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P59113

- FERM1_MOUSE

UniProt

P59113 - FERM1_MOUSE

Protein

Fermitin family homolog 1

Gene

Fermt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites By similarity.By similarity

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. establishment of epithelial cell polarity Source: UniProtKB
    3. keratinocyte migration Source: UniProtKB
    4. keratinocyte proliferation Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fermitin family homolog 1
    Alternative name(s):
    Kindlin-1
    Unc-112-related protein 1
    Gene namesi
    Name:Fermt1
    Synonyms:Kind1, Urp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2443583. Fermt1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Colocalizes with filamentous actin. Constituent of focal adhesions By similarity. Localized at the basal aspect of skin keratinocytes, close to the cell membrane By similarity. Upon TGFB1 treatment, it localizes to membrane ruffles By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. focal adhesion Source: MGI
    5. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are born with the expected Mendelian distribution and appear normal at birth, but fail to thrive, become dehydrated and die after three to five days. They develop skin atrophy and die due to a lethal intestinal epithelial dysfunction. The colon is shortened and swollen and presents signs of acute inflammation. At the time of death, about 80% of the colonic epithelium is detached.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 677677Fermitin family homolog 1PRO_0000219453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei170 – 1701PhosphoserineBy similarity
    Modified residuei179 – 1791PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP59113.
    PaxDbiP59113.
    PRIDEiP59113.

    PTM databases

    PhosphoSiteiP59113.

    Expressioni

    Gene expression databases

    BgeeiP59113.
    GenevestigatoriP59113.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3.By similarity

    Protein-protein interaction databases

    IntActiP59113. 1 interaction.
    MINTiMINT-4139673.

    Structurei

    Secondary structure

    677
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 55
    Beta strandi12 – 198
    Beta strandi26 – 338
    Helixi39 – 5012
    Beta strandi57 – 637
    Turni64 – 674
    Beta strandi68 – 703
    Helixi77 – 804
    Beta strandi88 – 925
    Beta strandi372 – 3798
    Beta strandi390 – 3978
    Beta strandi400 – 4067
    Helixi407 – 4093
    Beta strandi415 – 4195
    Beta strandi424 – 4307
    Turni431 – 4344
    Beta strandi435 – 44410
    Beta strandi447 – 45711
    Helixi458 – 47215
    Helixi482 – 49615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KMCNMR-A1-96[»]
    4BBKX-ray2.10A364-509[»]
    DisProtiDP00655.
    ProteinModelPortaliP59113.
    SMRiP59113. Positions 1-96, 370-497, 525-651.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP59113.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini96 – 653558FERMAdd
    BLAST
    Domaini377 – 47397PHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi147 – 1548Poly-Lys

    Domaini

    The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. The FERM domain contains the subdomains F1, F2 and F3. It is preceded by a F0 domain with a ubiquitin-like fold. The F0 domain is required for integrin activation and for localization at focal adhesions By similarity.By similarity

    Sequence similaritiesi

    Belongs to the kindlin family.Curated
    Contains 1 FERM domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG238024.
    GeneTreeiENSGT00390000013444.
    HOGENOMiHOG000231715.
    HOVERGENiHBG020688.
    InParanoidiA2ANX1.
    KOiK17082.
    OMAiVSPRCAK.
    OrthoDBiEOG7T7GSC.
    TreeFamiTF314677.

    Family and domain databases

    Gene3Di1.20.80.10. 2 hits.
    2.30.29.30. 2 hits.
    InterProiIPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    PROSITEiPS00661. FERM_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P59113-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSSGDLTSA SWELVVRVDH ANGEQQTEIT LRVSGDLHIG GVMLKLVEQM    50
    NIAQDWSDYA LWWEQKRCWL LKTHWTLDKC GVQADANLLF TPQHKMLRLR 100
    LPNAKTVRLR VSFSAVVFKA VADICKVLNI RRPEELSLLK PSSDYCKKKK 150
    KKEKNSKEPV IEDILNLESS STSSGSPVSP GLYSKTMTPT YDPINGTPAL 200
    STMTWFGDSP LTEQNCSVLA FSQPPPSPDV LADMFQPRSL VDKAKMNAGW 250
    LDSSRSLMEQ SIQEDEQLQL RFKYYTFFDL NPKYDAVRIN QLYEQARWAV 300
    LLEEIDCTEE EMLIFAALQY HISKLSQCAE IQDFATKSEV DEVEAALSSL 350
    EVTLEGGKAD NTLEDITDIP KLADYLKLFR PKKLMLKACK QYWFVFKDTS 400
    IAYFKNKELE QGEPIEKLNL RGCEIVPDVN VSGRKFGIKL LIPVADGMNE 450
    VYLRCDHEDQ YARWMAACIL ASKGKTMADS SYQPEVISIL SFLKMKNRNS 500
    SPLVASSLEN MDMNPECLVS PCCAKKHKSK QLAARILEAH HNVAQMPLVE 550
    AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVAYNRL IRIDAVTGIP 600
    VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY 650
    IFLSTRSKDQ NETLDEDLFH KLTGGQD 677
    Length:677
    Mass (Da):76,941
    Last modified:July 27, 2011 - v4
    Checksum:i9B8B1876FA7621EE
    GO

    Sequence cautioni

    The sequence AAH29093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti522 – 5221C → R in AAH29093. (PubMed:15489334)Curated
    Sequence conflicti586 – 5861A → S in AAH29093. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL831763 Genomic DNA. Translation: CAM20382.1.
    BC029093 mRNA. Translation: AAH29093.1. Different initiation.
    BC042792 mRNA. No translation available.
    AK050804 mRNA. Translation: BAC34417.1.
    CCDSiCCDS38248.1.
    RefSeqiNP_932146.2. NM_198029.2.
    UniGeneiMm.209784.

    Genome annotation databases

    EnsembliENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.
    GeneIDi241639.
    KEGGimmu:241639.
    UCSCiuc008mno.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL831763 Genomic DNA. Translation: CAM20382.1 .
    BC029093 mRNA. Translation: AAH29093.1 . Different initiation.
    BC042792 mRNA. No translation available.
    AK050804 mRNA. Translation: BAC34417.1 .
    CCDSi CCDS38248.1.
    RefSeqi NP_932146.2. NM_198029.2.
    UniGenei Mm.209784.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KMC NMR - A 1-96 [» ]
    4BBK X-ray 2.10 A 364-509 [» ]
    DisProti DP00655.
    ProteinModelPortali P59113.
    SMRi P59113. Positions 1-96, 370-497, 525-651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P59113. 1 interaction.
    MINTi MINT-4139673.

    PTM databases

    PhosphoSitei P59113.

    Proteomic databases

    MaxQBi P59113.
    PaxDbi P59113.
    PRIDEi P59113.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038280 ; ENSMUSP00000047616 ; ENSMUSG00000027356 .
    GeneIDi 241639.
    KEGGi mmu:241639.
    UCSCi uc008mno.1. mouse.

    Organism-specific databases

    CTDi 55612.
    MGIi MGI:2443583. Fermt1.

    Phylogenomic databases

    eggNOGi NOG238024.
    GeneTreei ENSGT00390000013444.
    HOGENOMi HOG000231715.
    HOVERGENi HBG020688.
    InParanoidi A2ANX1.
    KOi K17082.
    OMAi VSPRCAK.
    OrthoDBi EOG7T7GSC.
    TreeFami TF314677.

    Miscellaneous databases

    EvolutionaryTracei P59113.
    NextBioi 385110.
    PROi P59113.
    SOURCEi Search...

    Gene expression databases

    Bgeei P59113.
    Genevestigatori P59113.

    Family and domain databases

    Gene3Di 1.20.80.10. 2 hits.
    2.30.29.30. 2 hits.
    InterProi IPR019749. Band_41_domain.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    PROSITEi PS00661. FERM_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 1-152 AND 448-677.
      Tissue: Mammary fibroblast.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-677.
      Strain: C57BL/6J.
    4. "Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction."
      Ussar S., Moser M., Widmaier M., Rognoni E., Harrer C., Genzel-Boroviczeny O., Fassler R.
      PLoS Genet. 4:E1000289-E1000289(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "The structure of the N-terminus of kindlin-1: a domain important for alphaIIbbeta3 integrin activation."
      Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., Anthis N.J., Campbell I.D., Calderwood D.A., Barsukov I.L., Roberts G.C., Critchley D.R.
      J. Mol. Biol. 394:944-956(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-96, DOMAIN FERM.

    Entry informationi

    Entry nameiFERM1_MOUSE
    AccessioniPrimary (citable) accession number: P59113
    Secondary accession number(s): A2ANX1, Q8BQG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 108 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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