STRUCTURAL BIOLOGY & CHEMICAL EVIDENCEDataset v1.2 · Phase 6D · Comparative experimental recognition environments

Protein record

ARID4A

AT-rich interactive domain-containing protein 4A

P29374 at UniProt
Homo sapiens1257 amino acidsannotation supported
1annotated core in ARID4A
3PDB entries with observed PWWP1 coordinates
3model records for PWWP1
0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

1257 residues

PWWP annotation cores, other annotated regions, and deposited construct mappings share the canonical amino acid axis. The original Atlas PWWP intervals retain their source definitions.

PWWP annotation coreOther source annotationPredicted candidate, when present
2 additional source-supported regions · coordinates and evidence

UniProt feature coordinates accepted after exact canonical sequence identity check against the frozen Atlas. Source annotations can be inferred by sequence or curated from experiments; evidence codes remain attached. Other domain types link to their UniProt source because the Atlas records PWWP domains.

Source featureTypeAmino acidsEvidence
ARIDDomain309–401ECO:0000255 PROSITE-ProRule: PRU00355
Tudor-knotDomain576–628ECO:0000255

Deposited construct mapping

3 selected examples

Colored segments map deposited polymer sequences to this canonical protein; dark segments have observed coordinates. Unmapped tags and engineered residues are not assigned canonical positions. These are not certified whole-fold boundaries.

7V8Nchain A169–417
Mapped deposited segment 169–417 Observed canonical residues 169–272Observed canonical residues 303–417
Mapping and construct evidence

Deposited polymer length: 253 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 93 / 93 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–4.

2YRVchain A170–273
Mapped deposited segment 170–273 Observed canonical residues 170–273
Mapping and construct evidence

Deposited polymer length: 117 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 93 / 93 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–7, 112–117.

6L87chain A171–280, 304–414
Mapped deposited segment 171–280Mapped deposited segment 304–414 Observed canonical residues 171–280Observed canonical residues 304–414
Mapping and construct evidence

Deposited polymer length: 229 residues. Mapped sequence identity: 98.64%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 92 / 93 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Source-recorded sequence differences:

[
  {
    "construct": "K",
    "entity_position": 108,
    "reference": "D",
    "uniprot_position": 278
  },
  {
    "construct": "K",
    "entity_position": 110,
    "reference": "E",
    "uniprot_position": 280
  },
  {
    "construct": "K",
    "entity_position": 112,
    "reference": "E",
    "uniprot_position": 305
  }
]

Unmapped construct positions: 222–229.

One mapped example per native domain, preferring frozen experimental representatives; up to four distinct mapped intervals.

Validated isoform differences · 2 PWWP correspondence records

Only source-validated PWWP core correspondences from the frozen v1.2 isoform audit; other-domain architectures are not projected onto isoforms. Coordinates in the isoform column refer to the individual isoform sequence; deleted cores remain absent.

IsoformLengthPWWP coreSource-mapped positionsRetention / source edits
P29374-21203PWWP1170–262
93 / 93 mapped residues; span may contain gaps
complete
P29374-31188PWWP1170–262
93 / 93 mapped residues; span may contain gaps
complete
Viewing ARID4A PWWP1

Canonical annotation interval 170–262 · pfam via InterPro API. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 262,
    "identifier": "IPR012603",
    "integrated_identifier": null,
    "model": null,
    "name": "ARID4A/B, PWWP domain",
    "representative": false,
    "score": null,
    "source": "interpro",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P29374/?page_size=200",
    "start": 170
  },
  {
    "end": 262,
    "identifier": "PF08169",
    "integrated_identifier": "IPR012603",
    "model": "PF08169",
    "name": "RBB1NT (NUC162) domain",
    "representative": false,
    "score": 2.5e-33,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P29374/?page_size=200",
    "start": 170
  }
]

PWWP1 · source-classified Phase 6A evidence

Ligands & Bioactivity

Explore all domain compounds →

0 chemical or preparation profiles · 0 domain-attributed assay / association observations. Counts refer to the curated snapshot.

0 profiles

Deposited research ligands

No records in this category for the selected domain in the curated snapshot.

0 profiles

Studied without research structure

No records in this category for the selected domain in the curated snapshot.

0 profiles

Experiment-specific controls

No records in this category for the selected domain in the curated snapshot.

0 profiles

Ambiguous / indirect evidence

No records in this category for the selected domain in the curated snapshot.

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

3 entry / domain records

One representative chain per PDB entry and native domain. RMSD uses fixed UniProt correspondence and all common Cα atoms; it is reported only for ≥40 atoms and ≥80% core coverage. A value is descriptive, not a prediction benchmark.

PDBChainObserved core CαClassMethod / resolutionAF RMSD ÅReview
2YRVA93 / 93APOSOLUTION NMR1.98No classification flag
7V8NA93 / 93APOX-RAY DIFFRACTION
2.05 Å
1.82No classification flag
6L87A92 / 93APOSOLUTION NMR3.81No classification flag

PWWP1 · Measured preparations

Frozen v1.2 assay records

Explore evidence links

This retained table is the original source projection. The Phase 5 Ligands & Bioactivity section above includes added observations and reviewed target context. Values remain attached to their assay, construct and preparation. A crystal structure does not transfer affinity to another construct or stereoisomer. Assay pages preserve field-level source-verification states where reviewed; unreviewed null fields remain uncurated.

Preparation / identityAssay and resultConstructEvidence and source
No curated assay row for this domain. This does not establish that no literature evidence exists.

Scientific review queue

PWWP1 · Prediction evidence

Predicted models

3 model records

Domain retention uses independently reconstructed UniProt isoform edits. Local pLDDT is not experimental confirmation and does not establish interdomain orientation.

ModelOriginCore retentionCore mean pLDDTFull mean pLDDTCautions
AF-P29374-F1:v6
Canonical
GDMcomplete86.656.3
AF-P29374-2-F1:v6GDMcomplete86.856.7
AF-P29374-3-F1:v6GDMcomplete86.857.2

PWWP1 · Structural correspondence

Human annotation-core comparisons

17 pairs

Structural alignment establishes a residue correspondence for these cropped cores. It does not establish equivalent ligand pockets, function or selectivity.

Domain pairAligned CαUS-align RMSD ÅTM score A / BView
ARID4A PWWP1 BRD1 PWWP1592.160.501 / 0.543Aligned core viewer
ARID4A PWWP1 BRPF1 PWWP1591.940.521 / 0.567Aligned core viewer
ARID4A PWWP1 BRPF3 PWWP1591.830.526 / 0.572Aligned core viewer
ARID4A PWWP1 DNMT3A PWWP1591.840.539 / 0.787Aligned core viewer
ARID4A PWWP1 DNMT3B PWWP1591.720.544 / 0.795Aligned core viewer
ARID4A PWWP1 HDGF PWWP1572.680.469 / 0.67Aligned core viewer
ARID4A PWWP1 HDGFL2 PWWP1581.710.541 / 0.802Aligned core viewer
ARID4A PWWP1 HDGFL3 PWWP1571.970.51 / 0.745Aligned core viewer
ARID4A PWWP1 MSH6 PWWP1572.520.488 / 0.668Aligned core viewer
ARID4A PWWP1 NSD2 PWWP1552.160.493 / 0.664Aligned core viewer
ARID4A PWWP1 NSD3 PWWP1562.170.5 / 0.68Aligned core viewer
ARID4A PWWP1 NSD3 PWWP2591.910.533 / 0.736Aligned core viewer
ARID4A PWWP1 PSIP1 PWWP1602.420.504 / 0.67Aligned core viewer
ARID4A PWWP1 PWWP2B PWWP1522.340.459 / 0.653Aligned core viewer
ARID4A PWWP1 PWWP3A PWWP1552.920.438 / 0.596Aligned core viewer
ARID4A PWWP1 ZMYND11 PWWP1512.390.444 / 0.705Aligned core viewer
ARID4A PWWP1 ZMYND8 PWWP1512.220.447 / 0.72Aligned core viewer