Q99733 · NP1L4_HUMAN
- ProteinNucleosome assembly protein 1-like 4
- GeneNAP1L4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a histone chaperone in nucleosome assembly.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | histone binding | |
Molecular Function | nucleosome binding | |
Molecular Function | RNA binding | |
Molecular Function | unfolded protein binding | |
Biological Process | nucleosome assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNucleosome assembly protein 1-like 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99733
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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).
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
- Cellular component
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000185658 | 2-375 | UniProt | Nucleosome assembly protein 1-like 4 | |||
Sequence: ADHSFSDGVPSDSVEAAKNASNTEKLTDQVMQNPRVLAALQERLDNVPHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESEWHSENEEEEKLAGDMKSKVVVTEKAAATAEEPDPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNSVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFNPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 7 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 12 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 53 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 58 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 105 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 111 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 125 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 146 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 304 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S |
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
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99733 | NAP1L1 P55209 | 4 | EBI-2255116, EBI-356392 | |
XENO | Q99733 | tat P04608 | 3 | EBI-2255116, EBI-6164389 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MADHSFSDGVPSDSVEAAKNASNTEKLTDQV | ||||||
Compositional bias | 16-31 | Polar residues | ||||
Sequence: EAAKNASNTEKLTDQV | ||||||
Region | 116-137 | Disordered | ||||
Sequence: PTDAESEWHSENEEEEKLAGDM | ||||||
Motif | 265-271 | Nuclear localization signal | ||||
Sequence: IKKKQKH | ||||||
Region | 339-375 | Disordered | ||||
Sequence: AIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV | ||||||
Compositional bias | 340-368 | Acidic residues | ||||
Sequence: IEDDDNFEEGEEGEEEELEGDEEGEDEDD |
Sequence similarities
Belongs to the nucleosome assembly protein (NAP) family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length375
- Mass (Da)42,823
- Last updated1997-05-01 v1
- Checksum788E1F9F5BC8FD45
Q99733-2
- Name2
- SynonymsNAP1L4b
- Differences from canonical
- 375-375: V → KEPSQPAECKQQ
Computationally mapped potential isoform sequences
There are 14 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A8MXH2 | A8MXH2_HUMAN | NAP1L4 | 156 | ||
C9J6D1 | C9J6D1_HUMAN | NAP1L4 | 178 | ||
C9J1B1 | C9J1B1_HUMAN | NAP1L4 | 101 | ||
C9JZI7 | C9JZI7_HUMAN | NAP1L4 | 398 | ||
H0YCI4 | H0YCI4_HUMAN | NAP1L4 | 204 | ||
A0A0J9YXQ2 | A0A0J9YXQ2_HUMAN | NAP1L4 | 278 | ||
E9PS34 | E9PS34_HUMAN | NAP1L4 | 133 | ||
E9PNW0 | E9PNW0_HUMAN | NAP1L4 | 107 | ||
E9PNJ7 | E9PNJ7_HUMAN | NAP1L4 | 140 | ||
E9PP22 | E9PP22_HUMAN | NAP1L4 | 154 | ||
E9PKT8 | E9PKT8_HUMAN | NAP1L4 | 169 | ||
E9PJJ2 | E9PJJ2_HUMAN | NAP1L4 | 128 | ||
E9PKI2 | E9PKI2_HUMAN | NAP1L4 | 78 | ||
A0A994J3W0 | A0A994J3W0_HUMAN | NAP1L4 | 387 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-31 | Polar residues | ||||
Sequence: EAAKNASNTEKLTDQV | ||||||
Sequence conflict | 107 | in Ref. 3; BAG35491 | ||||
Sequence: R → K | ||||||
Compositional bias | 340-368 | Acidic residues | ||||
Sequence: IEDDDNFEEGEEGEEEELEGDEEGEDEDD | ||||||
Alternative sequence | VSP_053910 | 375 | in isoform 2 | |||
Sequence: V → KEPSQPAECKQQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |