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Q96AC1 (FERM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FERMT2
Synonyms:KIND2, MIG2, PLEKHC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.8 Ref.16 Ref.18 Ref.19 Ref.20

Subunit structure

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. Ref.3 Ref.8 Ref.15 Ref.16 Ref.18

Subcellular location

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. Ref.3 Ref.8 Ref.16 Ref.18 Ref.20

Tissue specificity

Ubiquitous. Found in numerous tumor tissues.

Induction

By serum in lung fetal fibroblast cultured cells. Ref.1

Domain

The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. Ref.19 Ref.20

The PH domain binds phospholipids. Binds preferentially phosphatidylinositol-3,4,5-trisphosphate, and has lower affinity for phosphatidylinositol-4,5-bisphosphate (Ref.19). Ref.19 Ref.20

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 (Ref.20). Ref.19 Ref.20

Sequence similarities

Belongs to the kindlin family.

Contains 1 FERM domain.

Contains 1 PH domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Cell shape
Wnt signaling pathway
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

cell junction assembly

Traceable author statement. Source: Reactome

cell-matrix adhesion

Inferred from mutant phenotype Ref.16. Source: UniProtKB

focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

integrin activation

Inferred from mutant phenotype Ref.19. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.16. Source: UniProtKB

protein localization to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentI band

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.18. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

filamentous actin

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from direct assay Ref.16. Source: UniProtKB

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

stress fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay Ref.16Ref.19. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P3522213EBI-4399465,EBI-491549
TCF4P158846EBI-4399465,EBI-533224

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96AC1-1)

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.
Isoform 2 (identifier: Q96AC1-2)

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.
Isoform 3 (identifier: Q96AC1-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 680680Fermitin family homolog 2
PRO_0000219456

Regions

Domain189 – 661473FERM
Domain380 – 47697PH
Region40 – 8142Interaction with membranes containing phosphatidylinositol phosphate

Sites

Binding site3831Phosphatidylinositol phosphate

Amino acid modifications

Modified residue1591Phosphoserine Ref.10 Ref.12 Ref.13 Ref.17
Modified residue1811Phosphoserine Ref.10
Modified residue3391Phosphoserine Ref.13
Modified residue3511Phosphoserine Ref.13 Ref.17
Modified residue6661Phosphoserine Ref.9 Ref.10 Ref.13 Ref.17

Natural variations

Alternative sequence5341Q → QPGYIRDL in isoform 2 and isoform 3.
VSP_008783
Alternative sequence625 – 6262TV → NS in isoform 2.
VSP_008784
Alternative sequence627 – 68054Missing in isoform 2.
VSP_008785

Experimental info

Mutagenesis401H → A: Abolishes lipid-binding via the N-terminus; when associated with 74-A--A-81. Ref.8 Ref.20
Mutagenesis74 – 818KTHWTLDK → ATAATLDA: Abolishes lipid-binding via the N-terminus; when associated with A-40. Ref.8 Ref.20
Mutagenesis3831K → A: Reduces phosphatidylinositol phosphate binding. Reduces integrin activation; when associated with A-385. Ref.8 Ref.19
Mutagenesis3851K → A: Reduces integrin activation; when associated with A-383. Ref.8 Ref.19
Mutagenesis3901K → A: Abolishes phosphatidylinositol phosphate binding. Ref.8 Ref.16
Mutagenesis3931K → A: Reduces phosphatidylinositol phosphate binding. Ref.8 Ref.19
Mutagenesis614 – 6152QW → AA: Impairs ITGB3 binding. Abolishes enhancement of talin-mediated integrin activation. Ref.8
Sequence conflict311V → I in CAA80852. Ref.1

Secondary structure

.................................. 680
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BAFF5AF2CD91C43C

FASTA68077,861
        10         20         30         40         50         60 
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE KLDVKKDWSD 

        70         80         90        100        110        120 
HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR LQLPNMKYVK VKVNFSDRVF 

       130        140        150        160        170        180 
KAVSDICKTF NIRHPEELSL LKKPRDPTKK KKKKLDDQSE DEALELEGPL ITPGSGSIYS 

       190        200        210        220        230        240 
SPGLYSKTMT PTYDAHDGSP LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ 

       250        260        270        280        290        300 
ALLDKAKINQ GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW 

       310        320        330        340        350        360 
AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL SDLEITLEGG 

       370        380        390        400        410        420 
KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK DTSISCYKSK EESSGTPAHQ 

       430        440        450        460        470        480 
MNLRGCEVTP DVNISGQKFN IKLLIPVAEG MNEIWLRCDN EKQYAHWMAA CRLASKGKTM 

       490        500        510        520        530        540 
ADSSYNLEVQ NILSFLKMQH LNPDPQLIPE QITTDITPEC LVSPRYLKKY KNKQITARIL 

       550        560        570        580        590        600 
EAHQNVAQMS LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST 

       610        620        630        640        650        660 
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI GGYIFLSTRA 

       670        680 
KDQNESLDEE MFYKLTSGWV 

« Hide

Isoform 2 [UniParc].

Checksum: EF95EB667653A1B4
Show »

FASTA63372,397
Isoform 3 [UniParc].

Checksum: A94A73D8399A348B
Show »

FASTA68778,675

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

FERMT2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45107.1. [Q96AC1-3]
CCDS45108.1. [Q96AC1-2]
CCDS9713.1. [Q96AC1-1]
PIRS69890.
RefSeqNP_001128471.1. NM_001134999.1. [Q96AC1-3]
NP_001128472.1. NM_001135000.1. [Q96AC1-2]
NP_006823.1. NM_006832.2. [Q96AC1-1]
UniGeneHs.509343.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LGXNMR-A1-105[»]
2LKONMR-A367-500[»]
4F7HX-ray1.90A328-499[»]
ProteinModelPortalQ96AC1.
SMRQ96AC1. Positions 1-94, 365-499, 528-654.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116175. 35 interactions.
IntActQ96AC1. 3 interactions.
MINTMINT-3050746.
STRING9606.ENSP00000342858.

PTM databases

PhosphoSiteQ96AC1.

Polymorphism databases

DMDM38258220.

Proteomic databases

MaxQBQ96AC1.
PaxDbQ96AC1.
PRIDEQ96AC1.

Protocols and materials databases

DNASU10979.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341590; ENSP00000340391; ENSG00000073712. [Q96AC1-1]
ENST00000343279; ENSP00000342858; ENSG00000073712. [Q96AC1-3]
ENST00000395631; ENSP00000378993; ENSG00000073712. [Q96AC1-1]
ENST00000399304; ENSP00000382243; ENSG00000073712. [Q96AC1-2]
ENST00000553373; ENSP00000451084; ENSG00000073712. [Q96AC1-3]
GeneID10979.
KEGGhsa:10979.
UCSCuc001xac.3. human. [Q96AC1-3]
uc001xad.3. human. [Q96AC1-1]
uc001xaf.3. human. [Q96AC1-2]

Organism-specific databases

CTD10979.
GeneCardsGC14M053323.
HGNCHGNC:15767. FERMT2.
HPAHPA040505.
MIM607746. gene.
neXtProtNX_Q96AC1.
PharmGKBPA162388349.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238024.
HOGENOMHOG000231715.
HOVERGENHBG020688.
KOK17083.
OMAMTPTYDS.
OrthoDBEOG7T7GSC.
PhylomeDBQ96AC1.
TreeFamTF314677.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ96AC1.
BgeeQ96AC1.
CleanExHS_FERMT2.
GenevestigatorQ96AC1.

Family and domain databases

Gene3D1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR018979. FERM_N.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 2 hits.
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFERMT2. human.
EvolutionaryTraceQ96AC1.
GeneWikiFERMT2.
GenomeRNAi10979.
NextBio41714.
PROQ96AC1.
SOURCESearch...

Entry information

Entry nameFERM2_HUMAN
AccessionPrimary (citable) accession number: Q96AC1
Secondary accession number(s): B5TJY2, Q14840, Q86TY7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM