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Q96AC1

- FERM2_HUMAN

UniProt

Q96AC1 - FERM2_HUMAN

Protein

Fermitin family homolog 2

Gene

FERMT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      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.6 Publications

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Biological processi

    Cell adhesion, Cell shape, Wnt signaling pathway

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_20649. Cell-extracellular matrix interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fermitin family homolog 2
    Alternative name(s):
    Kindlin-2
    Mitogen-inducible gene 2 protein
    Short name:
    MIG-2
    Pleckstrin homology domain-containing family C member 1
    Short name:
    PH domain-containing family C member 1
    Gene namesi
    Name:FERMT2
    Synonyms:KIND2, MIG2, PLEKHC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:15767. FERMT2.

    Subcellular locationi

    Cytoplasm. Cytoplasmcell cortex. Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. CytoplasmmyofibrilsarcomereI band By similarity. Cell surface By similarity
    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.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell surface Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    6. filamentous actin Source: Ensembl
    7. focal adhesion Source: UniProtKB
    8. I band Source: UniProtKB-SubCell
    9. lamellipodium membrane Source: UniProtKB-SubCell
    10. nucleus Source: UniProtKB
    11. stress fiber Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401H → A: Abolishes lipid-binding via the N-terminus; when associated with 74-A--A-81. 2 Publications
    Mutagenesisi74 – 818KTHWTLDK → ATAATLDA: Abolishes lipid-binding via the N-terminus; when associated with A-40. 1 Publication
    Mutagenesisi383 – 3831K → A: Reduces phosphatidylinositol phosphate binding. Reduces integrin activation; when associated with A-385. 2 Publications
    Mutagenesisi385 – 3851K → A: Reduces integrin activation; when associated with A-383. 2 Publications
    Mutagenesisi390 – 3901K → A: Abolishes phosphatidylinositol phosphate binding. 2 Publications
    Mutagenesisi393 – 3931K → A: Reduces phosphatidylinositol phosphate binding. 2 Publications
    Mutagenesisi614 – 6152QW → AA: Impairs ITGB3 binding. Abolishes enhancement of talin-mediated integrin activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA162388349.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 680680Fermitin family homolog 2PRO_0000219456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei159 – 1591Phosphoserine4 Publications
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei339 – 3391Phosphoserine1 Publication
    Modified residuei351 – 3511Phosphoserine2 Publications
    Modified residuei666 – 6661Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96AC1.
    PaxDbiQ96AC1.
    PRIDEiQ96AC1.

    PTM databases

    PhosphoSiteiQ96AC1.

    Expressioni

    Tissue specificityi

    Ubiquitous. Found in numerous tumor tissues.

    Inductioni

    By serum in lung fetal fibroblast cultured cells.1 Publication

    Gene expression databases

    ArrayExpressiQ96AC1.
    BgeeiQ96AC1.
    CleanExiHS_FERMT2.
    GenevestigatoriQ96AC1.

    Organism-specific databases

    HPAiHPA040505.

    Interactioni

    Subunit structurei

    Interacts with ILK By similarity. Interacts with FBLIM1. Interacts with ITGB1 and ITGB3. Interacts with active, unphosphorylated CTNNB1. Identified in a complex with CTNNB1 and TCF7L2/TCF4. Interacts with ITGB1; the interaction is inhibited in presence of ITGB1BP1.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P3522213EBI-4399465,EBI-491549
    TCF4P158846EBI-4399465,EBI-533224

    Protein-protein interaction databases

    BioGridi116175. 35 interactions.
    IntActiQ96AC1. 3 interactions.
    MINTiMINT-3050746.
    STRINGi9606.ENSP00000342858.

    Structurei

    Secondary structure

    1
    680
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni9 – 113
    Beta strandi12 – 165
    Turni25 – 284
    Helixi41 – 5111
    Beta strandi58 – 658
    Turni66 – 683
    Helixi79 – 824
    Helixi369 – 3713
    Beta strandi375 – 3828
    Beta strandi393 – 4008
    Beta strandi403 – 4086
    Helixi410 – 4123
    Beta strandi418 – 4225
    Beta strandi427 – 4337
    Turni434 – 4374
    Beta strandi438 – 44710
    Beta strandi450 – 46011
    Helixi461 – 47515
    Helixi484 – 49512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LGXNMR-A1-105[»]
    2LKONMR-A367-500[»]
    4F7HX-ray1.90A328-499[»]
    ProteinModelPortaliQ96AC1.
    SMRiQ96AC1. Positions 1-94, 365-499, 528-654.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96AC1.

    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 phosphateAdd
    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 (PubMed:22030399).1 Publication
    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.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG238024.
    HOGENOMiHOG000231715.
    HOVERGENiHBG020688.
    KOiK17083.
    OMAiMTPTYDS.
    OrthoDBiEOG7T7GSC.
    PhylomeDBiQ96AC1.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96AC1-1) [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

    MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE    50
    KLDVKKDWSD HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR 100
    LQLPNMKYVK VKVNFSDRVF KAVSDICKTF NIRHPEELSL LKKPRDPTKK 150
    KKKKLDDQSE DEALELEGPL ITPGSGSIYS SPGLYSKTMT PTYDAHDGSP 200
    LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ ALLDKAKINQ 250
    GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW 300
    AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL 350
    SDLEITLEGG KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK 400
    DTSISCYKSK EESSGTPAHQ MNLRGCEVTP DVNISGQKFN IKLLIPVAEG 450
    MNEIWLRCDN EKQYAHWMAA CRLASKGKTM ADSSYNLEVQ NILSFLKMQH 500
    LNPDPQLIPE QITTDITPEC LVSPRYLKKY KNKQITARIL EAHQNVAQMS 550
    LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST 600
    GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI 650
    GGYIFLSTRA KDQNESLDEE MFYKLTSGWV 680
    Length:680
    Mass (Da):77,861
    Last modified:December 1, 2001 - v1
    Checksum:iBAFF5AF2CD91C43C
    GO
    Isoform 2 (identifier: Q96AC1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         534-534: Q → QPGYIRDL
         625-626: TV → NS
         627-680: Missing.

    Note: May be due to an exon inclusion and an intron retention.

    Show »
    Length:633
    Mass (Da):72,397
    Checksum:iEF95EB667653A1B4
    GO
    Isoform 3 (identifier: Q96AC1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         534-534: Q → QPGYIRDL

    Show »
    Length:687
    Mass (Da):78,675
    Checksum:iA94A73D8399A348B
    GO

    Sequence cautioni

    The sequence CAA80852.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311V → I in CAA80852. (PubMed:8175911)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei534 – 5341Q → QPGYIRDL in isoform 2 and isoform 3. 2 PublicationsVSP_008783
    Alternative sequencei625 – 6262TV → NS in isoform 2. 1 PublicationVSP_008784
    Alternative sequencei627 – 68054Missing in isoform 2. 1 PublicationVSP_008785Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24725 mRNA. Translation: CAA80852.1. Different initiation.
    AF443279 mRNA. Translation: AAN75823.1.
    EU979385 mRNA. Translation: ACH73257.1.
    BX161467 mRNA. Translation: CAD61925.1.
    AL139317 Genomic DNA. No translation available.
    AL352979 Genomic DNA. No translation available.
    BC011125 mRNA. No translation available.
    BC017327 mRNA. Translation: AAH17327.1.
    CCDSiCCDS45107.1. [Q96AC1-3]
    CCDS45108.1. [Q96AC1-2]
    CCDS9713.1. [Q96AC1-1]
    PIRiS69890.
    RefSeqiNP_001128471.1. NM_001134999.1. [Q96AC1-3]
    NP_001128472.1. NM_001135000.1. [Q96AC1-2]
    NP_006823.1. NM_006832.2. [Q96AC1-1]
    UniGeneiHs.509343.

    Genome annotation databases

    EnsembliENST00000341590; ENSP00000340391; ENSG00000073712. [Q96AC1-1]
    ENST00000343279; ENSP00000342858; ENSG00000073712. [Q96AC1-3]
    ENST00000395631; ENSP00000378993; ENSG00000073712. [Q96AC1-1]
    ENST00000399304; ENSP00000382243; ENSG00000073712. [Q96AC1-2]
    ENST00000553373; ENSP00000451084; ENSG00000073712. [Q96AC1-3]
    GeneIDi10979.
    KEGGihsa:10979.
    UCSCiuc001xac.3. human. [Q96AC1-3]
    uc001xad.3. human. [Q96AC1-1]
    uc001xaf.3. human. [Q96AC1-2]

    Polymorphism databases

    DMDMi38258220.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    FERMT2 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24725 mRNA. Translation: CAA80852.1 . Different initiation.
    AF443279 mRNA. Translation: AAN75823.1 .
    EU979385 mRNA. Translation: ACH73257.1 .
    BX161467 mRNA. Translation: CAD61925.1 .
    AL139317 Genomic DNA. No translation available.
    AL352979 Genomic DNA. No translation available.
    BC011125 mRNA. No translation available.
    BC017327 mRNA. Translation: AAH17327.1 .
    CCDSi CCDS45107.1. [Q96AC1-3 ]
    CCDS45108.1. [Q96AC1-2 ]
    CCDS9713.1. [Q96AC1-1 ]
    PIRi S69890.
    RefSeqi NP_001128471.1. NM_001134999.1. [Q96AC1-3 ]
    NP_001128472.1. NM_001135000.1. [Q96AC1-2 ]
    NP_006823.1. NM_006832.2. [Q96AC1-1 ]
    UniGenei Hs.509343.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LGX NMR - A 1-105 [» ]
    2LKO NMR - A 367-500 [» ]
    4F7H X-ray 1.90 A 328-499 [» ]
    ProteinModelPortali Q96AC1.
    SMRi Q96AC1. Positions 1-94, 365-499, 528-654.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116175. 35 interactions.
    IntActi Q96AC1. 3 interactions.
    MINTi MINT-3050746.
    STRINGi 9606.ENSP00000342858.

    PTM databases

    PhosphoSitei Q96AC1.

    Polymorphism databases

    DMDMi 38258220.

    Proteomic databases

    MaxQBi Q96AC1.
    PaxDbi Q96AC1.
    PRIDEi Q96AC1.

    Protocols and materials databases

    DNASUi 10979.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341590 ; ENSP00000340391 ; ENSG00000073712 . [Q96AC1-1 ]
    ENST00000343279 ; ENSP00000342858 ; ENSG00000073712 . [Q96AC1-3 ]
    ENST00000395631 ; ENSP00000378993 ; ENSG00000073712 . [Q96AC1-1 ]
    ENST00000399304 ; ENSP00000382243 ; ENSG00000073712 . [Q96AC1-2 ]
    ENST00000553373 ; ENSP00000451084 ; ENSG00000073712 . [Q96AC1-3 ]
    GeneIDi 10979.
    KEGGi hsa:10979.
    UCSCi uc001xac.3. human. [Q96AC1-3 ]
    uc001xad.3. human. [Q96AC1-1 ]
    uc001xaf.3. human. [Q96AC1-2 ]

    Organism-specific databases

    CTDi 10979.
    GeneCardsi GC14M053323.
    HGNCi HGNC:15767. FERMT2.
    HPAi HPA040505.
    MIMi 607746. gene.
    neXtProti NX_Q96AC1.
    PharmGKBi PA162388349.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238024.
    HOGENOMi HOG000231715.
    HOVERGENi HBG020688.
    KOi K17083.
    OMAi MTPTYDS.
    OrthoDBi EOG7T7GSC.
    PhylomeDBi Q96AC1.
    TreeFami TF314677.

    Enzyme and pathway databases

    Reactomei REACT_20649. Cell-extracellular matrix interactions.

    Miscellaneous databases

    ChiTaRSi FERMT2. human.
    EvolutionaryTracei Q96AC1.
    GeneWikii FERMT2.
    GenomeRNAii 10979.
    NextBioi 41714.
    PROi Q96AC1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96AC1.
    Bgeei Q96AC1.
    CleanExi HS_FERMT2.
    Genevestigatori Q96AC1.

    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. "Identification of serum-inducible genes: different patterns of gene regulation during G0->S and G1->S progression."
      Wick M., Buerger C., Bruesselbach S., Lucibello F.C., Mueller R.
      J. Cell Sci. 107:227-239(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
      Tissue: Lung fibroblast.
    2. "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas."
      Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.
      Biochim. Biophys. Acta 1637:207-216(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENOMIC ORGANIZATION.
      Tissue: Colon tumor.
    3. "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation."
      Tu Y., Wu S., Shi X., Chen K., Wu C.
      Cell 113:37-47(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBLIM1.
      Tissue: Lung.
    4. Tan S.-M., Li Y.-F.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    6. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Choriocarcinoma, Lung carcinoma and Placenta.
    8. "Kindlin-2 (Mig-2): a co-activator of beta3 integrins."
      Ma Y.Q., Qin J., Wu C., Plow E.F.
      J. Cell Biol. 181:439-446(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ITGB3, SUBCELLULAR LOCATION, MUTAGENESIS OF 614-GLN-TRP-615.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-181 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-339; SER-351 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: INTERACTION WITH ITGB1.
    16. "Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins."
      Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J., Fukuda K., Qin J., Kretzler M., Wu C.
      J. Cell Sci. 124:879-891(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ITGB1 AND ITGB3, LIPID-BINDING, MUTAGENESIS OF LYS-390, SUBCELLULAR LOCATION.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-351 AND SER-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling."
      Yu Y., Wu J., Wang Y., Zhao T., Ma B., Liu Y., Fang W., Zhu W.G., Zhang H.
      EMBO Rep. 13:750-758(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTNNB1, IDENTIFICATION IN A COMPLEX WITH CTNNB1 AND TCF7L2, SUBCELLULAR LOCATION.
    19. "Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation."
      Liu J., Fukuda K., Xu Z., Ma Y.Q., Hirbawi J., Mao X., Wu C., Plow E.F., Qin J.
      J. Biol. Chem. 286:43334-43342(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 367-500 IN COMPLEX WITH PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE, FUNCTION, DOMAIN, MUTAGENESIS OF LYS-383; LYS-385 AND LYS-393, LIPID-BINDING.
    20. "Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation."
      Perera H.D., Ma Y.Q., Yang J., Hirbawi J., Plow E.F., Qin J.
      Structure 19:1664-1671(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-105, FUNCTION, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-40 AND 74-LYS--LYS-81, LIPID-BINDING.
    21. "Crystal structure of kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation."
      Liu Y., Zhu Y., Ye S., Zhang R.
      Protein Cell 3:434-440(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 328-499.

    Entry informationi

    Entry nameiFERM2_HUMAN
    AccessioniPrimary (citable) accession number: Q96AC1
    Secondary accession number(s): B5TJY2, Q14840, Q86TY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3