Full text data of NAP1L1
NAP1L1
(NRP)
[Confidence: high (present in two of the MS resources)]
Nucleosome assembly protein 1-like 1 (NAP-1-related protein; hNRP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nucleosome assembly protein 1-like 1 (NAP-1-related protein; hNRP; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00023860
IPI00023860 Nucleosome assembly protein 1-like 1 May be involved in modulating chromatin formation and contribute to regulation of cell proliferation 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 cytoplasmic and nuclear n/a expected molecular weight found in band found in band around 80 kdDa
IPI00023860 Nucleosome assembly protein 1-like 1 May be involved in modulating chromatin formation and contribute to regulation of cell proliferation 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 cytoplasmic and nuclear n/a expected molecular weight found in band found in band around 80 kdDa
UniProt
P55209
ID NP1L1_HUMAN Reviewed; 391 AA.
AC P55209;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=8297347;
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
RT nucleosome-assembly-protein-I-related gene product involved in the
RT induction of cell proliferation.";
RL Biochem. J. 297:389-397(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 [5]
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.,
RA Jaunbergs J., 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 [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-62; SER-69 AND
RP SER-143, AND MASS 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 [11]
RP INTERACTION WITH HIV-1 TAT.
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)
RT binds HIV-1 Tat and promotes viral transcription.";
RL Retrovirology 5:8-8(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND MASS
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND MASS
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, 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).
RN [18]
RP IDENTIFICATION 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in modulating chromatin formation and
CC contribute to regulation of cell proliferation.
CC -!- INTERACTION:
CC Q92793:CREBBP; NbExp=3; IntAct=EBI-356392, EBI-81215;
CC Q09472:EP300; NbExp=3; IntAct=EBI-356392, EBI-447295;
CC P10588:NR2F6; NbExp=2; IntAct=EBI-356392, EBI-2681496;
CC Q6ZVT0:TTLL10; NbExp=5; IntAct=EBI-356392, EBI-7844656;
CC -!- SUBCELLULAR LOCATION: Nucleus. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The acidic domains are probably involved in the
CC interaction with histones.
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.
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DR EMBL; M86667; AAC37544.1; -; mRNA.
DR EMBL; BT007023; AAP35669.1; -; mRNA.
DR EMBL; AL162068; CAB82405.1; -; mRNA.
DR EMBL; BC002387; AAH02387.1; -; mRNA.
DR PIR; S40510; S40510.
DR RefSeq; NP_004528.1; NM_004537.4.
DR RefSeq; NP_631946.1; NM_139207.2.
DR UniGene; Hs.524599; -.
DR UniGene; Hs.695185; -.
DR ProteinModelPortal; P55209; -.
DR SMR; P55209; 64-347.
DR IntAct; P55209; 46.
DR MINT; MINT-150144; -.
DR STRING; 9606.ENSP00000261182; -.
DR PhosphoSite; P55209; -.
DR DMDM; 1709337; -.
DR OGP; P55209; -.
DR PaxDb; P55209; -.
DR PRIDE; P55209; -.
DR DNASU; 4673; -.
DR Ensembl; ENST00000261182; ENSP00000261182; ENSG00000187109.
DR Ensembl; ENST00000393263; ENSP00000376947; ENSG00000187109.
DR GeneID; 4673; -.
DR KEGG; hsa:4673; -.
DR UCSC; uc001sxw.2; human.
DR CTD; 4673; -.
DR GeneCards; GC12M076438; -.
DR HGNC; HGNC:7637; NAP1L1.
DR HPA; HPA028861; -.
DR MIM; 164060; gene.
DR neXtProt; NX_P55209; -.
DR PharmGKB; PA31439; -.
DR eggNOG; NOG285183; -.
DR HOGENOM; HOG000171827; -.
DR HOVERGEN; HBG052653; -.
DR InParanoid; P55209; -.
DR KO; K11279; -.
DR OMA; FIYDHAD; -.
DR OrthoDB; EOG73Z2T8; -.
DR PhylomeDB; P55209; -.
DR ChiTaRS; NAP1L1; human.
DR GeneWiki; NAP1L1; -.
DR GenomeRNAi; 4673; -.
DR NextBio; 18010; -.
DR PMAP-CutDB; P55209; -.
DR PRO; PR:P55209; -.
DR ArrayExpress; P55209; -.
DR Bgee; P55209; -.
DR CleanEx; HS_NAP1L1; -.
DR Genevestigator; P55209; -.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
DR GO; GO:0008284; P:positive regulation of cell proliferation; 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; Lipoprotein; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 388 Nucleosome assembly protein 1-like 1.
FT /FTId=PRO_0000185652.
FT PROPEP 389 391 Removed in mature form (Probable).
FT /FTId=PRO_0000393943.
FT MOTIF 273 279 Nuclear localization signal (Potential).
FT COMPBIAS 10 30 Asp/Glu-rich (acidic).
FT COMPBIAS 129 145 Asp/Glu-rich (acidic).
FT COMPBIAS 348 378 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphoserine.
FT MOD_RES 62 62 Phosphothreonine.
FT MOD_RES 69 69 Phosphoserine.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 388 388 Cysteine methyl ester (Probable).
FT LIPID 388 388 S-farnesyl cysteine.
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
//
ID NP1L1_HUMAN Reviewed; 391 AA.
AC P55209;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=8297347;
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
RT nucleosome-assembly-protein-I-related gene product involved in the
RT induction of cell proliferation.";
RL Biochem. J. 297:389-397(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 [5]
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.,
RA Jaunbergs J., 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 [6]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-62; SER-69 AND
RP SER-143, AND MASS 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 [11]
RP INTERACTION WITH HIV-1 TAT.
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)
RT binds HIV-1 Tat and promotes viral transcription.";
RL Retrovirology 5:8-8(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND MASS
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND MASS
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, 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).
RN [18]
RP IDENTIFICATION 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in modulating chromatin formation and
CC contribute to regulation of cell proliferation.
CC -!- INTERACTION:
CC Q92793:CREBBP; NbExp=3; IntAct=EBI-356392, EBI-81215;
CC Q09472:EP300; NbExp=3; IntAct=EBI-356392, EBI-447295;
CC P10588:NR2F6; NbExp=2; IntAct=EBI-356392, EBI-2681496;
CC Q6ZVT0:TTLL10; NbExp=5; IntAct=EBI-356392, EBI-7844656;
CC -!- SUBCELLULAR LOCATION: Nucleus. Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The acidic domains are probably involved in the
CC interaction with histones.
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.
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DR EMBL; M86667; AAC37544.1; -; mRNA.
DR EMBL; BT007023; AAP35669.1; -; mRNA.
DR EMBL; AL162068; CAB82405.1; -; mRNA.
DR EMBL; BC002387; AAH02387.1; -; mRNA.
DR PIR; S40510; S40510.
DR RefSeq; NP_004528.1; NM_004537.4.
DR RefSeq; NP_631946.1; NM_139207.2.
DR UniGene; Hs.524599; -.
DR UniGene; Hs.695185; -.
DR ProteinModelPortal; P55209; -.
DR SMR; P55209; 64-347.
DR IntAct; P55209; 46.
DR MINT; MINT-150144; -.
DR STRING; 9606.ENSP00000261182; -.
DR PhosphoSite; P55209; -.
DR DMDM; 1709337; -.
DR OGP; P55209; -.
DR PaxDb; P55209; -.
DR PRIDE; P55209; -.
DR DNASU; 4673; -.
DR Ensembl; ENST00000261182; ENSP00000261182; ENSG00000187109.
DR Ensembl; ENST00000393263; ENSP00000376947; ENSG00000187109.
DR GeneID; 4673; -.
DR KEGG; hsa:4673; -.
DR UCSC; uc001sxw.2; human.
DR CTD; 4673; -.
DR GeneCards; GC12M076438; -.
DR HGNC; HGNC:7637; NAP1L1.
DR HPA; HPA028861; -.
DR MIM; 164060; gene.
DR neXtProt; NX_P55209; -.
DR PharmGKB; PA31439; -.
DR eggNOG; NOG285183; -.
DR HOGENOM; HOG000171827; -.
DR HOVERGEN; HBG052653; -.
DR InParanoid; P55209; -.
DR KO; K11279; -.
DR OMA; FIYDHAD; -.
DR OrthoDB; EOG73Z2T8; -.
DR PhylomeDB; P55209; -.
DR ChiTaRS; NAP1L1; human.
DR GeneWiki; NAP1L1; -.
DR GenomeRNAi; 4673; -.
DR NextBio; 18010; -.
DR PMAP-CutDB; P55209; -.
DR PRO; PR:P55209; -.
DR ArrayExpress; P55209; -.
DR Bgee; P55209; -.
DR CleanEx; HS_NAP1L1; -.
DR Genevestigator; P55209; -.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006334; P:nucleosome assembly; TAS:ProtInc.
DR GO; GO:0008284; P:positive regulation of cell proliferation; 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; Lipoprotein; Methylation; Nucleus;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 388 Nucleosome assembly protein 1-like 1.
FT /FTId=PRO_0000185652.
FT PROPEP 389 391 Removed in mature form (Probable).
FT /FTId=PRO_0000393943.
FT MOTIF 273 279 Nuclear localization signal (Potential).
FT COMPBIAS 10 30 Asp/Glu-rich (acidic).
FT COMPBIAS 129 145 Asp/Glu-rich (acidic).
FT COMPBIAS 348 378 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphoserine.
FT MOD_RES 62 62 Phosphothreonine.
FT MOD_RES 69 69 Phosphoserine.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 388 388 Cysteine methyl ester (Probable).
FT LIPID 388 388 S-farnesyl cysteine.
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
//
MIM
164060
*RECORD*
*FIELD* NO
164060
*FIELD* TI
*164060 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 1; NAP1L1
;;NAP1; NAP1L;;
NAPI-RELATED PROTEIN; NRP;;
read moreNUCLEOSOME ASSEMBLY PROTEIN I-RELATED PROTEIN
*FIELD* TX
CLONING
From a human thymus cDNA library, Simon et al. (1994) isolated a cDNA
encoding a protein with 54% amino acid similarity to yeast nucleosome
assembly protein I (NAPI). The deduced amino acid sequence of the
identified protein, designated NRP (for 'NAP-related protein'), has a
potential 7-residue nuclear localization motif, 3 clusters of highly
acidic residues, and other structural features found in various proteins
implicated in chromatin formation. NRP transcript was detected in all
human tissues and cell lines studied, but levels were somewhat increased
in rapidly proliferating cells. This and other observations suggested to
the authors that the NRP gene product participates in DNA replication
and therefore plays an important role in the process of cell
proliferation.
GENE FUNCTION
Hajkova et al. (2008) studied epigenetic changes in primordial germ
cells (PGCs) in the mouse lineage. They showed that the chromatin
changes occur in 2 steps. The first changes in nascent PGCs at embryonic
day 8.5 establish a distinctive chromatin signature that is reminiscent
of pluripotency. Next, when PGCs are residing in the gonads, major
changes occur in nuclear architecture accompanied by an extensive
erasure of several histone modifications and exchange of histone
variants. Furthermore, the histone chaperones HIRA (600237) and NAP1,
which are implicated in histone exchange, accumulate in PGC nuclei
undergoing reprogramming. Hajkova et al. (2008) therefore suggested that
the mechanism of histone replacement is critical for these chromatin
rearrangements to occur. The marked chromatin changes are intimately
linked with genomewide DNA demethylation. On the basis of the timing of
the observed events, Hajkova et al. (2008) proposed that if DNA
demethylation entails a DNA repair-based mechanism, the evident histone
replacement would represent a repair-induced response event rather than
being a prerequisite.
NAP1 and NAP2 (NAP1L4; 601651) 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.
BIOCHEMICAL FEATURES
Park and Luger (2006) resolved the crystal structure of yeast Nap1 to
3.0-angstrom resolution. They determined that a long alpha helix
mediates homodimerization, and a domain containing both alpha helices
and beta sheets mediates protein-protein interactions. A nuclear export
sequence embedded in the dimerization helix is almost completely masked
by an accessory domain containing several putative phosphorylation
sites. Human NAP1 shares conserved motifs and a similar protein
structure with yeast Nap1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAP1L1
gene to chromosome 12 (TMAP G19924).
*FIELD* RF
1. Hajkova, P.; Ancelin, K.; Waldmann, T.; Lacoste, N.; Lange, U.
C.; Cesari, F.; Lee, C.; Almouzni, G.; Schneider, R.; Surani, M. A.
: Chromatin dynamics during epigenetic reprogramming in the mouse
germ line. Nature 452: 877-881, 2008.
2. Park, Y.-J.; Luger, K.: The structure of nucleosome assembly protein
1. Proc. Nat. Acad. Sci. 103: 1248-1253, 2006.
3. Simon, H.-U.; Mills, G. B.; Kozlowski, M.; Hogg, D.; Branch, D.;
Ishimi, Y.; Siminovitch, K. A.: Molecular characterization of hNRP,
a cDNA encoding a human nucleosome-assembly-protein-I-related gene
product involved in the induction of cell proliferation. Biochem.
J. 297: 389-397, 1994.
4. 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
Patricia A. Hartz - updated: 02/06/2013
Ada Hamosh - updated: 8/12/2008
Patricia A. Hartz - updated: 3/24/2006
Moyra Smith - updated: 1/29/1997
*FIELD* CD
Victor A. McKusick: 4/2/1994
*FIELD* ED
mgross: 02/06/2013
alopez: 8/25/2008
terry: 8/12/2008
mgross: 3/29/2006
terry: 3/24/2006
mark: 1/30/1997
terry: 1/29/1997
mark: 9/11/1996
mark: 2/2/1996
carol: 4/2/1994
*RECORD*
*FIELD* NO
164060
*FIELD* TI
*164060 NUCLEOSOME ASSEMBLY PROTEIN 1-LIKE 1; NAP1L1
;;NAP1; NAP1L;;
NAPI-RELATED PROTEIN; NRP;;
read moreNUCLEOSOME ASSEMBLY PROTEIN I-RELATED PROTEIN
*FIELD* TX
CLONING
From a human thymus cDNA library, Simon et al. (1994) isolated a cDNA
encoding a protein with 54% amino acid similarity to yeast nucleosome
assembly protein I (NAPI). The deduced amino acid sequence of the
identified protein, designated NRP (for 'NAP-related protein'), has a
potential 7-residue nuclear localization motif, 3 clusters of highly
acidic residues, and other structural features found in various proteins
implicated in chromatin formation. NRP transcript was detected in all
human tissues and cell lines studied, but levels were somewhat increased
in rapidly proliferating cells. This and other observations suggested to
the authors that the NRP gene product participates in DNA replication
and therefore plays an important role in the process of cell
proliferation.
GENE FUNCTION
Hajkova et al. (2008) studied epigenetic changes in primordial germ
cells (PGCs) in the mouse lineage. They showed that the chromatin
changes occur in 2 steps. The first changes in nascent PGCs at embryonic
day 8.5 establish a distinctive chromatin signature that is reminiscent
of pluripotency. Next, when PGCs are residing in the gonads, major
changes occur in nuclear architecture accompanied by an extensive
erasure of several histone modifications and exchange of histone
variants. Furthermore, the histone chaperones HIRA (600237) and NAP1,
which are implicated in histone exchange, accumulate in PGC nuclei
undergoing reprogramming. Hajkova et al. (2008) therefore suggested that
the mechanism of histone replacement is critical for these chromatin
rearrangements to occur. The marked chromatin changes are intimately
linked with genomewide DNA demethylation. On the basis of the timing of
the observed events, Hajkova et al. (2008) proposed that if DNA
demethylation entails a DNA repair-based mechanism, the evident histone
replacement would represent a repair-induced response event rather than
being a prerequisite.
NAP1 and NAP2 (NAP1L4; 601651) 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.
BIOCHEMICAL FEATURES
Park and Luger (2006) resolved the crystal structure of yeast Nap1 to
3.0-angstrom resolution. They determined that a long alpha helix
mediates homodimerization, and a domain containing both alpha helices
and beta sheets mediates protein-protein interactions. A nuclear export
sequence embedded in the dimerization helix is almost completely masked
by an accessory domain containing several putative phosphorylation
sites. Human NAP1 shares conserved motifs and a similar protein
structure with yeast Nap1.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAP1L1
gene to chromosome 12 (TMAP G19924).
*FIELD* RF
1. Hajkova, P.; Ancelin, K.; Waldmann, T.; Lacoste, N.; Lange, U.
C.; Cesari, F.; Lee, C.; Almouzni, G.; Schneider, R.; Surani, M. A.
: Chromatin dynamics during epigenetic reprogramming in the mouse
germ line. Nature 452: 877-881, 2008.
2. Park, Y.-J.; Luger, K.: The structure of nucleosome assembly protein
1. Proc. Nat. Acad. Sci. 103: 1248-1253, 2006.
3. Simon, H.-U.; Mills, G. B.; Kozlowski, M.; Hogg, D.; Branch, D.;
Ishimi, Y.; Siminovitch, K. A.: Molecular characterization of hNRP,
a cDNA encoding a human nucleosome-assembly-protein-I-related gene
product involved in the induction of cell proliferation. Biochem.
J. 297: 389-397, 1994.
4. 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
Patricia A. Hartz - updated: 02/06/2013
Ada Hamosh - updated: 8/12/2008
Patricia A. Hartz - updated: 3/24/2006
Moyra Smith - updated: 1/29/1997
*FIELD* CD
Victor A. McKusick: 4/2/1994
*FIELD* ED
mgross: 02/06/2013
alopez: 8/25/2008
terry: 8/12/2008
mgross: 3/29/2006
terry: 3/24/2006
mark: 1/30/1997
terry: 1/29/1997
mark: 9/11/1996
mark: 2/2/1996
carol: 4/2/1994