FHOD1

FH1/FH2 domain-containing protein 1 is a protein that in humans is encoded by the FHOD1 gene.

FHOD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3DAD
Identifiers
Aliases	FHOD1, FHOS, formin homology 2 domain containing 1
External IDs	OMIM: 606881; MGI: 2679008; HomoloGene: 40860; GeneCards: FHOD1; OMA:FHOD1 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16q22.1 Start 67,229,387 bp End 67,247,481 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 D3 Start 106,055,795 bp End 106,074,585 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in spleen gastrocnemius muscle upper lobe of left lung muscle of thigh right lung apex of heart granulocyte right lobe of thyroid gland glutes right adrenal cortex Top expressed in granulocyte inner renal medulla glomerulus left lung lobe muscle of thigh neural layer of retina upper arm knee joint body of femur skeletal muscle tissue More reference expression data BioGPS More reference expression data
Gene ontology Molecular function actin binding protein binding identical protein binding protein domain specific binding protein self-association Cellular component cell projection bleb membrane nucleus cytoskeleton stress fiber cytoplasm cytosol intercalated disc Biological process positive regulation of stress fiber assembly nuclear migration establishment of centrosome localization positive regulation of transcription by RNA polymerase II regulation of stress fiber assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29109 234686 Ensembl ENSG00000135723 ENSMUSG00000014778 UniProt Q9Y613 Q6P9Q4 RefSeq (mRNA) NM_013241 NM_001318202 NM_177699 RefSeq (protein) NP_001305131 NP_037373 NP_808367 Location (UCSC) Chr 16: 67.23 – 67.25 Mb Chr 8: 106.06 – 106.07 Mb PubMed search
Wikidata
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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.

Interactions

FHOD1 has been shown to interact with RAC1.

Further reading

• Westendorf JJ (December 2001). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element". The Journal of Biological Chemistry. 276 (49): 46453–9. doi:10.1074/jbc.M105162200. PMID 11590143.
• Koka S, Neudauer CL, Li X, Lewis RE, McCarthy JB, Westendorf JJ (May 2003). "The formin-homology-domain-containing protein FHOD1 enhances cell migration". Journal of Cell Science. 116 (Pt 9): 1745–55. doi:10.1242/jcs.00386. PMID 12665555.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• Tojo H, Kaieda I, Hattori H, Katayama N, Yoshimura K, Kakimoto S, et al. (July 2003). "The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa". Molecular Endocrinology. 17 (7): 1216–29. doi:10.1210/me.2003-0056. PMID 12677009.
• Takeya R, Sumimoto H (November 2003). "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". Journal of Cell Science. 116 (Pt 22): 4567–75. doi:10.1242/jcs.00769. PMID 14576350. S2CID 25675089.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 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. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Katoh M, Katoh M (April 2004). "Identification and characterization of human FHOD3 gene in silico". International Journal of Molecular Medicine. 13 (4): 615–20. doi:10.3892/ijmm.13.4.615. PMID 15010865.
• Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME (June 2004). "Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells". The Journal of Biological Chemistry. 279 (23): 24420–6. doi:10.1074/jbc.M313823200. PMID 15051728.
• Westendorf JJ, Koka S (May 2004). "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics". Journal of Cellular Biochemistry. 92 (1): 29–41. doi:10.1002/jcb.20031. PMID 15095401. S2CID 40202935.
• Gill MB, Roecklein-Canfield J, Sage DR, Zambela-Soediono M, Longtine N, Uknis M, Fingeroth JD (June 2004). "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21". Journal of Cell Science. 117 (Pt 13): 2709–20. doi:10.1242/jcs.01113. PMID 15138285.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, et al. (June 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Lehner B, Sanderson CM (July 2004). "A protein interaction framework for human mRNA degradation". Genome Research. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Madrid R, Gasteier JE, Bouchet J, Schröder S, Geyer M, Benichou S, Fackler OT (January 2005). "Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities". FEBS Letters. 579 (2): 441–8. doi:10.1016/j.febslet.2004.12.009. PMID 15642356. S2CID 23740212.
• Gasteier JE, Schroeder S, Muranyi W, Madrid R, Benichou S, Fackler OT (May 2005). "FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation". Experimental Cell Research. 306 (1): 192–202. doi:10.1016/j.yexcr.2005.02.006. PMID 15878344.
• Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M (February 2006). "Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1". The Journal of Biological Chemistry. 281 (8): 5084–93. doi:10.1074/jbc.M509226200. PMID 16361249.