NAP1B_ARATH
ID NAP1B_ARATH Reviewed; 379 AA.
AC Q9ZUP3; B9DFH2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nucleosome assembly protein 1;2;
DE Short=AtNAP1;2;
DE AltName: Full=Nucleosome/chromatin assembly factor group A2;
DE Flags: Precursor;
GN Name=NAP1;2; Synonyms=NFA2; OrderedLocusNames=At2g19480; ORFNames=F3P11.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-227.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17122067; DOI=10.1105/tpc.106.046490;
RA Zhu Y., Dong A., Meyer D., Pichon O., Renou J.P., Cao K., Shen W.H.;
RT "Arabidopsis NRP1 and NRP2 encode histone chaperones and are required for
RT maintaining postembryonic root growth.";
RL Plant Cell 18:2879-2892(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=19825649; DOI=10.1093/mp/ssp026;
RA Liu Z.Q., Gao J., Dong A.W., Shen W.H.;
RT "A truncated Arabidopsis NUCLEOSOME ASSEMBLY PROTEIN 1, AtNAP1;3T, alters
RT plant growth responses to abscisic acid and salt in the Atnap1;3-2
RT mutant.";
RL Mol. Plant 2:688-699(2009).
RN [9]
RP GENE FAMILY, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION,
RP AND INTERACTION WITH HISTONE H2A.
RX PubMed=19228338; DOI=10.1111/j.1365-313x.2009.03844.x;
RA Liu Z., Zhu Y., Gao J., Yu F., Dong A., Shen W.H.;
RT "Molecular and reverse genetic characterization of NUCLEOSOME ASSEMBLY
RT PROTEIN1 (NAP1) genes unravels their function in transcription and
RT nucleotide excision repair in Arabidopsis thaliana.";
RL Plant J. 59:27-38(2009).
RN [10]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21571540; DOI=10.1016/j.plaphy.2011.04.012;
RA Shigeta T., Yasuda D., Mori T., Yoshimitsu Y., Nakamura Y., Yoshida S.,
RA Asami T., Okamoto S., Matsuo T.;
RT "Characterization of brassinosteroid-regulated proteins in a nuclear-
RT enriched fraction of Arabidopsis suspension-cultured cells.";
RL Plant Physiol. Biochem. 49:985-995(2011).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22534127; DOI=10.1105/tpc.112.096792;
RA Gao J., Zhu Y., Zhou W., Molinier J., Dong A., Shen W.H.;
RT "NAP1 family histone chaperones are required for somatic homologous
RT recombination in Arabidopsis.";
RL Plant Cell 24:1437-1447(2012).
CC -!- FUNCTION: May modulate chromatin structure by regulation of nucleosome
CC assembly/disassembly (By similarity). May function in nucleotide
CC excision repair (NER). Involved in somatic homologous recombination.
CC {ECO:0000250, ECO:0000269|PubMed:19228338,
CC ECO:0000269|PubMed:22534127}.
CC -!- SUBUNIT: Can form homomeric and heteromeric protein complexes with
CC NAP1;1, NAP1;3 and NAP1;4. Binds histone H2A.
CC {ECO:0000269|PubMed:19228338}.
CC -!- INTERACTION:
CC Q9ZUP3; Q9SZI2: NAP1;1; NbExp=4; IntAct=EBI-1997989, EBI-4424361;
CC Q9ZUP3; Q9ZUP3: NAP1;2; NbExp=2; IntAct=EBI-1997989, EBI-1997989;
CC Q9ZUP3; Q94K07: NAP1;3; NbExp=5; IntAct=EBI-1997989, EBI-4430887;
CC Q9ZUP3; F4JEI8: NAP1;4; NbExp=3; IntAct=EBI-1997989, EBI-6913300;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:19228338}. Note=Predominantly located in cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZUP3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17122067}.
CC -!- INDUCTION: By brassinosteroids. {ECO:0000269|PubMed:21571540}.
CC -!- DOMAIN: The acidic domain is probably involved in the interaction with
CC histones.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19228338, ECO:0000269|PubMed:19825649,
CC ECO:0000269|PubMed:22534127}.
CC -!- MISCELLANEOUS: Triple mutant nap1;1-nap1;2-nap1;3 has no obvious
CC visible phenotype but exhibits hypersensitivity to DNA damage after UV-
CC radiation, affected transcription of NER related genes
CC (PubMed:19228338), slight hypersensitive response to abscisic acid
CC (ABA) in seedling growth (PubMed:19825649) and impaired somatic
CC homologous recombination (PubMed:22534127).
CC {ECO:0000305|PubMed:19228338, ECO:0000305|PubMed:19825649,
CC ECO:0000305|PubMed:22534127}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; AC005917; AAD10147.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06885.1; -; Genomic_DNA.
DR EMBL; AY099771; AAM20622.1; -; mRNA.
DR EMBL; BT002602; AAO00962.1; -; mRNA.
DR EMBL; AK316769; BAH19489.1; -; mRNA.
DR PIR; C84577; C84577.
DR RefSeq; NP_179538.1; NM_127506.5. [Q9ZUP3-1]
DR AlphaFoldDB; Q9ZUP3; -.
DR SMR; Q9ZUP3; -.
DR BioGRID; 1822; 24.
DR IntAct; Q9ZUP3; 6.
DR STRING; 3702.AT2G19480.1; -.
DR iPTMnet; Q9ZUP3; -.
DR MetOSite; Q9ZUP3; -.
DR PaxDb; Q9ZUP3; -.
DR PRIDE; Q9ZUP3; -.
DR EnsemblPlants; AT2G19480.1; AT2G19480.1; AT2G19480. [Q9ZUP3-1]
DR GeneID; 816467; -.
DR Gramene; AT2G19480.1; AT2G19480.1; AT2G19480. [Q9ZUP3-1]
DR KEGG; ath:AT2G19480; -.
DR Araport; AT2G19480; -.
DR TAIR; locus:2050424; AT2G19480.
DR eggNOG; KOG1507; Eukaryota.
DR InParanoid; Q9ZUP3; -.
DR OrthoDB; 1216172at2759; -.
DR PhylomeDB; Q9ZUP3; -.
DR PRO; PR:Q9ZUP3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUP3; baseline and differential.
DR Genevisible; Q9ZUP3; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006281; P:DNA repair; IGI:TAIR.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0016444; P:somatic cell DNA recombination; IMP:UniProtKB.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Coiled coil; Cytoplasm; Lipoprotein;
KW Methylation; Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..376
FT /note="Nucleosome assembly protein 1;2"
FT /id="PRO_0000423678"
FT PROPEP 377..379
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT /id="PRO_0000423679"
FT REGION 298..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..80
FT /evidence="ECO:0000255"
FT MOTIF 47..62
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 222..227
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 300..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 376
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
FT LIPID 376
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SZI2"
SQ SEQUENCE 379 AA; 43543 MW; C5FAB1ABC318A8DC CRC64;
MSNDKDSMNM SDLSTALNEE DRAGLVNALK NKLQNLAGQH SDVLENLTPP VRKRVEFLRE
IQNQYDEMEA KFFEERAALE AKYQKLYQPL YTKRYEIVNG VVEVEGAAEE VKSEQGEDKS
AEEKGVPDFW LIALKNNEIT AEEITERDEG ALKYLKDIKW SRVEEPKGFK LEFFFDQNPY
FKNTVLTKTY HMIDEDEPIL EKALGTEIEW YPGKCLTQKI LKKKPKKGSK NTKPITKTED
CESFFNFFSP PQVPDDDEDL DDDMADELQG QMEHDYDIGS TIKEKIISHA VSWFTGEAVE
ADDLDIEDDD DEIDEDDDEE DEEDDEDDEE EDDEDDDEEE EADQGKKSKK KSSAGHKKAG
RSQLAEGQAG ERPPECKQQ
