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Q05860

- FMN1_MOUSE

UniProt

Q05860 - FMN1_MOUSE

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Protein

Formin-1

Gene

Fmn1

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

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. 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
Complete GO annotation...

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. cell junction Source: UniProtKB-KW
  3. cytoplasm Source: MGI
  4. microtubule cytoskeleton Source: MGI
  5. nucleus Source: MGI
  6. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

MaxQBiQ05860.
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

BgeeiQ05860.
CleanExiMM_FMN1.
ExpressionAtlasiQ05860. baseline and differential.
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119258.
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

        10         20         30         40         50
MEGTHCTLQL HNPIAELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC
60 70 80 90 100
YQVREGPDIT SLSQQPNEHP GDIFFKQTPT KNILTELYKL TAEKERLLDS
110 120 130 140 150
LLRSDNILGV SMGSQEGKLQ ELSVILATGD EYFQSAGNWR RELPVSSLIR
160 170 180 190 200
RSTQENKKPR RSGRRRESPE ELRQKRTRRK GRGCQESAFQ MGKDQVCSSS
210 220 230 240 250
SLSFRARPNL RLLEERGNLV PRGTLTSSLR RRESCPANIL RTPDADLAFG
260 270 280 290 300
NSGRTSEDTD LEGPLSPDSS PTEVGDADVG GQLKSSHQQE PPQPNVSESH
310 320 330 340 350
GKHAGAERWS SRTRKSKSLE RTCSKKPVSK VVAKIQEPSA PVKRIVRAHH
360 370 380 390 400
DGKGRVAYGP ETQTEFIPKA DFLTLPGGET ETHSSGRLEE EQPGIKSLRS
410 420 430 440 450
SAPERASITK EPASTEAAVN KVLRKVIESE KLDEATEGKR LGFSLNTRAT
460 470 480 490 500
HTFPETRSQR KAGLPQSGHK FLLLDLPHTV GPDSPQPKCD EKKPTPQVPT
510 520 530 540 550
ALGMVFNNSS PQSSAHKRLS PVPSPLSPRC PSPQQHHRIL LLPPLPSEGE
560 570 580 590 600
VVFNEYPSRK NDVSSGFPSA DTLEPSSTTK VTETKGASPT SLRASQTWLV
610 620 630 640 650
SEEASEKGLG PEKITAPPQH QLPPGIASEG FPCDNFKEQT AKDLPNKDGG
660 670 680 690 700
VWVPGYRAGP PCPFLLHEEK EKTSRSELYL DLNPDQSPTE QDDRTPGRLQ
710 720 730 740 750
AVWPPPKTKD TEEKVGLKYT EAEYQAAILH LKREHKEEIE TLQAQFELKT
760 770 780 790 800
FHIRGEHALV TARLEEAIEN LKQQLGKRRE GCEEMRDVCI STDDDCSPKA
810 820 830 840 850
FRNVCIQTDR ETFLKPCDAE SKATRSSQIV PKKLTISLTQ LSPSKDSKDI
860 870 880 890 900
HAPFQTREGT SSSSQHKISP PAPPTPPPLP PPLIPPPPPL PPGLGPLPPA
910 920 930 940 950
PPIPPVCPVS PPPPPPPPPP TPVPPSDGPP PPPPPPPPLP NVLALPNSGG
960 970 980 990 1000
PPPPPPPPPP GLAPPPPPGL SFGLSSSSSQ YPRKPAIEPS CPMKPLYWTR
1010 1020 1030 1040 1050
IQINDKSQDA APTLWDSLEE PHIRDTSEFE YLFSKDTTQQ KKKPLSEAYE
1060 1070 1080 1090 1100
KKNKVKKIIK LLDGKRSQTV GILISSLHLE MKDIQQAIFT VDDSVVDLET
1110 1120 1130 1140 1150
LAALYENRAQ EDELTKIRKY YETSKEEDLK LLDKPEQFLH ELAQIPNFAE
1160 1170 1180 1190 1200
RAQCIIFRAV FSEGITSLHR KVEIVTRASK GLLHMKSVKD ILALILAFGN
1210 1220 1230 1240 1250
YMNGGNRTRG QADGYSLEIL PKLKDVKSRD NGMNLVDYVV KYYLRYYDQC
1260 1270 1280 1290 1300
KHHDQEASCR GKDLFSLYFH IAVHPQRKSG LELKQEAGTD KSVFPLPEPQ
1310 1320 1330 1340 1350
DFFLASQVKF EDLLKDLRKL KRQLEASEQQ MKLVCKESPR EYLQPFKDKL
1360 1370 1380 1390 1400
EEFFKKAKKE HKMEESHLEN AQKSFETTVG YFGMKPKTGE KEVTPSYVFM
1410 1420 1430 1440 1450
VWFEFCSDFK TIWKRESKNI SKERLKMAQA SVSKLTSEKK VETKKINPTA
1460
SLKERLRQKE ASVATN
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:
EMBLi
GenBanki
DDBJi
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; ENSMUSG00000100934. [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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

MaxQBi Q05860.
PaxDbi Q05860.
PRIDEi Q05860.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081349 ; ENSMUSP00000080093 ; ENSMUSG00000100934 . [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 ENSGT00760000119258.
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

Bgeei Q05860.
CleanExi MM_FMN1.
ExpressionAtlasi Q05860. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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