Q96EP5 · DAZP1_HUMAN
- ProteinDAZ-associated protein 1
- GeneDAZAP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids407 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
RNA-binding protein, which may be required during spermatogenesis.
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 | cytosol | |
Cellular Component | male germ cell nucleus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | poly(G) binding | |
Molecular Function | poly(U) RNA binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA stem-loop binding | |
Biological Process | cell differentiation | |
Biological Process | fibroblast proliferation | |
Biological Process | maternal placenta development | |
Biological Process | positive regulation of mRNA splicing, via spliceosome | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDAZ-associated protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96EP5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly cytoplasmic (By similarity).
Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm (By similarity).
Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035480 | 381 | in a breast cancer sample; somatic mutation | |||
Sequence: S → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 331 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000081565 | 1-407 | UniProt | DAZ-associated protein 1 | |||
Sequence: MNNSGADEIGKLFVGGLDWSTTQETLRSYFSQYGEVVDCVIMKDKTTNQSRGFGFVKFKDPNCVGTVLASRPHTLDGRNIDPKPCTPRGMQPERTRPKEGWQKGPRSDNSKSNKIFVGGIPHNCGETELREYFKKFGVVTEVVMIYDAEKQRPRGFGFITFEDEQSVDQAVNMHFHDIMGKKVEVKRAEPRDSKSQAPGQPGASQWGSRVVPNAANGWAGQPPPTWQQGYGPQGMWVPAGQAIGGYGPPPAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQGYGAPPQFSFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPDMSKPPTAQPDFPYGQYAGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 150 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 253 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Acetylation at Lys-150 is predominantly observed in the nuclear fraction, and may regulate nucleocytoplasmic transport.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Mainly expressed in testis. Expressed to a lower level in thymus. Weakly or not expressed in heart, liver, brain, placenta, lung, skeletal muscle, kidney and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with DAZ and DAZL.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96EP5 | DAZ1 Q9NQZ3 | 3 | EBI-2133162, EBI-997955 | |
BINARY | Q96EP5 | SNRPA P09012 | 3 | EBI-2133162, EBI-607085 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-97 | RRM 1 | ||||
Sequence: GKLFVGGLDWSTTQETLRSYFSQYGEVVDCVIMKDKTTNQSRGFGFVKFKDPNCVGTVLASRPHTLDGRNIDPKPCTPRGMQPERTRP | ||||||
Region | 74-117 | Disordered | ||||
Sequence: TLDGRNIDPKPCTPRGMQPERTRPKEGWQKGPRSDNSKSNKIFV | ||||||
Domain | 113-190 | RRM 2 | ||||
Sequence: NKIFVGGIPHNCGETELREYFKKFGVVTEVVMIYDAEKQRPRGFGFITFEDEQSVDQAVNMHFHDIMGKKVEVKRAEP | ||||||
Region | 185-407 | Disordered | ||||
Sequence: VKRAEPRDSKSQAPGQPGASQWGSRVVPNAANGWAGQPPPTWQQGYGPQGMWVPAGQAIGGYGPPPAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQGYGAPPQFSFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPDMSKPPTAQPDFPYGQYAGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR | ||||||
Compositional bias | 197-211 | Polar residues | ||||
Sequence: APGQPGASQWGSRVV | ||||||
Compositional bias | 250-283 | Pro residues | ||||
Sequence: PAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQG | ||||||
Compositional bias | 291-333 | Pro residues | ||||
Sequence: SFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPD | ||||||
Compositional bias | 360-375 | Polar residues | ||||
Sequence: GQGFSDPSQQPPSYGG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q96EP5-1
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
- Length407
- Mass (Da)43,383
- Last updated2001-12-01 v1
- ChecksumCFEB42903F4D5AFB
Q96EP5-2
- Name2
- Differences from canonical
- 350-407: AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR → GLGSYSPAPPGCGPHFVYSLMVRLSSDVA
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 109 | in Ref. 1; AAF78364 | ||||
Sequence: N → Y | ||||||
Compositional bias | 197-211 | Polar residues | ||||
Sequence: APGQPGASQWGSRVV | ||||||
Compositional bias | 250-283 | Pro residues | ||||
Sequence: PAGRGAPPPPPPFTSYIVSTPPGGFPPPQGFPQG | ||||||
Compositional bias | 291-333 | Pro residues | ||||
Sequence: SFGYGPPPPPPDQFAPPGVPPPPATPGAAPLAFPPPPSQAAPD | ||||||
Alternative sequence | VSP_009441 | 350-407 | in isoform 2 | |||
Sequence: AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQGFHPYRR → GLGSYSPAPPGCGPHFVYSLMVRLSSDVA | ||||||
Compositional bias | 360-375 | Polar residues | ||||
Sequence: GQGFSDPSQQPPSYGG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF181719 EMBL· GenBank· DDBJ | AAF78364.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012062 EMBL· GenBank· DDBJ | AAH12062.1 EMBL· GenBank· DDBJ | mRNA | ||
AK056850 EMBL· GenBank· DDBJ | BAB71295.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |