ACTN4_RAT - dbPTM
ACTN4_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN4_RAT
UniProt AC Q9QXQ0
Protein Name Alpha-actinin-4 {ECO:0000305}
Gene Name Actn4 {ECO:0000312|RGD:61816}
Organism Rattus norvegicus (Rat).
Sequence Length 911
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. 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. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA..
Protein Sequence MVDYHAANQAYQYGPSSGGNGTGGGGGMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDNLGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTSVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANMVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHLRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAAPGALDYKSFSTALYGESDL
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
31PhosphorylationGGGGMGDYMAQEDDW
CCCCHHHCCCCCCCC		6.66-
50AcetylationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH		40.82-
66SuccinylationWCNSHLRKAGTQIEN
HHHHHHHHHCCCCCC		58.4926843850
114AcetylationHKINNVNKALDFIAS
EECCCHHHHHHHHHH		46.1522902405
121PhosphorylationKALDFIASKGVKLVS
HHHHHHHHCCCEEEE		25.7363847327
159PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH		31.596479445
214AcetylationPELIEYDKLRKDDPV
HHHHCHHHCCCCCCC		49.6522902405
217SuccinylationIEYDKLRKDDPVTNL
HCHHHCCCCCCCCCC		76.5426843850
249PhosphorylationDAEDIVNTARPDEKA
CHHHHHHCCCCCHHH		17.10-
260NitrationDEKAIMTYVSSFYHA
CHHHHHHHHHHHHHH		4.87-
265PhosphorylationMTYVSSFYHAFSGAQ
HHHHHHHHHHHHCHH		8.3240035
303PhosphorylationEDYERLASDLLEWIR
HHHHHHHHHHHHHHH		33.1222673903
331AcetylationTIQEMQQKLEDFRDY
HHHHHHHHHHHHHHH		36.6372601853
350UbiquitinationKPPKVQEKCQLEINF
CCCCHHHCEEEEEEC		15.36-
350AcetylationKPPKVQEKCQLEINF
CCCCHHHCEEEEEEC		15.361891877
359PhosphorylationQLEINFNTLQTKLRL
EEEEECCHHHHHHHH		18.9923984901
362PhosphorylationINFNTLQTKLRLSNR
EECCHHHHHHHHHCC		34.8523984901
381PhosphorylationPSEGRMVSDINNGWQ
CCCCCCCCCCCCCHH		24.3528689409
395AcetylationQHLEQAEKGYEEWLL
HHHHHHHHHHHHHHH		70.5726302492
417AcetylationRLDHLAEKFRQKASI
HHHHHHHHHHHHHHH		39.99134629
421UbiquitinationLAEKFRQKASIHEAW
HHHHHHHHHHHHHHH		39.58-
423PhosphorylationEKFRQKASIHEAWTD
HHHHHHHHHHHHHCC		31.3622817900
429PhosphorylationASIHEAWTDGKEAML
HHHHHHHCCHHHHHH		41.7530181290
432AcetylationHEAWTDGKEAMLKHR
HHHHCCHHHHHHHCC		45.1422902405
437AcetylationDGKEAMLKHRDYETA
CHHHHHHHCCCCCCC		24.4122902405
443PhosphorylationLKHRDYETATLSDIK
HHCCCCCCCCHHHHH		20.7925575281
445PhosphorylationHRDYETATLSDIKAL
CCCCCCCCHHHHHHH		33.9325575281
447PhosphorylationDYETATLSDIKALIR
CCCCCCHHHHHHHHH		32.7025575281
461PhosphorylationRKHEAFESDLAAHQD
HHHHHHHHHHHHCHH		31.3222673903
507PhosphorylationDQWDNLGSLTHSRRE
HCCHHHHHHHHHHHH		33.0125575281
509PhosphorylationWDNLGSLTHSRREAL
CHHHHHHHHHHHHHH		21.3625575281
511PhosphorylationNLGSLTHSRREALEK
HHHHHHHHHHHHHHH		28.0025575281
518AcetylationSRREALEKTEKQLET
HHHHHHHHHHHHHHH		63.9322902405
535AcetylationQLHLEYAKRAAPFNN
HHHHHHHHHHCCCCH		41.4922902405
592AcetylationEAILAIHKEAQRIAE
HHHHHHHHHHHHHHH		48.9422902405
606PhosphorylationESNHIKLSGSNPYTS
HHCCCCCCCCCCCCC		34.8625575281
608PhosphorylationNHIKLSGSNPYTSVT
CCCCCCCCCCCCCCC		31.1228689409
611PhosphorylationKLSGSNPYTSVTPQI
CCCCCCCCCCCCHHH		18.8530181290
612PhosphorylationLSGSNPYTSVTPQII
CCCCCCCCCCCHHHH		20.2725575281
613PhosphorylationSGSNPYTSVTPQIIN
CCCCCCCCCCHHHHH		20.3925575281
615PhosphorylationSNPYTSVTPQIINSK
CCCCCCCCHHHHHHC		14.8330181290
621PhosphorylationVTPQIINSKWEKVQQ
CCHHHHHHCHHHHHH		28.8330181290
622AcetylationTPQIINSKWEKVQQL
CHHHHHHCHHHHHHH		55.6822902405
625AcetylationIINSKWEKVQQLVPK
HHHHCHHHHHHHCCC		44.2022902405
632AcetylationKVQQLVPKRDHALLE
HHHHHCCCCHHHHHH		64.0822902405
656PhosphorylationHLRRQFASQANMVGP
HHHHHHHHHHHCCHH		30.9828689409
696PhosphorylationHLKQYERSIVDYKPN
HHHHHHHHHCCCCCC		18.28-
779AcetylationASFNHFDKDHGGALG
HHCCCCCCCCCCCCC		51.1622902405
859AcetylationFKVLAGDKNFITAEE
HHHHHCCCCEECHHH		53.49-
909PhosphorylationSTALYGESDL-----
HHHHCCCCCC-----		39.5922673903
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
423SPhosphorylationKinasePRKACAP00517
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN4_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACTN4_RAT !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTN4_RAT

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Related Literatures of Post-Translational Modification

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