Full text data of FHOD1
FHOD1
(FHOS, FHOS1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1; FHOS; Formin homology 2 domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1; FHOS; Formin homology 2 domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y613
ID FHOD1_HUMAN Reviewed; 1164 AA.
AC Q9Y613; Q59F76; Q6Y1F2; Q76MS8; Q8N521;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=FH1/FH2 domain-containing protein 1;
DE AltName: Full=Formin homolog overexpressed in spleen 1;
DE Short=FHOS;
DE AltName: Full=Formin homology 2 domain-containing protein 1;
GN Name=FHOD1; Synonyms=FHOS, FHOS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10352228; DOI=10.1016/S0378-1119(99)00127-4;
RA Westendorf J.J., Mernaugh R., Hiebert S.W.;
RT "Identification and characterization of a protein containing formin
RT homology (FH1/FH2) domains.";
RL Gene 232:173-182(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=14576350; DOI=10.1242/jcs.00769;
RA Takeya R., Sumimoto H.;
RT "Fhos, a mammalian formin, directly binds to F-actin via a region N-
RT terminal to the FH1 domain and forms a homotypic complex via the FH2
RT domain to promote actin fiber formation.";
RL J. Cell Sci. 116:4567-4575(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=15138285; DOI=10.1242/jcs.01113;
RA Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M.,
RA Longtine N., Uknis M., Fingeroth J.D.;
RT "EBV attachment stimulates FHOS/FHOD1 redistribution and co-
RT aggregation with CD21: formin interactions with the cytoplasmic domain
RT of human CD21.";
RL J. Cell Sci. 117:2709-2720(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AUTOINHIBITION, AND SUBCELLULAR LOCATION.
RX PubMed=15878344; DOI=10.1016/j.yexcr.2005.02.006;
RA Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S.,
RA Fackler O.T.;
RT "FHOD1 coordinates actin filament and microtubule alignment to mediate
RT cell elongation.";
RL Exp. Cell Res. 306:192-202(2005).
RN [8]
RP DOMAIN DAD, AND AUTOINHIBITION.
RX PubMed=16361249; DOI=10.1074/jbc.M509226200;
RA Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T.,
RA Geyer M.;
RT "Biochemical characterization of the diaphanous autoregulatory
RT interaction in the formin homology protein FHOD1.";
RL J. Biol. Chem. 281:5084-5093(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, AND
RP PHOSPHORYLATION.
RX PubMed=18694941; DOI=10.1074/jbc.M801800200;
RA Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J.,
RA Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R.,
RA Benichou S., Fackler O.T.;
RT "The diaphanous-related formin FHOD1 associates with ROCK1 and
RT promotes Src-dependent plasma membrane blebbing.";
RL J. Biol. Chem. 283:27891-27903(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498
RP AND SER-523, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523
RP AND SER-573, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC stress fibers. Depends on the Rho-ROCK cascade for its activity.
CC Contributes to the coordination of microtubules with actin fibers
CC and plays a role in cell elongation. Acts synergistically with
CC ROCK1 to promote SRC-dependent non-apoptotic plasma membrane
CC blebbing.
CC -!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via
CC its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-
CC terminus. Interacts with ROCK1 in a Src-dependent manner.
CC -!- INTERACTION:
CC Self; NbExp=9; IntAct=EBI-348433, EBI-348433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC projection, bleb. Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen.
CC -!- DOMAIN: The DAD domain regulates activation via by an
CC autoinhibitory interaction with the GBD/FH3 domain. This
CC autoinhibition is released upon competitive binding of an
CC activated GTPase. The release of DAD allows the FH2 domain to then
CC nucleate and elongate nonbranched actin filaments.
CC -!- PTM: Phosphorylated by ROCK1.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC 3) domain.
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DR EMBL; AF113615; AAD39906.1; -; mRNA.
DR EMBL; AB041046; BAD06250.1; -; mRNA.
DR EMBL; AY192154; AAO38757.1; -; mRNA.
DR EMBL; BC033084; AAH33084.1; -; mRNA.
DR EMBL; AB209584; BAD92821.1; -; mRNA.
DR RefSeq; NP_037373.2; NM_013241.2.
DR UniGene; Hs.95231; -.
DR PDB; 3DAD; X-ray; 2.30 A; A/B=1-339.
DR PDBsum; 3DAD; -.
DR DisProt; DP00448; -.
DR ProteinModelPortal; Q9Y613; -.
DR SMR; Q9Y613; 14-339, 651-1013.
DR DIP; DIP-31134N; -.
DR IntAct; Q9Y613; 13.
DR MINT; MINT-1033686; -.
DR STRING; 9606.ENSP00000258201; -.
DR PhosphoSite; Q9Y613; -.
DR DMDM; 62512187; -.
DR PaxDb; Q9Y613; -.
DR PeptideAtlas; Q9Y613; -.
DR PRIDE; Q9Y613; -.
DR Ensembl; ENST00000258201; ENSP00000258201; ENSG00000135723.
DR GeneID; 29109; -.
DR KEGG; hsa:29109; -.
DR UCSC; uc002esl.3; human.
DR CTD; 29109; -.
DR GeneCards; GC16M067263; -.
DR HGNC; HGNC:17905; FHOD1.
DR HPA; HPA024468; -.
DR MIM; 606881; gene.
DR neXtProt; NX_Q9Y613; -.
DR PharmGKB; PA28143; -.
DR eggNOG; NOG246341; -.
DR HOGENOM; HOG000015130; -.
DR HOVERGEN; HBG051615; -.
DR InParanoid; Q9Y613; -.
DR OMA; PKLCIGD; -.
DR OrthoDB; EOG71G9T2; -.
DR PhylomeDB; Q9Y613; -.
DR EvolutionaryTrace; Q9Y613; -.
DR GeneWiki; FHOD1; -.
DR GenomeRNAi; 29109; -.
DR NextBio; 52175; -.
DR PRO; PR:Q9Y613; -.
DR ArrayExpress; Q9Y613; -.
DR Bgee; Q9Y613; -.
DR CleanEx; HS_FHOD1; -.
DR Genevestigator; Q9Y613; -.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR027651; FHOD1/FHOD3.
DR InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR PANTHER; PTHR23213:SF3; PTHR23213:SF3; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; FALSE_NEG.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell projection; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1164 FH1/FH2 domain-containing protein 1.
FT /FTId=PRO_0000194905.
FT DOMAIN 53 458 GBD/FH3.
FT DOMAIN 487 615 FH1.
FT DOMAIN 616 1013 FH2.
FT DOMAIN 1053 1133 DAD.
FT REGION 612 807 Interaction with ROCK1.
FT COILED 884 921 Potential.
FT COMPBIAS 583 593 Poly-Pro.
FT COMPBIAS 597 605 Poly-Pro.
FT COMPBIAS 996 1001 Poly-Gln.
FT MOD_RES 367 367 Phosphoserine.
FT MOD_RES 486 486 Phosphoserine.
FT MOD_RES 495 495 Phosphothreonine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT MOD_RES 573 573 Phosphoserine.
FT MOD_RES 690 690 Phosphothreonine.
FT CONFLICT 249 249 S -> T (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT CONFLICT 264 264 E -> D (in Ref. 3; AAO38757).
FT CONFLICT 277 277 T -> M (in Ref. 2; BAD06250).
FT CONFLICT 307 308 EA -> DT (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT CONFLICT 359 359 E -> D (in Ref. 3; AAO38757).
FT CONFLICT 387 387 S -> T (in Ref. 3; AAO38757).
FT CONFLICT 533 533 P -> L (in Ref. 6; BAD92821).
FT CONFLICT 633 634 EL -> DV (in Ref. 1; AAD39906).
FT CONFLICT 689 689 R -> Q (in Ref. 3; AAO38757).
FT CONFLICT 700 700 S -> T (in Ref. 1; AAD39906).
FT CONFLICT 745 745 E -> G (in Ref. 3; AAO38757).
FT CONFLICT 751 751 E -> G (in Ref. 1; AAD39906).
FT CONFLICT 849 849 E -> D (in Ref. 1; AAD39906).
FT CONFLICT 1061 1061 P -> L (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT STRAND 15 22
FT STRAND 36 39
FT STRAND 42 46
FT HELIX 51 53
FT HELIX 55 61
FT STRAND 68 75
FT TURN 76 78
FT TURN 88 93
FT HELIX 98 100
FT HELIX 102 104
FT STRAND 109 114
FT HELIX 116 129
FT HELIX 132 147
FT HELIX 152 158
FT HELIX 161 169
FT HELIX 174 187
FT HELIX 191 199
FT HELIX 201 209
FT HELIX 210 212
FT HELIX 216 232
FT HELIX 234 236
FT HELIX 237 251
FT HELIX 257 263
FT TURN 264 267
FT HELIX 271 287
FT HELIX 291 303
FT HELIX 306 314
FT HELIX 321 338
SQ SEQUENCE 1164 AA; 126551 MW; E6C7AE1FB8DC3FC7 CRC64;
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LGAQIPAVHR
LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV
NAILEKLYSS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI
LRALGQLMLF VDGMLGVVAH SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF
IRAVNSVAST TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR RERRKPSSEE
GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL TGPASSPVGP PSGLQASVNL
FPTISVAPSA DTSSERSIYK ARFLENVAAA ETEKQVALAQ GRAETLAGAM PNEAGGHPDA
RQLWDSPETA PAARTPQSPA PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS
IGDLDFSDLG EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC ATLWASLDPV
SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS NAINIGLTTL PPVHVIKAAL
LNFDEFAVSK DGIEKLLTMM PTEEERQKIE EAQLANPDIP LGPAENFLMT LASIGGLAAR
LQLWAFKLDY DSMEREIAEP LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE
LSYLEKVSEV KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV CNRFHAFLLY
LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK QATYRERNKT RGRMITETEK
FSGVAGEAPS NPSVPVAVSS GPGRGDADSH ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI
MPTVGPSTAS PEEPPGSSLP SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR
TLKSGLGDDL VQALGLSKGP GLEV
//
ID FHOD1_HUMAN Reviewed; 1164 AA.
AC Q9Y613; Q59F76; Q6Y1F2; Q76MS8; Q8N521;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=FH1/FH2 domain-containing protein 1;
DE AltName: Full=Formin homolog overexpressed in spleen 1;
DE Short=FHOS;
DE AltName: Full=Formin homology 2 domain-containing protein 1;
GN Name=FHOD1; Synonyms=FHOS, FHOS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10352228; DOI=10.1016/S0378-1119(99)00127-4;
RA Westendorf J.J., Mernaugh R., Hiebert S.W.;
RT "Identification and characterization of a protein containing formin
RT homology (FH1/FH2) domains.";
RL Gene 232:173-182(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=14576350; DOI=10.1242/jcs.00769;
RA Takeya R., Sumimoto H.;
RT "Fhos, a mammalian formin, directly binds to F-actin via a region N-
RT terminal to the FH1 domain and forms a homotypic complex via the FH2
RT domain to promote actin fiber formation.";
RL J. Cell Sci. 116:4567-4575(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=15138285; DOI=10.1242/jcs.01113;
RA Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M.,
RA Longtine N., Uknis M., Fingeroth J.D.;
RT "EBV attachment stimulates FHOS/FHOD1 redistribution and co-
RT aggregation with CD21: formin interactions with the cytoplasmic domain
RT of human CD21.";
RL J. Cell Sci. 117:2709-2720(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AUTOINHIBITION, AND SUBCELLULAR LOCATION.
RX PubMed=15878344; DOI=10.1016/j.yexcr.2005.02.006;
RA Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S.,
RA Fackler O.T.;
RT "FHOD1 coordinates actin filament and microtubule alignment to mediate
RT cell elongation.";
RL Exp. Cell Res. 306:192-202(2005).
RN [8]
RP DOMAIN DAD, AND AUTOINHIBITION.
RX PubMed=16361249; DOI=10.1074/jbc.M509226200;
RA Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T.,
RA Geyer M.;
RT "Biochemical characterization of the diaphanous autoregulatory
RT interaction in the formin homology protein FHOD1.";
RL J. Biol. Chem. 281:5084-5093(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, AND
RP PHOSPHORYLATION.
RX PubMed=18694941; DOI=10.1074/jbc.M801800200;
RA Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J.,
RA Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R.,
RA Benichou S., Fackler O.T.;
RT "The diaphanous-related formin FHOD1 associates with ROCK1 and
RT promotes Src-dependent plasma membrane blebbing.";
RL J. Biol. Chem. 283:27891-27903(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498
RP AND SER-523, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523
RP AND SER-573, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC stress fibers. Depends on the Rho-ROCK cascade for its activity.
CC Contributes to the coordination of microtubules with actin fibers
CC and plays a role in cell elongation. Acts synergistically with
CC ROCK1 to promote SRC-dependent non-apoptotic plasma membrane
CC blebbing.
CC -!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via
CC its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-
CC terminus. Interacts with ROCK1 in a Src-dependent manner.
CC -!- INTERACTION:
CC Self; NbExp=9; IntAct=EBI-348433, EBI-348433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC projection, bleb. Note=Predominantly cytoplasmic.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen.
CC -!- DOMAIN: The DAD domain regulates activation via by an
CC autoinhibitory interaction with the GBD/FH3 domain. This
CC autoinhibition is released upon competitive binding of an
CC activated GTPase. The release of DAD allows the FH2 domain to then
CC nucleate and elongate nonbranched actin filaments.
CC -!- PTM: Phosphorylated by ROCK1.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC 3) domain.
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DR EMBL; AF113615; AAD39906.1; -; mRNA.
DR EMBL; AB041046; BAD06250.1; -; mRNA.
DR EMBL; AY192154; AAO38757.1; -; mRNA.
DR EMBL; BC033084; AAH33084.1; -; mRNA.
DR EMBL; AB209584; BAD92821.1; -; mRNA.
DR RefSeq; NP_037373.2; NM_013241.2.
DR UniGene; Hs.95231; -.
DR PDB; 3DAD; X-ray; 2.30 A; A/B=1-339.
DR PDBsum; 3DAD; -.
DR DisProt; DP00448; -.
DR ProteinModelPortal; Q9Y613; -.
DR SMR; Q9Y613; 14-339, 651-1013.
DR DIP; DIP-31134N; -.
DR IntAct; Q9Y613; 13.
DR MINT; MINT-1033686; -.
DR STRING; 9606.ENSP00000258201; -.
DR PhosphoSite; Q9Y613; -.
DR DMDM; 62512187; -.
DR PaxDb; Q9Y613; -.
DR PeptideAtlas; Q9Y613; -.
DR PRIDE; Q9Y613; -.
DR Ensembl; ENST00000258201; ENSP00000258201; ENSG00000135723.
DR GeneID; 29109; -.
DR KEGG; hsa:29109; -.
DR UCSC; uc002esl.3; human.
DR CTD; 29109; -.
DR GeneCards; GC16M067263; -.
DR HGNC; HGNC:17905; FHOD1.
DR HPA; HPA024468; -.
DR MIM; 606881; gene.
DR neXtProt; NX_Q9Y613; -.
DR PharmGKB; PA28143; -.
DR eggNOG; NOG246341; -.
DR HOGENOM; HOG000015130; -.
DR HOVERGEN; HBG051615; -.
DR InParanoid; Q9Y613; -.
DR OMA; PKLCIGD; -.
DR OrthoDB; EOG71G9T2; -.
DR PhylomeDB; Q9Y613; -.
DR EvolutionaryTrace; Q9Y613; -.
DR GeneWiki; FHOD1; -.
DR GenomeRNAi; 29109; -.
DR NextBio; 52175; -.
DR PRO; PR:Q9Y613; -.
DR ArrayExpress; Q9Y613; -.
DR Bgee; Q9Y613; -.
DR CleanEx; HS_FHOD1; -.
DR Genevestigator; Q9Y613; -.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR027651; FHOD1/FHOD3.
DR InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR PANTHER; PTHR23213:SF3; PTHR23213:SF3; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; FALSE_NEG.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell projection; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1164 FH1/FH2 domain-containing protein 1.
FT /FTId=PRO_0000194905.
FT DOMAIN 53 458 GBD/FH3.
FT DOMAIN 487 615 FH1.
FT DOMAIN 616 1013 FH2.
FT DOMAIN 1053 1133 DAD.
FT REGION 612 807 Interaction with ROCK1.
FT COILED 884 921 Potential.
FT COMPBIAS 583 593 Poly-Pro.
FT COMPBIAS 597 605 Poly-Pro.
FT COMPBIAS 996 1001 Poly-Gln.
FT MOD_RES 367 367 Phosphoserine.
FT MOD_RES 486 486 Phosphoserine.
FT MOD_RES 495 495 Phosphothreonine.
FT MOD_RES 498 498 Phosphoserine.
FT MOD_RES 523 523 Phosphoserine.
FT MOD_RES 573 573 Phosphoserine.
FT MOD_RES 690 690 Phosphothreonine.
FT CONFLICT 249 249 S -> T (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT CONFLICT 264 264 E -> D (in Ref. 3; AAO38757).
FT CONFLICT 277 277 T -> M (in Ref. 2; BAD06250).
FT CONFLICT 307 308 EA -> DT (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT CONFLICT 359 359 E -> D (in Ref. 3; AAO38757).
FT CONFLICT 387 387 S -> T (in Ref. 3; AAO38757).
FT CONFLICT 533 533 P -> L (in Ref. 6; BAD92821).
FT CONFLICT 633 634 EL -> DV (in Ref. 1; AAD39906).
FT CONFLICT 689 689 R -> Q (in Ref. 3; AAO38757).
FT CONFLICT 700 700 S -> T (in Ref. 1; AAD39906).
FT CONFLICT 745 745 E -> G (in Ref. 3; AAO38757).
FT CONFLICT 751 751 E -> G (in Ref. 1; AAD39906).
FT CONFLICT 849 849 E -> D (in Ref. 1; AAD39906).
FT CONFLICT 1061 1061 P -> L (in Ref. 1; AAD39906 and 3;
FT AAO38757).
FT STRAND 15 22
FT STRAND 36 39
FT STRAND 42 46
FT HELIX 51 53
FT HELIX 55 61
FT STRAND 68 75
FT TURN 76 78
FT TURN 88 93
FT HELIX 98 100
FT HELIX 102 104
FT STRAND 109 114
FT HELIX 116 129
FT HELIX 132 147
FT HELIX 152 158
FT HELIX 161 169
FT HELIX 174 187
FT HELIX 191 199
FT HELIX 201 209
FT HELIX 210 212
FT HELIX 216 232
FT HELIX 234 236
FT HELIX 237 251
FT HELIX 257 263
FT TURN 264 267
FT HELIX 271 287
FT HELIX 291 303
FT HELIX 306 314
FT HELIX 321 338
SQ SEQUENCE 1164 AA; 126551 MW; E6C7AE1FB8DC3FC7 CRC64;
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LGAQIPAVHR
LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV
NAILEKLYSS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI
LRALGQLMLF VDGMLGVVAH SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF
IRAVNSVAST TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR RERRKPSSEE
GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL TGPASSPVGP PSGLQASVNL
FPTISVAPSA DTSSERSIYK ARFLENVAAA ETEKQVALAQ GRAETLAGAM PNEAGGHPDA
RQLWDSPETA PAARTPQSPA PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS
IGDLDFSDLG EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC ATLWASLDPV
SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS NAINIGLTTL PPVHVIKAAL
LNFDEFAVSK DGIEKLLTMM PTEEERQKIE EAQLANPDIP LGPAENFLMT LASIGGLAAR
LQLWAFKLDY DSMEREIAEP LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE
LSYLEKVSEV KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV CNRFHAFLLY
LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK QATYRERNKT RGRMITETEK
FSGVAGEAPS NPSVPVAVSS GPGRGDADSH ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI
MPTVGPSTAS PEEPPGSSLP SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR
TLKSGLGDDL VQALGLSKGP GLEV
//
MIM
606881
*RECORD*
*FIELD* NO
606881
*FIELD* TI
*606881 FORMIN HOMOLOGY-2 DOMAIN-CONTAINING PROTEIN 1; FHOD1
;;FH1/FH2 DOMAIN-CONTAINING PROTEIN; FHOS
read more*FIELD* TX
DESCRIPTION
Formin homology-1 (FH1) and FH2 domains define a family of proteins
required for cell organization and limb development. The first members
of the family were termed formins because mutations caused improper limb
and renal formation in mice. For additional background information, see
FMN1 (136535).
CLONING
Using a portion of the AML-1B (RUNX1; 151385) transcription factor as
bait in a yeast-2 hybrid screen of a B-cell cDNA library, Westendorf et
al. (1999) identified a partial cDNA clone for FHOD1. The full-length
clone was obtained by screening a Burkitt lymphoma cell line and human
fetal and adult spleen cDNA libraries with the partial cDNA. The deduced
1,165-amino acid protein has a calculated molecular mass of 128 kD and
shows sequence homology to Diaphanous (see 300108) and FMN1 within the
FH1 and FH2 domains. It also contains a coiled-coil, a collagen-like
domain, 2 nuclear localization signals, and several potential PKC and
PKA phosphorylation sites. Westendorf et al. (1999) identified a 4-kb
transcript in several human erythroid leukemia cell lines and in all
tissues tested, with highest expression in spleen. Immunolocalization of
endogenous FHOD1 showed predominant cytoplasmic localization with
expression in a variety of human cell lines.
GENE FUNCTION
Using in vitro capture of FHOD1 with several recombinant Rho family GST
fusion proteins, Westendorf (2001) determined that FHOD1 interacts
specifically with Rac1 (602048) in a guanine nucleotide-independent
manner, and that FHOD1 does not interact with other members of the Rho
subfamily of GTPases. Immunoprecipitation studies confirmed direct
interaction between endogenous FHOD1 and Rac1.
MAPPING
By radiation hybrid analysis, Westendorf et al. (1999) mapped the FHOD1
gene to chromosome 16q22.
*FIELD* RF
1. Westendorf, J. J.: The formin/diaphanous-related protein, FHOS,
interacts with Rac1 and activates transcription from the serum response
element. J. Biol. Chem. 276: 46453-46459, 2001.
2. Westendorf, J. J.; Mernaugh, R.; Hiebert, S. W.: Identification
and characterization of a protein containing formin homology (FH1/FH2)
domains Gene 232: 173-182, 1999.
*FIELD* CD
Patricia A. Hartz: 4/24/2002
*FIELD* ED
wwang: 04/02/2010
mgross: 10/27/2005
carol: 4/25/2002
*RECORD*
*FIELD* NO
606881
*FIELD* TI
*606881 FORMIN HOMOLOGY-2 DOMAIN-CONTAINING PROTEIN 1; FHOD1
;;FH1/FH2 DOMAIN-CONTAINING PROTEIN; FHOS
read more*FIELD* TX
DESCRIPTION
Formin homology-1 (FH1) and FH2 domains define a family of proteins
required for cell organization and limb development. The first members
of the family were termed formins because mutations caused improper limb
and renal formation in mice. For additional background information, see
FMN1 (136535).
CLONING
Using a portion of the AML-1B (RUNX1; 151385) transcription factor as
bait in a yeast-2 hybrid screen of a B-cell cDNA library, Westendorf et
al. (1999) identified a partial cDNA clone for FHOD1. The full-length
clone was obtained by screening a Burkitt lymphoma cell line and human
fetal and adult spleen cDNA libraries with the partial cDNA. The deduced
1,165-amino acid protein has a calculated molecular mass of 128 kD and
shows sequence homology to Diaphanous (see 300108) and FMN1 within the
FH1 and FH2 domains. It also contains a coiled-coil, a collagen-like
domain, 2 nuclear localization signals, and several potential PKC and
PKA phosphorylation sites. Westendorf et al. (1999) identified a 4-kb
transcript in several human erythroid leukemia cell lines and in all
tissues tested, with highest expression in spleen. Immunolocalization of
endogenous FHOD1 showed predominant cytoplasmic localization with
expression in a variety of human cell lines.
GENE FUNCTION
Using in vitro capture of FHOD1 with several recombinant Rho family GST
fusion proteins, Westendorf (2001) determined that FHOD1 interacts
specifically with Rac1 (602048) in a guanine nucleotide-independent
manner, and that FHOD1 does not interact with other members of the Rho
subfamily of GTPases. Immunoprecipitation studies confirmed direct
interaction between endogenous FHOD1 and Rac1.
MAPPING
By radiation hybrid analysis, Westendorf et al. (1999) mapped the FHOD1
gene to chromosome 16q22.
*FIELD* RF
1. Westendorf, J. J.: The formin/diaphanous-related protein, FHOS,
interacts with Rac1 and activates transcription from the serum response
element. J. Biol. Chem. 276: 46453-46459, 2001.
2. Westendorf, J. J.; Mernaugh, R.; Hiebert, S. W.: Identification
and characterization of a protein containing formin homology (FH1/FH2)
domains Gene 232: 173-182, 1999.
*FIELD* CD
Patricia A. Hartz: 4/24/2002
*FIELD* ED
wwang: 04/02/2010
mgross: 10/27/2005
carol: 4/25/2002