ACTN4_MOUSE - dbPTM
ACTN4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN4_MOUSE
UniProt AC P57780
Protein Name Alpha-actinin-4 {ECO:0000305}
Gene Name Actn4 {ECO:0000312|MGI:MGI:1890773}
Organism Mus musculus (Mouse).
Sequence Length 912
Subcellular Localization Nucleus . Cytoplasm . Cell junction . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers.
Protein Description F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. 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 (By similarity). 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. [PubMed: 18332111 May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (By similarity]
Protein Sequence MVDYHAANQAYQYGPNSGGGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKQRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPSLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL
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----MVDYHAANQAY
----CCCCCCCCCCC
5.0724224561
32PhosphorylationGGGSMGDYMAQEDDW
CCCCHHHHHCCCCCC
6.6622996825
51UbiquitinationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH
40.82-
55UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.59-
55MalonylationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5926320211
58PhosphorylationKQQRKTFTAWCNSHL
HHHHHHHHHHHHHHH
25.2028542873
63PhosphorylationTFTAWCNSHLRKAGT
HHHHHHHHHHHHHCC
22.2928542873
70PhosphorylationSHLRKAGTQIENIDE
HHHHHHCCCCCCCCH
31.1029514104
115AcetylationHKINNVNKALDFIAS
EECCCHHHHHHHHHH
46.1523954790
122PhosphorylationKALDFIASKGVKLVS
HHHHHHHHCCCEEEE
25.7328542873
126UbiquitinationFIASKGVKLVSIGAE
HHHHCCCEEEEECCH
52.4122790023
160PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH
31.5926824392
164PhosphorylationQDISVEETSAKEGLL
HCCCCCCCCHHHCCH
22.0727742792
165PhosphorylationDISVEETSAKEGLLL
CCCCCCCCHHHCCHH
40.3927742792
182MalonylationQRKTAPYKNVNVQNF
CCCCCCCCCCCCCEE
54.0526320211
192PhosphorylationNVQNFHISWKDGLAF
CCCEEEEECCCCHHH
21.3623375375
213PhosphorylationHRPELIEYDKLRKDD
CCHHHHCHHHCCCCC
16.0426824392
215AcetylationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC
49.6522826441
215UbiquitinationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC
49.6522790023
218AcetylationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.5423236377
218UbiquitinationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC
76.5422790023
234UbiquitinationNAFEVAEKYLDIPKM
HHHHHHHHHCCCCCC
41.1822790023
235PhosphorylationAFEVAEKYLDIPKML
HHHHHHHHCCCCCCC
10.9162053
250PhosphorylationDAEDIVNTARPDEKA
CHHHHHHCCCCCHHH
17.1026824392
256UbiquitinationNTARPDEKAIMTYVS
HCCCCCHHHHHHHHH
51.06-
261PhosphorylationDEKAIMTYVSSFYHA
CHHHHHHHHHHHHHH
4.8723984901
263PhosphorylationKAIMTYVSSFYHAFS
HHHHHHHHHHHHHHH
12.3322499769
264PhosphorylationAIMTYVSSFYHAFSG
HHHHHHHHHHHHHHC
21.5622499769
266PhosphorylationMTYVSSFYHAFSGAQ
HHHHHHHHHHHHCHH
8.3226824392
270PhosphorylationSSFYHAFSGAQKAET
HHHHHHHHCHHHHHH
33.7222499769
274AcetylationHAFSGAQKAETAANR
HHHHCHHHHHHHHHH
47.8922826441
304PhosphorylationEDYERLASDLLEWIR
HHHHHHHHHHHHHHH
33.1273666003
324MalonylationLEDRVPQKTIQEMQQ
HHHCCCHHHHHHHHH
41.3426320211
324AcetylationLEDRVPQKTIQEMQQ
HHHCCCHHHHHHHHH
41.3423236377
332UbiquitinationTIQEMQQKLEDFRDY
HHHHHHHHHHHHHHH
36.6322790023
347UbiquitinationRRVHKPPKVQEKCQL
HHHCCCCCHHHCEEE
66.14-
351UbiquitinationKPPKVQEKCQLEINF
CCCCHHHCEEEEEEC
15.3622790023
352S-nitrosylationPPKVQEKCQLEINFN
CCCHHHCEEEEEECC
5.7020925432
352S-nitrosocysteinePPKVQEKCQLEINFN
CCCHHHCEEEEEECC
5.70-
360PhosphorylationQLEINFNTLQTKLRL
EEEEECCHHHHHHHH
18.9928464351
363PhosphorylationINFNTLQTKLRLSNR
EECCHHHHHHHHHCC
34.8528464351
368PhosphorylationLQTKLRLSNRPAFMP
HHHHHHHHCCCCCCC
25.1025266776
376PhosphorylationNRPAFMPSEGRMVSD
CCCCCCCCCCCCCCC
40.6828638064
382PhosphorylationPSEGRMVSDINNGWQ
CCCCCCCCCCCCCHH
24.3527087446
418AcetylationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH
39.9922826441
418UbiquitinationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH
39.9922790023
422UbiquitinationLAEKFRQKASIHEAW
HHHHHHHHHHHHHHC
39.5822790023
424PhosphorylationEKFRQKASIHEAWTD
HHHHHHHHHHHHCCC
31.3625521595
430PhosphorylationASIHEAWTDGKEAML
HHHHHHCCCHHHHHH
41.7523684622
433UbiquitinationHEAWTDGKEAMLKQR
HHHCCCHHHHHHHHC
45.1422790023
438MalonylationDGKEAMLKQRDYETA
CHHHHHHHHCCHHHC
30.1526320211
442PhosphorylationAMLKQRDYETATLSD
HHHHHCCHHHCCHHH
19.8522871156
446PhosphorylationQRDYETATLSDIKAL
HCCHHHCCHHHHHHH
33.9329514104
451UbiquitinationTATLSDIKALIRKHE
HCCHHHHHHHHHHHH
41.9722790023
462PhosphorylationRKHEAFESDLAAHQD
HHHHHHHHHHHHCHH
31.3227742792
508PhosphorylationDQWDNLGSLTHSRRE
HCCHHHHHHHHHHHH
33.0122817900
510PhosphorylationWDNLGSLTHSRREAL
CHHHHHHHHHHHHHH
21.3625168779
512PhosphorylationNLGSLTHSRREALEK
HHHHHHHHHHHHHHH
28.0025168779
522AcetylationEALEKTEKQLETIDQ
HHHHHHHHHHHHHHH
66.4723954790
593MalonylationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH
48.9426320211
593AcetylationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH
48.94-
605UbiquitinationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.11-
605AcetylationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.1123236377
605MalonylationIAESNHIKLSGSNPY
HHHHCCCCCCCCCCC
29.1126320211
607PhosphorylationESNHIKLSGSNPYTT
HHCCCCCCCCCCCCC
34.8629472430
609PhosphorylationNHIKLSGSNPYTTVT
CCCCCCCCCCCCCCC
31.1225195567
612PhosphorylationKLSGSNPYTTVTPQI
CCCCCCCCCCCCHHH
21.2029472430
613PhosphorylationLSGSNPYTTVTPQII
CCCCCCCCCCCHHHH
18.9529472430
614PhosphorylationSGSNPYTTVTPQIIN
CCCCCCCCCCHHHHH
19.2829472430
623AcetylationTPQIINSKWEKVQQL
CHHHHHHCHHHHHHH
55.6823236377
626AcetylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2023806337
626MalonylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2026320211
626SuccinylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC
44.2023806337
633MalonylationKVQQLVPKRDHALLE
HHHHHCCCCHHHHHH
64.0826320211
633UbiquitinationKVQQLVPKRDHALLE
HHHHHCCCCHHHHHH
64.08-
657PhosphorylationHLRRQFASQANMVGP
HHHHHHHHHHHCCHH
30.9827180971
692AcetylationEDQLSHLKQYERSIV
HHHHHHHHHHHHHHC
45.4723954790
697PhosphorylationHLKQYERSIVDYKPS
HHHHHHHHHCCCCCC
18.28-
702AcetylationERSIVDYKPSLDLLE
HHHHCCCCCCHHHHH
24.5423954790
728PhosphorylationFDNKHTNYTMEHIRV
HCCCCCCCCHHHHHH
14.4928464351
761UbiquitinationQILTRDAKGISQEQM
HHHCCCCCCCCHHHH
62.1522790023
780AcetylationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC
51.1623806337
794S-nitrosocysteineGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.41-
794GlutathionylationGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.4124333276
794S-nitrosylationGPEEFKACLISLGYD
CHHHHHHHHHHCCCC
3.4120925432
845PhosphorylationRETTDTDTADQVIAS
CCCCCCCCHHHHHHH
33.9426525534
860AcetylationFKVLAGDKNFITAEE
HHHHHCCCCEECHHH
53.4923806337
901PhosphorylationPGALDYKSFSTALYG
CCCCCCCHHHHHHCC
20.4229895711
903PhosphorylationALDYKSFSTALYGES
CCCCCHHHHHHCCCC
21.6229472430
904PhosphorylationLDYKSFSTALYGESD
CCCCHHHHHHCCCCC
20.7629472430
907PhosphorylationKSFSTALYGESDL--
CHHHHHHCCCCCC--
19.1829472430
910PhosphorylationSTALYGESDL-----
HHHHCCCCCC-----
39.5925521595

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN4_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 ACTN4_MOUSE !!

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

Oops, there are no PPI records of ACTN4_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTN4_MOUSE

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Related Literatures of Post-Translational Modification

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