Most amino acid molecules are polar in the sense that they have polar functional groups. Even the "least polar" amino acids like leucine and phenylalanine are likely soluble in water.
However, we also classify amino acids by the polarity of their side chains. When incorporated into proteins, clusters of amino acids with nonpolar side chains can create pockets of hydrophobicity in an otherwise aqueous environment.
Glycine is the only amino acid without a side chain. As such, it is not appropriate to classify its side chain as polar or nonpolar.
Polar acidic side chain: aspartic acid, glutamic acid
Polar basic side chain: arginine, histidine, lysine,
Other polar side chain: asparagine, glutamine, serine, threonine
Nonpolar weakly acidic side chain: cysteine, tyrosine
Other nonpolar side chain: alanine, isoleucine, leucine, methionine,
phenylalanine, proline, tryptophan, valine
No side chain: glycine