O43426: Synaptojanin-1 (SYNJ1)

Synaptojanin-1 (SYNJ1) is a 1573-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43426.

Gene
SYNJ1
Organism
Homo sapiens
Length
1573 residues
Mean pLDDT
67.1
Model
AF-O43426-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.1 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate33%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions36%

What pLDDT means and how to read it

Function

Phosphatase that hydrolyzes phosphate groups from the inositol ring of phosphoinositides and inositol phosphates, in a domain-specific manner (PubMed:10224048, PubMed:18093523, PubMed:23804563, PubMed:27435091, PubMed:33349335, PubMed:40969890). The 5-PPase domain catalyzes removal of the 5-phosphate from substrates such as phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol-1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) (PubMed:18093523, PubMed:23804563, PubMed:27435091, PubMed:33349335, PubMed:40969890). The SAC domain hydrolyzes phosphates at the 3- and 4-positions of the…

Subunit structure

Interacts with ASH/GRB2. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with AMPH, SH3GL1, SH3GL2 and SH3GL3 (PubMed:10542231, PubMed:18093523). Interacts with MYO1E (via SH3 domain) (PubMed:17257598). Interacts with BIN1 and DNM1 (By similarity). Interacts with EPS15 (By similarity)

Subcellular location

Cytoplasm, perinuclear region, Presynapse, Membrane

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
2VJ0X-ray1.6 ÅP=1477-1488
1W80X-ray1.9 ÅP=1477-1488, Q=1458-1469
7A0VX-ray2.3 ÅA/C/E=528-873
7A17X-ray2.73 ÅA=528-873, C/E=529-873
2DNRNMRA=894-971

More AlphaFold highlights

About this viewer

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