FHOD1

From Wikipedia, the free encyclopedia

Formin homology 2 domain containing 1

Identifiers

External IDs

OMIM: 606881 MGI: 2679008 HomoloGene: 40860

Gene ontology
Molecular Function:	• actin binding • protein binding
Cellular Component:	• nucleus • cytoplasm • cytoskeleton
Biological Process:	• cellular component organization and biogenesis • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_013241 (mRNA)
NP_037373 (protein)

NM_177699 (mRNA)
NP_808367 (protein)

Location

Chr 16: 65.82 - 65.84 Mb

Chr 8: 108.22 - 108.24 Mb

Pubmed search

[1]

[2]

Formin homology 2 domain containing 1, also known as FHOD1, is a human gene.^[1]

This gene encodes a protein which is a member of the formin/diaphanous family of proteins. The gene is ubiquitously expressed but is found in abundance in the spleen. The encoded protein has sequence homology to diaphanous and formin proteins within the Formin Homology (FH)1 and FH2 domains. It also contains a coiled-coil domain, a collagen-like domain, two nuclear localization signals, and several potential PKC and PKA phosphorylation sites. It is a predominantly cytoplasmic protein and is expressed in a variety of human cell lines.^[1]

[edit] References

^ ^a ^b Entrez Gene: FHOD1 formin homology 2 domain containing 1.

[edit] Further reading

Westendorf JJ, Mernaugh R, Hiebert SW (1999). "Identification and characterization of a protein containing formin homology (FH1/FH2) domains.". Gene 232 (2): 173-82. PMID 10352228.
Westendorf JJ (2002). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element.". J. Biol. Chem. 276 (49): 46453-9. doi:10.1074/jbc.M105162200. PMID 11590143.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Koka S, Neudauer CL, Li X, et al. (2004). "The formin-homology-domain-containing protein FHOD1 enhances cell migration.". J. Cell. Sci. 116 (Pt 9): 1745-55. PMID 12665555.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566-9. doi:10.1038/nbt810. PMID 12665801.
Tojo H, Kaieda I, Hattori H, et al. (2004). "The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa.". Mol. Endocrinol. 17 (7): 1216-29. doi:10.1210/me.2003-0056. PMID 12677009.
Takeya R, Sumimoto H (2004). "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation.". J. Cell. Sci. 116 (Pt 22): 4567-75. doi:10.1242/jcs.00769. PMID 14576350.
Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.". Genomics 83 (1): 153-67. PMID 14667819.
Katoh M, Katoh M (2004). "Identification and characterization of human FHOD3 gene in silico.". Int. J. Mol. Med. 13 (4): 615-20. PMID 15010865.
Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME (2004). "Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells.". J. Biol. Chem. 279 (23): 24420-6. doi:10.1074/jbc.M313823200. PMID 15051728.
Westendorf JJ, Koka S (2004). "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics.". J. Cell. Biochem. 92 (1): 29-41. doi:10.1002/jcb.20031. PMID 15095401.
Gill MB, Roecklein-Canfield J, Sage DR, et al. (2005). "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21.". J. Cell. Sci. 117 (Pt 13): 2709-20. doi:10.1242/jcs.01113. PMID 15138285.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707-16. doi:10.1038/nbt971. PMID 15146197.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315-23. doi:10.1101/gr.2122004. PMID 15231747.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. doi:10.1073/pnas.0404720101. PMID 15302935.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Madrid R, Gasteier JE, Bouchet J, et al. (2005). "Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities.". FEBS Lett. 579 (2): 441-8. doi:10.1016/j.febslet.2004.12.009. PMID 15642356.
Gasteier JE, Schroeder S, Muranyi W, et al. (2005). "FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation.". Exp. Cell Res. 306 (1): 192-202. doi:10.1016/j.yexcr.2005.02.006. PMID 15878344.
Boehm MB, Milius TJ, Zhou Y, et al. (2005). "The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway.". Biochem. Biophys. Res. Commun. 335 (4): 1090-4. doi:10.1016/j.bbrc.2005.07.191. PMID 16112087.
Schönichen A, Alexander M, Gasteier JE, et al. (2006). "Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1.". J. Biol. Chem. 281 (8): 5084-93. doi:10.1074/jbc.M509226200. PMID 16361249.