NP1L4_RAT
ID NP1L4_RAT Reviewed; 386 AA.
AC Q5U2Z3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Nucleosome assembly protein 1-like 4;
GN Name=Nap1l4;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-51; SER-53 AND
RP SER-125, AND 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: 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; BC085801; AAH85801.1; -; mRNA.
DR RefSeq; NP_001012170.1; NM_001012170.1.
DR RefSeq; XP_006230885.1; XM_006230823.3.
DR RefSeq; XP_006230886.1; XM_006230824.3.
DR AlphaFoldDB; Q5U2Z3; -.
DR SMR; Q5U2Z3; -.
DR BioGRID; 262874; 2.
DR IntAct; Q5U2Z3; 2.
DR STRING; 10116.ENSRNOP00000051745; -.
DR iPTMnet; Q5U2Z3; -.
DR PhosphoSitePlus; Q5U2Z3; -.
DR SwissPalm; Q5U2Z3; -.
DR jPOST; Q5U2Z3; -.
DR PaxDb; Q5U2Z3; -.
DR PRIDE; Q5U2Z3; -.
DR GeneID; 361684; -.
DR KEGG; rno:361684; -.
DR UCSC; RGD:1305391; rat.
DR CTD; 4676; -.
DR RGD; 1305391; Nap1l4.
DR VEuPathDB; HostDB:ENSRNOG00000020615; -.
DR eggNOG; KOG1507; Eukaryota.
DR InParanoid; Q5U2Z3; -.
DR OrthoDB; 1216172at2759; -.
DR PRO; PR:Q5U2Z3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020615; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; Q5U2Z3; baseline and differential.
DR Genevisible; Q5U2Z3; RN.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; 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: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 1: Evidence at protein 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_0000236214"
FT REGION 1..28
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:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78ZA7"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
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; 43917 MW; 7A7A5166964D7AFE CRC64;
MAENSLSDGG PADSVEAAKN ASNTEKLTDQ VMQNPQVLAA LQERLDNVSH TPSSYIETLP
KAVKRRINAL KQLQVRCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE
SAWHSENEED DKLAGDMKNK VVIAEKEAAA VEELNPKGIP EFWFTIFRNV DMLSELVQEY
DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPNDYFTNPV LTKTYKMKSE PDKADPFSFE
GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNESFF NFFSPLKASG
DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD
EEGEDEDDAD VNPKKEPIQP AECKQQ
