Also known as Nucleoplasmin, IPR004301
thumb|Fig 2. Cartoon image of nucleoplasmin core thumb|Fig 3. Comparison of NPM family domains in humans and Xenopus (original diagram in Spanish). Nucleoplasmin (NPM2), the first identified molecular chaperone, is a thermostable acidic protein with a pentameric structure. The protein was first isolated from Xenopus species, and is now recognized as a highly conserved histone chaperone found across animals and other eukaryotes.
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thumb|Fig 2. Cartoon image of nucleoplasmin core thumb|Fig 3. Comparison of NPM family domains in humans and Xenopus (original diagram in Spanish). Nucleoplasmin (NPM2), the first identified molecular chaperone, is a thermostable acidic protein with a pentameric structure. The protein was first isolated from Xenopus species, and is now recognized as a highly conserved histone chaperone found across animals and other eukaryotes.
== Family == The nucleoplasmin/nucleophosmin (NPM) protein family comprises Nucleophosmin (NPM1), Nucleoplasmin 2 (NPM2), Nucleoplasmin 3 (NPM3), and nucleoplasmin-like proteins (NLP). These proteins typically share a pentameric N-terminal β-sandwich core. While NPM1 functions broadly in nuclear organization and cellular homeostasis, NPM2 is primarily associated with histone chaperoning during early development and is most frequently described as the canonical nucleoplasmin. The human NPM1 gene is also of clinical interest, as mutations in it are linked to acute myeloid leukemia (AML).
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).