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Protein Page:
Kindlin-2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Kindlin-2 Participates in the connection between ECM adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites. Belongs to the kindlin family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis
Cellular Component: I band; filamentous actin; extrinsic to internal side of plasma membrane; cell surface; focal adhesion; cytoplasm; nucleolus; stress fiber; cell cortex; cytosol; nucleus
Molecular Function: protein binding; phosphatidylinositol-3,4,5-triphosphate binding
Biological Process: focal adhesion formation; integrin activation; integrin-mediated signaling pathway; regulation of cell shape; Wnt receptor signaling pathway; cell-matrix adhesion; transforming growth factor beta receptor signaling pathway
Reference #:  Q96AC1 (UniProtKB)
Alt. Names/Synonyms: DKFZp686G11125; FERM2; Fermitin family homolog 2; fermitin family homolog 2 (Drosophila); FERMT2; FLJ34213; FLJ44462; KIND2; kindlin 2; Kindlin-2; MIG-2; MIG2; mitogen inducible gene 2 protein; Mitogen-inducible gene 2 protein; PH domain-containing family C member 1; pleckstrin homology domain containing, family C (with FERM domain) member 1; pleckstrin homology domain containing, family C member 1; Pleckstrin homology domain-containing family C member 1; PLEKHC1; UNC112; UNC112B
Gene Symbols: FERMT2
Molecular weight: 77,861 Da
Basal Isoelectric point: 6.26  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Kindlin-2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 18 S159-p KKKLDDQsEDEALEL
0 1 T172-p ELEGPLItPGSGsIy
0 1 S177-p LItPGSGsIyssPGL
0 76 Y179-p tPGSGsIyssPGLyS
0 2 S180-p PGSGsIyssPGLySK
0 6 S181-p GSGsIyssPGLySKT
0 9 Y185-p IyssPGLySKTMTPT
0 3 Y193-p SKTMTPTyDAHDGSP
0 1 K247 QALLDKAKINQGWLD
0 1 K265 SLMEQDVKENEALLL
0 1 K275 EALLLRFKYYSFFDL
0 2 K285-u SFFDLNPkYDAIRIN
0 1 S328 QYHINKLSIMTSENH
0 5 S339-p SENHLNNsDKEVDEV
0 1 D347-ca DKEVDEVdAALsDLE
0 9 S351-p DEVdAALsDLEITLE
0 7 Y378-p SIPELADyIKVFKPK
0 2 Y395-p TLKGYKQyWCTFKDT
0 1 K555 QMSLIEAKMRFIQAW
0 312 Y590-p EELIGIAyNRLIRMD
0 11 S666-p RAKDQNEsLDEEMFY
  Kindlin-2 iso2  
S159 KKKLDDQSEDEALEL
T172 ELEGPLITPGSGSIY
S177 LITPGSGSIYSSPGL
Y179 TPGSGSIYSSPGLYS
S180 PGSGSIYSSPGLYSK
S181 GSGSIYSSPGLYSKT
Y185 IYSSPGLYSKTMTPT
Y193 SKTMTPTYDAHDGSP
K247 QALLDKAKINQGWLD
K265 SLMEQDVKENEALLL
K275 EALLLRFKYYSFFDL
K285 SFFDLNPKYDAIRIN
S328 QYHINKLSIMTSENH
S339 SENHLNNSDKEVDEV
D347 DKEVDEVDAALSDLE
S351 DEVDAALSDLEITLE
Y378 SIPELADYIKVFKPK
Y395 TLKGYKQYWCTFKDT
K562 QMSLIEAKMRFIQAW
Y597 EELIGIAYNRLIRMD
- under review  
  mouse

 
S159-p KKKLDDQsEDEALEL
M172 ELEGPLIMPGSGsIy
S177-p LIMPGSGsIySsPGL
Y179-p MPGSGsIySsPGLyS
S180 PGSGsIySsPGLySK
S181-p GSGsIySsPGLySKT
Y185-p IySsPGLySKTMTPT
Y193 SKTMTPTYDAHDGSP
K247-u QALLDKAkTNQGWLD
K265-u SLMEQDVkENEALLL
K275-u EALLLRFkYYSFFDL
K285-u SFFDLNPkYDAIRIN
S328-p QYHINKLsIMTSENH
S339-p SENHLNNsDKEVDEV
D347 DKEVDEVDAALsDLE
S351-p DEVDAALsDLEITLE
Y378 SIPELADYIKVFKPK
Y395 TLKGYKQYWCTFKDT
K555-u QMSLIEAkMRFIQAW
Y590 EELIGIAYNRLIRMD
S666-p RAKDQNEsLDEEMFY
  rat

 
S159-p KKKLDDQsEDEALEL
M172 ELEGPLIMPGSGSIY
S177 LIMPGSGSIYSSPGL
Y179 MPGSGSIYSSPGLYS
S180 PGSGSIYSSPGLYSK
S181 GSGSIYSSPGLYSKT
Y185 IYSSPGLYSKTMTPT
Y193 SKTMTPTYDAHDGSP
K247 QALLDKAKTNQGWLD
K265 SLMEQDVKENEALLL
K275 EALLLRFKYYSFFDL
K285 SFFDLNPKYDAIRIN
S328 QYHINKLSIMTSENH
S339 SENHLNNSDKEVDEV
D347 DKEVDEVDAALsDLE
S351-p DEVDAALsDLEITLE
Y378-p SIPELADyIKVFKPK
Y395 TLKGYKQYWCTFKDT
K555 QMSLIEAKMRFIQAW
Y590-p EELIGIAyNRLIRMD
S666 RAKDQNESLDEEMFY
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