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UniProtKB - Q96AC1 (FERM2_HUMAN)

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Protein

Fermitin family homolog 2

Gene

FERMT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei383Phosphatidylinositol phosphate1

GO - Molecular functioni

  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • cell junction assembly Source: Reactome
  • cell-matrix adhesion Source: UniProtKB
  • focal adhesion assembly Source: UniProtKB
  • integrin activation Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • protein localization to membrane Source: UniProtKB
  • regulation of cell shape Source: UniProtKB-KW
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywordsi

Biological processCell adhesion, Cell shape, Wnt signaling pathway
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-446353. 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:15767. FERMT2.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cell surface Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • filamentous actin Source: Ensembl
  • focal adhesion Source: UniProtKB
  • I band Source: UniProtKB-SubCell
  • lamellipodium membrane Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi40H → A: Abolishes lipid-binding via the N-terminus; when associated with 74-A--A-81. 1 Publication1
Mutagenesisi74 – 81KTHWTLDK → ATAATLDA: Abolishes lipid-binding via the N-terminus; when associated with A-40. 1 Publication8
Mutagenesisi383K → A: Reduces phosphatidylinositol phosphate binding. Reduces integrin activation; when associated with A-385. 1 Publication1
Mutagenesisi385K → A: Reduces integrin activation; when associated with A-383. 1 Publication1
Mutagenesisi390K → A: Abolishes phosphatidylinositol phosphate binding. 1 Publication1
Mutagenesisi393K → A: Reduces phosphatidylinositol phosphate binding. 1 Publication1
Mutagenesisi614 – 615QW → AA: Impairs ITGB3 binding. Abolishes enhancement of talin-mediated integrin activation. 1 Publication2

Organism-specific databases

DisGeNETi10979.
OpenTargetsiENSG00000073712.
PharmGKBiPA162388349.

Polymorphism and mutation databases

BioMutaiFERMT2.
DMDMi38258220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194561 – 680Fermitin family homolog 2Add BLAST680

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei159PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Modified residuei339PhosphoserineCombined sources1
Modified residuei351PhosphoserineCombined sources1
Modified residuei666PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96AC1.
MaxQBiQ96AC1.
PaxDbiQ96AC1.
PeptideAtlasiQ96AC1.
PRIDEiQ96AC1.

PTM databases

iPTMnetiQ96AC1.
PhosphoSitePlusiQ96AC1.
SwissPalmiQ96AC1.

Expressioni

Tissue specificityi

Ubiquitous. Found in numerous tumor tissues.

Inductioni

By serum in lung fetal fibroblast cultured cells.1 Publication

Gene expression databases

BgeeiENSG00000073712.
CleanExiHS_FERMT2.
ExpressionAtlasiQ96AC1. baseline and differential.
GenevisibleiQ96AC1. HS.

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

Show more details

Protein-protein interaction databases

BioGridi116175. 57 interactors.
IntActiQ96AC1. 11 interactors.
MINTiMINT-3050746.
STRINGi9606.ENSP00000342858.

Structurei

Secondary structure

1680
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 11Combined sources3
Beta strandi12 – 16Combined sources5
Turni25 – 28Combined sources4
Helixi41 – 51Combined sources11
Beta strandi58 – 65Combined sources8
Turni66 – 68Combined sources3
Helixi79 – 82Combined sources4
Turni347 – 353Combined sources7
Helixi354 – 357Combined sources4
Helixi369 – 371Combined sources3
Beta strandi375 – 382Combined sources8
Beta strandi393 – 400Combined sources8
Beta strandi403 – 408Combined sources6
Helixi410 – 412Combined sources3
Beta strandi418 – 422Combined sources5
Beta strandi427 – 433Combined sources7
Turni434 – 437Combined sources4
Beta strandi438 – 447Combined sources10
Beta strandi450 – 460Combined sources11
Helixi461 – 475Combined sources15
Helixi484 – 495Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LGXNMR-A1-105[»]
2LKONMR-A367-500[»]
2MSUNMR-A339-358[»]
4F7HX-ray1.90A328-499[»]
ProteinModelPortaliQ96AC1.
SMRiQ96AC1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96AC1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini189 – 661FERMAdd BLAST473
Domaini380 – 476PHPROSITE-ProRule annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 81Interaction with membranes containing phosphatidylinositol phosphateAdd BLAST42

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

Phylogenomic databases

eggNOGiKOG3727. Eukaryota.
ENOG410XS1B. LUCA.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiQ96AC1.
KOiK17083.
OMAiLKTWRYN.
OrthoDBiEOG091G03SD.
PhylomeDBiQ96AC1.
TreeFamiTF314677.

Family and domain databases

CDDicd14473. FERM_B-lobe. 1 hit.
Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiView protein in InterPro
IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
PfamiView protein in Pfam
PF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
SMARTiView protein in SMART
SM00295. B41. 1 hit.
SM00233. PH. 1 hit.
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 2 hits.
PROSITEiView protein in PROSITE
PS50003. PH_DOMAIN. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31V → I in CAA80852 (PubMed:8175911).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008783534Q → QPGYIRDL in isoform 2 and isoform 3. 2 Publications1
Alternative sequenceiVSP_008784625 – 626TV → NS in isoform 2. 1 Publication2
Alternative sequenceiVSP_008785627 – 680Missing in isoform 2. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q96AC1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiFERM2_HUMAN
AccessioniPrimary (citable) accession number: Q96AC1
Secondary accession number(s): B5TJY2, Q14840, Q86TY7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: December 1, 2001
Last modified: June 7, 2017
This is version 147 of the entry and version 1 of the sequence. See 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