NP1L1_HUMAN
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 03-AUG-2022, entry version 201.
DE RecName: Full=Nucleosome assembly protein 1-like 1;
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 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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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:26841755).
CC Participates also in several important DNA repair mechanisms: greatly
CC enhances ERCC6-mediated chromatin remodeling which is essential for
CC transcription-coupled nucleotide excision DNA repair (PubMed:28369616).
CC Stimulates also homologous recombination (HR) by RAD51 and RAD54 which
CC is essential in mitotic DNA double strand break (DSB) repair
CC (PubMed:24798879). Plays a key role in the regulation of embryonic
CC neurogenesis (By similarity). Promotes the proliferation of neural
CC progenitors and inhibits neuronal differentiation during cortical
CC development (By similarity). Regulates neurogenesis via the modulation
CC of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated
CC H3K4 methylation at the RASSF10 promoter (By similarity).
CC {ECO:0000250|UniProtKB:P28656, ECO:0000269|PubMed:20002496,
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=2; IntAct=EBI-356392, EBI-2255116;
CC P55209; P10588: NR2F6; NbExp=2; IntAct=EBI-356392, EBI-2681496;
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}. 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 acidic domains are probably involved in the interaction
CC with histones.
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}.
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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_001307924.2.
DR RefSeq; NP_001317160.1; NM_001330231.1. [P55209-1]
DR RefSeq; NP_001317161.1; NM_001330232.1.
DR RefSeq; NP_004528.1; NM_004537.6. [P55209-1]
DR RefSeq; NP_631946.1; NM_139207.4. [P55209-1]
DR RefSeq; XP_011536695.1; XM_011538393.2. [P55209-1]
DR RefSeq; XP_016874827.1; XM_017019338.1. [P55209-1]
DR PDB; 7BP5; X-ray; 1.90 A; C=371-377.
DR PDBsum; 7BP5; -.
DR AlphaFoldDB; P55209; -.
DR SMR; P55209; -.
DR BioGRID; 110754; 282.
DR CORUM; P55209; -.
DR IntAct; P55209; 137.
DR MINT; P55209; -.
DR STRING; 9606.ENSP00000477538; -.
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 EPD; P55209; -.
DR jPOST; P55209; -.
DR MassIVE; P55209; -.
DR MaxQB; P55209; -.
DR PaxDb; P55209; -.
DR PeptideAtlas; P55209; -.
DR PRIDE; P55209; -.
DR ProteomicsDB; 3510; -.
DR ProteomicsDB; 3741; -.
DR ProteomicsDB; 56810; -. [P55209-1]
DR ABCD; P55209; 1 sequenced antibody.
DR Antibodypedia; 29629; 206 antibodies from 29 providers.
DR DNASU; 4673; -.
DR Ensembl; ENST00000393263.7; ENSP00000376947.3; ENSG00000187109.15. [P55209-1]
DR Ensembl; ENST00000431879.7; ENSP00000409795.3; ENSG00000187109.15. [P55209-3]
DR Ensembl; ENST00000549596.5; ENSP00000447793.1; ENSG00000187109.15. [P55209-2]
DR Ensembl; ENST00000618691.5; ENSP00000477538.1; ENSG00000187109.15. [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 CTD; 4673; -.
DR DisGeNET; 4673; -.
DR GeneCards; NAP1L1; -.
DR HGNC; HGNC:7637; NAP1L1.
DR HPA; ENSG00000187109; Low tissue specificity.
DR MIM; 164060; gene.
DR neXtProt; NX_P55209; -.
DR OpenTargets; ENSG00000187109; -.
DR PharmGKB; PA31439; -.
DR VEuPathDB; HostDB:ENSG00000187109; -.
DR eggNOG; KOG1507; Eukaryota.
DR GeneTree; ENSGT00940000153362; -.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; P55209; -.
DR OMA; NSAYNDE; -.
DR PhylomeDB; P55209; -.
DR TreeFam; TF314349; -.
DR PathwayCommons; P55209; -.
DR SignaLink; P55209; -.
DR BioGRID-ORCS; 4673; 11 hits in 1048 CRISPR screens.
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 213 other tissues.
DR ExpressionAtlas; P55209; baseline and differential.
DR Genevisible; P55209; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Lipoprotein;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Prenylation;
KW 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 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: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 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
