TLN2_MOUSE - dbPTM
TLN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLN2_MOUSE
UniProt AC Q71LX4
Protein Name Talin-2
Gene Name Tln2
Organism Mus musculus (Mouse).
Sequence Length 2375
Subcellular Localization Cytoplasm . Cell junction, focal adhesion . Cell junction, synapse . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytoskeleton . Focal adhesion plaques and synapses.
Protein Description 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 (By similarity)..
Protein Sequence MVALSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEYKKKQRPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKKQSKDRFGLEGDEESTMLEESVSPKKRSTILQQQFNRTGKAEHGSVALPAVMRSGSSGPETFNVGSMPSPQQQVMVGQMHRGHMPPLTSAQQALMGTINTSMHAVQQAQDDLSELDSLPPLGQDMASRVWVQNKVDESKHEIHSQVDAITAGTASVVNLTAGDPADTDYTAVGCAITTISSNLTEMSKGVKLLAALMDDDVGSGEDLLRAARTLAGAVSDLLKAVQPTSGEPRQTVLTAAGSIGQASGDLLRQIGENETDERFQDVLMSLAKAVANAAAMLVLKAKNVAQVAEDTVLQNRVIAAATQCALSTSQLVACAKVVSPTISSPVCQEQLIEAGKLVDRSVENCVRACQAATSDSELLKQVSAAASVVSQALHDLLQHVRQFASRGEPIGRYDQATDTIMCVTESIFSSMGDAGEMVRQARVLAQATSDLVNAMRSDAEAEIDMENSKKLLAAAKLLADSTARMVEAAKGAAANPENEDQQQRLREAAEGLRVATNAAAQNAIKKKIVNRLEVAAKQAAAAATQTIAASQNAAISNKNPSAQQQLVQSCKAVADHIPQLVQGVRGSQAQAEDLSAQLALIISSQNFLQPGSKMVSSAKAAVPTVSDQAAAMQLSQCAKNLATSLAELRTASQKAHEACGPMEIDSALNTVQTLKNELQDAKMAAAESQLKPLPGETLEKCAQDLGSTSKGVGSSMAQLLTCAAQGNEHYTGVAARETAQALKTLAQAARGVAASTNDPEAAHAMLDSARDVMEGSAMLIQEAKQALIAPGDTESQQRLAQVAKAVSHSLNNCVNCLPGQKDVDVALKSIGEASKKLLVDSLPPSTKPFQEAQSELNQAAADLNQSAGEVVHATRGQSGELAAASGKFSDDFDEFLDAGIEMAGQAQTKEDQMQVIGNLKNISMASSKLLLAAKSLSVDPGAPNAKNLLAAAARAVTESINQLIMLCTQQAPGQKECDNALRELETVKGMLENPNEPVSDLSYFDCIESVMENSKVLGESMAGISQNAKTGDLPAFGECVGIASKALCGLTEAAAQAAYLVGISDPNSQAGHQGLVDPIQFARANQAIQMACQNLVDPGSSPSQVLSAATIVAKHTSALCNACRIASSKTANPVAKRHFVQSAKEVANSTANLVKTIKALDGDFSEDNRNKCRIATTPLIEAVENLTAFASNPEFASIPAQISSEGSQAQEPILVSAKTMLESSSYLIRTARSLAINPKDPPTWSVLAGHSHTVSDSIKSLITSIRDKAPGQRECDYSIDGINRCIRDIEQASLAAVSQSLATRDDISVEALQEQLTSVVQEIGHLIDPIATAARGEAAQLGHKVTQLASYFEPLILAAVGVASKMLDHQQQMTVLDQTKTLAESALQMLYAAKEGGGNPKAVHTAPEPKGTFVDYQTTVVKYSKAIAVTAQEMIGFQIRTRVQDLGHGCIFLVQKAGALQVCPTDSYTKRELIECARSVTEKVSLVLSALQAGNKGTQACITAATAVSGIIADLDTTIMFATAGTLNAENGETFADHRENILKTAKALVEDTKLLVSGAASTPDKLAQAAQSSAATITQLAEVVKLGAASLGSNDPETQVVLINAIKDVAKALSDLIGATKGAASKPADDPSMYQLKGAAKVMVTNVTSLLKTVKAVEDEATRGTRALEATIEYIKQELTVFQSKDIPEKTSSPEESIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRKAVSDMLIACKQASFYPDVSEEVRTRALRYGTECTLGYLDLLEHVLVILQKPTPELKHQLAAFSKRVAGAVTELIQAAEAMKGTEWVDPEDPTVIAETELLGAAASIEAAAKKLEQLKPRAKPKQADETLDFEEQILEAAKSIAAATSALVKSASAAQRELVAQGKVGSIPANAADDGQWSQGLISAARMVAAATSSLCEAANASVQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
18PhosphorylationRHCNVVKTMQFEPST
HHCCEEEEECCCCCH		12.4728576409
24PhosphorylationKTMQFEPSTAVYDAC
EEECCCCCHHHHHHH		23.0817242355
25PhosphorylationTMQFEPSTAVYDACR
EECCCCCHHHHHHHH		30.7528576409
28PhosphorylationFEPSTAVYDACRVIR
CCCCHHHHHHHHHHH		8.7226032504
69PhosphorylationIWLEAGRTLDYYMLR
EEEECCCCEEEEEHH		24.0626239621
72PhosphorylationEAGRTLDYYMLRNGD
ECCCCEEEEEHHCCC		8.22-
144PhosphorylationEEKKEEGTGTLKKDR
HHHHHHCCCCCCCCH		30.2126824392
146PhosphorylationKKEEGTGTLKKDRTL
HHHHCCCCCCCCHHH		34.9326824392
152PhosphorylationGTLKKDRTLLRDERK
CCCCCCHHHHHCHHH		40.0326824392
192PhosphorylationQGVDENETLLLRRKF
CCCCCCCCEEEEEHH		34.0020415495
201PhosphorylationLLRRKFFYSDQNVDS
EEEEHHHHCCCCCCC		17.9229514104
337UbiquitinationPRLLGITKDSVMRVD
HHHHCCCHHHEECCC		46.19-
426PhosphorylationESTMLEESVSPKKRS
HHHHHHHCCCHHHHH		20.6525521595
428PhosphorylationTMLEESVSPKKRSTI
HHHHHCCCHHHHHHH		40.0425521595
443PhosphorylationLQQQFNRTGKAEHGS
HHHHHHCCCCCCCCC		44.1025777480
450PhosphorylationTGKAEHGSVALPAVM
CCCCCCCCCCHHCHH		13.2122817900
459PhosphorylationALPAVMRSGSSGPET
CHHCHHCCCCCCCCC		25.5724899341
461PhosphorylationPAVMRSGSSGPETFN
HCHHCCCCCCCCCCC		33.1123737553
462PhosphorylationAVMRSGSSGPETFNV
CHHCCCCCCCCCCCC		62.9923737553
466PhosphorylationSGSSGPETFNVGSMP
CCCCCCCCCCCCCCC		24.5225521595
471PhosphorylationPETFNVGSMPSPQQQ
CCCCCCCCCCCHHHE		24.2027742792
474PhosphorylationFNVGSMPSPQQQVMV
CCCCCCCCHHHEEEH		27.0527180971
586PhosphorylationCAITTISSNLTEMSK
HHHHHHHCCHHHHHH		31.82-
589PhosphorylationTTISSNLTEMSKGVK
HHHHCCHHHHHHHHH		33.61-
624PhosphorylationRTLAGAVSDLLKAVQ
HHHHHHHHHHHHHHC		23.2322817900
634PhosphorylationLKAVQPTSGEPRQTV
HHHHCCCCCCCCCHH		48.0921454597
643PhosphorylationEPRQTVLTAAGSIGQ
CCCCHHHHHHHHHHH		15.3225338131
647PhosphorylationTVLTAAGSIGQASGD
HHHHHHHHHHHHHHH		20.8627180971
691UbiquitinationAMLVLKAKNVAQVAE
HHHHHHHCCHHHHHH		50.82-
728PhosphorylationVACAKVVSPTISSPV
HHHHHHHCCCCCCHH		21.2225195567
733PhosphorylationVVSPTISSPVCQEQL
HHCCCCCCHHHHHHH		19.9425195567
763PhosphorylationRACQAATSDSELLKQ
HHHHHCCCCHHHHHH		34.1228973931
765PhosphorylationCQAATSDSELLKQVS
HHHCCCCHHHHHHHH		29.8825521595
846PhosphorylationDLVNAMRSDAEAEID
HHHHHHHCCCCHHCC		28.2527180971
870PhosphorylationAAKLLADSTARMVEA
HHHHHHHHHHHHHHH		20.5426239621
871PhosphorylationAKLLADSTARMVEAA
HHHHHHHHHHHHHHH		20.8726239621
1024PhosphorylationQAAAMQLSQCAKNLA
HHHHHHHHHHHHHHH		13.30-
1032PhosphorylationQCAKNLATSLAELRT
HHHHHHHHHHHHHHH		27.6926824392
1033PhosphorylationCAKNLATSLAELRTA
HHHHHHHHHHHHHHH		21.7027180971
1119PhosphorylationAAQGNEHYTGVAARE
HHHCCCCCCHHHHHH		10.06-
1267PhosphorylationVHATRGQSGELAAAS
HHHCCCCCCCCHHHC		36.7428464351
1326PhosphorylationLLAAKSLSVDPGAPN
HHHHHHCCCCCCCCC		31.4027180971
1356S-palmitoylationINQLIMLCTQQAPGQ
HHHHHHHHHCCCCCH		1.4628680068
1506PhosphorylationTIVAKHTSALCNACR
HHHHHHHHHHHHHHH		20.97-
1538PhosphorylationSAKEVANSTANLVKT
HHHHHHHHHHHHHHH		21.1129514104
1544UbiquitinationNSTANLVKTIKALDG
HHHHHHHHHHHHHCC		47.93-
1644PhosphorylationAGHSHTVSDSIKSLI
CCCCCCHHHHHHHHH		27.1325338131
1666PhosphorylationPGQRECDYSIDGINR
CCCCCCCCCCCCHHH		21.1317242355
1667PhosphorylationGQRECDYSIDGINRC
CCCCCCCCCCCHHHH		10.8425521595
1843PhosphorylationGHGCIFLVQKAGALQ
CCCCEEEEEECCCCE		3.69-
1947PhosphorylationEDTKLLVSGAASTPD
HCCEEECCCCCCCHH		23.7629472430
1951PhosphorylationLLVSGAASTPDKLAQ
EECCCCCCCHHHHHH		39.6823737553
1952PhosphorylationLVSGAASTPDKLAQA
ECCCCCCCHHHHHHH		30.6826824392
1963PhosphorylationLAQAAQSSAATITQL
HHHHHHHHCHHHHHH		15.16-
1980PhosphorylationVVKLGAASLGSNDPE
HHHHCHHHCCCCCHH		32.50-
2035PhosphorylationGAAKVMVTNVTSLLK
HHHHHEEEEHHHHHH		13.0820531401
2038PhosphorylationKVMVTNVTSLLKTVK
HHEEEEHHHHHHHHH		18.7429472430
2039PhosphorylationVMVTNVTSLLKTVKA
HEEEEHHHHHHHHHH		27.6727180971
2042UbiquitinationTNVTSLLKTVKAVED
EEHHHHHHHHHHHHH		57.47-
2043PhosphorylationNVTSLLKTVKAVEDE
EHHHHHHHHHHHHHH		27.4922871156
2082PhosphorylationKDIPEKTSSPEESIR
CCCCCCCCCHHHHHH		55.7729899451
2083PhosphorylationDIPEKTSSPEESIRM
CCCCCCCCHHHHHHH		41.3825521595
2100UbiquitinationGITMATAKAVAAGNS
CCHHHHHHHHHCCCC		38.75-
2234AcetylationSIEAAAKKLEQLKPR
HHHHHHHHHHHCCCC		53.1622826441
2239AcetylationAKKLEQLKPRAKPKQ
HHHHHHCCCCCCCCC		31.9522826441
2263PhosphorylationQILEAAKSIAAATSA
HHHHHHHHHHHHHHH		16.8426824392
2316PhosphorylationARMVAAATSSLCEAA
HHHHHHHHHHHHHHH		17.7022871156
2338PhosphorylationASEEKLISSAKQVAA
CCHHHHHHHHHHHHH		34.3820139300
2339PhosphorylationSEEKLISSAKQVAAS
CHHHHHHHHHHHHHH		32.2722871156
2531Methylation-------------------------------------------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------------------------------------------------------------------		-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TLN2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLN2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TLN2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TLN2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND TYR-1666, ANDMASS SPECTROMETRY.

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