Full text data of NAP1L4
NAP1L4
(NAP2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2; NAP-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nucleosome assembly protein 1-like 4 (Nucleosome assembly protein 2; NAP-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00017763
IPI00017763 Nucleosome assembly protein 1-like 4 ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 80 kdDa
IPI00017763 Nucleosome assembly protein 1-like 4 ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 80 kdDa
UniProt
Q99733
ID NP1L4_HUMAN Reviewed; 375 AA.
AC Q99733;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
DE AltName: Full=Nucleosome assembly protein 2;
DE Short=NAP-2;
GN Name=NAP1L4; Synonyms=NAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and adult tissues.";
RL Hum. Mol. Genet. 5:1743-1748(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND SER-125, AND MASS
RP SPECTROMETRY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-304, AND
RP MASS SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-7; SER-12; THR-51; SER-54 AND SER-125,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-7; SER-12 AND SER-125, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- INTERACTION:
CC P04608:tat (xeno); NbExp=3; IntAct=EBI-2255116, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Biallelically expressed in fetal
CC and adult tissues. Highest levels in testis.
CC -!- PTM: Polyglutamylated by TTLL4, a modification that occurs
CC exclusively on glutamate residues and results in polyglutamate
CC chains on the gamma-carboxyl group. Some residues may also be
CC monoglycylated but not polyglycylated due to the absence of
CC functional TTLL10 in human (By similarity).
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U77456; AAC50870.1; -; mRNA.
DR EMBL; BC022090; AAH22090.1; -; mRNA.
DR RefSeq; NP_005960.1; NM_005969.3.
DR UniGene; Hs.731784; -.
DR ProteinModelPortal; Q99733; -.
DR SMR; Q99733; 53-340.
DR IntAct; Q99733; 6.
DR MINT; MINT-5001909; -.
DR STRING; 9606.ENSP00000369915; -.
DR PhosphoSite; Q99733; -.
DR DMDM; 2498672; -.
DR PaxDb; Q99733; -.
DR PRIDE; Q99733; -.
DR DNASU; 4676; -.
DR Ensembl; ENST00000380542; ENSP00000369915; ENSG00000205531.
DR GeneID; 4676; -.
DR KEGG; hsa:4676; -.
DR UCSC; uc001lxc.3; human.
DR CTD; 4676; -.
DR GeneCards; GC11M002965; -.
DR HGNC; HGNC:7640; NAP1L4.
DR HPA; CAB011567; -.
DR MIM; 601651; gene.
DR neXtProt; NX_Q99733; -.
DR PharmGKB; PA31442; -.
DR eggNOG; NOG285183; -.
DR HOGENOM; HOG000171827; -.
DR HOVERGEN; HBG052653; -.
DR KO; K11282; -.
DR ChiTaRS; NAP1L4; human.
DR GeneWiki; NAP1L4; -.
DR GenomeRNAi; 4676; -.
DR NextBio; 18024; -.
DR PMAP-CutDB; Q99733; -.
DR PRO; PR:Q99733; -.
DR ArrayExpress; Q99733; -.
DR Bgee; Q99733; -.
DR CleanEx; HS_NAP1L4; -.
DR Genevestigator; Q99733; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 375 Nucleosome assembly protein 1-like 4.
FT /FTId=PRO_0000185658.
FT MOTIF 265 271 Nuclear localization signal (Potential).
FT COMPBIAS 126 131 Poly-Glu.
FT COMPBIAS 301 310 Asp/Glu-rich (acidic).
FT COMPBIAS 347 370 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 51 51 Phosphothreonine.
FT MOD_RES 54 54 Phosphoserine.
FT MOD_RES 125 125 Phosphoserine.
FT MOD_RES 304 304 Phosphoserine.
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
//
ID NP1L4_HUMAN Reviewed; 375 AA.
AC Q99733;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1997, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
DE AltName: Full=Nucleosome assembly protein 2;
DE Short=NAP-2;
GN Name=NAP1L4; Synonyms=NAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and adult tissues.";
RL Hum. Mol. Genet. 5:1743-1748(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND SER-125, AND MASS
RP SPECTROMETRY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-304, AND
RP MASS SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-7; SER-12; THR-51; SER-54 AND SER-125,
RP AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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.,
RA Buerckstuemmer T., 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5; SER-7; SER-12 AND SER-125, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- INTERACTION:
CC P04608:tat (xeno); NbExp=3; IntAct=EBI-2255116, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Biallelically expressed in fetal
CC and adult tissues. Highest levels in testis.
CC -!- PTM: Polyglutamylated by TTLL4, a modification that occurs
CC exclusively on glutamate residues and results in polyglutamate
CC chains on the gamma-carboxyl group. Some residues may also be
CC monoglycylated but not polyglycylated due to the absence of
CC functional TTLL10 in human (By similarity).
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U77456; AAC50870.1; -; mRNA.
DR EMBL; BC022090; AAH22090.1; -; mRNA.
DR RefSeq; NP_005960.1; NM_005969.3.
DR UniGene; Hs.731784; -.
DR ProteinModelPortal; Q99733; -.
DR SMR; Q99733; 53-340.
DR IntAct; Q99733; 6.
DR MINT; MINT-5001909; -.
DR STRING; 9606.ENSP00000369915; -.
DR PhosphoSite; Q99733; -.
DR DMDM; 2498672; -.
DR PaxDb; Q99733; -.
DR PRIDE; Q99733; -.
DR DNASU; 4676; -.
DR Ensembl; ENST00000380542; ENSP00000369915; ENSG00000205531.
DR GeneID; 4676; -.
DR KEGG; hsa:4676; -.
DR UCSC; uc001lxc.3; human.
DR CTD; 4676; -.
DR GeneCards; GC11M002965; -.
DR HGNC; HGNC:7640; NAP1L4.
DR HPA; CAB011567; -.
DR MIM; 601651; gene.
DR neXtProt; NX_Q99733; -.
DR PharmGKB; PA31442; -.
DR eggNOG; NOG285183; -.
DR HOGENOM; HOG000171827; -.
DR HOVERGEN; HBG052653; -.
DR KO; K11282; -.
DR ChiTaRS; NAP1L4; human.
DR GeneWiki; NAP1L4; -.
DR GenomeRNAi; 4676; -.
DR NextBio; 18024; -.
DR PMAP-CutDB; Q99733; -.
DR PRO; PR:Q99733; -.
DR ArrayExpress; Q99733; -.
DR Bgee; Q99733; -.
DR CleanEx; HS_NAP1L4; -.
DR Genevestigator; Q99733; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 375 Nucleosome assembly protein 1-like 4.
FT /FTId=PRO_0000185658.
FT MOTIF 265 271 Nuclear localization signal (Potential).
FT COMPBIAS 126 131 Poly-Glu.
FT COMPBIAS 301 310 Asp/Glu-rich (acidic).
FT COMPBIAS 347 370 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 7 7 Phosphoserine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 51 51 Phosphothreonine.
FT MOD_RES 54 54 Phosphoserine.
FT MOD_RES 125 125 Phosphoserine.
FT MOD_RES 304 304 Phosphoserine.
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
//
MIM
601651
*RECORD*
*FIELD* NO
601651
*FIELD* TI
*601651 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 4; NAP1L4
;;NUCLEOSOME ASSEMBLY PROTEIN 2-LIKE; NAP2L;;
read moreNAP2
*FIELD* TX
CLONING
Hu et al. (1996) used a positional cloning approach to isolate a gene
which is located 100 kb centromeric to the proximal Beckwith-Wiedemann
breakpoint cluster region (BWS; 130650) on chromosome 11p15. This gene
is homologous to the yeast nucleosome assembly protein NAP1 (164060).
The authors designated the new gene NAP2. They demonstrated that this
gene shows biallelic expression in all tissues tested and that it
therefore diverges in its expression from IGF2 (147470), H19 (103280),
and p57(KIP2) (600856), which also map to 11p15.5 in the vicinity of the
BWS gene. The NAP2 gene encodes a highly acidic protein of 375 amino
acids.
GENE STRUCTURE
Rodriguez et al. (1997) reported that the NAP1L4 gene consists of 14
exons and spans approximately 30.5 kb. A 1,200-bp 3-prime untranslated
region was present.
MAPPING
Hu et al. (1996) mapped the NAP1L4 gene to chromosome 11p15.5.
GENE FUNCTION
Histones are thought to play a key role in regulating gene expression at
the level of DNA packaging. The deduced amino acid sequence of NAP2
indicates that it is a protein with a potential nuclear localization
motif and 2 clusters of highly acidic residues. By functional analysis
of recombinant NAP2 protein purified from Escherichia coli, Rodriguez et
al. (1997) found that this protein can interact with both core and
linker histones (see 142709). They demonstrated that recombinant NAP2
can transfer histones onto naked DNA templates. Subcellular localization
studies of NAP2 indicated that it can shuttle between the cytoplasm and
nucleus, suggesting a role as a histone chaperone.
NAP1 and NAP2 facilitate nucleosome assembly by first depositing
preformed tetramers made up of 2 molecules each of histones H3 (see
602810) and H4 (see 602822) onto DNA prior to the addition of tetramers
made up of 2 molecules each of histones H2A (see 142720) and H2B (see
609904). Using recombinant human proteins in an in vitro nucleosome
formation assay, Tachiwana et al. (2008) confirmed that both NAP1 and
NAP2 promoted formation of nucleosomes containing the conventional
histones H2A, H2B, H3.1 (see 602810), and H4. NAP1 could also promote
nucleosome assembly with the H3 variants H3.2 (HIST2H3C; 142780), H3.3
(see 601128), and CENPA (117139), but not the testis-specific H3 variant
H3T (HIST3H3; 602820). In contrast, NAP2 promoted nucleosome assembly
with H3T, bound H3T/H4 tetramers efficiently, and was released from
H3T/H4 tetramers in the presence of DNA. Mutation analysis revealed that
a change of ala111, which is conserved among H3.1, H3.2, and H3.3, to
val in H3T was responsible for the differential binding of these H3
variants to NAP1.
MOLECULAR GENETICS
NAP1L4 maps to a region implicated in Wilms tumor etiology (see 194071).
Rodriguez et al. (1997) analyzed the gene encoding NAP2 for mutations
and found no evidence of nonsense, frameshift, or deletion mutations.
Their findings, coupled with tumor suppression assays in Wilms tumor
cells, did not support a role for NAP2 in the etiology of that neoplasm.
*FIELD* RF
1. Hu, R.-J.; Lee, M. P.; Johnson, L. A.; Feinberg, A. P.: A novel
human homologue of yeast nucleosome assembly protein, 65 kb centromeric
to the p57(KIP2) gene, is biallelically expressed in fetal and adult
tissues. Hum. Molec. Genet. 5: 1743-1748, 1996.
2. Rodriguez, P.; Munroe, D.; Prawitt, D.; Chu, L. L.; Bric, E.; Kim,
J.; Reid, L. H.; Davies, C.; Nakagama, H.; Loebbert, R.; Winterpacht,
A.; Petruzzi, M.-J.; Higgins, M. J.; Nowak, N.; Evans, G.; Shows,
T.; Weissman, B. E.; Zabel, B.; Housman, D. E.; Pelletier, J.: Functional
characterization of human nucleosome assembly protein-2 (NAP1L4) suggests
a role as a histone chaperone. Genomics 44: 253-265, 1997.
3. Tachiwana, H.; Osakabe, A.; Kimura, H.; Kurumizaka, H.: Nucleosome
formation with the testis-specific histone H3 variant, H3t, by human
nucleosome assembly proteins in vitro. Nucleic Acids Res. 36: 2208-2218,
2008.
*FIELD* CN
Victor A. McKusick - updated: 10/14/1997
*FIELD* CD
Moyra Smith: 1/28/1997
*FIELD* ED
mgross: 02/06/2013
terry: 10/16/1997
terry: 10/14/1997
mark: 6/4/1997
mark: 1/30/1997
mark: 1/29/1997
terry: 1/29/1997
mark: 1/28/1997
*RECORD*
*FIELD* NO
601651
*FIELD* TI
*601651 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 4; NAP1L4
;;NUCLEOSOME ASSEMBLY PROTEIN 2-LIKE; NAP2L;;
read moreNAP2
*FIELD* TX
CLONING
Hu et al. (1996) used a positional cloning approach to isolate a gene
which is located 100 kb centromeric to the proximal Beckwith-Wiedemann
breakpoint cluster region (BWS; 130650) on chromosome 11p15. This gene
is homologous to the yeast nucleosome assembly protein NAP1 (164060).
The authors designated the new gene NAP2. They demonstrated that this
gene shows biallelic expression in all tissues tested and that it
therefore diverges in its expression from IGF2 (147470), H19 (103280),
and p57(KIP2) (600856), which also map to 11p15.5 in the vicinity of the
BWS gene. The NAP2 gene encodes a highly acidic protein of 375 amino
acids.
GENE STRUCTURE
Rodriguez et al. (1997) reported that the NAP1L4 gene consists of 14
exons and spans approximately 30.5 kb. A 1,200-bp 3-prime untranslated
region was present.
MAPPING
Hu et al. (1996) mapped the NAP1L4 gene to chromosome 11p15.5.
GENE FUNCTION
Histones are thought to play a key role in regulating gene expression at
the level of DNA packaging. The deduced amino acid sequence of NAP2
indicates that it is a protein with a potential nuclear localization
motif and 2 clusters of highly acidic residues. By functional analysis
of recombinant NAP2 protein purified from Escherichia coli, Rodriguez et
al. (1997) found that this protein can interact with both core and
linker histones (see 142709). They demonstrated that recombinant NAP2
can transfer histones onto naked DNA templates. Subcellular localization
studies of NAP2 indicated that it can shuttle between the cytoplasm and
nucleus, suggesting a role as a histone chaperone.
NAP1 and NAP2 facilitate nucleosome assembly by first depositing
preformed tetramers made up of 2 molecules each of histones H3 (see
602810) and H4 (see 602822) onto DNA prior to the addition of tetramers
made up of 2 molecules each of histones H2A (see 142720) and H2B (see
609904). Using recombinant human proteins in an in vitro nucleosome
formation assay, Tachiwana et al. (2008) confirmed that both NAP1 and
NAP2 promoted formation of nucleosomes containing the conventional
histones H2A, H2B, H3.1 (see 602810), and H4. NAP1 could also promote
nucleosome assembly with the H3 variants H3.2 (HIST2H3C; 142780), H3.3
(see 601128), and CENPA (117139), but not the testis-specific H3 variant
H3T (HIST3H3; 602820). In contrast, NAP2 promoted nucleosome assembly
with H3T, bound H3T/H4 tetramers efficiently, and was released from
H3T/H4 tetramers in the presence of DNA. Mutation analysis revealed that
a change of ala111, which is conserved among H3.1, H3.2, and H3.3, to
val in H3T was responsible for the differential binding of these H3
variants to NAP1.
MOLECULAR GENETICS
NAP1L4 maps to a region implicated in Wilms tumor etiology (see 194071).
Rodriguez et al. (1997) analyzed the gene encoding NAP2 for mutations
and found no evidence of nonsense, frameshift, or deletion mutations.
Their findings, coupled with tumor suppression assays in Wilms tumor
cells, did not support a role for NAP2 in the etiology of that neoplasm.
*FIELD* RF
1. Hu, R.-J.; Lee, M. P.; Johnson, L. A.; Feinberg, A. P.: A novel
human homologue of yeast nucleosome assembly protein, 65 kb centromeric
to the p57(KIP2) gene, is biallelically expressed in fetal and adult
tissues. Hum. Molec. Genet. 5: 1743-1748, 1996.
2. Rodriguez, P.; Munroe, D.; Prawitt, D.; Chu, L. L.; Bric, E.; Kim,
J.; Reid, L. H.; Davies, C.; Nakagama, H.; Loebbert, R.; Winterpacht,
A.; Petruzzi, M.-J.; Higgins, M. J.; Nowak, N.; Evans, G.; Shows,
T.; Weissman, B. E.; Zabel, B.; Housman, D. E.; Pelletier, J.: Functional
characterization of human nucleosome assembly protein-2 (NAP1L4) suggests
a role as a histone chaperone. Genomics 44: 253-265, 1997.
3. Tachiwana, H.; Osakabe, A.; Kimura, H.; Kurumizaka, H.: Nucleosome
formation with the testis-specific histone H3 variant, H3t, by human
nucleosome assembly proteins in vitro. Nucleic Acids Res. 36: 2208-2218,
2008.
*FIELD* CN
Victor A. McKusick - updated: 10/14/1997
*FIELD* CD
Moyra Smith: 1/28/1997
*FIELD* ED
mgross: 02/06/2013
terry: 10/16/1997
terry: 10/14/1997
mark: 6/4/1997
mark: 1/30/1997
mark: 1/29/1997
terry: 1/29/1997
mark: 1/28/1997