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Q05860

- FMN1_MOUSE

UniProt

Q05860 - FMN1_MOUSE

Protein

Formin-1

Gene

Fmn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Plays a role in the formation of adherens junction and the polymerization of linear actin cables.2 Publications

    GO - Molecular functioni

    1. microtubule binding Source: MGI
    2. protein binding Source: MGI
    3. SH3 domain binding Source: MGI

    GO - Biological processi

    1. actin nucleation Source: InterPro
    2. dendrite morphogenesis Source: MGI
    3. forelimb morphogenesis Source: MGI
    4. gene expression Source: MGI
    5. hindlimb morphogenesis Source: MGI
    6. kidney development Source: MGI
    7. limb development Source: MGI
    8. positive regulation of actin filament polymerization Source: MGI
    9. positive regulation of actin nucleation Source: MGI
    10. positive regulation of focal adhesion assembly Source: MGI
    11. skeletal system morphogenesis Source: MGI
    12. ureteric bud invasion Source: MGI

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formin-1
    Alternative name(s):
    Limb deformity protein
    Gene namesi
    Name:Fmn1
    Synonyms:Fmn, Ld
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:101815. Fmn1.

    Subcellular locationi

    Nucleus. Cytoplasm. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Localization to the adherens junctions is alpha-catenin-dependent. Also localizes to F-actin bundles originating from adherens junctions.
    Isoform 2 : Cytoplasmcytoskeleton
    Note: Isoform 2 localizes to microtubules.

    GO - Cellular componenti

    1. actin filament Source: InterPro
    2. adherens junction Source: UniProtKB-SubCell
    3. cytoplasm Source: MGI
    4. microtubule cytoskeleton Source: MGI
    5. nucleus Source: MGI
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14661466Formin-1PRO_0000194886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on serine and possibly threonine residues.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ05860.
    PRIDEiQ05860.

    PTM databases

    PhosphoSiteiQ05860.

    Expressioni

    Tissue specificityi

    It is present in the adult kidney, testis, limb, ovary, brain, small intestine, salivary gland and harderian gland. Isoforms 1, 2 and 5 are detected in skin and keratinocytes. Isoform 5 is found throughout the embryo.2 Publications

    Developmental stagei

    It is present throughout the embryo. In the developing limb bud, the protein is expressed in the apical ectodermal ridge and the mesenchymal compartment, predominantly in the posterior region. During kidney morphogenesis, expression is initially restricted to the epithelial compartment of the pronephros and mesonephros. Isoform 5 is found in the apical ectodermal ridge and the mesenchymal compartment of the developing limb bud.

    Gene expression databases

    ArrayExpressiQ05860.
    BgeeiQ05860.
    CleanExiMM_FMN1.
    GenevestigatoriQ05860.

    Interactioni

    Subunit structurei

    Interacts with alpha-catenin and may interact with tubulin.2 Publications

    Protein-protein interaction databases

    BioGridi199711. 6 interactions.
    DIPiDIP-646N.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JUPNMR-P881-888[»]
    2RLYNMR-P874-881[»]
    2RM0NMR-P880-888[»]
    ProteinModelPortaliQ05860.
    SMRiQ05860. Positions 970-1424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05860.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini870 – 970101FH1Add
    BLAST
    Domaini983 – 1435453FH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 624624Microtubule-bindingAdd
    BLAST
    Regioni458 – 842385Mediates interaction with alpha-cateninAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili722 – 78665Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi870 – 995126Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG264408.
    GeneTreeiENSGT00750000117268.
    HOGENOMiHOG000168579.
    HOVERGENiHBG107922.
    InParanoidiQ05860.
    KOiK10367.
    OMAiDSKSPDH.
    OrthoDBiEOG78M01H.
    PhylomeDBiQ05860.
    TreeFamiTF351317.

    Family and domain databases

    InterProiIPR015425. FH2_Formin.
    IPR001265. Formin_Cappuccino_subfam.
    [Graphical view]
    PfamiPF02181. FH2. 1 hit.
    [Graphical view]
    PRINTSiPR00828. FORMIN.
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    PROSITEiPS51444. FH2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q05860-1) [UniParc]FASTAAdd to Basket

    Also known as: IA

    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

    MEGTHCTLQL HNPIAELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC     50
    YQVREGPDIT SLSQQPNEHP GDIFFKQTPT KNILTELYKL TAEKERLLDS 100
    LLRSDNILGV SMGSQEGKLQ ELSVILATGD EYFQSAGNWR RELPVSSLIR 150
    RSTQENKKPR RSGRRRESPE ELRQKRTRRK GRGCQESAFQ MGKDQVCSSS 200
    SLSFRARPNL RLLEERGNLV PRGTLTSSLR RRESCPANIL RTPDADLAFG 250
    NSGRTSEDTD LEGPLSPDSS PTEVGDADVG GQLKSSHQQE PPQPNVSESH 300
    GKHAGAERWS SRTRKSKSLE RTCSKKPVSK VVAKIQEPSA PVKRIVRAHH 350
    DGKGRVAYGP ETQTEFIPKA DFLTLPGGET ETHSSGRLEE EQPGIKSLRS 400
    SAPERASITK EPASTEAAVN KVLRKVIESE KLDEATEGKR LGFSLNTRAT 450
    HTFPETRSQR KAGLPQSGHK FLLLDLPHTV GPDSPQPKCD EKKPTPQVPT 500
    ALGMVFNNSS PQSSAHKRLS PVPSPLSPRC PSPQQHHRIL LLPPLPSEGE 550
    VVFNEYPSRK NDVSSGFPSA DTLEPSSTTK VTETKGASPT SLRASQTWLV 600
    SEEASEKGLG PEKITAPPQH QLPPGIASEG FPCDNFKEQT AKDLPNKDGG 650
    VWVPGYRAGP PCPFLLHEEK EKTSRSELYL DLNPDQSPTE QDDRTPGRLQ 700
    AVWPPPKTKD TEEKVGLKYT EAEYQAAILH LKREHKEEIE TLQAQFELKT 750
    FHIRGEHALV TARLEEAIEN LKQQLGKRRE GCEEMRDVCI STDDDCSPKA 800
    FRNVCIQTDR ETFLKPCDAE SKATRSSQIV PKKLTISLTQ LSPSKDSKDI 850
    HAPFQTREGT SSSSQHKISP PAPPTPPPLP PPLIPPPPPL PPGLGPLPPA 900
    PPIPPVCPVS PPPPPPPPPP TPVPPSDGPP PPPPPPPPLP NVLALPNSGG 950
    PPPPPPPPPP GLAPPPPPGL SFGLSSSSSQ YPRKPAIEPS CPMKPLYWTR 1000
    IQINDKSQDA APTLWDSLEE PHIRDTSEFE YLFSKDTTQQ KKKPLSEAYE 1050
    KKNKVKKIIK LLDGKRSQTV GILISSLHLE MKDIQQAIFT VDDSVVDLET 1100
    LAALYENRAQ EDELTKIRKY YETSKEEDLK LLDKPEQFLH ELAQIPNFAE 1150
    RAQCIIFRAV FSEGITSLHR KVEIVTRASK GLLHMKSVKD ILALILAFGN 1200
    YMNGGNRTRG QADGYSLEIL PKLKDVKSRD NGMNLVDYVV KYYLRYYDQC 1250
    KHHDQEASCR GKDLFSLYFH IAVHPQRKSG LELKQEAGTD KSVFPLPEPQ 1300
    DFFLASQVKF EDLLKDLRKL KRQLEASEQQ MKLVCKESPR EYLQPFKDKL 1350
    EEFFKKAKKE HKMEESHLEN AQKSFETTVG YFGMKPKTGE KEVTPSYVFM 1400
    VWFEFCSDFK TIWKRESKNI SKERLKMAQA SVSKLTSEKK VETKKINPTA 1450
    SLKERLRQKE ASVATN 1466
    Length:1,466
    Mass (Da):163,581
    Last modified:July 24, 2007 - v2
    Checksum:i5482F8AAB66CBF32
    GO
    Isoform 2 (identifier: Q05860-2) [UniParc]FASTAAdd to Basket

    Also known as: IB

    The sequence of this isoform differs from the canonical sequence as follows:
         1250-1285: Missing.

    Show »
    Length:1,430
    Mass (Da):159,391
    Checksum:i6A90287624580946
    GO
    Isoform 3 (identifier: Q05860-3) [UniParc]FASTAAdd to Basket

    Also known as: II

    The sequence of this isoform differs from the canonical sequence as follows:
         625-722: Missing.

    Show »
    Length:1,368
    Mass (Da):152,641
    Checksum:iF34DEB5CF39489AA
    GO
    Isoform 4 (identifier: Q05860-4) [UniParc]FASTAAdd to Basket

    Also known as: III

    The sequence of this isoform differs from the canonical sequence as follows:
         626-627: IA → SV
         628-1466: Missing.

    Show »
    Length:627
    Mass (Da):68,996
    Checksum:iF25AF953C733E24F
    GO
    Isoform 5 (identifier: Q05860-5) [UniParc]FASTAAdd to Basket

    Also known as: IV

    The sequence of this isoform differs from the canonical sequence as follows:
         1-682: Missing.
         683-683: N → MEEVGNSLSS...PADSPSDPKS
         1250-1285: Missing.

    Show »
    Length:1,204
    Mass (Da):133,207
    Checksum:i8724170303A83D33
    GO
    Isoform 6 (identifier: Q05860-6) [UniParc]FASTAAdd to Basket

    Also known as: V

    The sequence of this isoform differs from the canonical sequence as follows:
         1-623: Missing.
         624-624: P → MVTTGSPPFNTMGACYRYNPRYGQPISVPKVWKCRHRRSVTPDE
         1250-1285: Missing.

    Show »
    Length:850
    Mass (Da):95,723
    Checksum:i173EC42FD49F66D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti220 – 2201V → A in CAA37668. (PubMed:2392150)Curated
    Sequence conflicti776 – 7761G → E in CAA37668. (PubMed:2392150)Curated
    Sequence conflicti776 – 7761G → E in CAA44244. (PubMed:1339380)Curated
    Sequence conflicti866 – 8661H → Q in CAA37668. (PubMed:2392150)Curated
    Sequence conflicti866 – 8661H → Q in CAA44244. (PubMed:1339380)Curated
    Sequence conflicti950 – 9501G → GPP in CAA37668. (PubMed:2392150)Curated
    Sequence conflicti950 – 9501G → GPP in CAA44244. (PubMed:1339380)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 682682Missing in isoform 5. 1 PublicationVSP_027214Add
    BLAST
    Alternative sequencei1 – 623623Missing in isoform 6. CuratedVSP_029424Add
    BLAST
    Alternative sequencei624 – 6241P → MVTTGSPPFNTMGACYRYNP RYGQPISVPKVWKCRHRRSV TPDE in isoform 6. CuratedVSP_029425
    Alternative sequencei625 – 72298Missing in isoform 3. CuratedVSP_001570Add
    BLAST
    Alternative sequencei626 – 6272IA → SV in isoform 4. CuratedVSP_001571
    Alternative sequencei628 – 1466839Missing in isoform 4. CuratedVSP_001572Add
    BLAST
    Alternative sequencei683 – 6831N → MEEVGNSLSSRDVLEPDKSE AGLEMAQSILSKFSMKSLFG FTNKLDSLEPEEEDAVLKAF RSLEGDPAPERGDPSKGSDQ PQAEAPVPPDLKNDGKSARA ETGSEGSQGKGRSNTSSPGY ELSPATVSVDNEEVIWVRGT LVHTTSDSDSEDGDQEAEEE SSLDTQKPTTVVLCEPSQEP KDRAGDSEENTDTGNTDDTE LCAEESQRTLPETSSKLELG GDGSHPAEHSPRQDQAAEEG SQIPPAATDQTVGALASTVS KREAPEEKPFQLPAFFSGLR VLKKGATAEAGETITEIKPK DGDLALLKLTQRVQKSLGQG GPQTVKSPGRATDPKATPTL LEQLSQLLNIDMPRTEQKEA DPEFHGADEMGYSTDQESHK SPRDAHVQGGQVKARTPETA LEAFKALFIRPPKKGSTADT SELEALKRKMKHEKESLRAV FERSKSRPADSPSDPKS in isoform 5. 1 PublicationVSP_027215
    Alternative sequencei1250 – 128536Missing in isoform 2, isoform 5 and isoform 6. 1 PublicationVSP_027216Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53599 mRNA. Translation: CAA37668.1.
    X62379 mRNA. Translation: CAA44244.1.
    AL672253, AL691437 Genomic DNA. Translation: CAM14988.1.
    AL672253, AL691437, AL691466 Genomic DNA. Translation: CAM14989.1.
    AL691466, AL672253, AL691437 Genomic DNA. Translation: CAM18143.1.
    AL691437, AL672253 Genomic DNA. Translation: CAM18583.1.
    AL691437, AL672253, AL691466 Genomic DNA. Translation: CAM18585.1.
    CCDSiCCDS16559.1. [Q05860-1]
    CCDS71113.1. [Q05860-5]
    PIRiS11515.
    S24407.
    RefSeqiNP_001272388.1. NM_001285459.1. [Q05860-5]
    NP_034360.2. NM_010230.2. [Q05860-1]
    UniGeneiMm.4938.

    Genome annotation databases

    EnsembliENSMUST00000081349; ENSMUSP00000080093; ENSMUSG00000044042. [Q05860-5]
    ENSMUST00000099576; ENSMUSP00000097171; ENSMUSG00000044042. [Q05860-2]
    ENSMUST00000102547; ENSMUSP00000099606; ENSMUSG00000044042. [Q05860-1]
    GeneIDi14260.
    KEGGimmu:14260.
    UCSCiuc008lpl.1. mouse. [Q05860-1]
    uc008lpm.1. mouse. [Q05860-2]
    uc008lpn.1. mouse. [Q05860-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53599 mRNA. Translation: CAA37668.1 .
    X62379 mRNA. Translation: CAA44244.1 .
    AL672253 , AL691437 Genomic DNA. Translation: CAM14988.1 .
    AL672253 , AL691437 , AL691466 Genomic DNA. Translation: CAM14989.1 .
    AL691466 , AL672253 , AL691437 Genomic DNA. Translation: CAM18143.1 .
    AL691437 , AL672253 Genomic DNA. Translation: CAM18583.1 .
    AL691437 , AL672253 , AL691466 Genomic DNA. Translation: CAM18585.1 .
    CCDSi CCDS16559.1. [Q05860-1 ]
    CCDS71113.1. [Q05860-5 ]
    PIRi S11515.
    S24407.
    RefSeqi NP_001272388.1. NM_001285459.1. [Q05860-5 ]
    NP_034360.2. NM_010230.2. [Q05860-1 ]
    UniGenei Mm.4938.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JUP NMR - P 881-888 [» ]
    2RLY NMR - P 874-881 [» ]
    2RM0 NMR - P 880-888 [» ]
    ProteinModelPortali Q05860.
    SMRi Q05860. Positions 970-1424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199711. 6 interactions.
    DIPi DIP-646N.

    PTM databases

    PhosphoSitei Q05860.

    Proteomic databases

    PaxDbi Q05860.
    PRIDEi Q05860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081349 ; ENSMUSP00000080093 ; ENSMUSG00000044042 . [Q05860-5 ]
    ENSMUST00000099576 ; ENSMUSP00000097171 ; ENSMUSG00000044042 . [Q05860-2 ]
    ENSMUST00000102547 ; ENSMUSP00000099606 ; ENSMUSG00000044042 . [Q05860-1 ]
    GeneIDi 14260.
    KEGGi mmu:14260.
    UCSCi uc008lpl.1. mouse. [Q05860-1 ]
    uc008lpm.1. mouse. [Q05860-2 ]
    uc008lpn.1. mouse. [Q05860-5 ]

    Organism-specific databases

    CTDi 342184.
    MGIi MGI:101815. Fmn1.

    Phylogenomic databases

    eggNOGi NOG264408.
    GeneTreei ENSGT00750000117268.
    HOGENOMi HOG000168579.
    HOVERGENi HBG107922.
    InParanoidi Q05860.
    KOi K10367.
    OMAi DSKSPDH.
    OrthoDBi EOG78M01H.
    PhylomeDBi Q05860.
    TreeFami TF351317.

    Miscellaneous databases

    EvolutionaryTracei Q05860.
    NextBioi 285597.
    PROi Q05860.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05860.
    Bgeei Q05860.
    CleanExi MM_FMN1.
    Genevestigatori Q05860.

    Family and domain databases

    InterProi IPR015425. FH2_Formin.
    IPR001265. Formin_Cappuccino_subfam.
    [Graphical view ]
    Pfami PF02181. FH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00828. FORMIN.
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    PROSITEi PS51444. FH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "'Formins': proteins deduced from the alternative transcripts of the limb deformity gene."
      Woychik R.P., Maas R.L., Zeller R., Vogt T.F., Leder P.
      Nature 346:850-853(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Kidney and Testis.
    2. "A variant limb deformity transcript expressed in the embryonic mouse limb defines a novel formin."
      Grusby-Jackson L., Kuo A., Leder P.
      Genes Dev. 6:29-37(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING.
      Tissue: Embryo.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "Formins: phosphoprotein isoforms encoded by the mouse limb deformity locus."
      Vogt T.F., Jackson-Grusby L., Rush J., Leder P.
      Proc. Natl. Acad. Sci. U.S.A. 90:5554-5558(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
    5. "The mouse formin (Fmn) gene: genomic structure, novel exons, and genetic mapping."
      Wang C.C., Chan D.C., Leder P.
      Genomics 39:303-311(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
    6. "Mouse limb deformity mutations disrupt a global control region within the large regulatory landscape required for Gremlin expression."
      Zuniga A., Michos O., Spitz F., Haramis A.-P.G., Panman L., Galli A., Vintersten K., Klasen C., Mansfield W., Kuc S., Duboule D., Dono R., Zeller R.
      Genes Dev. 18:1553-1564(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables."
      Kobielak A., Pasolli H.A., Fuchs E.
      Nat. Cell Biol. 6:21-30(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALPHA-CATENIN, TISSUE SPECIFICITY.
    8. "Formin-1 protein associates with microtubules through a peptide domain encoded by exon-2."
      Zhou F., Leder P., Martin S.S.
      Exp. Cell Res. 312:1119-1126(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TUBULIN.

    Entry informationi

    Entry nameiFMN1_MOUSE
    AccessioniPrimary (citable) accession number: Q05860
    Secondary accession number(s): A2AFY9, A2AFZ0, Q05859
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Was originally thought to play a role in limb bud development based on the fact that limb deformity (ld) mutants are associated with Fmn1 gene disruption. However, PubMed:15198975 shows that limb deformity mutations rather affects Grem1 cis-regulatory regions localized in Fmn1 gene and that loss of Grem1 (gremlin-1) expression is the cause of limb malformations.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3