Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NZ56

- FMN2_HUMAN

UniProt

Q9NZ56 - FMN2_HUMAN

Protein

Formin-2

Gene

FMN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 4 (15 Jan 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis 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. 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 similarity2 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. cellular response to hypoxia Source: UniProtKB
    3. establishment of meiotic spindle localization Source: BHF-UCL
    4. formin-nucleated actin cable assembly Source: UniProtKB
    5. homologous chromosome movement towards spindle pole involved in homologous chromosome segregation Source: BHF-UCL
    6. intracellular signal transduction Source: InterPro
    7. intracellular transport Source: UniProtKB
    8. multicellular organismal development Source: UniProtKB-KW
    9. negative regulation of apoptotic process Source: UniProtKB
    10. negative regulation of protein catabolic process Source: UniProtKB
    11. oogenesis Source: BHF-UCL
    12. polar body extrusion after meiotic divisions Source: BHF-UCL
    13. protein transport Source: UniProtKB-KW
    14. vesicle-mediated transport Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    DNA damage, Protein transport, Stress response, Transport

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    SignaLinkiQ9NZ56.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formin-2
    Gene namesi
    Name:FMN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:14074. FMN2.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cytoplasmcytosol. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcell cortex By similarity. Nucleusnucleolus
    Note: Recruited to the membranes via its interaction with SPIRE1. Colocalizes with the actin cytoskeleton. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion By similarity.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cytoplasmic vesicle membrane Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1715 – 17151K → A or E: Abolishes interaction with SPIRE1. 1 Publication
    Mutagenesisi1717 – 17171K → A: Strongly reduces interaction with SPIRE1. 1 Publication
    Mutagenesisi1721 – 17211K → A or E: Strongly reduces interaction with SPIRE1. 1 Publication

    Organism-specific databases

    PharmGKBiPA28185.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17221722Formin-2PRO_0000194888Add
    BLAST

    Proteomic databases

    MaxQBiQ9NZ56.
    PaxDbiQ9NZ56.
    PRIDEiQ9NZ56.

    PTM databases

    PhosphoSiteiQ9NZ56.

    Expressioni

    Tissue specificityi

    Expressed almost exclusively in the developing and mature central nervous system.1 Publication

    Inductioni

    Up-regulated in response to cellular stress, hypoxia and DNA damage via NF-kappa-B.1 Publication

    Gene expression databases

    ArrayExpressiQ9NZ56.
    BgeeiQ9NZ56.
    CleanExiHS_FMN2.
    GenevestigatoriQ9NZ56.

    Organism-specific databases

    HPAiHPA004937.

    Interactioni

    Subunit structurei

    Interacts with SPIRE1. Binds actin. Interacts with CDKN1A.4 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000318884.

    Structurei

    Secondary structure

    1
    1722
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1706 – 17083
    Helixi1714 – 17196

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YLEX-ray1.80B1694-1722[»]
    3R7GX-ray2.20B1701-1722[»]
    ProteinModelPortaliQ9NZ56.
    SMRiQ9NZ56. Positions 1308-1699.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini758 – 1268511FH1Add
    BLAST
    Domaini1283 – 1698416FH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1715 – 17228Important for interaction with SPIRE1

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili193 – 23139Sequence AnalysisAdd
    BLAST
    Coiled coili670 – 70637Sequence AnalysisAdd
    BLAST
    Coiled coili1567 – 159731Sequence AnalysisAdd
    BLAST
    Coiled coili1677 – 169923Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi200 – 22728Gln-richAdd
    BLAST
    Compositional biasi758 – 1268511Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG264408.
    HOGENOMiHOG000112618.
    HOVERGENiHBG107923.
    InParanoidiQ9NZ56.
    KOiK02184.
    OMAiEHRPKDA.
    OrthoDBiEOG78M01H.
    PhylomeDBiQ9NZ56.
    TreeFamiTF326072.

    Family and domain databases

    InterProiIPR000591. DEP_dom.
    IPR015425. FH2_Formin.
    IPR009408. Formin_homology_1.
    [Graphical view]
    PfamiPF06346. Drf_FH1. 4 hits.
    PF02181. FH2. 1 hit.
    [Graphical view]
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    PROSITEiPS51444. FH2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZ56-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNQDGKLKR SAGDALHEGG GGAEDALGPR DVEATKKGSG GKKALGKHGK     50
    GGGGGGGGGE SGKKKSKSDS RASVFSNLRI RKNLSKGKGA GGSREDVLDS 100
    QALQTGELDS AHSLLTKTPD LSLSADEAGL SDTECADPFE VTGPGGPGPA 150
    EARVGGRPIA EDVETAAGAQ DGQRTSSGSD TDIYSFHSAT EQEDLLSDIQ 200
    QAIRLQQQQQ QQLQLQLQQQ QQQQQLQGAE EPAAPPTAVS PQPGAFLGLD 250
    RFLLGPSGGA GEAPGSPDTE QALSALSDLP ESLAAEPREP QQPPSPGGLP 300
    VSEAPSLPAA QPAAKDSPSS TAFPFPEAGP GEEAAGAPVR GAGDTDEEGE 350
    EDAFEDAPRG SPGEEWAPEV GEDAPQRLGE EPEEEAQGPD APAAASLPGS 400
    PAPSQRCFKP YPLITPCYIK TTTRQLSSPN HSPSQSPNQS PRIKRRPEPS 450
    LSRGSRTALA SVAAPAKKHR ADGGLAAGLS RSADWTEELG ARTPRVGGSA 500
    HLLERGVASD SGGGVSPALA AKASGAPAAA DGFQNVFTGR TLLEKLFSQQ 550
    ENGPPEEAEK FCSRIIAMGL LLPFSDCFRE PCNQNAQTNA ASFDQDQLYT 600
    WAAVSQPTHS LDYSEGQFPR RVPSMGPPSK PPDEEHRLED AETESQSAVS 650
    ETPQKRSDAV QKEVVDMKSE GQATVIQQLE QTIEDLRTKI AELERQYPAL 700
    DTEVASGHQG LENGVTASGD VCLEALRLEE KEVRHHRILE AKSIQTSPTE 750
    EGGVLTLPPV DGLPGRPPCP PGAESGPQTK FCSEISLIVS PRRISVQLDS 800
    HQPTQSISQP PPPPSLLWSA GQGQPGSQPP HSISTEFQTS HEHSVSSAFK 850
    NSCNIPSPPP LPCTESSSSM PGLGMVPPPP PPLPGMTVPT LPSTAIPQPP 900
    PLQGTEMLPP PPPPLPGAGI PPPPPLPGAG ILPLPPLPGA GIPPPPPLPG 950
    AAIPPPPPLP GAGIPLPPPL PGAGIPPPPP LPGAGIPPPP PLPGAGIPPP 1000
    PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPGAG IPPPPPLPGA 1050
    GIPPPPPLPG AGIPPPPPLP GAGIPPPPPL PGAGIPPPPP LPGAGIPPPP 1100
    PLPGVGIPPP PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPRVG 1150
    IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GVGIPPPPPL PGVGIPPPPP 1200
    LPGAGIPPPP PLPGMGIPPA PAPPLPPPGT GIPPPPLLPV SGPPLLPQVG 1250
    SSTLPTPQVC GFLPPPLPSG LFGLGMNQDK GSRKQPIEPC RPMKPLYWTR 1300
    IQLHSKRDSS TSLIWEKIEE PSIDCHEFEE LFSKTAVKER KKPISDTISK 1350
    TKAKQVVKLL SNKRSQAVGI LMSSLHLDMK DIQHAVVNLD NSVVDLETLQ 1400
    ALYENRAQSD ELEKIEKHGR SSKDKENAKS LDKPEQFLYE LSLIPNFSER 1450
    VFCILFQSTF SESICSIRRK LELLQKLCET LKNGPGVMQV LGLVLAFGNY 1500
    MNGGNKTRGQ ADGFGLDILP KLKDVKSSDN SRSLLSYIVS YYLRNFDEDA 1550
    GKEQCLFPLP EPQDLFQASQ MKFEDFQKDL RKLKKDLKAC EVEAGKVYQV 1600
    SSKEHMQPFK ENMEQFIIQA KIDQEAEENS LTETHKCFLE TTAYFFMKPK 1650
    LGEKEVSPNA FFSIWHEFSS DFKDFWKKEN KLLLQERVKE AEEVCRQKKG 1700
    KSLYKIKPRH DSGIKAKISM KT 1722
    Length:1,722
    Mass (Da):180,106
    Last modified:January 15, 2008 - v4
    Checksum:i26525AC7868A949C
    GO
    Isoform 2 (identifier: Q9NZ56-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-1405: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:318
    Mass (Da):36,871
    Checksum:i3FA270C7B4D1E07A
    GO

    Sequence cautioni

    The sequence AAF72884.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti644 – 6441E → EDDGE in BAD92390. 1 PublicationCurated
    Sequence conflicti768 – 7681P → T in BAD92390. 1 PublicationCurated
    Sequence conflicti1426 – 14272EN → TR in AAF72885. (PubMed:10781961)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1148 – 11481R → G.1 Publication
    Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
    VAR_059290
    Natural varianti1291 – 12911R → G.
    Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
    VAR_049094
    Natural varianti1468 – 14681R → H.1 Publication
    Corresponds to variant rs3795677 [ dbSNP | Ensembl ].
    VAR_033932

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 14051404Missing in isoform 2. 1 PublicationVSP_056095Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298141 mRNA. Translation: BAG60417.1.
    AL359918
    , AL513342, AL590490, AL646016 Genomic DNA. Translation: CAQ10135.1.
    AL513342
    , AL359918, AL590490, AL646016 Genomic DNA. Translation: CAQ10526.1.
    AL590490
    , AL359918, AL513342, AL646016 Genomic DNA. Translation: CAQ10976.1.
    AL646016
    , AL359918, AL513342, AL590490 Genomic DNA. Translation: CAQ08405.1.
    AB209153 mRNA. Translation: BAD92390.1.
    AF218941 mRNA. Translation: AAF72884.1. Sequence problems.
    AF218942 mRNA. Translation: AAF72885.1.
    CCDSiCCDS31069.2.
    RefSeqiNP_064450.3. NM_020066.4.
    UniGeneiHs.24889.

    Genome annotation databases

    EnsembliENST00000319653; ENSP00000318884; ENSG00000155816.
    ENST00000545751; ENSP00000437918; ENSG00000155816.
    GeneIDi56776.
    KEGGihsa:56776.
    UCSCiuc010pyd.2. human.

    Polymorphism databases

    DMDMi166215083.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298141 mRNA. Translation: BAG60417.1 .
    AL359918
    , AL513342 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10135.1 .
    AL513342
    , AL359918 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10526.1 .
    AL590490
    , AL359918 , AL513342 , AL646016 Genomic DNA. Translation: CAQ10976.1 .
    AL646016
    , AL359918 , AL513342 , AL590490 Genomic DNA. Translation: CAQ08405.1 .
    AB209153 mRNA. Translation: BAD92390.1 .
    AF218941 mRNA. Translation: AAF72884.1 . Sequence problems.
    AF218942 mRNA. Translation: AAF72885.1 .
    CCDSi CCDS31069.2.
    RefSeqi NP_064450.3. NM_020066.4.
    UniGenei Hs.24889.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YLE X-ray 1.80 B 1694-1722 [» ]
    3R7G X-ray 2.20 B 1701-1722 [» ]
    ProteinModelPortali Q9NZ56.
    SMRi Q9NZ56. Positions 1308-1699.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000318884.

    PTM databases

    PhosphoSitei Q9NZ56.

    Polymorphism databases

    DMDMi 166215083.

    Proteomic databases

    MaxQBi Q9NZ56.
    PaxDbi Q9NZ56.
    PRIDEi Q9NZ56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319653 ; ENSP00000318884 ; ENSG00000155816 .
    ENST00000545751 ; ENSP00000437918 ; ENSG00000155816 .
    GeneIDi 56776.
    KEGGi hsa:56776.
    UCSCi uc010pyd.2. human.

    Organism-specific databases

    CTDi 56776.
    GeneCardsi GC01P240177.
    H-InvDB HIX0021237.
    HGNCi HGNC:14074. FMN2.
    HPAi HPA004937.
    MIMi 606373. gene.
    neXtProti NX_Q9NZ56.
    PharmGKBi PA28185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264408.
    HOGENOMi HOG000112618.
    HOVERGENi HBG107923.
    InParanoidi Q9NZ56.
    KOi K02184.
    OMAi EHRPKDA.
    OrthoDBi EOG78M01H.
    PhylomeDBi Q9NZ56.
    TreeFami TF326072.

    Enzyme and pathway databases

    SignaLinki Q9NZ56.

    Miscellaneous databases

    GenomeRNAii 56776.
    NextBioi 62219.
    PROi Q9NZ56.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZ56.
    Bgeei Q9NZ56.
    CleanExi HS_FMN2.
    Genevestigatori Q9NZ56.

    Family and domain databases

    InterProi IPR000591. DEP_dom.
    IPR015425. FH2_Formin.
    IPR009408. Formin_homology_1.
    [Graphical view ]
    Pfami PF06346. Drf_FH1. 4 hits.
    PF02181. FH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    PROSITEi PS51444. FH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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 395-1722 (ISOFORM 1), VARIANTS GLY-1148 AND HIS-1468.
      Tissue: Brain.
    4. "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] OF 396-727 AND 1426-1722 (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    5. "Effects of genistein on beta-catenin signaling and subcellular distribution of actin-binding proteins in human umbilical CD105-positive stromal cells."
      Shieh D.B., Li R.Y., Liao J.M., Chen G.D., Liou Y.M.
      J. Cell. Physiol. 223:423-434(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.
    6. "Differential role of actin-binding proteins in controlling the adipogenic differentiation of human CD105-positive Wharton's Jelly cells."
      Peng K.W., Liou Y.M.
      Biochim. Biophys. Acta 1820:469-481(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21."
      Yamada K., Ono M., Perkins N.D., Rocha S., Lamond A.I.
      Mol. Cell 49:922-933(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDKN1A, SUBCELLULAR LOCATION, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "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: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1694-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1.
    9. "Structure and function of the interacting domains of Spire and Fmn-family formins."
      Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1701-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1, MUTAGENESIS OF LYS-1715; LYS-1717 AND LYS-1721.

    Entry informationi

    Entry nameiFMN2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZ56
    Secondary accession number(s): B0QZA7
    , B4DP05, Q59GF6, Q5VU37, Q9NZ55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 115 of the entry and version 4 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, Reference proteome

    Documents

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

    External Data

    Dasty 3