Q99733 · NP1L4_HUMAN

  • Protein
    Nucleosome assembly protein 1-like 4
  • Gene
    NAP1L4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a histone chaperone in nucleosome assembly.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionchromatin binding
Molecular Functionhistone binding
Molecular Functionnucleosome binding
Molecular FunctionRNA binding
Molecular Functionunfolded protein binding
Biological Processnucleosome assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nucleosome assembly protein 1-like 4
  • Alternative names
    • Nucleosome assembly protein 2
      (NAP-2
      )

Gene names

    • Name
      NAP1L4
    • Synonyms
      NAP2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q99733
  • Secondary accessions
    • B2R6J4
    • F5HFY4

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Note: Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase (PubMed:9325046).
Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas dephosphorylation leads to relocalization into the nucleus at the G1/S-boundary (PubMed:10764593).

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 646 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00001856582-375UniProtNucleosome assembly protein 1-like 4
Modified residue5UniProtPhosphoserine
Modified residue (large scale data)5PRIDEPhosphoserine
Modified residue7UniProtPhosphoserine
Modified residue (large scale data)7PRIDEPhosphoserine
Modified residue12UniProtPhosphoserine
Modified residue (large scale data)12PRIDEPhosphoserine
Modified residue (large scale data)14PRIDEPhosphoserine
Modified residue51UniProtPhosphothreonine
Modified residue (large scale data)51PRIDEPhosphothreonine
Modified residue53UniProtPhosphoserine
Modified residue (large scale data)53PRIDEPhosphoserine
Modified residue54UniProtPhosphoserine
Modified residue (large scale data)54PRIDEPhosphoserine
Modified residue (large scale data)55PRIDEPhosphotyrosine
Modified residue58UniProtPhosphothreonine
Modified residue (large scale data)58PRIDEPhosphothreonine
Modified residue (large scale data)85PRIDEPhosphotyrosine
Modified residue105UniProtN6-acetyllysine
Modified residue (large scale data)111PRIDEPhosphothreonine
Modified residue (large scale data)117PRIDEPhosphothreonine
Modified residue (large scale data)121PRIDEPhosphoserine
Modified residue125UniProtPhosphoserine
Modified residue (large scale data)125PRIDEPhosphoserine
Modified residue146UniProtN6-acetyllysine
Modified residue304UniProtPhosphoserine
Modified residue (large scale data)304PRIDEPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine

Post-translational modification

Phosphorylated at the G0/G1 boundary but it is not phosphorylated in S-phase. Phosphorylated protein remains in the cytoplasm in a complex with histones during the G0/G1 transition, whereas dephosphorylation triggers its transport into the nucleus at the G1/S-boundary.
Polyglutamylated by TTLL4, a modification that occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Some residues may also be monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous. Biallelically expressed in fetal and adult tissues. Highest levels in testis.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with core (H2A, CD2APH2B, H3, H4) and linker (H1) histones.
(Microbial infection) Interacts with Chikungunya virus non-structural protein 3 (via C-terminus).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q99733NAP1L1 P552094EBI-2255116, EBI-356392
XENO Q99733tat P046083EBI-2255116, EBI-6164389

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region1-31Disordered
Compositional bias16-31Polar residues
Region116-137Disordered
Motif265-271Nuclear localization signal
Region339-375Disordered
Compositional bias340-368Acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q99733-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    375
  • Mass (Da)
    42,823
  • Last updated
    1997-05-01 v1
  • Checksum
    788E1F9F5BC8FD45
MADHSFSDGVPSDSVEAAKNASNTEKLTDQVMQNPRVLAALQERLDNVPHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESEWHSENEEEEKLAGDMKSKVVVTEKAAATAEEPDPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNSVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFNPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV

Q99733-2

  • Name
    2
  • Synonyms
    NAP1L4b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 14 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A8MXH2A8MXH2_HUMANNAP1L4156
C9J6D1C9J6D1_HUMANNAP1L4178
C9J1B1C9J1B1_HUMANNAP1L4101
C9JZI7C9JZI7_HUMANNAP1L4398
H0YCI4H0YCI4_HUMANNAP1L4204
A0A0J9YXQ2A0A0J9YXQ2_HUMANNAP1L4278
E9PS34E9PS34_HUMANNAP1L4133
E9PNW0E9PNW0_HUMANNAP1L4107
E9PNJ7E9PNJ7_HUMANNAP1L4140
E9PP22E9PP22_HUMANNAP1L4154
E9PKT8E9PKT8_HUMANNAP1L4169
E9PJJ2E9PJJ2_HUMANNAP1L4128
E9PKI2E9PKI2_HUMANNAP1L478
A0A994J3W0A0A994J3W0_HUMANNAP1L4387

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias16-31Polar residues
Sequence conflict107in Ref. 3; BAG35491
Compositional bias340-368Acidic residues
Alternative sequenceVSP_053910375in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U77456
EMBL· GenBank· DDBJ
AAC50870.1
EMBL· GenBank· DDBJ
mRNA
AB500094
EMBL· GenBank· DDBJ
BAH95827.1
EMBL· GenBank· DDBJ
mRNA
AK312599
EMBL· GenBank· DDBJ
BAG35491.1
EMBL· GenBank· DDBJ
mRNA
AC131971
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC022090
EMBL· GenBank· DDBJ
AAH22090.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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