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Protein Page:
Kindlin-2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Motility/polarity/chemotaxis; Cytoskeletal protein
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-mediated signaling pathway; integrin activation; 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 1 T32-p TDLNRDVtLRVtGEV
0 1 T36-p RDVtLRVtGEVHIGG
0 1 K56-ac VEKLDVKkDWsDHAL
0 1 S59-p LDVKkDWsDHALWWE
0 1 K68-ac HALWWEKkRTWLLKT
0 1 T129-p AVSDICKtFNIRHPE
0 22 S159-p KKKLDDQsEDEALEL
0 3 T172-p ELEGPLItPGsGsIy
0 1 S175-p GPLItPGsGsIyssP
0 2 S177-p LItPGsGsIyssPGL
0 76 Y179-p tPGsGsIyssPGLys
0 3 S180-p PGsGsIyssPGLysK
0 6 S181-p GsGsIyssPGLysKT
0 10 Y185-p IyssPGLysKTMTPt
0 2 S186-p yssPGLysKTMTPty
0 1 T192-p ysKTMTPtyDAHDGs
0 3 Y193-p sKTMTPtyDAHDGsP
0 1 S199-p tyDAHDGsPLSPtSA
0 1 T204-p DGsPLSPtSAWFGDS
0 1 K245 KPQALLDKAKINQGW
0 1 K247 QALLDKAKINQGWLD
0 1 K247 QALLDKAKINQGWLD
0 1 S258-p GWLDSSRsLMEQDVK
0 1 K265 sLMEQDVKENEALLL
0 1 K275 EALLLRFKYYSFFDL
0 1 K285-ac SFFDLNPkYDAIRIN
0 2 K285-ub SFFDLNPkYDAIRIN
0 1 S328 QYHINKLSIMTSENH
0 1 S332 NKLSIMTSENHLNNs
0 8 S339-p SENHLNNsDKEVDEV
0 1 D347-ca DKEVDEVdAALsDLE
0 11 S351-p DEVdAALsDLEITLE
0 7 Y378-p SIPELADyIKVFKPK
0 2 Y395-p TLKGYKQyWCTFKDT
0 1 S403-p WCTFKDTsISCYKSK
0 1 S409 TsISCYKSKEESsGt
0 1 S414-p YKSKEESsGtPAHQM
0 2 T416-p SKEESsGtPAHQMNL
0 1 S435-p VTPDVNIsGQKFNIK
0 2 S523-p ITPECLVsPRYLKKY
0 1 K555 QMSLIEAKMRFIQAW
0 321 Y590-p EELIGIAyNRLIRMD
0 15 S666-p RAKDQNEsLDEEMFY
  Kindlin-2 iso2  
T32 TDLNRDVTLRVTGEV
T36 RDVTLRVTGEVHIGG
K56 VEKLDVKKDWSDHAL
S59 LDVKKDWSDHALWWE
K68 HALWWEKKRTWLLKT
T129 AVSDICKTFNIRHPE
S159 KKKLDDQSEDEALEL
T172 ELEGPLITPGSGSIY
S175 GPLITPGSGSIYSSP
S177 LITPGSGSIYSSPGL
Y179 TPGSGSIYSSPGLYS
S180 PGSGSIYSSPGLYSK
S181 GSGSIYSSPGLYSKT
Y185 IYSSPGLYSKTMTPT
S186 YSSPGLYSKTMTPTY
T192 YSKTMTPTYDAHDGS
Y193 SKTMTPTYDAHDGSP
S199 TYDAHDGSPLSPTSA
T204 DGSPLSPTSAWFGDS
K245 KPQALLDKAKINQGW
K247 QALLDKAKINQGWLD
K247 QALLDKAKINQGWLD
S258 GWLDSSRSLMEQDVK
K265 SLMEQDVKENEALLL
K275 EALLLRFKYYSFFDL
K285 SFFDLNPKYDAIRIN
K285 SFFDLNPKYDAIRIN
S328 QYHINKLSIMTSENH
S332 NKLSIMTSENHLNNS
S339 SENHLNNSDKEVDEV
D347 DKEVDEVDAALSDLE
S351 DEVDAALSDLEITLE
Y378 SIPELADYIKVFKPK
Y395 TLKGYKQYWCTFKDT
S403 WCTFKDTSISCYKSK
S409 TSISCYKSKEESSGT
S414 YKSKEESSGTPAHQM
T416 SKEESSGTPAHQMNL
S435 VTPDVNISGQKFNIK
S523-p ITPECLVsPRYLKKY
K562 QMSLIEAKMRFIQAW
Y597 EELIGIAYNRLIRMD
- gap
  mouse

 
T32 TDLNRDVTLRVTGEV
T36 RDVTLRVTGEVHIGG
K56 VEKLDVKKDWSDHAL
S59 LDVKKDWSDHALWWE
K68 HALWWEKKRTWLLKT
T129 AVSDICKTFNIRHPE
S159-p KKKLDDQsEDEALEL
M172 ELEGPLIMPGSGsIy
S175 GPLIMPGSGsIySsP
S177-p LIMPGSGsIySsPGL
Y179-p MPGSGsIySsPGLyS
S180 PGSGsIySsPGLySK
S181-p GSGsIySsPGLySKT
Y185-p IySsPGLySKTMTPt
S186 ySsPGLySKTMTPtY
T192-p ySKTMTPtYDAHDGs
Y193 SKTMTPtYDAHDGsP
S199-p tYDAHDGsPLSPTSA
T204 DGsPLSPTSAWFGDS
K245-ac KPQALLDkAkTNQGW
K247-ac QALLDkAkTNQGWLD
K247-ub QALLDkAkTNQGWLD
S258 GWLDSSRSLMEQDVk
K265-ub SLMEQDVkENEALLL
K275-ub EALLLRFkYYSFFDL
K285 SFFDLNPKYDAIRIN
K285-ub SFFDLNPkYDAIRIN
S328-p QYHINKLsIMTsENH
S332-p NKLsIMTsENHLNNs
S339-p sENHLNNsDKEVDEV
D347 DKEVDEVDAALsDLE
S351-p DEVDAALsDLEITLE
Y378 SIPELADYIKVFKPK
Y395 TLKGYKQYWCTFKDT
S403 WCTFKDTSISCYKsR
S409-p TSISCYKsREESSGt
S414 YKsREESSGtPAHQL
T416-p sREESSGtPAHQLNL
S435 VTPDVNISGQKFNIK
S523 VNPECLVSPRYLKKY
K555-ub QMSLIEAkMRFIQAW
Y590 EELIGIAYNRLIRMD
S666-p RAKDQNEsLDEEMFY
  rat

 
T32 TDLNRDVTLRVTGEV
T36 RDVTLRVTGEVHIGG
K56 VEKLDVKKDWSDHAL
S59 LDVKKDWSDHALWWE
K68 HALWWEKKKTWLLKT
T129 AVSDICKTFNIRHPE
S159-p KKKLDDQsEDEALEL
M172 ELEGPLIMPGSGSIY
S175 GPLIMPGSGSIYSSP
S177 LIMPGSGSIYSSPGL
Y179 MPGSGSIYSSPGLYS
S180 PGSGSIYSSPGLYSK
S181 GSGSIYSSPGLYSKT
Y185 IYSSPGLYSKTMTPT
S186 YSSPGLYSKTMTPTY
T192 YSKTMTPTYDAHDGS
Y193 SKTMTPTYDAHDGSP
S199 TYDAHDGSPLSPTSA
T204 DGSPLSPTSAWFGDS
K245 KPQALLDKAKTNQGW
K247 QALLDKAKTNQGWLD
K247 QALLDKAKTNQGWLD
S258 GWLDSSRSLMEQDVK
K265 SLMEQDVKENEALLL
K275 EALLLRFKYYSFFDL
K285-ac SFFDLNPkYDAIRIN
K285 SFFDLNPKYDAIRIN
S328 QYHINKLSIMTSENH
S332 NKLSIMTSENHLNNs
S339-p SENHLNNsDKEVDEV
D347 DKEVDEVDAALsDLE
S351-p DEVDAALsDLEITLE
Y378-p SIPELADyIKVFKPK
Y395 TLKGYKQYWCTFKDT
S403 WCTFKDTSISCYKSR
S409 TSISCYKSREEASGT
S414 YKSREEASGTPAHQM
T416 SREEASGTPAHQMNL
S435 VTPDVNISGQKFNIK
S523 INPECLVSPRYLKKY
K555 QMSLIEAKMRFIQAW
Y590-p EELIGIAyNRLIRMD
S666-p RAKDQNEsLDEEMFY
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