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Protein

FH1/FH2 domain-containing protein 1

Gene

FHOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135723-MONOMER.
SIGNORiQ9Y613.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FHOD1
Synonyms:FHOS, FHOS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17905. FHOD1.

Subcellular locationi

GO - Cellular componenti

  • bleb Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytoskeleton Source: UniProtKB-SubCell
  • intercalated disc Source: Ensembl
  • membrane Source: UniProtKB
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi29109.
OpenTargetsiENSG00000135723.
PharmGKBiPA28143.

Polymorphism and mutation databases

BioMutaiFHOD1.
DMDMi62512187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001949052 – 1164FH1/FH2 domain-containing protein 1Add BLAST1163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei367PhosphoserineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Modified residuei495PhosphothreonineCombined sources1
Modified residuei498PhosphoserineCombined sources1
Modified residuei523PhosphoserineCombined sources1
Modified residuei573PhosphoserineCombined sources1
Modified residuei690PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated by ROCK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y613.
MaxQBiQ9Y613.
PaxDbiQ9Y613.
PeptideAtlasiQ9Y613.
PRIDEiQ9Y613.

PTM databases

iPTMnetiQ9Y613.
PhosphoSitePlusiQ9Y613.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in spleen.

Gene expression databases

BgeeiENSG00000135723.
CleanExiHS_FHOD1.
ExpressionAtlasiQ9Y613. baseline and differential.
GenevisibleiQ9Y613. HS.

Organism-specific databases

HPAiHPA024468.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-348433,EBI-348433

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi118877. 30 interactors.
DIPiDIP-31134N.
IntActiQ9Y613. 15 interactors.
MINTiMINT-1033686.
STRINGi9606.ENSP00000258201.

Structurei

Secondary structure

11164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 22Combined sources8
Beta strandi36 – 39Combined sources4
Beta strandi42 – 46Combined sources5
Helixi51 – 53Combined sources3
Helixi55 – 61Combined sources7
Beta strandi68 – 75Combined sources8
Turni76 – 78Combined sources3
Turni88 – 93Combined sources6
Helixi98 – 100Combined sources3
Helixi102 – 104Combined sources3
Beta strandi109 – 114Combined sources6
Helixi116 – 129Combined sources14
Helixi132 – 147Combined sources16
Helixi152 – 158Combined sources7
Helixi161 – 169Combined sources9
Helixi174 – 187Combined sources14
Helixi191 – 199Combined sources9
Helixi201 – 209Combined sources9
Helixi210 – 212Combined sources3
Helixi216 – 232Combined sources17
Helixi234 – 236Combined sources3
Helixi237 – 251Combined sources15
Helixi257 – 263Combined sources7
Turni264 – 267Combined sources4
Helixi271 – 287Combined sources17
Helixi291 – 303Combined sources13
Helixi306 – 314Combined sources9
Helixi321 – 338Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DADX-ray2.30A/B1-339[»]
DisProtiDP00448.
ProteinModelPortaliQ9Y613.
SMRiQ9Y613.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y613.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 458GBD/FH3PROSITE-ProRule annotationAdd BLAST406
Domaini487 – 615FH1Add BLAST129
Domaini616 – 1013FH2PROSITE-ProRule annotationAdd BLAST398
Domaini1053 – 1133DADAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni612 – 807Interaction with ROCK11 PublicationAdd BLAST196

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili884 – 921Sequence analysisAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi583 – 593Poly-ProAdd BLAST11
Compositional biasi597 – 605Poly-Pro9
Compositional biasi996 – 1001Poly-Gln6

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00860000133772.
HOGENOMiHOG000015130.
HOVERGENiHBG051615.
InParanoidiQ9Y613.
OMAiPCATLWA.
OrthoDBiEOG091G0147.
PhylomeDBiQ9Y613.
TreeFamiTF316268.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR027647. FHDC1.
IPR014768. GBD/FH3_dom.
[Graphical view]
PANTHERiPTHR23213:SF189. PTHR23213:SF189. 2 hits.
PfamiPF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP
60 70 80 90 100
LGAQIPAVHR LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE
110 120 130 140 150
EISKGRKPTL ILRTQLSVRV NAILEKLYSS SGPELRRSLF SLKQIFQEDK
160 170 180 190 200
DLVPEFVHSE GLSCLIRVGA AADHNYQSYI LRALGQLMLF VDGMLGVVAH
210 220 230 240 250
SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF IRAVNSVAST
260 270 280 290 300
TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA
310 320 330 340 350
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR
360 370 380 390 400
RERRKPSSEE GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL
410 420 430 440 450
TGPASSPVGP PSGLQASVNL FPTISVAPSA DTSSERSIYK ARFLENVAAA
460 470 480 490 500
ETEKQVALAQ GRAETLAGAM PNEAGGHPDA RQLWDSPETA PAARTPQSPA
510 520 530 540 550
PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS IGDLDFSDLG
560 570 580 590 600
EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP
610 620 630 640 650
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC
660 670 680 690 700
ATLWASLDPV SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS
710 720 730 740 750
NAINIGLTTL PPVHVIKAAL LNFDEFAVSK DGIEKLLTMM PTEEERQKIE
760 770 780 790 800
EAQLANPDIP LGPAENFLMT LASIGGLAAR LQLWAFKLDY DSMEREIAEP
810 820 830 840 850
LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE LSYLEKVSEV
860 870 880 890 900
KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG
910 920 930 940 950
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV
960 970 980 990 1000
CNRFHAFLLY LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK
1010 1020 1030 1040 1050
QATYRERNKT RGRMITETEK FSGVAGEAPS NPSVPVAVSS GPGRGDADSH
1060 1070 1080 1090 1100
ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI MPTVGPSTAS PEEPPGSSLP
1110 1120 1130 1140 1150
SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR TLKSGLGDDL
1160
VQALGLSKGP GLEV
Length:1,164
Mass (Da):126,551
Last modified:January 23, 2007 - v3
Checksum:iE6C7AE1FB8DC3FC7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti249S → T in AAD39906 (PubMed:10352228).Curated1
Sequence conflicti249S → T in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti264E → D in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti277T → M in BAD06250 (PubMed:14576350).Curated1
Sequence conflicti307 – 308EA → DT in AAD39906 (PubMed:10352228).Curated2
Sequence conflicti307 – 308EA → DT in AAO38757 (PubMed:15138285).Curated2
Sequence conflicti359E → D in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti387S → T in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti533P → L in BAD92821 (Ref. 6) Curated1
Sequence conflicti633 – 634EL → DV in AAD39906 (PubMed:10352228).Curated2
Sequence conflicti689R → Q in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti700S → T in AAD39906 (PubMed:10352228).Curated1
Sequence conflicti745E → G in AAO38757 (PubMed:15138285).Curated1
Sequence conflicti751E → G in AAD39906 (PubMed:10352228).Curated1
Sequence conflicti849E → D in AAD39906 (PubMed:10352228).Curated1
Sequence conflicti1061P → L in AAD39906 (PubMed:10352228).Curated1
Sequence conflicti1061P → L in AAO38757 (PubMed:15138285).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10834.1.
RefSeqiNP_037373.2. NM_013241.2.
UniGeneiHs.95231.

Genome annotation databases

EnsembliENST00000258201; ENSP00000258201; ENSG00000135723.
GeneIDi29109.
KEGGihsa:29109.
UCSCiuc002esl.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10834.1.
RefSeqiNP_037373.2. NM_013241.2.
UniGeneiHs.95231.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DADX-ray2.30A/B1-339[»]
DisProtiDP00448.
ProteinModelPortaliQ9Y613.
SMRiQ9Y613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118877. 30 interactors.
DIPiDIP-31134N.
IntActiQ9Y613. 15 interactors.
MINTiMINT-1033686.
STRINGi9606.ENSP00000258201.

PTM databases

iPTMnetiQ9Y613.
PhosphoSitePlusiQ9Y613.

Polymorphism and mutation databases

BioMutaiFHOD1.
DMDMi62512187.

Proteomic databases

EPDiQ9Y613.
MaxQBiQ9Y613.
PaxDbiQ9Y613.
PeptideAtlasiQ9Y613.
PRIDEiQ9Y613.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258201; ENSP00000258201; ENSG00000135723.
GeneIDi29109.
KEGGihsa:29109.
UCSCiuc002esl.4. human.

Organism-specific databases

CTDi29109.
DisGeNETi29109.
GeneCardsiFHOD1.
HGNCiHGNC:17905. FHOD1.
HPAiHPA024468.
MIMi606881. gene.
neXtProtiNX_Q9Y613.
OpenTargetsiENSG00000135723.
PharmGKBiPA28143.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00860000133772.
HOGENOMiHOG000015130.
HOVERGENiHBG051615.
InParanoidiQ9Y613.
OMAiPCATLWA.
OrthoDBiEOG091G0147.
PhylomeDBiQ9Y613.
TreeFamiTF316268.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135723-MONOMER.
SIGNORiQ9Y613.

Miscellaneous databases

EvolutionaryTraceiQ9Y613.
GeneWikiiFHOD1.
GenomeRNAii29109.
PROiQ9Y613.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135723.
CleanExiHS_FHOD1.
ExpressionAtlasiQ9Y613. baseline and differential.
GenevisibleiQ9Y613. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR027647. FHDC1.
IPR014768. GBD/FH3_dom.
[Graphical view]
PANTHERiPTHR23213:SF189. PTHR23213:SF189. 2 hits.
PfamiPF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFHOD1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y613
Secondary accession number(s): Q59F76
, Q6Y1F2, Q76MS8, Q8N521
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.