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Q96AC1

- FERM2_HUMAN

UniProt

Q96AC1 - FERM2_HUMAN

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Protein

Fermitin family homolog 2

Gene

FERMT2

Organism
Homo sapiens (Human)
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.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

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
Complete GO annotation...

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 projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. filamentous actin Source: Ensembl
  6. focal adhesion Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. stress fiber Source: Ensembl
Complete GO annotation...

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. 1 Publication
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. 1 Publication
Mutagenesisi385 – 3851K → A: Reduces integrin activation; when associated with A-383. 1 Publication
Mutagenesisi390 – 3901K → A: Abolishes phosphatidylinositol phosphate binding. 1 Publication
Mutagenesisi393 – 3931K → A: Reduces phosphatidylinositol phosphate binding. 1 Publication
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

BgeeiQ96AC1.
CleanExiHS_FERMT2.
ExpressionAtlasiQ96AC1. baseline and differential.
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. 36 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[»]
2MSUNMR-A339-358[»]
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.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiQ96AC1.
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

        10         20         30         40         50
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE
60 70 80 90 100
KLDVKKDWSD HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR
110 120 130 140 150
LQLPNMKYVK VKVNFSDRVF KAVSDICKTF NIRHPEELSL LKKPRDPTKK
160 170 180 190 200
KKKKLDDQSE DEALELEGPL ITPGSGSIYS SPGLYSKTMT PTYDAHDGSP
210 220 230 240 250
LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ ALLDKAKINQ
260 270 280 290 300
GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW
310 320 330 340 350
AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL
360 370 380 390 400
SDLEITLEGG KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK
410 420 430 440 450
DTSISCYKSK EESSGTPAHQ MNLRGCEVTP DVNISGQKFN IKLLIPVAEG
460 470 480 490 500
MNEIWLRCDN EKQYAHWMAA CRLASKGKTM ADSSYNLEVQ NILSFLKMQH
510 520 530 540 550
LNPDPQLIPE QITTDITPEC LVSPRYLKKY KNKQITARIL EAHQNVAQMS
560 570 580 590 600
LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST
610 620 630 640 650
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI
660 670 680
GGYIFLSTRA KDQNESLDEE MFYKLTSGWV
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 [» ]
2MSU NMR - A 339-358 [» ]
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. 36 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.
GeneTreei ENSGT00390000013444.
HOGENOMi HOG000231715.
HOVERGENi HBG020688.
InParanoidi Q96AC1.
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

Bgeei Q96AC1.
CleanExi HS_FERMT2.
ExpressionAtlasi Q96AC1. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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