ACTN4_HUMAN - dbPTM
ACTN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN4_HUMAN
UniProt AC O43707
Protein Name Alpha-actinin-4 {ECO:0000305}
Gene Name ACTN4 {ECO:0000312|HGNC:HGNC:166}
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Nucleus . Cytoplasm . Cell junction . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers. Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclus
Protein Description F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. [PubMed: 15772161 Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA]
Protein Sequence MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
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
4Phosphorylation----MVDYHAANQSY
----CCCCCCCCCCC
5.0722996817
10PhosphorylationDYHAANQSYQYGPSS
CCCCCCCCCCCCCCC
17.6324043423
11PhosphorylationYHAANQSYQYGPSSA
CCCCCCCCCCCCCCC
8.9426552605
13PhosphorylationAANQSYQYGPSSAGN
CCCCCCCCCCCCCCC
23.8326552605
16PhosphorylationQSYQYGPSSAGNGAG
CCCCCCCCCCCCCCC
28.5826552605
17PhosphorylationSYQYGPSSAGNGAGG
CCCCCCCCCCCCCCC
43.2427251275
27PhosphorylationNGAGGGGSMGDYMAQ
CCCCCCCCHHHHHCC
23.9027251275
31PhosphorylationGGGSMGDYMAQEDDW
CCCCHHHHHCCCCCC
6.6626552605
50MalonylationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH
40.8226320211
50UbiquitinationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH
40.82-
54UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5921890473
54AcetylationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5926051181
54MalonylationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5926320211
54UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.59-
55PhosphorylationWEKQQRKTFTAWCNS
HHHHHHHHHHHHHHH
28.5426437602
57PhosphorylationKQQRKTFTAWCNSHL
HHHHHHHHHHHHHHH
25.2026437602
62PhosphorylationTFTAWCNSHLRKAGT
HHHHHHHHHHHHHCC
22.2926437602
66AcetylationWCNSHLRKAGTQIEN
HHHHHHHHHCCCCCC
58.4926051181
66MalonylationWCNSHLRKAGTQIEN
HHHHHHHHHCCCCCC
58.4926320211
66UbiquitinationWCNSHLRKAGTQIEN
HHHHHHHHHCCCCCC
58.49-
69PhosphorylationSHLRKAGTQIENIDE
HHHHHHCCCCCCCCH
31.1025849741
83UbiquitinationEDFRDGLKLMLLLEV
HHHHHHHHHHHHHHH
37.06-
85SulfoxidationFRDGLKLMLLLEVIS
HHHHHHHHHHHHHHC
2.0730846556
92PhosphorylationMLLLEVISGERLPKP
HHHHHHHCCCCCCCC
39.51-
95 (in isoform 3)Phosphorylation-60.8724905233
96 (in isoform 3)Phosphorylation-5.7924905233
98 (in isoform 3)Phosphorylation-65.1924905233
103 (in isoform 3)Phosphorylation-29.7424905233
108UbiquitinationRGKMRVHKINNVNKA
CCCCCEEECCCHHHH
44.25-
112UbiquitinationRVHKINNVNKALDFI
CEEECCCHHHHHHHH
7.22-
114AcetylationHKINNVNKALDFIAS
EECCCHHHHHHHHHH
46.1519608861
121PhosphorylationKALDFIASKGVKLVS
HHHHHHHHCCCEEEE
25.7363745159
122AcetylationALDFIASKGVKLVSI
HHHHHHHCCCEEEEE
59.7127452117
122SuccinylationALDFIASKGVKLVSI
HHHHHHHCCCEEEEE
59.7123954790
122UbiquitinationALDFIASKGVKLVSI
HHHHHHHCCCEEEEE
59.71-
125AcetylationFIASKGVKLVSIGAE
HHHHCCCEEEEECCH
52.4126051181
125UbiquitinationFIASKGVKLVSIGAE
HHHHCCCEEEEECCH
52.41-
128PhosphorylationSKGVKLVSIGAEEIV
HCCCEEEEECCHHEE
26.2428348404
131UbiquitinationVKLVSIGAEEIVDGN
CEEEEECCHHEECCC
15.0221906983
142PhosphorylationVDGNAKMTLGMIWTI
ECCCCHHHHHHHHHH
21.32-
159PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH
31.5919664994
163PhosphorylationQDISVEETSAKEGLL
HCCCCCCCCHHHCCH
22.0723927012
164PhosphorylationDISVEETSAKEGLLL
CCCCCCCCHHHCCHH
40.3923927012
173GlutathionylationKEGLLLWCQRKTAPY
HHCCHHHHCCCCCCC
2.5722555962
173S-palmitoylationKEGLLLWCQRKTAPY
HHCCHHHHCCCCCCC
2.5729575903
181MalonylationQRKTAPYKNVNVQNF
CCCCCCCCCCCCCEE
54.0526320211
181UbiquitinationQRKTAPYKNVNVQNF
CCCCCCCCCCCCCEE
54.0521890473
191PhosphorylationNVQNFHISWKDGLAF
CCCEEEEECCCCHHH
21.3628857561
202UbiquitinationGLAFNALIHRHRPEL
CHHHHHHHHHCCHHH
2.2021906983
212PhosphorylationHRPELIEYDKLRKDD
CCHHHHCHHHCCCCC
16.04119481
214AcetylationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC
49.6525825284
214MalonylationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC
49.6526320211
214UbiquitinationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC
49.6519608861
217AcetylationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.5426051181
217MalonylationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.5426320211
217SuccinylationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.5423954790
217UbiquitinationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.54-
233AcetylationNAFEVAEKYLDIPKM
HHHHHHHHHCCCCCC
41.1825825284
233UbiquitinationNAFEVAEKYLDIPKM
HHHHHHHHHCCCCCC
41.1821906983
234PhosphorylationAFEVAEKYLDIPKML
HHHHHHHHCCCCCCC
10.9123403867
235UbiquitinationFEVAEKYLDIPKMLD
HHHHHHHCCCCCCCC
7.7321890473
239UbiquitinationEKYLDIPKMLDAEDI
HHHCCCCCCCCHHHH
53.05-
240SulfoxidationKYLDIPKMLDAEDIV
HHCCCCCCCCHHHHH
3.2530846556
242UbiquitinationLDIPKMLDAEDIVNT
CCCCCCCCHHHHHHC
44.4021890473
249PhosphorylationDAEDIVNTARPDEKA
CHHHHHHCCCCCHHH
17.1028857561
255UbiquitinationNTARPDEKAIMTYVS
HCCCCCHHHHHHHHH
51.06-
258SulfoxidationRPDEKAIMTYVSSFY
CCCHHHHHHHHHHHH
2.3630846556
259PhosphorylationPDEKAIMTYVSSFYH
CCHHHHHHHHHHHHH
18.0428152594
260PhosphorylationDEKAIMTYVSSFYHA
CHHHHHHHHHHHHHH
4.8728152594
262PhosphorylationKAIMTYVSSFYHAFS
HHHHHHHHHHHHHHH
12.3326657352
263PhosphorylationAIMTYVSSFYHAFSG
HHHHHHHHHHHHHHC
21.5628152594
265PhosphorylationMTYVSSFYHAFSGAQ
HHHHHHHHHHHHCHH
8.3222617229
269PhosphorylationSSFYHAFSGAQKAET
HHHHHHHHCHHHHHH
33.7222617229
276PhosphorylationSGAQKAETAANRICK
HCHHHHHHHHHHHHH
35.6125348954
280MethylationKAETAANRICKVLAV
HHHHHHHHHHHHHHH
30.84-
283AcetylationTAANRICKVLAVNQE
HHHHHHHHHHHHCCC
37.6025825284
295SulfoxidationNQENEHLMEDYEKLA
CCCCHHHHHHHHHHH
3.8730846556
298PhosphorylationNEHLMEDYEKLASDL
CHHHHHHHHHHHHHH
11.14110736575
303PhosphorylationEDYEKLASDLLEWIR
HHHHHHHHHHHHHHH
38.9523403867
310MethylationSDLLEWIRRTIPWLE
HHHHHHHHHHCHHHH
30.66-
312PhosphorylationLLEWIRRTIPWLEDR
HHHHHHHHCHHHHHC
22.8821406692
319MethylationTIPWLEDRVPQKTIQ
HCHHHHHCCCHHHHH
32.42-
323AcetylationLEDRVPQKTIQEMQQ
HHHCCCHHHHHHHHH
41.3426051181
323MalonylationLEDRVPQKTIQEMQQ
HHHCCCHHHHHHHHH
41.3426320211
323UbiquitinationLEDRVPQKTIQEMQQ
HHHCCCHHHHHHHHH
41.34-
324PhosphorylationEDRVPQKTIQEMQQK
HHCCCHHHHHHHHHH
23.7362150667
328SulfoxidationPQKTIQEMQQKLEDF
CHHHHHHHHHHHHHH
2.6830846556
331AcetylationTIQEMQQKLEDFRDY
HHHHHHHHHHHHHHH
36.6325825284
331UbiquitinationTIQEMQQKLEDFRDY
HHHHHHHHHHHHHHH
36.63-
338PhosphorylationKLEDFRDYRRVHKPP
HHHHHHHHHHHCCCC
8.9628152594
346UbiquitinationRRVHKPPKVQEKCQL
HHHCCCCCHHHCEEE
66.14-
350AcetylationKPPKVQEKCQLEINF
CCCCHHHCEEEEEEC
15.3626051181
350UbiquitinationKPPKVQEKCQLEINF
CCCCHHHCEEEEEEC
15.3621906983
351GlutathionylationPPKVQEKCQLEINFN
CCCHHHCEEEEEECC
5.7022555962
351S-nitrosylationPPKVQEKCQLEINFN
CCCHHHCEEEEEECC
5.7022178444
351S-palmitoylationPPKVQEKCQLEINFN
CCCHHHCEEEEEECC
5.7029575903
359PhosphorylationQLEINFNTLQTKLRL
EEEEECCHHHHHHHH
18.9926657352
362PhosphorylationINFNTLQTKLRLSNR
EECCHHHHHHHHHCC
34.8521712546
367PhosphorylationLQTKLRLSNRPAFMP
HHHHHHHHCCCCCCC
25.1054885953
375PhosphorylationNRPAFMPSEGKMVSD
CCCCCCCCCCCCCCC
47.3926437602
378UbiquitinationAFMPSEGKMVSDINN
CCCCCCCCCCCCCCC
31.8821906983
379SulfoxidationFMPSEGKMVSDINNG
CCCCCCCCCCCCCCC
5.2630846556
381PhosphorylationPSEGKMVSDINNGWQ
CCCCCCCCCCCCCHH
29.3128857561
385UbiquitinationKMVSDINNGWQHLEQ
CCCCCCCCCHHHHHH
54.11-
397PhosphorylationLEQAEKGYEEWLLNE
HHHHHHHHHHHHHHH
23.03110736583
403UbiquitinationGYEEWLLNEIRRLER
HHHHHHHHHHHHHHH
40.24-
406AcetylationEWLLNEIRRLERLDH
HHHHHHHHHHHHHHH
30.84-
406UbiquitinationEWLLNEIRRLERLDH
HHHHHHHHHHHHHHH
30.84-
413UbiquitinationRRLERLDHLAEKFRQ
HHHHHHHHHHHHHHH
31.37-
417AcetylationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH
39.9925825284
417MalonylationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH
39.9926320211
417UbiquitinationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH
39.9919608861
421UbiquitinationLAEKFRQKASIHEAW
HHHHHHHHHHHHHHH
39.5821890473
423PhosphorylationEKFRQKASIHEAWTD
HHHHHHHHHHHHHCC
31.3628355574
429PhosphorylationASIHEAWTDGKEAML
HHHHHHHCCHHHHHH
41.7526074081
432AcetylationHEAWTDGKEAMLKHR
HHHHCCHHHHHHHCC
45.1426051181
432UbiquitinationHEAWTDGKEAMLKHR
HHHHCCHHHHHHHCC
45.14-
437AcetylationDGKEAMLKHRDYETA
CHHHHHHHCCCCCCC
24.4125953088
441PhosphorylationAMLKHRDYETATLSD
HHHHCCCCCCCCHHH
18.3528152594
443PhosphorylationLKHRDYETATLSDIK
HHCCCCCCCCHHHHH
20.7928152594
445PhosphorylationHRDYETATLSDIKAL
CCCCCCCCHHHHHHH
33.9328152594
447PhosphorylationDYETATLSDIKALIR
CCCCCCHHHHHHHHH
32.707303209
450AcetylationTATLSDIKALIRKHE
CCCHHHHHHHHHHHH
41.9727452117
450UbiquitinationTATLSDIKALIRKHE
CCCHHHHHHHHHHHH
41.97-
455AcetylationDIKALIRKHEAFESD
HHHHHHHHHHHHHHH
38.5125825284
455UbiquitinationDIKALIRKHEAFESD
HHHHHHHHHHHHHHH
38.51-
461PhosphorylationRKHEAFESDLAAHQD
HHHHHHHHHHHHCHH
31.3226657352
469UbiquitinationDLAAHQDRVEQIAAI
HHHHCHHHHHHHHHH
27.5721890473
469MethylationDLAAHQDRVEQIAAI
HHHHCHHHHHHHHHH
27.57-
485PhosphorylationQELNELDYYDSHNVN
HHHHHCCCCCCCCCC
23.0737817035
486PhosphorylationELNELDYYDSHNVNT
HHHHCCCCCCCCCCH
15.6121406692
488PhosphorylationNELDYYDSHNVNTRC
HHCCCCCCCCCCHHH
10.8037817047
493PhosphorylationYDSHNVNTRCQKICD
CCCCCCCHHHHHHHH
28.6537817053
497AcetylationNVNTRCQKICDQWDA
CCCHHHHHHHHHHHH
49.2625953088
497UbiquitinationNVNTRCQKICDQWDA
CCCHHHHHHHHHHHH
49.26-
499S-nitrosocysteineNTRCQKICDQWDALG
CHHHHHHHHHHHHHH
4.02-
499GlutathionylationNTRCQKICDQWDALG
CHHHHHHHHHHHHHH
4.0222555962
499S-nitrosylationNTRCQKICDQWDALG
CHHHHHHHHHHHHHH
4.0222178444
499S-palmitoylationNTRCQKICDQWDALG
CHHHHHHHHHHHHHH
4.0229575903
507PhosphorylationDQWDALGSLTHSRRE
HHHHHHHHCHHHHHH
30.839418949
509PhosphorylationWDALGSLTHSRREAL
HHHHHHCHHHHHHHH
21.3623403867
511PhosphorylationALGSLTHSRREALEK
HHHHCHHHHHHHHHH
28.0023403867
518AcetylationSRREALEKTEKQLEA
HHHHHHHHHHHHHHH
63.9325953088
521AcetylationEALEKTEKQLEAIDQ
HHHHHHHHHHHHHHH
66.4725953088
521UbiquitinationEALEKTEKQLEAIDQ
HHHHHHHHHHHHHHH
66.47-
533PhosphorylationIDQLHLEYAKRAAPF
HHHHHHHHHHHHCCC
24.6328258704
592AcetylationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH
48.9419608861
592MalonylationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH
48.9426320211
592UbiquitinationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH
48.9419608861
604AcetylationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.1125953088
604MalonylationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.1126320211
604UbiquitinationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.11-
606PhosphorylationESNHIKLSGSNPYTT
HHCCCCCCCCCCCCC
34.8626657352
608PhosphorylationNHIKLSGSNPYTTVT
CCCCCCCCCCCCCCC
31.1228152594
611PhosphorylationKLSGSNPYTTVTPQI
CCCCCCCCCCCCHHH
21.20110736599
612PhosphorylationLSGSNPYTTVTPQII
CCCCCCCCCCCHHHH
18.9528152594
613PhosphorylationSGSNPYTTVTPQIIN
CCCCCCCCCCHHHHH
19.2828152594
615PhosphorylationSNPYTTVTPQIINSK
CCCCCCCCHHHHHHC
13.8472246255
621PhosphorylationVTPQIINSKWEKVQQ
CCHHHHHHCHHHHHH
28.8322817900
622AcetylationTPQIINSKWEKVQQL
CHHHHHHCHHHHHHH
55.6825825284
622UbiquitinationTPQIINSKWEKVQQL
CHHHHHHCHHHHHHH
55.68-
625AcetylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2019608861
625MalonylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2026320211
625UbiquitinationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2021890473
632MalonylationKVQQLVPKRDHALLE
HHHHHCCCCHHHHHH
64.0826320211
632UbiquitinationKVQQLVPKRDHALLE
HHHHHCCCCHHHHHH
64.0821890473
640UbiquitinationRDHALLEEQSKQQSN
CHHHHHHHHHHHHCH
61.19-
642PhosphorylationHALLEEQSKQQSNEH
HHHHHHHHHHHCHHH
35.39108826509
643UbiquitinationALLEEQSKQQSNEHL
HHHHHHHHHHCHHHH
52.64-
656PhosphorylationHLRRQFASQANVVGP
HHHHHHHHHCCCCCH
30.9826657352
667PhosphorylationVVGPWIQTKMEEIGR
CCCHHHHHHHHHHCC
24.1922817900
668UbiquitinationVGPWIQTKMEEIGRI
CCHHHHHHHHHHCCE
28.12-
679SulfoxidationIGRISIEMNGTLEDQ
HCCEEEEECCCHHHH
5.5228183972
682PhosphorylationISIEMNGTLEDQLSH
EEEEECCCHHHHHHH
23.2122817900
693PhosphorylationQLSHLKQYERSIVDY
HHHHHHHHHHHHCCC
16.2428064214
696PhosphorylationHLKQYERSIVDYKPN
HHHHHHHHHCCCCCC
18.28101545089
700PhosphorylationYERSIVDYKPNLDLL
HHHHHCCCCCCHHHH
19.90119485
701AcetylationERSIVDYKPNLDLLE
HHHHCCCCCCHHHHH
23.9826051181
701UbiquitinationERSIVDYKPNLDLLE
HHHHCCCCCCHHHHH
23.98-
725PhosphorylationLIFDNKHTNYTMEHI
HHHCCCCCCCCHHHH
31.3728152594
727PhosphorylationFDNKHTNYTMEHIRV
HCCCCCCCCHHHHHH
14.4928152594
728PhosphorylationDNKHTNYTMEHIRVG
CCCCCCCCHHHHHHC
20.3926437602
729SulfoxidationNKHTNYTMEHIRVGW
CCCCCCCHHHHHHCH
2.2030846556
741PhosphorylationVGWEQLLTTIARTIN
HCHHHHHHHHHHHHH
25.4221712546
746PhosphorylationLLTTIARTINEVENQ
HHHHHHHHHHHHHHH
21.0920860994
756PhosphorylationEVENQILTRDAKGIS
HHHHHHHCCCCCCCC
28.297303829
760UbiquitinationQILTRDAKGISQEQM
HHHCCCCCCCCHHHH
62.15-
763PhosphorylationTRDAKGISQEQMQEF
CCCCCCCCHHHHHHH
36.0121712546
767SulfoxidationKGISQEQMQEFRASF
CCCCHHHHHHHHHHC
3.9728465586
773PhosphorylationQMQEFRASFNHFDKD
HHHHHHHHCCCCCCC
23.48113301157
779AcetylationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC
51.1625825284
779MalonylationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC
51.1626320211
779MethylationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC
51.16-
779UbiquitinationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC
51.16-
793S-nitrosocysteineGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.41-
793S-nitrosylationGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.4122178444
793S-palmitoylationGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.4129575903
796PhosphorylationEFKACLISLGYDVEN
HHHHHHHHCCCCCCC
11.6463750705
799PhosphorylationACLISLGYDVENDRQ
HHHHHCCCCCCCCCC
23.3129496963
805MethylationGYDVENDRQGEAEFN
CCCCCCCCCCHHHHH
58.97-
839PhosphorylationIDFMSRETTDTDTAD
HHHHCCCCCCCCCHH
28.9421712546
840PhosphorylationDFMSRETTDTDTADQ
HHHCCCCCCCCCHHH
31.95110736607
842PhosphorylationMSRETTDTDTADQVI
HCCCCCCCCCHHHHH
32.91110736615
844PhosphorylationRETTDTDTADQVIAS
CCCCCCCCHHHHHHH
33.9427251275
851PhosphorylationTADQVIASFKVLAGD
CHHHHHHHHHHHHCC
17.9324719451
853AcetylationDQVIASFKVLAGDKN
HHHHHHHHHHHCCCC
33.5724846083
859AcetylationFKVLAGDKNFITAEE
HHHHHCCCCEECHHH
53.4925825284
859UbiquitinationFKVLAGDKNFITAEE
HHHHHCCCCEECHHH
53.4921906983
868MethylationFITAEELRRELPPDQ
EECHHHHHHHCCCCH
33.05-
878PhosphorylationLPPDQAEYCIARMAP
CCCCHHHHHHHHCCC
7.6828152594
883SulfoxidationAEYCIARMAPYQGPD
HHHHHHHCCCCCCCC
3.0530846556
886PhosphorylationCIARMAPYQGPDAVP
HHHHCCCCCCCCCCC
19.3021406692
898PhosphorylationAVPGALDYKSFSTAL
CCCCCCCCCHHHHHH
14.9121406692
899AcetylationVPGALDYKSFSTALY
CCCCCCCCHHHHHHC
44.7070505
900PhosphorylationPGALDYKSFSTALYG
CCCCCCCHHHHHHCC
20.4227251275
902PhosphorylationALDYKSFSTALYGES
CCCCCHHHHHHCCCC
21.6227251275
903PhosphorylationLDYKSFSTALYGESD
CCCCHHHHHHCCCCC
20.7628152594
906PhosphorylationKSFSTALYGESDL--
CHHHHHHCCCCCC--
19.1828152594
909PhosphorylationSTALYGESDL-----
HHHHCCCCCC-----
39.5928152594

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 ACTN4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN4_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

Oops, there are no SNP-PTM records of ACTN4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYOZ2_HUMANMYOZ2physical
16189514
MYOZ1_HUMANMYOZ1physical
16189514
PDLI1_HUMANPDLIM1physical
16189514
KCC2A_HUMANCAMK2Aphysical
11160423
KCC2B_HUMANCAMK2Bphysical
11160423
LRRC7_RATLrrc7physical
11160423
INO80_HUMANINO80physical
20197409
MEF2A_HUMANMEF2Aphysical
16980305
ESR1_HUMANESR1physical
21078666
VDR_HUMANVDRphysical
21078666
THIO_HUMANTXNphysical
21988832
RS27_HUMANRPS27physical
21988832
POTE1_HUMANPOT1physical
21988832
IMA1_HUMANKPNA2physical
21988832
MK07_HUMANMAPK7physical
21988832
ACTN1_HUMANACTN1physical
22863883
HGS_HUMANHGSphysical
22863883
SF3A3_HUMANSF3A3physical
22863883
ACTN3_HUMANACTN3physical
25416956
BMP7_HUMANBMP7physical
25416956
MYOZ2_HUMANMYOZ2physical
25416956
RARA_HUMANRARAphysical
22351778
KCRB_HUMANCKBphysical
26344197
CY1_HUMANCYC1physical
26344197
ECSIT_HUMANECSITphysical
26344197
MCFD2_HUMANMCFD2physical
26344197
PSB8_HUMANPSMB8physical
26344197
TPM1_HUMANTPM1physical
26344197
TPM3_HUMANTPM3physical
26344197
TPM4_HUMANTPM4physical
26344197
CTNB1_HUMANCTNNB1physical
25241761
HGS_HUMANHGSphysical
26819309
NFYA_HUMANNFYAphysical
15364540
ACT_SCHPOact1physical
27075176

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603278Focal segmental glomerulosclerosis 1 (FSGS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTN4_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-114; LYS-214; LYS-417;LYS-592 AND LYS-625, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-265, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-378, AND MASSSPECTROMETRY.

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