NP1L1_RAT
ID NP1L1_RAT Reviewed; 390 AA.
AC Q9Z2G8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Nucleosome assembly protein 1-like 1;
DE AltName: Full=NAP-1-related protein;
DE Flags: Precursor;
GN Name=Nap1l1; Synonyms=Nrp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Cataldo L.M., Zhang Y., Ravid K.;
RT "Mpl-ligand stimulates the expression of multiple mRNAs encoding a family
RT of nucleosome assembly proteins.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND THR-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Histone chaperone that plays a role in the nuclear import of
CC H2A-H2B and nucleosome assembly. Participates also in several important
CC DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin
CC remodeling which is essential for transcription-coupled nucleotide
CC excision DNA repair. Stimulates also homologous recombination (HR) by
CC RAD51 and RAD54 which is essential in mitotic DNA double strand break
CC (DSB) repair (By similarity). Plays a key role in the regulation of
CC embryonic neurogenesis (By similarity). Promotes the proliferation of
CC neural progenitors and inhibits neuronal differentiation during
CC cortical development (By similarity). Regulates neurogenesis via the
CC modulation of RASSF10; regulates RASSF10 expression by promoting
CC SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By
CC similarity). {ECO:0000250|UniProtKB:P28656,
CC ECO:0000250|UniProtKB:P55209}.
CC -!- SUBUNIT: Homodimer. The dimer binds strongly and sequentially to single
CC and double H2A-H2B heterodimers. Interacts with ERCC6; this interaction
CC increases ERCC6 processivity. Interacts with RAD54 (By similarity).
CC Interacts with SETD1A (By similarity). {ECO:0000250|UniProtKB:P28656,
CC ECO:0000250|UniProtKB:P55209}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28656}.
CC Melanosome {ECO:0000250|UniProtKB:P55209}. Cytoplasm
CC {ECO:0000250|UniProtKB:P28656}.
CC -!- DOMAIN: The acidic domains are probably involved in the interaction
CC with histones.
CC -!- PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in
CC polyglycine chains on the gamma-carboxyl group. Both polyglutamylation
CC and polyglycylation modifications can coexist on the same protein on
CC adjacent residues, and lowering polyglycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P28656}.
CC -!- PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in
CC polyglutamate chains on the gamma-carboxyl group. Both
CC polyglutamylation and polyglycylation 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; AF062594; AAC67388.1; -; mRNA.
DR RefSeq; NP_446013.2; NM_053561.2.
DR BioGRID; 250147; 3.
DR IntAct; Q9Z2G8; 1.
DR STRING; 10116.ENSRNOP00000005286; -.
DR iPTMnet; Q9Z2G8; -.
DR PhosphoSitePlus; Q9Z2G8; -.
DR SwissPalm; Q9Z2G8; -.
DR jPOST; Q9Z2G8; -.
DR PaxDb; Q9Z2G8; -.
DR PeptideAtlas; Q9Z2G8; -.
DR PRIDE; Q9Z2G8; -.
DR GeneID; 89825; -.
DR KEGG; rno:89825; -.
DR UCSC; RGD:71094; rat.
DR CTD; 4673; -.
DR RGD; 71094; Nap1l1.
DR eggNOG; KOG1507; Eukaryota.
DR InParanoid; Q9Z2G8; -.
DR PhylomeDB; Q9Z2G8; -.
DR PRO; PR:Q9Z2G8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
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:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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 GO; GO:0014010; P:Schwann cell proliferation; IEP:RGD.
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 Acetylation; Cytoplasm; Isopeptide bond; Lipoprotein; Methylation;
KW Neurogenesis; Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT CHAIN 2..387
FT /note="Nucleosome assembly protein 1-like 1"
FT /id="PRO_0000185654"
FT PROPEP 388..390
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT /id="PRO_0000396688"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..278
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 345..374
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 358
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 359
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 387
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 387
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
SQ SEQUENCE 390 AA; 45314 MW; 3D59D3C2AE1A71EB CRC64;
MADIDNKEQS ELDQDLEDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA ALQERLDGLV
DTPTGYIESL PKVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI
INAIYEPTEE ECEWKPDEED EVSEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNDLL
SDMVQEHDEP ILKHLKDIKV KFSDAGQPMS FILEFHFEPN EYFTNEVLTK TYRMRSEPDD
SDPFSFDGPE IMGCTGCQID WKKGKNVTLK TIKKKQKHKG RGTVRTVTKT VSKTSFFNFF
APPEVPENGD LDDDXEAILA ADFEIGHFLR ERIIPRSVLY FTGEAIEDDD DDYDEEGEEA
DEEGEEEGDE ENDPDYDPKK DQNPAECKQQ
