Protein record

PWWP3A

PWWP domain-containing DNA repair factor 3A

Q2TAK8 at UniProt

Homo sapiens710 amino acidsannotation supported

1annotated core in PWWP3A

1PDB 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

710 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

0 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.

Deposited construct mapping

1 selected example

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.

3PMIchain A405–538

Mapping and construct evidence

Deposited polymer length: 134 residues. Mapped sequence identity: 100.0%. no sequence difference detected by mapping; not proof of wild type.

PWWP1: 62 / 62 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.

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.

Isoform	Length	PWWP core	Source-mapped positions	Retention / source edits
Q2TAK8-2	642	PWWP1	343–404 62 / 62 mapped residues; span may contain gaps	complete
Q2TAK8-3	731	PWWP1	411–472 62 / 62 mapped residues; span may contain gaps	complete

Viewing PWWP3A PWWP1

Canonical annotation interval 411–472 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance

[
  {
    "end": 488,
    "identifier": "PF20884",
    "integrated_identifier": "IPR035504",
    "model": "PF20884",
    "name": "MUM1-like, PWWP domain",
    "representative": false,
    "score": 4.9e-38,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q2TAK8/?page_size=200",
    "start": 409
  },
  {
    "end": 499,
    "identifier": "IPR035504",
    "integrated_identifier": null,
    "model": null,
    "name": "MUM1-like, PWWP domain",
    "representative": false,
    "score": null,
    "source": "interpro",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q2TAK8/?page_size=200",
    "start": 409
  },
  {
    "end": 499,
    "identifier": "cd06080",
    "integrated_identifier": "IPR035504",
    "model": "cd06080",
    "name": "PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins",
    "representative": false,
    "score": 1.1363e-34,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q2TAK8/?page_size=200",
    "start": 409
  }
]

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.

1 other deposited components in this domain (not pharmacological ligands)

Buffers, ions, cryoprotectants and solvents remain recorded as deposited chemical components.

DI(HYDROXYETHYL)ETHER · Other PDB component · not a studied ligand

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

1 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
3PMI	A	62 / 62	Unclassified_Review	X-RAY DIFFRACTION 2.82 Å	0.484	Required

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

3 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
AF-Q2TAK8-F1:v6 Canonical	GDM	complete	92	63.1
AF-Q2TAK8-2-F1:v6	GDM	complete	92.2	60.5
AF-Q2TAK8-3-F1:v6	GDM	complete	92.6	59.4

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 pair	Aligned Cα	US-align RMSD Å	TM score A / B	View
ARID4A PWWP1 PWWP3A PWWP1	55	2.92	0.438 / 0.596	Aligned core viewer
BRD1 PWWP1 PWWP3A PWWP1	51	2.91	0.464 / 0.592	Aligned core viewer
BRPF1 PWWP1 PWWP3A PWWP1	51	2.29	0.483 / 0.616	Aligned core viewer
BRPF3 PWWP1 PWWP3A PWWP1	51	2.22	0.479 / 0.609	Aligned core viewer
DNMT3A PWWP1 PWWP3A PWWP1	52	2.32	0.691 / 0.664	Aligned core viewer
DNMT3B PWWP1 PWWP3A PWWP1	51	2.0	0.699 / 0.671	Aligned core viewer
HDGF PWWP1 PWWP3A PWWP1	50	2.37	0.607 / 0.579	Aligned core viewer
HDGFL2 PWWP1 PWWP3A PWWP1	51	2.23	0.68 / 0.645	Aligned core viewer
HDGFL3 PWWP1 PWWP3A PWWP1	50	2.18	0.676 / 0.64	Aligned core viewer
MSH6 PWWP1 PWWP3A PWWP1	53	2.33	0.629 / 0.637	Aligned core viewer
NSD2 PWWP1 PWWP3A PWWP1	52	2.08	0.638 / 0.663	Aligned core viewer
NSD3 PWWP1 PWWP3A PWWP1	53	2.17	0.627 / 0.643	Aligned core viewer
NSD3 PWWP2 PWWP3A PWWP1	50	2.42	0.583 / 0.59	Aligned core viewer
PSIP1 PWWP1 PWWP3A PWWP1	50	2.37	0.593 / 0.607	Aligned core viewer
PWWP2B PWWP1 PWWP3A PWWP1	52	1.69	0.712 / 0.702	Aligned core viewer
PWWP3A PWWP1 ZMYND11 PWWP1	51	2.1	0.64 / 0.731	Aligned core viewer
PWWP3A PWWP1 ZMYND8 PWWP1	50	2.19	0.61 / 0.705	Aligned core viewer