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FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1) (FHOS) (Formin homology 2 domain-containing protein 1)

 FHOD1_HUMAN             Reviewed;        1164 AA.
Q9Y613; Q59F76; Q6Y1F2; Q76MS8; Q8N521;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 165.
RecName: Full=FH1/FH2 domain-containing protein 1;
AltName: Full=Formin homolog overexpressed in spleen 1;
Short=FHOS;
AltName: Full=Formin homology 2 domain-containing protein 1;
Name=FHOD1; Synonyms=FHOS, FHOS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10352228; DOI=10.1016/S0378-1119(99)00127-4;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
PubMed=14576350; DOI=10.1242/jcs.00769;
Takeya R., Sumimoto H.;
"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. 116:4567-4575(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=15138285; DOI=10.1242/jcs.01113;
Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M.,
Longtine N., Uknis M., Fingeroth J.D.;
"EBV attachment stimulates FHOS/FHOD1 redistribution and co-
aggregation with CD21: formin interactions with the cytoplasmic domain
of human CD21.";
J. Cell Sci. 117:2709-2720(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AUTOINHIBITION, AND SUBCELLULAR LOCATION.
PubMed=15878344; DOI=10.1016/j.yexcr.2005.02.006;
Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S.,
Fackler O.T.;
"FHOD1 coordinates actin filament and microtubule alignment to mediate
cell elongation.";
Exp. Cell Res. 306:192-202(2005).
[8]
DOMAIN DAD, AND AUTOINHIBITION.
PubMed=16361249; DOI=10.1074/jbc.M509226200;
Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T.,
Geyer M.;
"Biochemical characterization of the diaphanous autoregulatory
interaction in the formin homology protein FHOD1.";
J. Biol. Chem. 281:5084-5093(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, AND
PHOSPHORYLATION.
PubMed=18694941; DOI=10.1074/jbc.M801800200;
Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J.,
Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R.,
Benichou S., Fackler O.T.;
"The diaphanous-related formin FHOD1 associates with ROCK1 and
promotes Src-dependent plasma membrane blebbing.";
J. Biol. Chem. 283:27891-27903(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498
AND SER-523, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523
AND SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-498; SER-523
AND THR-690, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Required for the assembly of F-actin structures, such as
stress fibers. Depends on the Rho-ROCK cascade for its activity.
Contributes to the coordination of microtubules with actin fibers
and plays a role in cell elongation. Acts synergistically with
ROCK1 to promote SRC-dependent non-apoptotic plasma membrane
blebbing. {ECO:0000269|PubMed:14576350,
ECO:0000269|PubMed:15878344, ECO:0000269|PubMed:18694941}.
-!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via
its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-
terminus. Interacts with ROCK1 in a Src-dependent manner.
{ECO:0000269|PubMed:14576350, ECO:0000269|PubMed:15138285,
ECO:0000269|PubMed:18694941}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-348433, EBI-348433;
Q8WXH0:SYNE2; NbExp=4; IntAct=EBI-348433, EBI-2372294;
Q6ZWQ0-1:Syne2 (xeno); NbExp=2; IntAct=EBI-348433, EBI-16108623;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
projection, bleb. Note=Predominantly cytoplasmic.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen.
-!- DOMAIN: The DAD domain regulates activation via by an
autoinhibitory interaction with the GBD/FH3 domain. This
autoinhibition is released upon competitive binding of an
activated GTPase. The release of DAD allows the FH2 domain to then
nucleate and elongate nonbranched actin filaments.
{ECO:0000269|PubMed:16361249}.
-!- PTM: Phosphorylated by ROCK1. {ECO:0000269|PubMed:18694941}.
-!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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EMBL; AF113615; AAD39906.1; -; mRNA.
EMBL; AB041046; BAD06250.1; -; mRNA.
EMBL; AY192154; AAO38757.1; -; mRNA.
EMBL; BC033084; AAH33084.1; -; mRNA.
EMBL; AB209584; BAD92821.1; -; mRNA.
CCDS; CCDS10834.1; -.
RefSeq; NP_037373.2; NM_013241.2.
UniGene; Hs.95231; -.
PDB; 3DAD; X-ray; 2.30 A; A/B=1-339.
PDBsum; 3DAD; -.
DisProt; DP00448; -.
ProteinModelPortal; Q9Y613; -.
SMR; Q9Y613; -.
BioGrid; 118877; 33.
DIP; DIP-31134N; -.
IntAct; Q9Y613; 22.
MINT; Q9Y613; -.
STRING; 9606.ENSP00000258201; -.
iPTMnet; Q9Y613; -.
PhosphoSitePlus; Q9Y613; -.
BioMuta; FHOD1; -.
DMDM; 62512187; -.
EPD; Q9Y613; -.
MaxQB; Q9Y613; -.
PaxDb; Q9Y613; -.
PeptideAtlas; Q9Y613; -.
PRIDE; Q9Y613; -.
ProteomicsDB; 86575; -.
Ensembl; ENST00000258201; ENSP00000258201; ENSG00000135723.
GeneID; 29109; -.
KEGG; hsa:29109; -.
UCSC; uc002esl.4; human.
CTD; 29109; -.
DisGeNET; 29109; -.
EuPathDB; HostDB:ENSG00000135723.13; -.
GeneCards; FHOD1; -.
HGNC; HGNC:17905; FHOD1.
HPA; HPA024468; -.
MIM; 606881; gene.
neXtProt; NX_Q9Y613; -.
OpenTargets; ENSG00000135723; -.
PharmGKB; PA28143; -.
eggNOG; KOG1925; Eukaryota.
eggNOG; ENOG410XRBZ; LUCA.
GeneTree; ENSGT00870000136417; -.
HOGENOM; HOG000015130; -.
HOVERGEN; HBG051615; -.
InParanoid; Q9Y613; -.
OMA; PKLCIGD; -.
OrthoDB; EOG091G0147; -.
PhylomeDB; Q9Y613; -.
TreeFam; TF316268; -.
SIGNOR; Q9Y613; -.
EvolutionaryTrace; Q9Y613; -.
GeneWiki; FHOD1; -.
GenomeRNAi; 29109; -.
PRO; PR:Q9Y613; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000135723; Expressed in 165 organ(s), highest expression level in spleen.
CleanEx; HS_FHOD1; -.
ExpressionAtlas; Q9Y613; baseline and differential.
Genevisible; Q9Y613; HS.
GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0043621; F:protein self-association; IMP:CAFA.
GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0051492; P:regulation of stress fiber assembly; IMP:CAFA.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015425; FH2_Formin.
InterPro; IPR027647; FHOD1.
InterPro; IPR014768; GBD/FH3_dom.
PANTHER; PTHR23213:SF189; PTHR23213:SF189; 2.
Pfam; PF02181; FH2; 1.
SMART; SM00498; FH2; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51444; FH2; 1.
PROSITE; PS51232; GBD_FH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 1164 FH1/FH2 domain-containing protein 1.
/FTId=PRO_0000194905.
DOMAIN 53 458 GBD/FH3. {ECO:0000255|PROSITE-
ProRule:PRU00579}.
DOMAIN 487 615 FH1.
DOMAIN 616 1013 FH2. {ECO:0000255|PROSITE-
ProRule:PRU00774}.
DOMAIN 1053 1133 DAD.
REGION 612 807 Interaction with ROCK1.
{ECO:0000269|PubMed:18694941}.
COILED 884 921 {ECO:0000255}.
COMPBIAS 583 593 Poly-Pro.
COMPBIAS 597 605 Poly-Pro.
COMPBIAS 996 1001 Poly-Gln.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 495 495 Phosphothreonine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 690 690 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CONFLICT 249 249 S -> T (in Ref. 1; AAD39906 and 3;
AAO38757). {ECO:0000305}.
CONFLICT 264 264 E -> D (in Ref. 3; AAO38757).
{ECO:0000305}.
CONFLICT 277 277 T -> M (in Ref. 2; BAD06250).
{ECO:0000305}.
CONFLICT 307 308 EA -> DT (in Ref. 1; AAD39906 and 3;
AAO38757). {ECO:0000305}.
CONFLICT 359 359 E -> D (in Ref. 3; AAO38757).
{ECO:0000305}.
CONFLICT 387 387 S -> T (in Ref. 3; AAO38757).
{ECO:0000305}.
CONFLICT 533 533 P -> L (in Ref. 6; BAD92821).
{ECO:0000305}.
CONFLICT 633 634 EL -> DV (in Ref. 1; AAD39906).
{ECO:0000305}.
CONFLICT 689 689 R -> Q (in Ref. 3; AAO38757).
{ECO:0000305}.
CONFLICT 700 700 S -> T (in Ref. 1; AAD39906).
{ECO:0000305}.
CONFLICT 745 745 E -> G (in Ref. 3; AAO38757).
{ECO:0000305}.
CONFLICT 751 751 E -> G (in Ref. 1; AAD39906).
{ECO:0000305}.
CONFLICT 849 849 E -> D (in Ref. 1; AAD39906).
{ECO:0000305}.
CONFLICT 1061 1061 P -> L (in Ref. 1; AAD39906 and 3;
AAO38757). {ECO:0000305}.
STRAND 15 22 {ECO:0000244|PDB:3DAD}.
STRAND 36 39 {ECO:0000244|PDB:3DAD}.
STRAND 42 46 {ECO:0000244|PDB:3DAD}.
HELIX 51 53 {ECO:0000244|PDB:3DAD}.
HELIX 55 61 {ECO:0000244|PDB:3DAD}.
STRAND 68 75 {ECO:0000244|PDB:3DAD}.
TURN 76 78 {ECO:0000244|PDB:3DAD}.
TURN 88 93 {ECO:0000244|PDB:3DAD}.
HELIX 98 100 {ECO:0000244|PDB:3DAD}.
HELIX 102 104 {ECO:0000244|PDB:3DAD}.
STRAND 109 114 {ECO:0000244|PDB:3DAD}.
HELIX 116 129 {ECO:0000244|PDB:3DAD}.
HELIX 132 147 {ECO:0000244|PDB:3DAD}.
HELIX 152 158 {ECO:0000244|PDB:3DAD}.
HELIX 161 169 {ECO:0000244|PDB:3DAD}.
HELIX 174 187 {ECO:0000244|PDB:3DAD}.
HELIX 191 199 {ECO:0000244|PDB:3DAD}.
HELIX 201 209 {ECO:0000244|PDB:3DAD}.
HELIX 210 212 {ECO:0000244|PDB:3DAD}.
HELIX 216 232 {ECO:0000244|PDB:3DAD}.
HELIX 234 236 {ECO:0000244|PDB:3DAD}.
HELIX 237 251 {ECO:0000244|PDB:3DAD}.
HELIX 257 263 {ECO:0000244|PDB:3DAD}.
TURN 264 267 {ECO:0000244|PDB:3DAD}.
HELIX 271 287 {ECO:0000244|PDB:3DAD}.
HELIX 291 303 {ECO:0000244|PDB:3DAD}.
HELIX 306 314 {ECO:0000244|PDB:3DAD}.
HELIX 321 338 {ECO:0000244|PDB:3DAD}.
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


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AS11 1752 Antibody: AtFH14 | Formin-like protein 14 (100 ug), Immunogen: recombinant formin of Arabidopsis thaliana, amino acids 340-520, NP_17446, Host: mouse, monoclonal, Confirmed reactivity: Arabidopsis tha 100
AS11 1750 Antibody: AtFH14 | Formin-like protein 14 (50 ug), Immunogen: recombinant formin of Arabidopsis thaliana, amino acids 340-520, NP_17446, Host: mouse, monoclonal, Confirmed reactivity: Arabidopsis thal 50
CSB-EL025978MO Mouse WW domain binding protein 4 (formin binding protein 21) (WBP4) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL025978CH Chicken WW domain binding protein 4 (formin binding protein 21) (WBP4) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL025978HU Human WW domain binding protein 4 (formin binding protein 21) (WBP4) ELISA kit, Species Human, Sample Type serum, plasma 96T
ING2 INF2 Gene inverted formin, FH2 and WH2 domain containing
EIAAB14440 CDEP,Chondrocyte-derived ezrin-like protein,FARP1,FERM, RhoGEF and pleckstrin domain-containing protein 1,Homo sapiens,Human,PH domain-containing family C member 2,Pleckstrin homology domain-containin
WBP4 WBP4 Gene WW domain binding protein 4 (formin binding protein 21)


 

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