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Protein

FH1/FH2 domain-containing protein 1

Gene

Fhod1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

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:Fhos1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2679008. Fhod1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 11971196FH1/FH2 domain-containing protein 1PRO_0000194906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei499 – 4991PhosphothreonineBy similarity
Modified residuei502 – 5021PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei722 – 7221PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated by ROCK1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6P9Q4.
MaxQBiQ6P9Q4.
PaxDbiQ6P9Q4.
PeptideAtlasiQ6P9Q4.
PRIDEiQ6P9Q4.

PTM databases

iPTMnetiQ6P9Q4.
PhosphoSiteiQ6P9Q4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000014778.
CleanExiMM_FHOD1.
GenevisibleiQ6P9Q4. MM.

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 (By similarity). Interacts with ROCK1 in a Src-dependent manner (By similarity).By similarity

Protein-protein interaction databases

BioGridi231560. 1 interaction.
IntActiQ6P9Q4. 3 interactions.
MINTiMINT-4111564.
STRINGi10090.ENSMUSP00000014922.

Structurei

3D structure databases

ProteinModelPortaliQ6P9Q4.
SMRiQ6P9Q4. Positions 14-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 462410GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 647157FH1Add
BLAST
Domaini648 – 1045398FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1085 – 116682DADAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni644 – 839196Interaction with ROCK1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi491 – 641151Pro-richAdd
BLAST
Compositional biasi1028 – 10314Poly-Gln

Domaini

Regulated by intramolecular binding to a C-terminal auto-inhibitory domain. Effector binding abolishes this interaction and activates the protein (By similarity).By similarity
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 (By similarity).By similarity

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

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00810000125396.
HOGENOMiHOG000015130.
HOVERGENiHBG051615.
InParanoidiQ6P9Q4.
OMAiPCATLWA.
OrthoDBiEOG091G0147.
PhylomeDBiQ6P9Q4.
TreeFamiTF316268.

Family and domain databases

InterProiIPR016024. 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.

Q6P9Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGEEERGDG DPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP
60 70 80 90 100
LSAQIPALHR LLGAPLKLED CALQVSPSGY YLDPELSLEE QREMLEGFYE
110 120 130 140 150
EISKGRKPTL ILRTQLSVRV NAILEKLYGS SGPELRRSLF SLKQIFQEDK
160 170 180 190 200
DLVPEFVHSE GLSCLIRVGA AADHNYQSYI LRALGQLMLF VDGMLGVVAH
210 220 230 240 250
SETVQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF IQAVNAVASA
260 270 280 290 300
TGTLPWANLV SILEEKNGAD AELLVYTVTL INKTLAALPD QDSFYDVTDA
310 320 330 340 350
LEQQGMEALV QRFLGTAGTD VDLRTQLTLY ESALRLEDGD MEEAAAAAAA
360 370 380 390 400
GGRRERRKPS SEEGKRSRRS LEGGGCPVRA PEPGSTGSAS PVGSTPSTGS
410 420 430 440 450
APPTNPAFSS TGPASGLLRT SVNLFPTISV GPSVDSSCER SVYKARFLEN
460 470 480 490 500
VAAAETEKQA ALAQGRAETL AGATVDDTDG SSGTRELWDS PEPASAPRTP
510 520 530 540 550
QSPVSRILLR TQRSLEPEPK KPVSPPSPKA EPIQEPPTCV PKLCIGDLDF
560 570 580 590 600
SDLGEDEDQD TLNVESVEAG KASPFLSSLS PSLSGGPPPP PPPPPPITGS
610 620 630 640 650
CPPPPPPPLP PPATGSCPPP PPPPPPPIIG SCPPPPPLAA PFTHSALDGP
660 670 680 690 700
RHPTKRKTVK LFWRELKLTG GPGCSRSRFG PCPTLWASLE PVSVDTARLE
710 720 730 740 750
HLFESRAKDV LPTKKAGEGR RTMTVVLDPK RSNAINIGLT TLPPVHVIKA
760 770 780 790 800
ALLNFDEFAV SKDGIEKLLT MMPTEEERQK IEEAQLANPD VPLGPAENFL
810 820 830 840 850
MTLASIGGLA ARLQLWAFKL DYESMEREIA EPLFDLKVGM EQLVHNATFR
860 870 880 890 900
CILATLLAVG NFLNGSQSSG FELSYLEKVS EVKDTVRRQS LLYHLCSLVL
910 920 930 940 950
QTRPDSSDLY SEIPALTRCA KVDFEQLTEN LGQLECRSQA AEDSLRSLAK
960 970 980 990 1000
HELSPALRAR LTHFLAQCTR RVAMLRVVHR RVCNRFHAFL LYLGYTPQAA
1010 1020 1030 1040 1050
RDVRIMQFCH TLREFALEYR TCRERVLQQQ QKRATYRERN KTRGRMITET
1060 1070 1080 1090 1100
EKFSGVAGEA PNNLSVPVAV GSGPGQGDTD NHASMKSLLT SRPEDATHSR
1110 1120 1130 1140 1150
RSRGMVQSSS PVSHTAVGPS AASPEETAAS GLPTDTSDEI MDLLVQSVTK
1160 1170 1180 1190
SGPRALAARE RKRSRGNRKS LRRTLKSGLG DDLVQALGLS KAPGLEV
Length:1,197
Mass (Da):129,600
Last modified:January 23, 2007 - v3
Checksum:i162634FAB9715F01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti323 – 3231L → Q in BAC27106 (PubMed:16141072).Curated
Sequence conflicti929 – 9291E → K in BAC27106 (PubMed:16141072).Curated
Sequence conflicti1196 – 11961E → G in BAC27106 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041045 mRNA. Translation: BAE06182.1.
AK030737 mRNA. Translation: BAC27106.1.
BC060654 mRNA. Translation: AAH60654.1.
CCDSiCCDS22600.1.
RefSeqiNP_808367.2. NM_177699.4.
UniGeneiMm.87724.

Genome annotation databases

EnsembliENSMUST00000014922; ENSMUSP00000014922; ENSMUSG00000014778.
GeneIDi234686.
KEGGimmu:234686.
UCSCiuc009nct.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041045 mRNA. Translation: BAE06182.1.
AK030737 mRNA. Translation: BAC27106.1.
BC060654 mRNA. Translation: AAH60654.1.
CCDSiCCDS22600.1.
RefSeqiNP_808367.2. NM_177699.4.
UniGeneiMm.87724.

3D structure databases

ProteinModelPortaliQ6P9Q4.
SMRiQ6P9Q4. Positions 14-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231560. 1 interaction.
IntActiQ6P9Q4. 3 interactions.
MINTiMINT-4111564.
STRINGi10090.ENSMUSP00000014922.

PTM databases

iPTMnetiQ6P9Q4.
PhosphoSiteiQ6P9Q4.

Proteomic databases

EPDiQ6P9Q4.
MaxQBiQ6P9Q4.
PaxDbiQ6P9Q4.
PeptideAtlasiQ6P9Q4.
PRIDEiQ6P9Q4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014922; ENSMUSP00000014922; ENSMUSG00000014778.
GeneIDi234686.
KEGGimmu:234686.
UCSCiuc009nct.2. mouse.

Organism-specific databases

CTDi29109.
MGIiMGI:2679008. Fhod1.

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00810000125396.
HOGENOMiHOG000015130.
HOVERGENiHBG051615.
InParanoidiQ6P9Q4.
OMAiPCATLWA.
OrthoDBiEOG091G0147.
PhylomeDBiQ6P9Q4.
TreeFamiTF316268.

Miscellaneous databases

ChiTaRSiFhod1. mouse.
PROiQ6P9Q4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000014778.
CleanExiMM_FHOD1.
GenevisibleiQ6P9Q4. MM.

Family and domain databases

InterProiIPR016024. 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_MOUSE
AccessioniPrimary (citable) accession number: Q6P9Q4
Secondary accession number(s): Q8BMK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.