NP1L1_BOVIN
ID NP1L1_BOVIN Reviewed; 391 AA.
AC A6H767;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nucleosome assembly protein 1-like 1;
DE Flags: Precursor;
GN Name=NAP1L1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC146131; AAI46132.1; -; mRNA.
DR RefSeq; NP_001092685.1; NM_001099215.2.
DR RefSeq; XP_015326352.1; XM_015470866.1.
DR AlphaFoldDB; A6H767; -.
DR SMR; A6H767; -.
DR STRING; 9913.ENSBTAP00000027852; -.
DR PaxDb; A6H767; -.
DR PeptideAtlas; A6H767; -.
DR PRIDE; A6H767; -.
DR GeneID; 790872; -.
DR KEGG; bta:790872; -.
DR CTD; 4673; -.
DR eggNOG; KOG1507; Eukaryota.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; A6H767; -.
DR OrthoDB; 1216172at2759; -.
DR TreeFam; TF314349; -.
DR Proteomes; UP000009136; Unplaced.
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: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:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript 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..388
FT /note="Nucleosome assembly protein 1-like 1"
FT /id="PRO_0000317139"
FT PROPEP 389..391
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT /id="PRO_0000396685"
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 345..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 345..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:0000250|UniProtKB:P55209"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
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 359
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 360
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 388
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 388
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P55209"
SQ SEQUENCE 391 AA; 45376 MW; C65ACB2870B17F30 CRC64;
MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA ALQERLDGLV
ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI
INAIYEPTEE ECEWKPDEED EISEELKEKA KVEDEKKDEE KEDPKGIPEF WLTVFKNVDL
LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD
DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF
FAPPEVPESG DLDDDSEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE
ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q
