Q4U0Y4 · NPL1A_XENLA

Function

function

Acts as a chaperone for the linker histone to facilitate deposition of histone B4 onto linker DNA (PubMed:14550533, PubMed:15811954, PubMed:15928086, PubMed:16982648).
Required for both remodeling of sperm chromatin into nucleosomes, and linker histone binding to nucleosome core dimers. Plays a role in tissue-specific gene regulation. Required for primitive hemopoiesis, acting upstream of tal1/scl (PubMed:14550533, PubMed:15811954, PubMed:15928086, PubMed:16982648).

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 Functioncyclin binding
Molecular Functionhistone binding
Molecular Functionidentical protein binding
Biological Processnucleosome assembly
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processprimitive hemopoiesis
Biological Processspermatogenesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Nucleosome assembly protein 1-like 1-A
  • Short names
    xNAP1L-A
  • Alternative names
    • Nucleosome assembly protein 1
      (NAP-1
      ; NAP1
      ; xNAP-1
      ; xNAP1
      )

Gene names

    • Name
      nap1l1-a
    • Synonyms
      nap1-a

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q4U0Y4
  • Secondary accessions
    • Q4U0Y3
    • Q6NUD1
    • Q9I8H9

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Cytoplasmic prior to the midblastula transition, becoming predominantly nuclear subsequently.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003456341-392Nucleosome assembly protein 1-like 1-A

Post-translational modification

Phosphorylated by cyclin B-cdc2 kinase complexes.

Keywords

Expression

Tissue specificity

Initially expressed throughout the embryo with expression higher at the animal pole. Becomes localized to presumptive ectoderm by gastrula stages. By stage 18 (neurula), expressed in the neural plate and posterior to the cement gland. In late neurula/early tailbud stages, expressed in the neural crest, neural tube, eyes, tailbud and ventral blood islands. Adult expression is predominantly in ovaries.

Developmental stage

Expressed both maternally and zygotically. Expression levels remain constant during embryonic development, increasing at the swimming tadpole stage.

Gene expression databases

    • 398176Expressed in lung and 19 other cell types or tissues

Interaction

Subunit

Forms homomultimers. Interacts with histone B4. Interacts with the B-type cyclins ccnb1 and ccnb2.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region1-37Disordered
Compositional bias15-29Acidic residues
Motif126-150NAP1L motif
Motif273-279Nuclear localization signal
Compositional bias346-375Acidic residues
Region346-392Disordered

Domain

The NAP1L motif is required for the histone chaperone activity.
The acidic domains are probably involved in the interaction with histones.

Sequence similarities

Belongs to the nucleosome assembly protein (NAP) family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q4U0Y4-1

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.

  • Name
    1
  • Synonyms
    p60A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    392
  • Mass (Da)
    45,187
  • Last updated
    2005-07-19 v1
  • Checksum
    74960F50F2BA0E78
MANIDNKGQTELDQQDMEDVEDVEEEETGEDANSKARQLTAQMMQNPQVLAALQERLDDLVGTPTGYIESLPKVVKRRVNALKNLQVKCAQIEAKFYEEVHELERKYAALYQPLFDKRSDIINATYEPTEEECEWKVEEEDISGDLKEKAKLEEEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMLQEHDEPILKHLKDIKVKFSDAGQPMSFTLEFYFEPNEFFTNEVLTKTYKMRSEPDESDPFSFDGPEIMGCTGCLIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVPNDSFFNFFTPPEVPENGELDDDAEAILTADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADDEEGEEEADEDNDPDYEPKKGQNPAECKQQ

Q4U0Y4-2

  • Name
    2
  • Synonyms
    p56A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAF86278.1 differs from that shown. Reason: Miscellaneous discrepancy C-terminus does not match that of displayed sequence.
The sequence AAH68664.1 differs from that shown. Reason: Frameshift

Features

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

TypeIDPosition(s)Description
Sequence conflict3in Ref. 1
Sequence conflict8in Ref. 1 and 3; AAH68664
Compositional bias15-29Acidic residues
Sequence conflict27-29in Ref. 4; AAF86278
Sequence conflict37in Ref. 3; AAH68664
Sequence conflict182in Ref. 1 and 4; AAF86278
Compositional bias346-375Acidic residues
Sequence conflict357in Ref. 1 and 4; AAF86278
Sequence conflict365-368in Ref. 1 and 4; AAF86278
Alternative sequenceVSP_052856382-392in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ020268
EMBL· GenBank· DDBJ
AAY43229.1
EMBL· GenBank· DDBJ
mRNA
DQ020269
EMBL· GenBank· DDBJ
AAY43230.1
EMBL· GenBank· DDBJ
mRNA
BC068664
EMBL· GenBank· DDBJ
AAH68664.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AF278538
EMBL· GenBank· DDBJ
AAF86278.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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