TLN2_HUMAN - dbPTM
TLN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TLN2_HUMAN
UniProt AC Q9Y4G6
Protein Name Talin-2
Gene Name TLN2
Organism Homo sapiens (Human).
Sequence Length 2542
Subcellular Localization Cytoplasm . Cell junction, focal adhesion . Cell junction, synapse . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytoskeleton . Focal adhesion plaques and synapses (PubMed:12422219).
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 MVALSLKICVRHCNVVKTMQFEPSTAVYDACRVIRERVPEAQTGQASDYGLFLSDEDPRKGIWLEAGRTLDYYMLRNGDILEYKKKQRPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKKQSKDRFGLEGDEESTMLEESVSPKKSTILQQQFNRTGKAEHGSVALPAVMRSGSSGPETFNVGSMPSPQQQVMVGQMHRGHMPPLTSAQQALMGTINTSMHAVQQAQDDLSELDSLPPLGQDMASRVWVQNKVDESKHEIHSQVDAITAGTASVVNLTAGDPADTDYTAVGCAITTISSNLTEMSKGVKLLAALMDDEVGSGEDLLRAARTLAGAVSDLLKAVQPTSGEPRQTVLTAAGSIGQASGDLLRQIGENETDERFQDVLMSLAKAVANAAAMLVLKAKNVAQVAEDTVLQNRVIAAATQCALSTSQLVACAKVVSPTISSPVCQEQLIEAGKLVDRSVENCVRACQAATTDSELLKQVSAAASVVSQALHDLLQHVRQFASRGEPIGRYDQATDTIMCVTESIFSSMGDAGEMVRQARVLAQATSDLVNAMRSDAEAEIDMENSKKLLAAAKLLADSTARMVEAAKGAAANPENEDQQQRLREAAEGLRVATNAAAQNAIKKKIVNRLEVAAKQAAAAATQTIAASQNAAVSNKNPAAQQQLVQSCKAVADHIPQLVQGVRGSQAQAEDLSAQLALIISSQNFLQPGSKMVSSAKAAVPTVSDQAAAMQLSQCAKNLATSLAELRTASQKAHEACGPMEIDSALNTVQTLKNELQDAKMAAVESQLKPLPGETLEKCAQDLGSTSKAVGSSMAQLLTCAAQGNEHYTGVAARETAQALKTLAQAARGVAASTTDPAAAHAMLDSARDVMEGSAMLIQEAKQALIAPGDAERQQRLAQVAKAVSHSLNNCVNCLPGQKDVDVALKSIGESSKKLLVDSLPPSTKPFQEAQSELNQAAADLNQSAGEVVHATRGQSGELAAASGKFSDDFDEFLDAGIEMAGQAQTKEDQIQVIGNLKNISMASSKLLLAAKSLSVDPGAPNAKNLLAAAARAVTESINQLITLCTQQAPGQKECDNALRELETVKGMLDNPNEPVSDLSYFDCIESVMENSKVLGESMAGISQNAKTGDLPAFGECVGIASKALCGLTEAAAQAAYLVGISDPNSQAGHQGLVDPIQFARANQAIQMACQNLVDPGSSPSQVLSAATIVAKHTSALCNACRIASSKTANPVAKRHFVQSAKEVANSTANLVKTIKALDGDFSEDNRNKCRIATAPLIEAVENLTAFASNPEFVSIPAQISSEGSQAQEPILVSAKTMLESSSYLIRTARSLAINPKDPPTWSVLAGHSHTVSDSIKSLITSIRDKAPGQRECDYSIDGINRCIRDIEQASLAAVSQSLATRDDISVEALQEQLTSVVQEIGHLIDPIATAARGEAAQLGHKVTQLASYFEPLILAAVGVASKILDHQQQMTVLDQTKTLAESALQMLYAAKEGGGNPKAQHTHDAITEAAQLMKEAVDDIMVTLNEAASEVGLVGGMVDAIAEAMSKLDEGTPPEPKGTFVDYQTTVVKYSKAIAVTAQEMMTKSVTNPEELGGLASQMTSDYGHLAFQGQMAAATAEPEEIGFQIRTRVQDLGHGCIFLVQKAGALQVCPTDSYTKRELIECARAVTEKVSLVLSALQAGNKGTQACITAATAVSGIIADLDTTIMFATAGTLNAENSETFADHRENILKTAKALVEDTKLLVSGAASTPDKLAQAAQSSAATITQLAEVVKLGAASLGSDDPETQVVLINAIKDVAKALSDLISATKGAASKPVDDPSMYQLKGAAKVMVTNVTSLLKTVKAVEDEATRGTRALEATIECIKQELTVFQSKDVPEKTSSPEESIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRKAVSDMLTACKQASFHPDVSDEVRTRALRFGTECTLGYLDLLEHVLVILQKPTPEFKQQLAAFSKRVAGAVTELIQAAEAMKGTEWVDPEDPTVIAETELLGAAASIEAAAKKLEQLKPRAKPKQADETLDFEEQILEAAKSIAAATSALVKSASAAQRELVAQGKVGSIPANAADDGQWSQGLISAARMVAAATSSLCEAANASVQGHASEEKLISSAKQVAASTAQLLVACKVKADQDSEAMRRLQAAGNAVKRASDNLVRAAQKAAFGKADDDDVVVKTKFVGGIAQIIAAQEEMLKKERELEEARKKLAQIRQQQYKFLPTELREDEG
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
5Phosphorylation---MVALSLKICVRH
---CCCHHHEHHHHH
20.2024719451
17MalonylationVRHCNVVKTMQFEPS
HHHCCEEEEECCCCC
33.7226320211
17UbiquitinationVRHCNVVKTMQFEPS
HHHCCEEEEECCCCC
33.7229967540
18PhosphorylationRHCNVVKTMQFEPST
HHCCEEEEECCCCCH
12.4726074081
24PhosphorylationKTMQFEPSTAVYDAC
EEECCCCCHHHHHHH
23.0826074081
25PhosphorylationTMQFEPSTAVYDACR
EECCCCCHHHHHHHH
30.7526074081
28PhosphorylationFEPSTAVYDACRVIR
CCCCHHHHHHHHHHH
8.7225884760
49PhosphorylationQTGQASDYGLFLSDE
CCCCCCCCCCCCCCC
17.1522817900
69PhosphorylationIWLEAGRTLDYYMLR
EEEECCCCEEEEEHH
24.06-
72PhosphorylationEAGRTLDYYMLRNGD
ECCCCEEEEEHHCCC
8.2225884760
73PhosphorylationAGRTLDYYMLRNGDI
CCCCEEEEEHHCCCH
6.8527642862
109PhosphorylationVMVDDSKTVGELLVT
EEECCCCCHHHHHHH
37.3829083192
116PhosphorylationTVGELLVTICSRIGI
CHHHHHHHHHHHCCC
19.0829083192
119PhosphorylationELLVTICSRIGITNY
HHHHHHHHHCCCCCH
24.0729083192
144PhosphorylationEEKKEEGTGTLKKDR
HHHHHHCCCCCCCCH
30.2123403867
146PhosphorylationKKEEGTGTLKKDRTL
HHHHCCCCCCCCHHH
34.9323403867
152PhosphorylationGTLKKDRTLLRDERK
CCCCCCHHHHHCHHH
40.0326437602
166UbiquitinationKMEKLKAKLHTDDDL
HHHHHHHHCCCCCCC
38.9329967540
169PhosphorylationKLKAKLHTDDDLNWL
HHHHHCCCCCCCHHH
52.1120068231
179PhosphorylationDLNWLDHSRTFREQG
CCHHHHHCHHHHHCC
32.4620068231
192PhosphorylationQGVDENETLLLRRKF
CCCCCCCCEEEEEHH
34.0028857561
201PhosphorylationLLRRKFFYSDQNVDS
EEEEHHHHCCCCCCC
17.9222817900
307PhosphorylationKYVKLARSLRTYGVS
HHHHHHHHHHHHCCE
19.3223312004
310PhosphorylationKLARSLRTYGVSFFL
HHHHHHHHHCCEEEE
29.8923882029
311PhosphorylationLARSLRTYGVSFFLV
HHHHHHHHCCEEEEE
14.75-
314PhosphorylationSLRTYGVSFFLVKEK
HHHHHCCEEEEECHH
13.10-
327UbiquitinationEKMKGKNKLVPRLLG
HHHCCCCCCHHHHHC
55.1127667366
336PhosphorylationVPRLLGITKDSVMRV
HHHHHCCCHHHEECC
27.31-
337UbiquitinationPRLLGITKDSVMRVD
HHHHCCCHHHEECCC
46.1930230243
339PhosphorylationLLGITKDSVMRVDEK
HHCCCHHHEECCCHH
21.26-
365PhosphorylationTVKRWAASPKSFTLD
HHHHHCCCCCEEEEC
25.7224719451
420PhosphorylationGLEGDEESTMLEESV
CCCCCHHHHHHHCCC
19.6430576142
421PhosphorylationLEGDEESTMLEESVS
CCCCHHHHHHHCCCC
29.1130576142
426PhosphorylationESTMLEESVSPKKST
HHHHHHCCCCCCHHH
20.6530576142
428PhosphorylationTMLEESVSPKKSTIL
HHHHCCCCCCHHHHH
40.0419664994
432PhosphorylationESVSPKKSTILQQQF
CCCCCCHHHHHHHHH
27.1428857561
433PhosphorylationSVSPKKSTILQQQFN
CCCCCHHHHHHHHHH
34.2928857561
442PhosphorylationLQQQFNRTGKAEHGS
HHHHHHCCCCCCCCC
44.1028555341
449PhosphorylationTGKAEHGSVALPAVM
CCCCCCCCCCHHCHH
13.2128857561
458PhosphorylationALPAVMRSGSSGPET
CHHCHHCCCCCCCCC
25.5726657352
460PhosphorylationPAVMRSGSSGPETFN
HCHHCCCCCCCCCCC
33.1122199227
461PhosphorylationAVMRSGSSGPETFNV
CHHCCCCCCCCCCCC
62.9922199227
465PhosphorylationSGSSGPETFNVGSMP
CCCCCCCCCCCCCCC
24.5222199227
470PhosphorylationPETFNVGSMPSPQQQ
CCCCCCCCCCCHHHE
24.2028857561
473PhosphorylationFNVGSMPSPQQQVMV
CCCCCCCCHHHEEEH
27.0522199227
521PhosphorylationDDLSELDSLPPLGQD
HCHHHHHCCCCCCCC
56.2324275569
623PhosphorylationRTLAGAVSDLLKAVQ
HHHHHHHHHHHHHHC
23.2327251275
632PhosphorylationLLKAVQPTSGEPRQT
HHHHHCCCCCCCCCH
32.07-
633PhosphorylationLKAVQPTSGEPRQTV
HHHHCCCCCCCCCHH
48.09-
639PhosphorylationTSGEPRQTVLTAAGS
CCCCCCCHHHHHHHH
20.8220068231
642PhosphorylationEPRQTVLTAAGSIGQ
CCCCHHHHHHHHHHH
15.3220068231
646PhosphorylationTVLTAAGSIGQASGD
HHHHHHHHHHHHHHH
20.8620068231
651PhosphorylationAGSIGQASGDLLRQI
HHHHHHHHHHHHHHH
25.5920068231
673PhosphorylationRFQDVLMSLAKAVAN
HHHHHHHHHHHHHHH
22.48-
690UbiquitinationAMLVLKAKNVAQVAE
HHHHHHHCCHHHHHH
50.8229967540
727PhosphorylationVACAKVVSPTISSPV
HHHHHHHCCCCCCHH
21.2229802988
729PhosphorylationCAKVVSPTISSPVCQ
HHHHHCCCCCCHHHH
26.4528348404
731PhosphorylationKVVSPTISSPVCQEQ
HHHCCCCCCHHHHHH
30.9428348404
732PhosphorylationVVSPTISSPVCQEQL
HHCCCCCCHHHHHHH
19.9429802988
761PhosphorylationVRACQAATTDSELLK
HHHHHHCCCCHHHHH
33.8629396449
762PhosphorylationRACQAATTDSELLKQ
HHHHHCCCCHHHHHH
32.5729396449
764PhosphorylationCQAATTDSELLKQVS
HHHCCCCHHHHHHHH
28.2229396449
845PhosphorylationDLVNAMRSDAEAEID
HHHHHHHCCCCHHCC
28.2527251275
878UbiquitinationARMVEAAKGAAANPE
HHHHHHHHHHHCCCC
57.0129967540
1000PhosphorylationQNFLQPGSKMVSSAK
CCCCCCCCHHHHCCH
25.02-
1004PhosphorylationQPGSKMVSSAKAAVP
CCCCHHHHCCHHHCC
22.53-
1005PhosphorylationPGSKMVSSAKAAVPT
CCCHHHHCCHHHCCC
23.52-
1023PhosphorylationQAAAMQLSQCAKNLA
HHHHHHHHHHHHHHH
13.3028857561
1031PhosphorylationQCAKNLATSLAELRT
HHHHHHHHHHHHHHH
27.6925850435
1032PhosphorylationCAKNLATSLAELRTA
HHHHHHHHHHHHHHH
21.7025850435
1118PhosphorylationAAQGNEHYTGVAARE
HHHCCCCCCHHHHHH
10.0626356563
1119PhosphorylationAQGNEHYTGVAARET
HHCCCCCCHHHHHHH
27.3926356563
1156PhosphorylationAAHAMLDSARDVMEG
HHHHHHHHHHHHHHH
22.6520068231
1195PhosphorylationAQVAKAVSHSLNNCV
HHHHHHHHHHHHHHC
16.5327251275
1197PhosphorylationVAKAVSHSLNNCVNC
HHHHHHHHHHHHCCC
25.8627251275
1266PhosphorylationVHATRGQSGELAAAS
HHHCCCCCCCCHHHC
36.7427251275
1271UbiquitinationGQSGELAAASGKFSD
CCCCCCHHHCCCCCC
18.1323000965
1277PhosphorylationAAASGKFSDDFDEFL
HHHCCCCCCCHHHHH
39.49-
1277UbiquitinationAAASGKFSDDFDEFL
HHHCCCCCCCHHHHH
39.4923000965
1296PhosphorylationEMAGQAQTKEDQIQV
HHCCCCCCHHHHHHH
39.14-
1311PhosphorylationIGNLKNISMASSKLL
HHCHHHHHHHHHHHH
20.0721964256
1316UbiquitinationNISMASSKLLLAAKS
HHHHHHHHHHHHHHH
40.4323000965
1322UbiquitinationSKLLLAAKSLSVDPG
HHHHHHHHHCCCCCC
46.4523000965
1325PhosphorylationLLAAKSLSVDPGAPN
HHHHHHCCCCCCCCC
31.4028348404
1408PhosphorylationNSKVLGESMAGISQN
CCCHHCCHHHCCCCC
16.4827251275
1488PhosphorylationQNLVDPGSSPSQVLS
HHCCCCCCCHHHHHH
44.4528348404
1489PhosphorylationNLVDPGSSPSQVLSA
HCCCCCCCHHHHHHH
34.1928348404
1498UbiquitinationSQVLSAATIVAKHTS
HHHHHHHHHHHHHHH
18.7221890473
1501UbiquitinationLSAATIVAKHTSALC
HHHHHHHHHHHHHHH
8.2823000965
1504PhosphorylationATIVAKHTSALCNAC
HHHHHHHHHHHHHHH
18.2627732954
1505PhosphorylationTIVAKHTSALCNACR
HHHHHHHHHHHHHHH
20.9727732954
1537PhosphorylationSAKEVANSTANLVKT
HHHHHHHHHHHHHHH
21.1124275569
1543AcetylationNSTANLVKTIKALDG
HHHHHHHHHHHHHCC
47.9322648109
1543MalonylationNSTANLVKTIKALDG
HHHHHHHHHHHHHCC
47.9326320211
1543UbiquitinationNSTANLVKTIKALDG
HHHHHHHHHHHHHCC
47.9323000965
1546UbiquitinationANLVKTIKALDGDFS
HHHHHHHHHHCCCCC
48.4023000965
1611PhosphorylationSAKTMLESSSYLIRT
EHHHHHHCCCHHHHH
22.1827174698
1612PhosphorylationAKTMLESSSYLIRTA
HHHHHHCCCHHHHHH
17.3927174698
1613PhosphorylationKTMLESSSYLIRTAR
HHHHHCCCHHHHHHH
32.9827174698
1614PhosphorylationTMLESSSYLIRTARS
HHHHCCCHHHHHHHH
14.2227174698
1618PhosphorylationSSSYLIRTARSLAIN
CCCHHHHHHHHHCCC
21.3027174698
1621O-linked_GlycosylationYLIRTARSLAINPKD
HHHHHHHHHCCCCCC
21.4930379171
1641PhosphorylationVLAGHSHTVSDSIKS
HHCCCCCCHHHHHHH
25.3923403867
1643PhosphorylationAGHSHTVSDSIKSLI
CCCCCCHHHHHHHHH
27.1326657352
1645PhosphorylationHSHTVSDSIKSLITS
CCCCHHHHHHHHHHH
25.1423403867
1651PhosphorylationDSIKSLITSIRDKAP
HHHHHHHHHHHHCCC
24.3220068231
1652PhosphorylationSIKSLITSIRDKAPG
HHHHHHHHHHHCCCC
14.5020068231
1665PhosphorylationPGQRECDYSIDGINR
CCCCCCCCCCCCHHH
21.1321082442
1666PhosphorylationGQRECDYSIDGINRC
CCCCCCCCCCCHHHH
10.8428152594
1686PhosphorylationQASLAAVSQSLATRD
HHHHHHHHHHHCCCC
14.8822210691
1793PhosphorylationGNPKAQHTHDAITEA
CCCCHHHHHHHHHHH
14.9020068231
1798PhosphorylationQHTHDAITEAAQLMK
HHHHHHHHHHHHHHH
22.6920068231
1838AcetylationAIAEAMSKLDEGTPP
HHHHHHHCCCCCCCC
47.0411790157
1843PhosphorylationMSKLDEGTPPEPKGT
HHCCCCCCCCCCCCC
33.3519664994
1854PhosphorylationPKGTFVDYQTTVVKY
CCCCCCCCCCEEEEH
11.4925884760
1856PhosphorylationGTFVDYQTTVVKYSK
CCCCCCCCEEEEHHH
18.48-
1943PhosphorylationGALQVCPTDSYTKRE
CCCEECCCCCCCHHH
32.2423312004
1945PhosphorylationLQVCPTDSYTKRELI
CEECCCCCCCHHHHH
36.8623312004
1947PhosphorylationVCPTDSYTKRELIEC
ECCCCCCCHHHHHHH
27.8123312004
2025MalonylationENILKTAKALVEDTK
HHHHHHHHHHHHCCE
47.7026320211
2031O-linked_GlycosylationAKALVEDTKLLVSGA
HHHHHHCCEEECCCC
15.3030379171
2036O-linked_GlycosylationEDTKLLVSGAASTPD
HCCEEECCCCCCCHH
23.7630379171
2036PhosphorylationEDTKLLVSGAASTPD
HCCEEECCCCCCCHH
23.7621406692
2040PhosphorylationLLVSGAASTPDKLAQ
EECCCCCCCHHHHHH
39.6821406692
2041PhosphorylationLVSGAASTPDKLAQA
ECCCCCCCHHHHHHH
30.6821815630
2077PhosphorylationLGSDDPETQVVLINA
CCCCCHHHHHHHHHH
31.86-
2086UbiquitinationVVLINAIKDVAKALS
HHHHHHHHHHHHHHH
43.6823000965
2089UbiquitinationINAIKDVAKALSDLI
HHHHHHHHHHHHHHH
11.0923000965
2116MalonylationDPSMYQLKGAAKVMV
CHHHHHHHHHHHHEE
30.8632601280
2124PhosphorylationGAAKVMVTNVTSLLK
HHHHHEEEEHHHHHH
13.0824117733
2127PhosphorylationKVMVTNVTSLLKTVK
HHEEEEHHHHHHHHH
18.7422199227
2128PhosphorylationVMVTNVTSLLKTVKA
HEEEEHHHHHHHHHH
27.6728355574
2131UbiquitinationTNVTSLLKTVKAVED
EEHHHHHHHHHHHHC
57.4723000965
2132PhosphorylationNVTSLLKTVKAVEDE
EHHHHHHHHHHHHCH
27.4925599653
2134MalonylationTSLLKTVKAVEDEAT
HHHHHHHHHHHCHHH
52.5326320211
2134UbiquitinationTSLLKTVKAVEDEAT
HHHHHHHHHHHCHHH
52.5323000965
2144UbiquitinationEDEATRGTRALEATI
HCHHHHHHHHHHHHH
14.9624816145
2169UbiquitinationQSKDVPEKTSSPEES
ECCCCCCCCCCHHHH
47.8730230243
2170PhosphorylationSKDVPEKTSSPEESI
CCCCCCCCCCHHHHH
32.5426437602
2171PhosphorylationKDVPEKTSSPEESIR
CCCCCCCCCHHHHHH
55.7728857561
2172PhosphorylationDVPEKTSSPEESIRM
CCCCCCCCHHHHHHH
41.3826437602
2176PhosphorylationKTSSPEESIRMTKGI
CCCCHHHHHHHCCCC
17.5228857561
2180PhosphorylationPEESIRMTKGITMAT
HHHHHHHCCCCHHHH
19.1028270605
2181UbiquitinationEESIRMTKGITMATA
HHHHHHCCCCHHHHH
38.68-
2184PhosphorylationIRMTKGITMATAKAV
HHHCCCCHHHHHHHH
14.9328270605
2187PhosphorylationTKGITMATAKAVAAG
CCCCHHHHHHHHHCC
20.1928270605
2189UbiquitinationGITMATAKAVAAGNS
CCHHHHHHHHHCCCC
38.7524816145
2196PhosphorylationKAVAAGNSCRQEDVI
HHHHCCCCCCHHHHH
15.1226074081
2198MethylationVAAGNSCRQEDVIAT
HHCCCCCCHHHHHHH
42.62-
2214PhosphorylationNLSRKAVSDMLTACK
CCCHHHHHHHHHHHH
23.35-
2218PhosphorylationKAVSDMLTACKQASF
HHHHHHHHHHHHHCC
24.30-
2282PhosphorylationKRVAGAVTELIQAAE
HHHHHHHHHHHHHHH
25.2521406692
2352PhosphorylationQILEAAKSIAAATSA
HHHHHHHHHHHHHHH
16.8422199227
2357PhosphorylationAKSIAAATSALVKSA
HHHHHHHHHHHHHCC
15.1428060719
2358PhosphorylationKSIAAATSALVKSAS
HHHHHHHHHHHHCCC
18.1928060719
2427PhosphorylationASEEKLISSAKQVAA
CCHHHHHHHHHHHHH
34.3828060719
2428PhosphorylationSEEKLISSAKQVAAS
CHHHHHHHHHHHHHH
32.27-
2465UbiquitinationQAAGNAVKRASDNLV
HHHHHHHHHHHHHHH
39.5824816145
2477AcetylationNLVRAAQKAAFGKAD
HHHHHHHHHHHCCCC
36.6320167786
2477MethylationNLVRAAQKAAFGKAD
HHHHHHHHHHHCCCC
36.63-
2482MethylationAQKAAFGKADDDDVV
HHHHHHCCCCCCCCE
42.03-
2491UbiquitinationDDDDVVVKTKFVGGI
CCCCCEEEEECHHHH
34.0924816145
2521UbiquitinationELEEARKKLAQIRQQ
HHHHHHHHHHHHHHH
43.4324816145
2530PhosphorylationAQIRQQQYKFLPTEL
HHHHHHHHCCCCHHH
10.2023186163
2535PhosphorylationQQYKFLPTELREDEG
HHHCCCCHHHHCCCC
50.2024719451
2536UbiquitinationQYKFLPTELREDEG-
HHCCCCHHHHCCCC-
43.8424816145

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TLN2_HUMAN !!

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
2134Malonylation2137 (3)EK;Qrs35997243
  • Immature fraction of reticulocytes
27863252

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TWF2_HUMANTWF2physical
22939629

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TLN2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1543, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1665, AND MASSSPECTROMETRY.

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