Osteoclast Stimulating Factor 1 (OSF)

OSTF1; OSF; SH3P2

SPN	V356
HGNC	8510
MGI	700012
PubMed	15054860
RGD	628849
UniProt	Q92882
Wiki	OSTF1

Reddy et al. (1998) cloned human OSTF1, which they designated OSF, from an osteoclast-like multinucleated cell (OST-like MNC) expression library. The deduced 214-amino acid OSTF1 protein has a predicted molecular mass of 28 kD and shares 95% sequence identity with the mouse homolog. It contains an N-terminal proline-rich region and a potential N-glycosylation site, but lacks a signal sequence. OSTF1 has ankyrin repeats and an Src homology-3 (SH3) domain that is homologous to the SH3 domain of GRB2 and FYN. Northern blot analysis detected ubiquitous expression of a 1.3-kb transcript in multiple human tissues. In situ hybridization demonstrated OSTF1 expression in giant cells isolated from osteosarcoma and in osteoclast-like cells in long-term bone marrow cultures.

Reference

"Isolation and characterization of a cDNA clone encoding a novel peptide (OSF) that enhances osteoclast formation and bone resorption."
J. Cell. Physiol. 177:636-645(1998) [PubMed] [Europe PMC] [Abstract]

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"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

Unpublished observations (NOV-2000)

"Osteoclast-stimulating factor interacts with the spinal muscular atrophy gene product to stimulate osteoclast formation."
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"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
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"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
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"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
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J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Solution structure of the SH3 domain of human osteoclast-stimulating factor 1 (OSTF1)."
Submitted (APR-2005) to the PDB data bank