. [P55209-1] DR GeneID; 4673; -. DR KEGG; hsa:4673; -. DR MANE-Select; ENST00000618691.5; ENSP00000477538.1; NM_004537.7; NP_004528.1. DR UCSC; uc001sxw.3; human. [P55209-1] DR AGR; HGNC:7637; -. DR ClinPGx; PA31439; -. DR CTD; 4673; -. DR DisGeNET; 4673; -. DR GeneCards; NAP1L1; -. DR HGNC; HGNC:7637; NAP1L1. DR HPA; ENSG00000187109; Low tissue specificity. DR MIM; 164060; gene. DR OpenTargets; ENSG00000187109; -. DR VEuPathDB; HostDB:ENSG00000187109; -. DR eggNOG; KOG1507; Eukaryota. DR GeneTree; ENSGT00940000153362; -. DR HOGENOM; CLU_038841_3_0_1; -. DR InParanoid; P55209; -. DR OMA; AAECKQN; -. DR OrthoDB; 27325at2759; -. DR PAN-GO; P55209; 5 GO annotations based on evolutionary models. DR PhylomeDB; P55209; -. DR PathwayCommons; P55209; -. DR SignaLink; P55209; -. DR Agora; ENSG00000187109; -. DR BioGRID-ORCS; 4673; 12 hits in 1127 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; NAP1L1; human. DR GeneWiki; NAP1L1; -. DR GenomeRNAi; 4673; -. DR Pharos; P55209; Tbio. DR PRO; PR:P55209; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P55209; protein. DR Bgee; ENSG00000187109; Expressed in calcaneal tendon and 215 other cell types or tissues. DR ExpressionAtlas; P55209; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0140713; F:histone chaperone activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; TAS:ProtInc. DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB. DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB. DR FunFam; 1.20.5.1500:FF:000001; Nucleosome assembly protein 1-like 1; 1. DR FunFam; 3.30.1120.90:FF:000001; Nucleosome assembly protein 1-like 1; 1. DR Gene3D; 1.20.5.1500; -; 1. DR Gene3D; 3.30.1120.90; Nucleosome assembly protein; 1. DR InterPro; IPR002164; NAP. DR InterPro; IPR037231; NAP-like_sf. DR PANTHER; PTHR11875; TESTIS-SPECIFIC Y-ENCODED PROTEIN; 1. DR Pfam; PF00956; NAP; 1. DR SUPFAM; SSF143113; NAP-like; 1. DR PDBsum; 7BP5; -. DR PDBsum; 7UN3; -. DR PDBsum; 7UN6; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Chromosome; KW Cytoplasm; Lipoprotein; Methylation; Neurogenesis; Nucleus; Phosphoprotein; KW Prenylation; Proteomics identification; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..388 FT /note="Nucleosome assembly protein 1-like 1" FT /id="PRO_0000185652" FT PROPEP 389..391 FT /note="Removed in mature form" FT /evidence="ECO:0000305" FT /id="PRO_0000393943" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 132..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 125..150 FT /note="NAP1L motif" FT /evidence="ECO:0000269|PubMed:21211722" FT MOTIF 273..279 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 1..10 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..28 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 132..143 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..163 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..376 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..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:0007744|PubMed:19413330" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 62 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P28656" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 116 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 388 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000305" FT LIPID 388 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000269|PubMed:15308774" FT VAR_SEQ 1..41 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057357" FT VAR_SEQ 117..143 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057358" FT VAR_SEQ 364..391 FT /note="EGEEEGDEENDPDYDPKKDQNPAECKQQ -> VMFTK (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053909" FT MUTAGEN 126 FT /note="E->A: Impaired binding to histones and ability to FT mediate histone chaperone activity." FT /evidence="ECO:0000269|PubMed:21211722" FT MUTAGEN 130 FT /note="E->A: Impaired binding to histones and ability to FT mediate histone chaperone activity." FT /evidence="ECO:0000269|PubMed:21211722" FT MUTAGEN 134 FT /note="W->A: Impaired binding to histones and ability to FT mediate histone chaperone activity." FT /evidence="ECO:0000269|PubMed:21211722" FT HELIX 74..121 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 170..177 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:7UN6" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 227..236 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 249..256 FT /evidence="ECO:0007829|PDB:7UN6" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 269..278 FT /evidence="ECO:0007829|PDB:7UN6" FT TURN 280..282 FT /evidence="ECO:0007829|PDB:7UN6" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 303..307 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 314..329 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 330..334 FT /evidence="ECO:0007829|PDB:7UN6" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:7UN6" FT HELIX 338..342 FT /evidence="ECO:0007829|PDB:7UN6" FT MOD_RES P55209-3:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 391 AA; 45374 MW; E5B2EAA4EAE551D2 CRC64; MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA ALQERLDGLV ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q //