ACTN3_HUMAN - dbPTM
ACTN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN3_HUMAN
UniProt AC Q08043
Protein Name Alpha-actinin-3
Gene Name ACTN3
Organism Homo sapiens (Human).
Sequence Length 901
Subcellular Localization
Protein Description F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein..
Protein Sequence MMMVMQPEGLGAGEGRFAGGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEEYEKLASELLEWIRRTVPWLENRVGEPSMSAMQRKLEDFRDYRRLHKPPRIQEKCQLEINFNTLQTKLRLSHRPAFMPSEGKLVSDIANAWRGLEQVEKGYEDWLLSEIRRLQRLQHLAEKFRQKASLHEAWTRGKEEMLSQRDYDSALLQEVRALLRRHEAFESDLAAHQDRVEHIAALAQELNELDYHEAASVNSRCQAICDQWDNLGTLTQKRRDALERMEKLLETIDRLQLEFARRAAPFNNWLDGAVEDLQDVWLVHSVEETQSLLTAHDQFKATLPEADRERGAIMGIQGEIQKICQTYGLRPCSTNPYITLSPQDINTKWDMVRKLVPSCDQTLQEELARQQVNERLRRQFAAQANAIGPWIQAKVEEVGRLAAGLAGSLEEQMAGLRQQEQNIINYKTNIDRLEGDHQLLQESLVFDNKHTVYSMEHIRVGWEQLLTSIARTINEVENQVLTRDAKGLSQEQLNEFRASFNHFDRKQNGMMEPDDFRACLISMGYDLGEVEFARIMTMVDPNAAGVVTFQAFIDFMTRETAETDTTEQVVASFKILAGDKNYITPEELRRELPAKQAEYCIRRMVPYKGSGAPAGALDYVAFSSALYGESDL
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
1Acetylation-------MMMVMQPE
-------CCCCCCCC		3.3622223895
26PhosphorylationGGGGGGEYMEQEEDW
CCCCCCCCCCCCCCC		14.8225954137
49UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH		43.5921890473
50PhosphorylationWEKQQRKTFTAWCNS
HHHHHHHHHHHHHHH		28.5426437602
52PhosphorylationKQQRKTFTAWCNSHL
HHHHHHHHHHHHHHH		25.2026437602
57PhosphorylationTFTAWCNSHLRKAGT
HHHHHHHHHHHHHCH		22.2926437602
64PhosphorylationSHLRKAGTQIENIEE
HHHHHHCHHHHCHHH		31.1016097034
90MethylationLEVISGERLPRPDKG
HHHHCCCCCCCCCCC		54.22-
93MethylationISGERLPRPDKGKMR
HCCCCCCCCCCCCCC		57.55-
116PhosphorylationKALDFIASKGVKLVS
HHHHHHHHCCCEEEE		25.7363745159
123PhosphorylationSKGVKLVSIGAEEIV
HCCCEEEEECCHHEE		26.24-
137PhosphorylationVDGNLKMTLGMIWTI
ECCCHHHHHHHHHHH		20.69-
154PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH		31.5919664994
158PhosphorylationQDISVEETSAKEGLL
HCCCCCCCCHHHCCH		22.0723927012
159PhosphorylationDISVEETSAKEGLLL
CCCCCCCCHHHCCHH		40.3923927012
168S-palmitoylationKEGLLLWCQRKTAPY
HHCCHHHHHCCCCCC		2.5729575903
185PhosphorylationVNVQNFHTSWKDGLA
CCCCCCCCCHHHHHH		31.9526437602
197PhosphorylationGLALCALIHRHRPDL
HHHHHHHHHHHCCCH		1.1127251275
201PhosphorylationCALIHRHRPDLIDYA
HHHHHHHCCCHHCHH		26.7827251275
229PhosphorylationAFEVAEKYLDIPKML
HHHHHHHHCCCCCCC		10.9124719451
244PhosphorylationDAEDIVNTPKPDEKA
CHHHHCCCCCCCHHH		23.0726437602
250AcetylationNTPKPDEKAIMTYVS
CCCCCCHHHHHHHHH		51.067681773
257PhosphorylationKAIMTYVSCFYHAFA
HHHHHHHHHHHHHHC		6.52-
260PhosphorylationMTYVSCFYHAFAGAE
HHHHHHHHHHHCCHH		9.1431136895
275MethylationQAETAANRICKVLAV
HHHHHHHHHHHHHHH		30.84-
278AcetylationTAANRICKVLAVNQE
HHHHHHHHHHHHCHH		37.607681783
298PhosphorylationEEYEKLASELLEWIR
HHHHHHHHHHHHHHH		38.9373403059
319PhosphorylationENRVGEPSMSAMQRK
HCCCCCCCHHHHHHH		22.5219764811
321PhosphorylationRVGEPSMSAMQRKLE
CCCCCCHHHHHHHHH		25.5619764811
333PhosphorylationKLEDFRDYRRLHKPP
HHHHHHHHHHHCCCC		8.0628152594
346S-palmitoylationPPRIQEKCQLEINFN
CCCHHHHEEEEEECC		5.7029575903
354PhosphorylationQLEINFNTLQTKLRL
EEEEECCHHHHHHHH		18.9926657352
357PhosphorylationINFNTLQTKLRLSHR
EECCHHHHHHHHHCC		34.8521712546
362PhosphorylationLQTKLRLSHRPAFMP
HHHHHHHHCCCCCCC		15.8327251275
376PhosphorylationPSEGKLVSDIANAWR
CCCCCCHHHHHHHHH		33.4637817029
397PhosphorylationKGYEDWLLSEIRRLQ
HHHHHHHHHHHHHHH		3.6327251275
398PhosphorylationGYEDWLLSEIRRLQR
HHHHHHHHHHHHHHH		28.8924719451
418PhosphorylationEKFRQKASLHEAWTR
HHHHHHHHHHHHHHH		36.9873401291
436PhosphorylationEMLSQRDYDSALLQE
HHHHCCCHHHHHHHH		17.6282570319
438PhosphorylationLSQRDYDSALLQEVR
HHCCCHHHHHHHHHH		18.0020860994
456PhosphorylationRRHEAFESDLAAHQD
HHHHHHHHHHHHCHH		31.3226437602
461PhosphorylationFESDLAAHQDRVEHI
HHHHHHHCHHHHHHH		25.1927251275
502PhosphorylationDQWDNLGTLTQKRRD
HCCCCHHHHHHHHHH		29.7826437602
504PhosphorylationWDNLGTLTQKRRDAL
CCCHHHHHHHHHHHH		31.7026437602
506AcetylationNLGTLTQKRRDALER
CHHHHHHHHHHHHHH		44.1330586727
602PhosphorylationTYGLRPCSTNPYITL
HHCCCCCCCCCCEEC		33.6226437602
606PhosphorylationRPCSTNPYITLSPQD
CCCCCCCCEECCHHH		14.4924260401
737PhosphorylationGWEQLLTSIARTINE
CHHHHHHHHHHHHHH		17.7719764811
741PhosphorylationLLTSIARTINEVENQ
HHHHHHHHHHHHHHH		21.0926437602
751PhosphorylationEVENQVLTRDAKGLS
HHHHHHHCCCCCCCC		27.8726437602
758PhosphorylationTRDAKGLSQEQLNEF
CCCCCCCCHHHHHHH		40.1028188228
768PhosphorylationQLNEFRASFNHFDRK
HHHHHHHHHHHHHHH		23.4826437602
829PhosphorylationIDFMTRETAETDTTE
HHHHCCCCCCCCCHH		26.8822468782
841PhosphorylationTTEQVVASFKILAGD
CHHHHHHHHHHHHCC		18.5724719451
851PhosphorylationILAGDKNYITPEELR
HHHCCCCCCCHHHHH		16.3524484179
853PhosphorylationAGDKNYITPEELRRE
HCCCCCCCHHHHHHH		17.8122468782
876PhosphorylationCIRRMVPYKGSGAPA
HHHHHCCCCCCCCCC		19.3051458179
899PhosphorylationSSALYGESDL-----
HHHHHCCCCC-----		39.59-
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 ACTN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN3_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 ACTN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN2_HUMANACTN2physical
9675099
ACTN3_HUMANACTN3physical
25416956
REL_HUMANRELphysical
25416956
TRAF1_HUMANTRAF1physical
25416956
TRAF2_HUMANTRAF2physical
25416956
NEBL_HUMANNEBLphysical
25416956
ABI3_HUMANABI3physical
25416956
RN111_HUMANRNF111physical
25416956
PKHG2_HUMANPLEKHG2physical
25416956
CA094_HUMANC1orf94physical
25416956
KCTD6_HUMANKCTD6physical
25416956
BRCA1_HUMANBRCA1physical
25184681
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 ACTN3_HUMAN

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Related Literatures of Post-Translational Modification

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