Native domain record

ARID4B PWWP1

AT-rich interactive domain-containing protein 4B

Q4LE39 at UniProt

Homo sapiens1312 amino acidsannotation supportedUP:Q4LE39:PWWP1

1annotated core in ARID4B

0PDB entries with observed PWWP1 coordinates

4model records for PWWP1

0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

1312 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 feature	Type	Amino acids	Evidence
ARID	Domain	306–398	ECO:0000255 PROSITE-ProRule: PRU00355
Tudor-knot	Domain	572–624	ECO:0000255

Deposited construct mapping

0 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.

No selected deposited construct with observed PWWP core coordinates is mapped in this snapshot.

Validated isoform differences · 3 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.

Isoform	Length	PWWP core	Source-mapped positions	Retention / source edits
Q4LE39-2	1226	PWWP1	170–262 93 / 93 mapped residues; span may contain gaps	complete
Q4LE39-3	1153	PWWP1	170–262 93 / 93 mapped residues; span may contain gaps	complete
Q4LE39-4	803	PWWP1	None	absent

Viewing ARID4B 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/Q4LE39/?page_size=200",
    "start": 170
  },
  {
    "end": 262,
    "identifier": "PF08169",
    "integrated_identifier": "IPR012603",
    "model": "PF08169",
    "name": "RBB1NT (NUC162) domain",
    "representative": false,
    "score": 3.1e-33,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q4LE39/?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

0 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.

PDB	Chain	Observed core Cα	Class	Method / resolution	AF RMSD Å	Review
No experimental entry is mapped to this domain in the frozen snapshot.

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 / identity	Assay and result	Construct	Evidence 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

4 model records

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

Model	Origin	Core retention	Core mean pLDDT	Full mean pLDDT	Cautions
AF-Q4LE39-F1:v6 Canonical	GDM	complete	85.9	55.7
AF-Q4LE39-2-F1:v6	GDM	complete	86.4	55.2
AF-Q4LE39-3-F1:v6	GDM	complete	85.8	56
AF-Q4LE39-4-F1:v6	GDM	absent	—	54.7	partial_or_absent_mapped_core

PWWP1 · Structural correspondence

Human annotation-core comparisons

0 pairs

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

Domain pair	Aligned Cα	US-align RMSD Å	TM score A / B	View
No eligible experimental representative for a cross-domain comparison.