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Protein Page:
talin 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
talin 2 As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis
Cellular Component: ruffle; focal adhesion; cytoplasm; plasma membrane; synapse; intercellular junction; fascia adherens; actin cytoskeleton
Molecular Function: protein binding; structural constituent of cytoskeleton; actin binding; structural molecule activity; insulin receptor binding
Biological Process: intercellular junction assembly; cytoskeletal anchoring; cell adhesion
Reference #:  Q9Y4G6 (UniProtKB)
Alt. Names/Synonyms: DKFZp451B1011; DKFZp686I0976; DKFZp686K0979; KIAA0320; talin 2; Talin-2; TLN2
Gene Symbols: TLN2
Molecular weight: 271,613 Da
Basal Isoelectric point: 5.4  Predict pI for various phosphorylation states
Select Structure to View Below

talin 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

 
0 49 Y28-p FEPSTAVyDACRVIR
0 13 Y49-p QTGQASDyGLFLSDE
0 5 T69-p IWLEAGRtLDyYMLR
0 22 Y72-p EAGRtLDyYMLRNGD
0 1 T144 EEKKEEGTGtLKKDR
0 3 T146-p KKEEGTGtLKKDRTL
0 1 T192 QGVDENETLLLRRKF
0 4 Y201-p LLRRKFFySDQNVDS
0 1 K337 PRLLGITKDsVMRVD
0 2 S339-p LLGITKDsVMRVDEK
0 5 S428-p TMLEESVsPKKSTIL
0 1 S449 TGKAEHGSVALPAVM
0 1 S460 PAVMRSGSSGPETFN
0 2 S473-p FNVGSMPsPQQQVMV
0 2 S623-p RTLAGAVsDLLKAVQ
0 1 T639-p TSGEPRQtVLTAAGS
0 1 K690 AMLVLKAKNVAQVAE
0 1 S1032 CAKNLATSLAELRTA
0 4 Y1118-p AAQGNEHyTGVAARE
0 4 K1543-u NSTANLVkTIKALDG
0 483 Y1665-p PGQRECDysIDGINR
0 12 S1666-p GQRECDysIDGINRC
0 1 T1793-p GNPKAQHtHDAITEA
0 40 T1843-p MSKLDEGtPPEPKGT
0 3 Y1854-p PKGTFVDyQTTVVKY
0 1 T2282-p KRVAGAVtELIQAAE
0 1 K2477-a NLVRAAQkAAFGKAD
0 3 Y2530-p AQIRQQQyKFLPTEL
  mouse

 
Y28-p FEPSTAVyDACRVIR
Y49 QTGQASDYGLFLSDE
T69 IWLEAGRTLDyYMLR
Y72-p EAGRTLDyYMLRNGD
T144-p EEKKEEGtGtLKKDR
T146-p KKEEGtGtLKKDRTL
T192-p QGVDENEtLLLRRKF
Y201 LLRRKFFYSDQNVDS
K337-u PRLLGITkDSVMRVD
S339 LLGITkDSVMRVDEK
S428-p TMLEESVsPKKSTIL
S449-p TGKAEHGsVALPAVM
S460-p PAVMRSGsSGPETFN
S473-p FNVGSMPsPQQQVMV
S623-p RTLAGAVsDLLKAVQ
T639 TSGEPRQTVLTAAGS
K690-u AMLVLKAkNVAQVAE
S1032-p CAKNLATsLAELRTA
Y1118-p AAQGNEHyTGVAARE
K1543-u NSTANLVkTIKALDG
Y1665-p PGQRECDysIDGINR
S1666-p GQRECDysIDGINRC
T1793 GNPKAQHTHDAITEA
T1843-p MSKLDEGtPPEPKGT
Y1854 PKGTFVDYQTTVVKY
T2282 KRVAGAVTELIQAAE
K2477 NLVRAAQKAAFGKAD
Y2530 AQIRQQQYKFLPTEL
  rat

 
Y30-p FEPSTAVyDACRVIR
Y51-p QTGQASDyGLFLSDE
T71 IWLEAGRTLDYYMLR
Y74 EAGRTLDYYMLRNGD
T146 EEKKEEGTGTLRKDR
T148 KKEEGTGTLRKDRTL
T194 QGVDENETLLLRRKF
Y203 LLRRKFFYSDQNVDS
K339 PRLLGITKDSVMRVD
S341 LLGITKDSVMRVDEK
S430 TMLEESVSPKKSTIL
S451 TGKAEHGSVALPAVM
S462 PAVMRSGSSGPETFN
S475 FNVGSMPSPQQQVMV
S625 RTLAGAVSDLLKAVQ
T641 TSGEPRQTVLTAAGS
K692 AMLVLKAKNVAQVAE
S1034 CAKNLATSLAELRTA
Y1120 AAQGNEHYTGVAARE
K1545 NSTANLVKTIKALDG
Y1667-p PGQRECDySIDGINR
S1668 GQRECDySIDGINRC
T1795 GNPKAQHTHDAITEA
T1845-p MSKLDEGtPPEPKGT
Y1856 PKGTFVDYQTTVVKY
T2284 KRVAGAVTELIQAAE
K2479 NLVRAAQKAAFGKAD
Y2532 AQIRQQQYKFLPTEL
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