Q91ZM2: SH2B adapter protein 1 (Sh2b1)

SH2B adapter protein 1 (Sh2b1) is a 756-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q91ZM2.

Gene
Sh2b1
Organism
Mus musculus
Length
756 residues
Mean pLDDT
56.8
Model
AF-Q91ZM2-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.8 (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 accurate20%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions60%

What pLDDT means and how to read it

Function

Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases, including the receptors of insulin (INS), insulin-like growth factor 1 (IGF1), nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial cell line-derived neurotrophic factor (GDNF), platelet-derived growth factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1, which in turn is phosphorylated by JAK2 on tyrosine residues. These phosphotyrosines form potential binding sites for other signaling proteins. GH also…

Subunit structure

Self-associates. Homopentamer (By similarity). Forms a heteromultimeric complex with SH2B2 (By similarity). Interacts with SH2B2. Isoform 1 interacts via its SH2 domain with JAK2. Isoform 2 interacts via its SH2 domain and its N-terminus with JAK2; the SH2 domain is required for the major interaction with JAK2 phosphorylated on tyrosine residues; the N-terminus provides a low-affinity binding to…

Subcellular location

Cytoplasm, Membrane, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2HDVX-ray2.0 ÅA/B=519-627
2HDXX-ray2.35 ÅA/B/C/D/E/F=519-627
8ATKNMRA=519-628

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