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Q8CIB5

- FERM2_MOUSE

UniProt

Q8CIB5 - FERM2_MOUSE

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Protein

Fermitin family homolog 2

Gene

Fermt2

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

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
Complete GO annotation...

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 projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

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

BgeeiQ8CIB5.
CleanExiMM_FERMT2.
ExpressionAtlasiQ8CIB5. baseline and differential.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE
60 70 80 90 100
KLDVKKDWSD HALWWEKKRT WLLKTHWTLD KCGIQADAKL QFTPQHKLLR
110 120 130 140 150
LQLPNMKYVK VKVNFSDRVF KAVSDICKTF NIRHPEELSL LKKPRDPTKK
160 170 180 190 200
KKKKLDDQSE DEALELEGPL IMPGSGSIYS SPGLYSKTMT PTYDAHDGSP
210 220 230 240 250
LSPTSAWFGD SALSEGNPGI LAVSQPVTSP EILAKMFKPQ ALLDKAKTNQ
260 270 280 290 300
GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW
310 320 330 340 350
ALLLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL
360 370 380 390 400
SDLEITLEGG KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK
410 420 430 440 450
DTSISCYKSR EESSGTPAHQ LNLRGCEVTP DVNISGQKFN IKLLIPVAEG
460 470 480 490 500
MNEIWLRCDN EKQYAHWMAA CRLASKGKTM ADSSYNLEVQ NILSFLKMQH
510 520 530 540 550
LNPDPQLIPD QITTDVNPEC LVSPRYLKKY KSKQITARIL EAHQNVAQMS
560 570 580 590 600
LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KREELIGIAY NRLIRMDAST
610 620 630 640 650
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI
660 670 680
GGYIFLSTRA KDQNESLDEE MFYKLTSGWV
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

Bgeei Q8CIB5.
CleanExi MM_FERMT2.
ExpressionAtlasi Q8CIB5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 100 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