NP1L4_BOVIN
ID NP1L4_BOVIN Reviewed; 386 AA.
AC Q2TA40;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
GN Name=NAP1L4;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as histone chaperone in nucleosome assembly.
CC {ECO:0000250|UniProtKB:Q99733}.
CC -!- SUBUNIT: Interacts with core (H2A, H2B, H3, H4) and linker (H1)
CC histones. {ECO:0000250|UniProtKB:Q99733}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99733}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99733}. Note=Present in the cytoplasm and
CC excluded from the nucleus during G0/G1 phase, then relocates to the
CC nucleus by the time cells are in S phase. Phosphorylated form localizes
CC in the cytoplasm during the G0/G1 transition, whereas dephosphorylation
CC leads to relocalization into the nucleus at the G1/S-boundary.
CC {ECO:0000250|UniProtKB:Q99733}.
CC -!- PTM: Polyglutamylated and polyglycylated. These 2 modifications occur
CC exclusively on glutamate residues and result in either polyglutamate or
CC polyglycine chains on the gamma-carboxyl group. Both modifications can
CC coexist on the same protein on adjacent residues, and lowering
CC polyglycylation levels increases polyglutamylation, and reciprocally.
CC Polyglutamylated by TTLL4. {ECO:0000250|UniProtKB:Q78ZA7}.
CC -!- PTM: Phosphorylated at the G0/G1 boundary but it is not phosphorylated
CC in S-phase. Phosphorylated protein remains in the cytoplasm in a
CC complex with histones during the G0/G1 transition, whereas
CC dephosphorylation triggers its transport into the nucleus at the G1/S-
CC boundary. {ECO:0000250|UniProtKB:Q99733}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; BC111130; AAI11131.1; -; mRNA.
DR RefSeq; NP_001033183.1; NM_001038094.2.
DR AlphaFoldDB; Q2TA40; -.
DR SMR; Q2TA40; -.
DR STRING; 9913.ENSBTAP00000029889; -.
DR PaxDb; Q2TA40; -.
DR PeptideAtlas; Q2TA40; -.
DR PRIDE; Q2TA40; -.
DR GeneID; 513028; -.
DR KEGG; bta:513028; -.
DR CTD; 4676; -.
DR eggNOG; KOG1507; Eukaryota.
DR InParanoid; Q2TA40; -.
DR OrthoDB; 1216172at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; 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; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT CHAIN 2..386
FT /note="Nucleosome assembly protein 1-like 4"
FT /id="PRO_0000317140"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..271
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 340..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28656"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99733"
SQ SEQUENCE 386 AA; 43986 MW; B3DF233CB1CB1453 CRC64;
MADNSFSDGV PSDSLEAAKN ASNTEKLTDQ VMQNPQVLAA LQERLDNVSH TPSSYIETLP
KAVKRRINAL KQLQVKCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE
SEWHSETEEE DKLAGDMKNK AVIAEKEAAA AEEPAPRGIP EFWFTIFRNV DMLSELVQEY
DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPDDYFTNPV LTKTYKMKSE PDKADPFSFE
GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNDSFF NFFSPLRASG
DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD
EEAEDDDDAE INPKKEPSQP SECKQQ
