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Q9Y613 (FHOD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FH1/FH2 domain-containing protein 1
Alternative name(s):
Formin homolog overexpressed in spleen 1
Short name=FHOS
Formin homology 2 domain-containing protein 1
Gene names
Name:FHOD1
Synonyms:FHOS, FHOS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1164 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.7 Ref.9

Subunit structure

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. Ref.2 Ref.3 Ref.9

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell projectionbleb. Note: Predominantly cytoplasmic. Ref.7 Ref.9

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. Ref.8

Post-translational modification

Phosphorylated by ROCK1. Ref.9

Sequence similarities

Belongs to the formin homology family.

Contains 1 DAD (diaphanous autoregulatory) domain.

Contains 1 FH1 (formin homology 1) domain.

Contains 1 FH2 (formin homology 2) domain.

Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself8EBI-348433,EBI-348433

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 11641163FH1/FH2 domain-containing protein 1
PRO_0000194905

Regions

Domain53 – 458406GBD/FH3
Domain487 – 615129FH1
Domain616 – 1013398FH2
Domain1053 – 113381DAD
Region612 – 807196Interaction with ROCK1
Coiled coil884 – 92138 Potential
Compositional bias583 – 59311Poly-Pro
Compositional bias597 – 6059Poly-Pro
Compositional bias996 – 10016Poly-Gln

Amino acid modifications

Modified residue3671Phosphoserine Ref.11 Ref.12
Modified residue4861Phosphoserine Ref.12
Modified residue4951Phosphothreonine Ref.11
Modified residue4981Phosphoserine Ref.10 Ref.11
Modified residue5231Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue5731Phosphoserine Ref.12
Modified residue6901Phosphothreonine Ref.13

Experimental info

Sequence conflict2491S → T in AAD39906. Ref.1
Sequence conflict2491S → T in AAO38757. Ref.3
Sequence conflict2641E → D in AAO38757. Ref.3
Sequence conflict2771T → M in BAD06250. Ref.2
Sequence conflict307 – 3082EA → DT in AAD39906. Ref.1
Sequence conflict307 – 3082EA → DT in AAO38757. Ref.3
Sequence conflict3591E → D in AAO38757. Ref.3
Sequence conflict3871S → T in AAO38757. Ref.3
Sequence conflict5331P → L in BAD92821. Ref.6
Sequence conflict633 – 6342EL → DV in AAD39906. Ref.1
Sequence conflict6891R → Q in AAO38757. Ref.3
Sequence conflict7001S → T in AAD39906. Ref.1
Sequence conflict7451E → G in AAO38757. Ref.3
Sequence conflict7511E → G in AAD39906. Ref.1
Sequence conflict8491E → D in AAD39906. Ref.1
Sequence conflict10611P → L in AAD39906. Ref.1
Sequence conflict10611P → L in AAO38757. Ref.3

Secondary structure

..................................................... 1164
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y613 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E6C7AE1FB8DC3FC7

FASTA1,164126,551
        10         20         30         40         50         60 
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LGAQIPAVHR 

        70         80         90        100        110        120 
LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV 

       130        140        150        160        170        180 
NAILEKLYSS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI 

       190        200        210        220        230        240 
LRALGQLMLF VDGMLGVVAH SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF 

       250        260        270        280        290        300 
IRAVNSVAST TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA 

       310        320        330        340        350        360 
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR RERRKPSSEE 

       370        380        390        400        410        420 
GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL TGPASSPVGP PSGLQASVNL 

       430        440        450        460        470        480 
FPTISVAPSA DTSSERSIYK ARFLENVAAA ETEKQVALAQ GRAETLAGAM PNEAGGHPDA 

       490        500        510        520        530        540 
RQLWDSPETA PAARTPQSPA PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS 

       550        560        570        580        590        600 
IGDLDFSDLG EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP 

       610        620        630        640        650        660 
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC ATLWASLDPV 

       670        680        690        700        710        720 
SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS NAINIGLTTL PPVHVIKAAL 

       730        740        750        760        770        780 
LNFDEFAVSK DGIEKLLTMM PTEEERQKIE EAQLANPDIP LGPAENFLMT LASIGGLAAR 

       790        800        810        820        830        840 
LQLWAFKLDY DSMEREIAEP LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE 

       850        860        870        880        890        900 
LSYLEKVSEV KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG 

       910        920        930        940        950        960 
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV CNRFHAFLLY 

       970        980        990       1000       1010       1020 
LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK QATYRERNKT RGRMITETEK 

      1030       1040       1050       1060       1070       1080 
FSGVAGEAPS NPSVPVAVSS GPGRGDADSH ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI 

      1090       1100       1110       1120       1130       1140 
MPTVGPSTAS PEEPPGSSLP SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR 

      1150       1160 
TLKSGLGDDL VQALGLSKGP GLEV 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a protein containing formin homology (FH1/FH2) domains."
Westendorf J.J., Mernaugh R., Hiebert S.W.
Gene 232:173-182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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."
Takeya R., Sumimoto H.
J. Cell Sci. 116:4567-4575(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
[3]"EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21."
Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M., Longtine N., Uknis M., Fingeroth J.D.
J. Cell Sci. 117:2709-2720(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[5]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Tissue: Platelet.
[6]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
Tissue: Spleen.
[7]"FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation."
Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S., Fackler O.T.
Exp. Cell Res. 306:192-202(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOINHIBITION, SUBCELLULAR LOCATION.
[8]"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1."
Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T., Geyer M.
J. Biol. Chem. 281:5084-5093(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN DAD, AUTOINHIBITION.
[9]"The diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing."
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.
J. Biol. Chem. 283:27891-27903(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, PHOSPHORYLATION.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498 AND SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF113615 mRNA. Translation: AAD39906.1.
AB041046 mRNA. Translation: BAD06250.1.
AY192154 mRNA. Translation: AAO38757.1.
BC033084 mRNA. Translation: AAH33084.1.
AB209584 mRNA. Translation: BAD92821.1.
CCDSCCDS10834.1.
RefSeqNP_037373.2. NM_013241.2.
UniGeneHs.95231.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DADX-ray2.30A/B1-339[»]
DisProtDP00448.
ProteinModelPortalQ9Y613.
SMRQ9Y613. Positions 14-339, 651-1013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118877. 21 interactions.
DIPDIP-31134N.
IntActQ9Y613. 13 interactions.
MINTMINT-1033686.
STRING9606.ENSP00000258201.

PTM databases

PhosphoSiteQ9Y613.

Polymorphism databases

DMDM62512187.

Proteomic databases

MaxQBQ9Y613.
PaxDbQ9Y613.
PeptideAtlasQ9Y613.
PRIDEQ9Y613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258201; ENSP00000258201; ENSG00000135723.
GeneID29109.
KEGGhsa:29109.
UCSCuc002esl.3. human.

Organism-specific databases

CTD29109.
GeneCardsGC16M067263.
HGNCHGNC:17905. FHOD1.
HPAHPA024468.
MIM606881. gene.
neXtProtNX_Q9Y613.
PharmGKBPA28143.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246341.
HOGENOMHOG000015130.
HOVERGENHBG051615.
InParanoidQ9Y613.
OMAPKLCIGD.
OrthoDBEOG71G9T2.
PhylomeDBQ9Y613.
TreeFamTF316268.

Gene expression databases

ArrayExpressQ9Y613.
BgeeQ9Y613.
CleanExHS_FHOD1.
GenevestigatorQ9Y613.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR027647. FHDC1.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERPTHR23213:SF189. PTHR23213:SF189. 1 hit.
PfamPF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y613.
GeneWikiFHOD1.
GenomeRNAi29109.
NextBio52175.
PROQ9Y613.
SOURCESearch...

Entry information

Entry nameFHOD1_HUMAN
AccessionPrimary (citable) accession number: Q9Y613
Secondary accession number(s): Q59F76 expand/collapse secondary AC list , Q6Y1F2, Q76MS8, Q8N521
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM