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Protein

Formin-2

Gene

Fmn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis.By similarity5 Publications

GO - Molecular functioni

GO - Biological processi

  • actin filament bundle assembly Source: MGI
  • actin nucleation Source: InterPro
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hypoxia Source: UniProtKB
  • establishment of meiotic spindle localization Source: UniProtKB
  • formin-nucleated actin cable assembly Source: UniProtKB
  • homologous chromosome movement towards spindle pole involved in homologous chromosome segregation Source: BHF-UCL
  • intracellular transport Source: UniProtKB
  • meiotic chromosome movement towards spindle pole Source: MGI
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of protein catabolic process Source: UniProtKB
  • oogenesis Source: BHF-UCL
  • polar body extrusion after meiotic divisions Source: BHF-UCL
  • protein transport Source: UniProtKB-KW
  • vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

DNA damage, Protein transport, Stress response, Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-2
Gene namesi
Name:Fmn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1859252. Fmn2.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: InterPro
  • cell cortex Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: MGI
  • microvillus Source: MGI
  • nucleolus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype in male mice, but female mice show reduced fertility and produce at most one to three pups per litter. Female mice display defects in asymmetric spindle positioning, asymmetric cell division and polar body extrusion during oocyte meiosis. During early pregnancy, females present normal numbers of implantation sites, but only very few normal-looking embryos. Most of the embryos show developmental delays and gross morphological defects, leading to embronic death.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1571 – 15711K → A or E: Strongly reduced interaction with SPIRE1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15781578Formin-2PRO_0000194889Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891PhosphoserineCombined sources
Modified residuei459 – 4591PhosphoserineCombined sources
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei493 – 4931PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JL04.
MaxQBiQ9JL04.
PaxDbiQ9JL04.
PRIDEiQ9JL04.

PTM databases

iPTMnetiQ9JL04.
PhosphoSiteiQ9JL04.

Expressioni

Tissue specificityi

Detected in brain and in oocytes (at protein level). Expressed almost exclusively in the developing and mature central nervous system. Detected in oocytes.2 Publications

Developmental stagei

Expression begins at embryonic day 9.5 in the developing spinal cord and brain structures and continues in neonatal and adult brain structures including the olfactory bulb, cortex, thalamus, hypothalamus, hippocampus and cerebellum.

Gene expression databases

BgeeiQ9JL04.
CleanExiMM_FMN2.
ExpressionAtlasiQ9JL04. baseline and differential.
GenevisibleiQ9JL04. MM.

Interactioni

Subunit structurei

Interacts with CDKN1A (By similarity). Interacts with SPIRE1. Binds actin.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60685N.
STRINGi10090.ENSMUSP00000030039.

Structurei

3D structure databases

ProteinModelPortaliQ9JL04.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini735 – 1124390FH1Add
BLAST
Repeati919 – 929111Add
BLAST
Repeati930 – 940112Add
BLAST
Repeati941 – 951113Add
BLAST
Repeati952 – 962114Add
BLAST
Repeati963 – 973115Add
BLAST
Repeati974 – 984116Add
BLAST
Repeati985 – 995117Add
BLAST
Repeati996 – 1006118Add
BLAST
Repeati1007 – 1017119Add
BLAST
Repeati1018 – 10281110Add
BLAST
Repeati1029 – 10391111Add
BLAST
Repeati1040 – 10501112Add
BLAST
Domaini1139 – 1554416FH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni919 – 103912112 X 11 AA tandem repeats of [MV]-G-I-P-P-P-P-P-L-P-GAdd
BLAST
Regioni1571 – 15788Important for interaction with SPIRE1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili643 – 68341Sequence analysisAdd
BLAST
Coiled coili1419 – 145537Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 558Poly-Gly
Compositional biasi202 – 2076Poly-Gln
Compositional biasi797 – 8015Poly-Pro
Compositional biasi861 – 8644Poly-Pro
Compositional biasi908 – 91710Poly-Pro
Compositional biasi922 – 9287Poly-Pro
Compositional biasi933 – 9397Poly-Pro
Compositional biasi955 – 9617Poly-Pro
Compositional biasi966 – 9727Poly-Pro
Compositional biasi977 – 9837Poly-Pro
Compositional biasi988 – 9947Poly-Pro
Compositional biasi999 – 10057Poly-Pro
Compositional biasi1010 – 10167Poly-Pro
Compositional biasi1021 – 10277Poly-Pro
Compositional biasi1032 – 10387Poly-Pro
Compositional biasi1043 – 10497Poly-Pro
Compositional biasi1054 – 10574Poly-Pro
Compositional biasi1065 – 10717Poly-Pro
Compositional biasi1076 – 10838Poly-Pro
Compositional biasi1088 – 10914Poly-Pro

Sequence similaritiesi

Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410KDHS. Eukaryota.
ENOG410XQWC. LUCA.
GeneTreeiENSGT00810000125396.
HOGENOMiHOG000112618.
HOVERGENiHBG107923.
InParanoidiQ9JL04.
KOiK02184.
OMAiCTEHVRA.
OrthoDBiEOG78M01H.
PhylomeDBiQ9JL04.
TreeFamiTF326072.

Family and domain databases

InterProiIPR015425. FH2_Formin.
IPR001265. Formin_Cappuccino_subfam.
IPR009408. Formin_homology_1.
[Graphical view]
PfamiPF06346. Drf_FH1. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSiPR00828. FORMIN.
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
PROSITEiPS51444. FH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JL04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNQDGKLKR SAGDASHEGG GAEDAAGPRD AEITKKASGS KKALGKHGKG
60 70 80 90 100
GGGSGETSKK KSKSDSRASV FSNLRIRKNL TKGKGACDSR EDVLDSQALP
110 120 130 140 150
IGELDSAHSI VTKTPDLSLS AEETGLSDTE CADPFEVIHP GASRPAEAGV
160 170 180 190 200
GIQATAEDLE TAAGAQDGQR TSSGSDTDIY SFHSATEQED LLSDIQQAIR
210 220 230 240 250
LQQQQQQKLL LQDSEEPAAP PTAISPQPGA FLGLDQFLLG PRSEAEKDTV
260 270 280 290 300
QALPVRPDLP ETTKSLVPEH PPSSGSHLTS ETPGYATAPS AVTDSLSSPA
310 320 330 340 350
FTFPEAGPGE GAAGVPVAGT GDTDEECEED AFEDAPRGSP GEEWVPEVEE
360 370 380 390 400
ASQRLEKEPE EGMRESITSA VVSLPGSPAP SPRCFKPYPL ITPCYIKTTT
410 420 430 440 450
RQLSSPNHSP SQSPNQSPRI KKRPDPSVSR SSRTALASAA APAKKHRLEG
460 470 480 490 500
GLTGGLSRSA DWTEELGVRT PGAGGSVHLL GRGATADDSG GGSPVLAAKA
510 520 530 540 550
PGAPATADGF QNVFTGRTLL EKLFSQQENG PPEEAEKFCS RIIAMGLLLP
560 570 580 590 600
FSDCFREPCN QNAGSSSAPF DQDQLYTWAA VSQPTHSMDY SEGQFPRREP
610 620 630 640 650
SMWPSSKLPE EEPSPKDVDT EPKSSILESP KKCSNGVQQE VFDVKSEGQA
660 670 680 690 700
TVIQQLEQTI EDLRTKIAEL EKQYPALDLE GPRGLSGLEN GLTASADVSL
710 720 730 740 750
DALVLHGKVA QPPRTLEAKS IQTSPTEEGR ILTLPPPKAP PEGLLGSPAA
760 770 780 790 800
ASGESALLTS PSGPQTKFCS EISLIVSPRR ISVQLDAQQI QSASQLPPPP
810 820 830 840 850
PLLGSDSQGQ PSQPSLHTES ETSHEHSVSS SFGNNCNVPP APPLPCTESS
860 870 880 890 900
SFMPGLGMAI PPPPCLSDIT VPALPSPTAP ALQFSNLQGP EMLPAPPQPP
910 920 930 940 950
PLPGLGVPPP PPAPPLPGMG IPPPPPLPGM GIPPPPPLPG MGISPLPPLP
960 970 980 990 1000
GMGIPPPPPL PGVGIPPPPP LPGVGIPPPP PLPGVGIPPP PPLPGVGIPP
1010 1020 1030 1040 1050
PPPLPGVGIP PPPPLPGVGI PPPPPLPGVG IPPPPPLPGV GIPPPPPLPG
1060 1070 1080 1090 1100
SGIPPPPALP GVAIPPPPPL PGMGVPPPAP PPPGAGIPPP PLLPGSGPPH
1110 1120 1130 1140 1150
SSQVGSSTLP AAPQGCGFLF PPLPTGLFGL GMNQDRVARK QLIEPCRPMK
1160 1170 1180 1190 1200
PLYWTRIQLH SKRDSSPSLI WEKIEEPSID CHEFEELFSK TAVKERKKPI
1210 1220 1230 1240 1250
SDTISKTKAK QVVKLLSNKR SQAVGILMSS LHLDMKDIQH AVVNLDNSVV
1260 1270 1280 1290 1300
DLETLQALYE NRAQSDELEK IEKHSRSSKD KENAKSLDKP EQFLYELSLI
1310 1320 1330 1340 1350
PNFSERVFCI LFQSTFSESI CSIRRKLELL QKLCETLKNG PGVMQVLGLV
1360 1370 1380 1390 1400
LAFGNYMNAG NKTRGQADGF GLDILPKLKD VKSSDNSRSL LSYIVSYYLR
1410 1420 1430 1440 1450
NFDEDAGKEQ CVFPLAEPQE LFQASQMKFE DFQKDLRKLK KDLKACEAEA
1460 1470 1480 1490 1500
GKVYQVSSAE HMQPFKENME QFISQAKIDQ ESQEAALTET HKCFLETTAY
1510 1520 1530 1540 1550
YFMKPKLGEK EVSPNVFFSV WHEFSSDFKD AWKKENKLIL QERVKEAEEV
1560 1570
CRQKKGKSLY KVKPRHDSGI KAKISMKT
Length:1,578
Mass (Da):167,387
Last modified:January 15, 2008 - v2
Checksum:iDD0FDC8FC25C47DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331I → T in AAH94606 (PubMed:15489334).Curated
Sequence conflicti348 – 3481V → M in AAH94606 (PubMed:15489334).Curated
Sequence conflicti372 – 3721V → A in AAH94606 (PubMed:15489334).Curated
Sequence conflicti430 – 4323RSS → PSP in AAH94606 (PubMed:15489334).Curated
Sequence conflicti745 – 7451L → P in AAH94606 (PubMed:15489334).Curated
Sequence conflicti936 – 94611Missing in AAH94606 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti1040 – 10401V → M in AAH94606 (PubMed:15489334).Curated
Sequence conflicti1142 – 11421L → P in AAH94606 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218940 mRNA. Translation: AAF72883.1.
BC094606 mRNA. Translation: AAH94606.1.
CCDSiCCDS48459.1.
RefSeqiNP_062318.2. NM_019445.2.
UniGeneiMm.330620.

Genome annotation databases

EnsembliENSMUST00000030039; ENSMUSP00000030039; ENSMUSG00000028354.
GeneIDi54418.
KEGGimmu:54418.
UCSCiuc007dtd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218940 mRNA. Translation: AAF72883.1.
BC094606 mRNA. Translation: AAH94606.1.
CCDSiCCDS48459.1.
RefSeqiNP_062318.2. NM_019445.2.
UniGeneiMm.330620.

3D structure databases

ProteinModelPortaliQ9JL04.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60685N.
STRINGi10090.ENSMUSP00000030039.

PTM databases

iPTMnetiQ9JL04.
PhosphoSiteiQ9JL04.

Proteomic databases

EPDiQ9JL04.
MaxQBiQ9JL04.
PaxDbiQ9JL04.
PRIDEiQ9JL04.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030039; ENSMUSP00000030039; ENSMUSG00000028354.
GeneIDi54418.
KEGGimmu:54418.
UCSCiuc007dtd.2. mouse.

Organism-specific databases

CTDi56776.
MGIiMGI:1859252. Fmn2.

Phylogenomic databases

eggNOGiENOG410KDHS. Eukaryota.
ENOG410XQWC. LUCA.
GeneTreeiENSGT00810000125396.
HOGENOMiHOG000112618.
HOVERGENiHBG107923.
InParanoidiQ9JL04.
KOiK02184.
OMAiCTEHVRA.
OrthoDBiEOG78M01H.
PhylomeDBiQ9JL04.
TreeFamiTF326072.

Miscellaneous databases

ChiTaRSiFmn2. mouse.
PROiQ9JL04.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JL04.
CleanExiMM_FMN2.
ExpressionAtlasiQ9JL04. baseline and differential.
GenevisibleiQ9JL04. MM.

Family and domain databases

InterProiIPR015425. FH2_Formin.
IPR001265. Formin_Cappuccino_subfam.
IPR009408. Formin_homology_1.
[Graphical view]
PfamiPF06346. Drf_FH1. 1 hit.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSiPR00828. FORMIN.
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
PROSITEiPS51444. FH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Formin-2, a novel formin homology protein of the cappuccino subfamily, is highly expressed in the developing and adult central nervous system."
    Leader B., Leder P.
    Mech. Dev. 93:221-231(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes."
    Leader B., Lim H., Carabatsos M.J., Harrington A., Ecsedy J., Pellman D., Maas R., Leder P.
    Nat. Cell Biol. 4:921-928(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  4. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  5. "Spindle positioning in mouse oocytes relies on a dynamic meshwork of actin filaments."
    Azoury J., Lee K.W., Georget V., Rassinier P., Leader B., Verlhac M.H.
    Curr. Biol. 18:1514-1519(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "A new model for asymmetric spindle positioning in mouse oocytes."
    Schuh M., Ellenberg J.
    Curr. Biol. 18:1986-1992(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-459; SER-489 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Spleen.
  8. "Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division."
    Pfender S., Kuznetsov V., Pleiser S., Kerkhoff E., Schuh M.
    Curr. Biol. 21:955-960(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex."
    Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.
    J. Biol. Chem. 286:30732-30739(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPIRE1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-1571.
  10. "An actin-dependent mechanism for long-range vesicle transport."
    Schuh M.
    Nat. Cell Biol. 13:1431-1436(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFMN2_MOUSE
AccessioniPrimary (citable) accession number: Q9JL04
Secondary accession number(s): Q505D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 15, 2008
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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.