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Q8CIB5

- FERM2_MOUSE

UniProt

Q8CIB5 - FERM2_MOUSE

Protein

Fermitin family homolog 2

Gene

Fermt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei383 – 3831Phosphatidylinositol phosphateBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB

    GO - Biological processi

    1. cell-matrix adhesion Source: UniProtKB
    2. focal adhesion assembly Source: UniProtKB
    3. integrin activation Source: UniProtKB
    4. integrin-mediated signaling pathway Source: UniProtKB
    5. protein localization to membrane Source: UniProtKB
    6. regulation of cell shape Source: UniProtKB-KW
    7. substrate adhesion-dependent cell spreading Source: UniProtKB
    8. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    9. Wnt signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion, Cell shape, Wnt signaling pathway

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fermitin family homolog 2
    Alternative name(s):
    Kindlin-2
    Pleckstrin homology domain-containing family C member 1
    Gene namesi
    Name:Fermt2
    Synonyms:Plekhc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:2385001. Fermt2.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionlamellipodium membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity. CytoplasmmyofibrilsarcomereI band. Cell surface
    Note: Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides By similarity.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell surface Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytoskeleton Source: UniProtKB-SubCell
    5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    6. focal adhesion Source: UniProtKB
    7. I band Source: UniProtKB-SubCell
    8. lamellipodium membrane Source: UniProtKB-SubCell
    9. nucleus Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    Complete embryonic lethality at peri-implantation stage, due to severe detachment of the endoderm and epiblast from the basement membrane. Heterozygous mice lacking one copy of Fermt2 show no visible phenotype, but show decreased tumor angiogenesis upon transplantation of tumor cells, and their blood vessels are abnormally leaky.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi614 – 6152QW → AA: Abolishes interaction with integrins ITGB1 and ITGB3. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 680680Fermitin family homolog 2PRO_0000219457Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei159 – 1591PhosphoserineBy similarity
    Modified residuei181 – 1811PhosphoserineBy similarity
    Modified residuei339 – 3391PhosphoserineBy similarity
    Modified residuei351 – 3511PhosphoserineBy similarity
    Modified residuei666 – 6661PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8CIB5.
    PaxDbiQ8CIB5.
    PRIDEiQ8CIB5.

    PTM databases

    PhosphoSiteiQ8CIB5.

    Expressioni

    Tissue specificityi

    Detected in adult heart muscle (at protein level). Detected in heart, skeletal muscle and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ8CIB5.
    BgeeiQ8CIB5.
    CleanExiMM_FERMT2.
    GenevestigatoriQ8CIB5.

    Interactioni

    Subunit structurei

    Interacts with ITGB1; the interaction is inhibited in presence of ITGB1BP1. Interacts with FBLIM1. Interacts with active, unphosphorylated CTNNB1. Identified in a complex with CTNNB1 and TCF7L2/TCF4 By similarity. Interacts with ILK, ITGB1 and ITGB3.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi230085. 2 interactions.
    IntActiQ8CIB5. 2 interactions.
    MINTiMINT-4107681.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CIB5.
    SMRiQ8CIB5. Positions 1-94, 365-499, 528-654.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini189 – 661473FERMAdd
    BLAST
    Domaini380 – 47697PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 8142Interaction with membranes containing phosphatidylinositol phosphateBy similarityAdd
    BLAST

    Domaini

    The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain.
    The PH domain binds phospholipids. Binds preferentially phosphatidylinositol-3,4,5-trisphosphate, and has lower affinity for phosphatidylinositol-4,5-bisphosphate By similarity.By similarity
    The N-terminal region displays a ubiquitin-type fold and mediates interaction with membranes containing negatively charged phosphatidylinositol phosphate via a surface enriched in positively charged residues.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.
    InParanoidiQ8CIB5.
    KOiK17083.
    OMAiMTPTYDS.
    OrthoDBiEOG7T7GSC.
    PhylomeDBiQ8CIB5.
    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.
    IPR018979. FERM_N.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 2 hits.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8CIB5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE    50
    KLDVKKDWSD HALWWEKKRT WLLKTHWTLD KCGIQADAKL QFTPQHKLLR 100
    LQLPNMKYVK VKVNFSDRVF KAVSDICKTF NIRHPEELSL LKKPRDPTKK 150
    KKKKLDDQSE DEALELEGPL IMPGSGSIYS SPGLYSKTMT PTYDAHDGSP 200
    LSPTSAWFGD SALSEGNPGI LAVSQPVTSP EILAKMFKPQ ALLDKAKTNQ 250
    GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW 300
    ALLLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL 350
    SDLEITLEGG KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK 400
    DTSISCYKSR EESSGTPAHQ LNLRGCEVTP DVNISGQKFN IKLLIPVAEG 450
    MNEIWLRCDN EKQYAHWMAA CRLASKGKTM ADSSYNLEVQ NILSFLKMQH 500
    LNPDPQLIPD QITTDVNPEC LVSPRYLKKY KSKQITARIL EAHQNVAQMS 550
    LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KREELIGIAY NRLIRMDAST 600
    GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI 650
    GGYIFLSTRA KDQNESLDEE MFYKLTSGWV 680
    Length:680
    Mass (Da):77,800
    Last modified:March 1, 2003 - v1
    Checksum:i89767FA0E34B543B
    GO

    Sequence cautioni

    The sequence AAH34168.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491K → R in BAC37692. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC033436 mRNA. Translation: AAH33436.1.
    BC034168 mRNA. Translation: AAH34168.1. Different initiation.
    AK079588 mRNA. Translation: BAC37692.1.
    CCDSiCCDS26977.1.
    RefSeqiNP_666166.2. NM_146054.2.
    UniGeneiMm.210018.

    Genome annotation databases

    EnsembliENSMUST00000045905; ENSMUSP00000044554; ENSMUSG00000037712.
    GeneIDi218952.
    KEGGimmu:218952.
    UCSCiuc007tgq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC033436 mRNA. Translation: AAH33436.1 .
    BC034168 mRNA. Translation: AAH34168.1 . Different initiation.
    AK079588 mRNA. Translation: BAC37692.1 .
    CCDSi CCDS26977.1.
    RefSeqi NP_666166.2. NM_146054.2.
    UniGenei Mm.210018.

    3D structure databases

    ProteinModelPortali Q8CIB5.
    SMRi Q8CIB5. Positions 1-94, 365-499, 528-654.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230085. 2 interactions.
    IntActi Q8CIB5. 2 interactions.
    MINTi MINT-4107681.

    PTM databases

    PhosphoSitei Q8CIB5.

    Proteomic databases

    MaxQBi Q8CIB5.
    PaxDbi Q8CIB5.
    PRIDEi Q8CIB5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045905 ; ENSMUSP00000044554 ; ENSMUSG00000037712 .
    GeneIDi 218952.
    KEGGi mmu:218952.
    UCSCi uc007tgq.1. mouse.

    Organism-specific databases

    CTDi 10979.
    MGIi MGI:2385001. Fermt2.

    Phylogenomic databases

    eggNOGi NOG238024.
    GeneTreei ENSGT00390000013444.
    HOGENOMi HOG000231715.
    HOVERGENi HBG020688.
    InParanoidi Q8CIB5.
    KOi K17083.
    OMAi MTPTYDS.
    OrthoDBi EOG7T7GSC.
    PhylomeDBi Q8CIB5.
    TreeFami TF314677.

    Miscellaneous databases

    ChiTaRSi FERMT2. mouse.
    NextBioi 376495.
    PROi Q8CIB5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CIB5.
    Bgeei Q8CIB5.
    CleanExi MM_FERMT2.
    Genevestigatori Q8CIB5.

    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.
    IPR018979. FERM_N.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00295. B41. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 2 hits.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: FVB/N.
      Tissue: Mammary tumor.
    2. "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 1-149.
      Strain: C57BL/6J.
      Tissue: Spinal cord.
    3. "Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function."
      Dowling J.J., Gibbs E., Russell M., Goldman D., Minarcik J., Golden J.A., Feldman E.L.
      Circ. Res. 102:423-431(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Kindlin-2 controls bidirectional signaling of integrins."
      Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M., Fassler R.
      Genes Dev. 22:1325-1330(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH ILK; ITGB1 AND ITGB3, MUTAGENESIS OF 614-GLN-TRP-615.
    5. "The integrin coactivator kindlin-2 plays a critical role in angiogenesis in mice and zebrafish."
      Pluskota E., Dowling J.J., Gordon N., Golden J.A., Szpak D., West X.Z., Nestor C., Ma Y.Q., Bialkowska K., Byzova T., Plow E.F.
      Blood 117:4978-4987(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    6. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
      Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
      J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiFERM2_MOUSE
    AccessioniPrimary (citable) accession number: Q8CIB5
    Secondary accession number(s): Q8C542, Q8K035
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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

    External Data

    Dasty 3