Protein record

Hdgfl3

Hepatoma-derived growth factor-related protein 3

Q9JMG7 at UniProt

Mus musculus202 amino acidsannotation supported

1annotated core in Hdgfl3

1PDB entries with observed PWWP1 coordinates

2model records for PWWP1

0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

202 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.

1N27chain A8–90

Mapping and construct evidence

Deposited polymer length: 96 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 58 / 58 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, 91–96.

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

Validated isoform differences · 1 PWWP correspondence record

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
Q9JMG7-2	205	PWWP1	11–68 58 / 58 mapped residues; span may contain gaps	complete

Viewing Hdgfl3 PWWP1

Canonical annotation interval 11–68 · UniProtKB DOMAIN. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance

No alternative annotation record is available in this snapshot.

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

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
1N27	A	58 / 58	APO	SOLUTION NMR	1.32	No 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 / 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

2 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-Q9JMG7-F1:v6 Canonical	GDM	complete	88.5	69.5
AF-Q9JMG7-2-F1:v6	GDM	complete	89.2	70.3

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.