FHOD1: Difference between revisions

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{{Infobox_gene}}
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'''FH1/FH2 domain-containing protein 1''' is a [[protein]] that in humans is encoded by the ''FHOD1'' [[gene]].<ref name="pmid10352228">{{cite journal |vauthors=Westendorf JJ, Mernaugh R, Hiebert SW | title = Identification and characterization of a protein containing formin homology (FH1/FH2) domains | journal = Gene | volume = 232 | issue = 2 | pages = 173–82 |date=Jul 1999 | pmid = 10352228 | pmc =  | doi =10.1016/S0378-1119(99)00127-4 }}</ref><ref name="pmid16112087">{{cite journal |vauthors=Boehm MB, Milius TJ, Zhou Y, Westendorf JJ, Koka S | title = The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway | journal = Biochem Biophys Res Commun | volume = 335 | issue = 4 | pages = 1090–4 |date=Aug 2005 | pmid = 16112087 | pmc =  | doi = 10.1016/j.bbrc.2005.07.191 }}</ref><ref name="entrez"/>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Formin homology 2 domain containing 1
| HGNCid = 17905
| Symbol = FHOD1
| AltSymbols =; FHOS
| OMIM = 606881
| ECnumber =
| Homologene = 40860
| MGIid = 2679008
  | GeneAtlas_image1 = PBB_GE_FHOD1_218530_at_tn.png
  | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0016043 |text = cellular component organization and biogenesis}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 29109
    | Hs_Ensembl = ENSG00000135723
    | Hs_RefseqProtein = NP_037373
    | Hs_RefseqmRNA = NM_013241
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 65820800
    | Hs_GenLoc_end = 65838896
    | Hs_Uniprot = Q9Y613
    | Mm_EntrezGene = 234686
    | Mm_Ensembl = ENSMUSG00000014778
    | Mm_RefseqmRNA = NM_177699
    | Mm_RefseqProtein = NP_808367
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 108218293
    | Mm_GenLoc_end = 108237082
    | Mm_Uniprot = Q6P9Q4
  }}
}}
'''Formin homology 2 domain containing 1''', also known as '''FHOD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FHOD1 formin homology 2 domain containing 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29109| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: FHOD1 formin homology 2 domain containing 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29109| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: FHOD1 formin homology 2 domain containing 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29109| accessdate = }}</ref>
}}
}}
==Interactions==
FHOD1 has been shown to [[Protein-protein interaction|interact]] with [[RAC1]].<ref name=pmid11590143>{{cite journal |last=Westendorf |first=J J |date=Dec 2001 |title=The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element |journal=J. Biol. Chem. |volume=276 |issue=49 |pages=46453–9 |publisher= |location = United States| issn = 0021-9258| pmid = 11590143 |doi = 10.1074/jbc.M105162200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Westendorf JJ, Mernaugh R, Hiebert SW |title=Identification and characterization of a protein containing formin homology (FH1/FH2) domains. |journal=Gene |volume=232 |issue= 2 |pages= 173-82 |year= 1999 |pmid= 10352228 |doi= }}
*{{cite journal  | author=Westendorf JJ |title=The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 46453–9 |year= 2002 |pmid= 11590143 |doi= 10.1074/jbc.M105162200 }}
*{{cite journal  | author=Westendorf JJ |title=The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 46453-9 |year= 2002 |pmid= 11590143 |doi= 10.1074/jbc.M105162200 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Koka S, Neudauer CL, Li X |title=The formin-homology-domain-containing protein FHOD1 enhances cell migration |journal=J. Cell Sci. |volume=116 |issue= Pt 9 |pages= 1745–55 |year= 2004 |pmid= 12665555 |doi=10.1242/jcs.00386  |display-authors=etal}}
*{{cite journal  | author=Koka S, Neudauer CL, Li X, ''et al.'' |title=The formin-homology-domain-containing protein FHOD1 enhances cell migration. |journal=J. Cell. Sci. |volume=116 |issue= Pt 9 |pages= 1745-55 |year= 2004 |pmid= 12665555 |doi= }}
*{{cite journal  |vauthors=Gevaert K, Goethals M, Martens L |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 |display-authors=etal}}
*{{cite journal  | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  |vauthors=Tojo H, Kaieda I, Hattori H |title=The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa |journal=Mol. Endocrinol. |volume=17 |issue= 7 |pages= 1216–29 |year= 2004 |pmid= 12677009 |doi= 10.1210/me.2003-0056 |display-authors=etal}}
*{{cite journal  | author=Tojo H, Kaieda I, Hattori H, ''et al.'' |title=The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa. |journal=Mol. Endocrinol. |volume=17 |issue= 7 |pages= 1216-29 |year= 2004 |pmid= 12677009 |doi= 10.1210/me.2003-0056 }}
*{{cite journal  |vauthors=Takeya R, Sumimoto H |title=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=J. Cell Sci. |volume=116 |issue= Pt 22 |pages= 4567–75 |year= 2004 |pmid= 14576350 |doi= 10.1242/jcs.00769 }}
*{{cite journal  | author=Takeya R, Sumimoto H |title=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=J. Cell. Sci. |volume=116 |issue= Pt 22 |pages= 4567-75 |year= 2004 |pmid= 14576350 |doi= 10.1242/jcs.00769 }}
*{{cite journal  |vauthors=Lehner B, Semple JI, Brown SE |title=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 |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0  |display-authors=etal}}
*{{cite journal  | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=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. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi=  }}
*{{cite journal  |vauthors=Katoh M, Katoh M |title=Identification and characterization of human FHOD3 gene in silico |journal=Int. J. Mol. Med. |volume=13 |issue= 4 |pages= 615–20 |year= 2004 |pmid= 15010865 |doi=  10.3892/ijmm.13.4.615}}
*{{cite journal  | author=Katoh M, Katoh M |title=Identification and characterization of human FHOD3 gene in silico. |journal=Int. J. Mol. Med. |volume=13 |issue= 4 |pages= 615-20 |year= 2004 |pmid= 15010865 |doi= }}
*{{cite journal  |vauthors=Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME |title=Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells |journal=J. Biol. Chem. |volume=279 |issue= 23 |pages= 24420–6 |year= 2004 |pmid= 15051728 |doi= 10.1074/jbc.M313823200 }}
*{{cite journal  | author=Wang Y, El-Zaru MR, Surks HK, Mendelsohn ME |title=Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=279 |issue= 23 |pages= 24420-6 |year= 2004 |pmid= 15051728 |doi= 10.1074/jbc.M313823200 }}
*{{cite journal  |vauthors=Westendorf JJ, Koka S |title=Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics |journal=J. Cell. Biochem. |volume=92 |issue= 1 |pages= 29–41 |year= 2004 |pmid= 15095401 |doi= 10.1002/jcb.20031 }}
*{{cite journal  | author=Westendorf JJ, Koka S |title=Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics. |journal=J. Cell. Biochem. |volume=92 |issue= 1 |pages= 29-41 |year= 2004 |pmid= 15095401 |doi= 10.1002/jcb.20031 }}
*{{cite journal  |vauthors=Gill MB, Roecklein-Canfield J, Sage DR |title=EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21 |journal=J. Cell Sci. |volume=117 |issue= Pt 13 |pages= 2709–20 |year= 2005 |pmid= 15138285 |doi= 10.1242/jcs.01113 |display-authors=etal}}
*{{cite journal  | author=Gill MB, Roecklein-Canfield J, Sage DR, ''et al.'' |title=EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21. |journal=J. Cell. Sci. |volume=117 |issue= Pt 13 |pages= 2709-20 |year= 2005 |pmid= 15138285 |doi= 10.1242/jcs.01113 }}
*{{cite journal  |vauthors=Brandenberger R, Wei H, Zhang S |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |display-authors=etal}}
*{{cite journal  | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{cite journal  |vauthors=Lehner B, Sanderson CM |title=A Protein Interaction Framework for Human mRNA Degradation |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004  | pmc=442147 }}
*{{cite journal  | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
*{{cite journal  |vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101  | pmc=514446 |display-authors=etal}}
*{{cite journal  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Madrid R, Gasteier JE, Bouchet J |title=Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities |journal=FEBS Lett. |volume=579 |issue= 2 |pages= 441–8 |year= 2005 |pmid= 15642356 |doi= 10.1016/j.febslet.2004.12.009 |display-authors=etal}}
*{{cite journal  | author=Madrid R, Gasteier JE, Bouchet J, ''et al.'' |title=Oligomerization of the diaphanous-related formin FHOD1 requires a coiled-coil motif critical for its cytoskeletal and transcriptional activities. |journal=FEBS Lett. |volume=579 |issue= 2 |pages= 441-8 |year= 2005 |pmid= 15642356 |doi= 10.1016/j.febslet.2004.12.009 }}
*{{cite journal  |vauthors=Gasteier JE, Schroeder S, Muranyi W |title=FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation |journal=Exp. Cell Res. |volume=306 |issue= 1 |pages= 192–202 |year= 2005 |pmid= 15878344 |doi= 10.1016/j.yexcr.2005.02.006 |display-authors=etal}}
*{{cite journal  | author=Gasteier JE, Schroeder S, Muranyi W, ''et al.'' |title=FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation. |journal=Exp. Cell Res. |volume=306 |issue= 1 |pages= 192-202 |year= 2005 |pmid= 15878344 |doi= 10.1016/j.yexcr.2005.02.006 }}
*{{cite journal  |vauthors=Schönichen A, Alexander M, Gasteier JE |title=Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1 |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 5084–93 |year= 2006 |pmid= 16361249 |doi= 10.1074/jbc.M509226200 |display-authors=etal}}
*{{cite journal  | author=Boehm MB, Milius TJ, Zhou Y, ''et al.'' |title=The mammalian formin FHOD1 interacts with the ERK MAP kinase pathway. |journal=Biochem. Biophys. Res. Commun. |volume=335 |issue= 4 |pages= 1090-4 |year= 2005 |pmid= 16112087 |doi= 10.1016/j.bbrc.2005.07.191 }}
*{{cite journal  | author=Schönichen A, Alexander M, Gasteier JE, ''et al.'' |title=Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 5084-93 |year= 2006 |pmid= 16361249 |doi= 10.1074/jbc.M509226200 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 19:55, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
View/Edit Human

FH1/FH2 domain-containing protein 1 is a protein that in humans is encoded by the FHOD1 gene.[1][2][3]

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.[3]

Interactions

FHOD1 has been shown to interact with RAC1.[4]

References

  1. ↑ Westendorf JJ, Mernaugh R, Hiebert SW (Jul 1999). "Identification and characterization of a protein containing formin homology (FH1/FH2) domains". Gene. 232 (2): 173–82. doi:10.1016/S0378-1119(99)00127-4. PMID 10352228.
  2. ↑ Boehm MB, Milius TJ, Zhou Y, Westendorf JJ, Koka S (Aug 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.
  3. ↑ 3.0 3.1 "Entrez Gene: FHOD1 formin homology 2 domain containing 1".
  4. ↑ Westendorf, J J (Dec 2001). "The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element". J. Biol. Chem. United States. 276 (49): 46453–9. doi:10.1074/jbc.M105162200. ISSN 0021-9258. PMID 11590143.

Further reading



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