OPA1_HUMAN - dbPTM
OPA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OPA1_HUMAN
UniProt AC O60313
Protein Name Dynamin-like 120 kDa protein, mitochondrial
Gene Name OPA1 {ECO:0000303|PubMed:11810270, ECO:0000303|PubMed:28746876, ECO:0000312|HGNC:HGNC:8140}
Organism Homo sapiens (Human).
Sequence Length 960
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein . Mitochondrion intermembrane space . Mitochondrion membrane . Detected at contact sites between endoplamic reticulum and mitochondrion membranes.
Protein Description Dynamin-related GTPase that is essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. [PubMed: 16778770]
Protein Sequence MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFEKIRKALPSSEDLVKLAPDFDKIVESLSLLKDFFTSGSPEETAFRATDRGSESDKHFRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
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
21PhosphorylationCQSLVKHSSGIKGSL
HHHHHHCCCCCCCCC		25.2517924679
22PhosphorylationQSLVKHSSGIKGSLP
HHHHHCCCCCCCCCC		44.2317924679
107PhosphorylationLRYLILGSAVGGGYT
HHHHHHHCCCCCCHH		19.1418452278
114PhosphorylationSAVGGGYTAKKTFDQ
CCCCCCHHHHHHHHH		34.9618452278
117UbiquitinationGGGYTAKKTFDQWKD
CCCHHHHHHHHHHHH		52.54-
123UbiquitinationKKTFDQWKDMIPDLS
HHHHHHHHHHCCCHH		31.61-
132PhosphorylationMIPDLSEYKWIVPDI
HCCCHHHCCEECCHH		14.30-
154UbiquitinationIDFEKIRKALPSSED
CCHHHHHHHCCCCHH		58.72-
154UbiquitinationIDFEKIRKALPSSED
CCHHHHHHHCCCCHH		58.72-
158PhosphorylationKIRKALPSSEDLVKL
HHHHHCCCCHHHHHH		47.4022210691
159PhosphorylationIRKALPSSEDLVKLA
HHHHCCCCHHHHHHC		32.9422210691
164UbiquitinationPSSEDLVKLAPDFDK
CCCHHHHHHCCCHHH		46.35-
177PhosphorylationDKIVESLSLLKDFFT
HHHHHHHHHHHHHHC		40.7224719451
192AcetylationSGSPEETAFRATDRG
CCCHHHHCCCCCCCC		8.6619608861
192UbiquitinationSGSPEETAFRATDRG
CCCHHHHCCCCCCCC		8.6619608861
197 (in isoform 10)Phosphorylation-52.5422496350
197 (in isoform 11)Phosphorylation-52.5422496350
199 (in isoform 9)Phosphorylation-38.28-
2042-HydroxyisobutyrylationDRGSESDKHFRKVSD
CCCCCCHHHHHCCCC		54.65-
214UbiquitinationRKVSDKEKIDQLQEE
HCCCCHHHHHHHHHH		58.27-
228AcetylationELLHTQLKYQRILER
HHHHHHHHHHHHHHH		29.5319608861
228UbiquitinationELLHTQLKYQRILER
HHHHHHHHHHHHHHH		29.5321890473
228 (in isoform 1)Ubiquitination-29.5321890473
229AcetylationLLHTQLKYQRILERL
HHHHHHHHHHHHHHH		16.1819608861
229UbiquitinationLLHTQLKYQRILERL
HHHHHHHHHHHHHHH		16.1819608861
235 (in isoform 2)Phosphorylation-44.71-
243 (in isoform 2)Ubiquitination-6.63-
246AcetylationENKELRKLVLQKDDK
HCHHHHHHHHCCCCC		3.6219608861
246UbiquitinationENKELRKLVLQKDDK
HCHHHHHHHHCCCCC		3.6219608861
253PhosphorylationLVLQKDDKGIHHRKL
HHHCCCCCCCCHHHH		70.65-
2532-HydroxyisobutyrylationLVLQKDDKGIHHRKL
HHHCCCCCCCCHHHH		70.65-
253PhosphorylationLVLQKDDKGIHHRKL
HHHCCCCCCCCHHHH		70.65-
253 (in isoform 10)Phosphorylation-70.65-
261UbiquitinationGIHHRKLKKSLIDMY
CCCHHHHHHHHHHHH		43.27-
265AcetylationRKLKKSLIDMYSEVL
HHHHHHHHHHHHHHH		3.5519608861
265UbiquitinationRKLKKSLIDMYSEVL
HHHHHHHHHHHHHHH		3.5519608861
265 (in isoform 2)Ubiquitination-3.5521890473
268PhosphorylationKKSLIDMYSEVLDVL
HHHHHHHHHHHHHHH		9.64-
283UbiquitinationSDYDASYNTQDHLPR
CCCCCCCCCCCCCCE		28.8621906983
283AcetylationSDYDASYNTQDHLPR
CCCCCCCCCCCCCCE		28.8619608861
283UbiquitinationSDYDASYNTQDHLPR
CCCCCCCCCCCCCCE		28.8619608861
298PhosphorylationVVVVGDQSAGKTSVL
EEEEECCCCCCHHHH		43.6720068231
301UbiquitinationVGDQSAGKTSVLEMI
EECCCCCCHHHHHHH		37.03-
302PhosphorylationGDQSAGKTSVLEMIA
ECCCCCCHHHHHHHH		24.13-
318PhosphorylationARIFPRGSGEMMTRS
CCCCCCCCCCCCCCC		32.6228985074
323PhosphorylationRGSGEMMTRSPVKVT
CCCCCCCCCCCEEEE		27.0428985074
325PhosphorylationSGEMMTRSPVKVTLS
CCCCCCCCCEEEEEC		25.5328985074
338 (in isoform 2)Ubiquitination-4.50-
3422-HydroxyisobutyrylationPHHVALFKDSSREFD
CCEEEEECCCCCCCC		58.51-
344PhosphorylationHVALFKDSSREFDLT
EEEEECCCCCCCCCC		31.7021406692
345PhosphorylationVALFKDSSREFDLTK
EEEECCCCCCCCCCH		46.0621406692
351PhosphorylationSSREFDLTKEEDLAA
CCCCCCCCHHHHHHH		37.9521406692
352UbiquitinationSREFDLTKEEDLAAL
CCCCCCCHHHHHHHH		67.42-
356UbiquitinationDLTKEEDLAALRHEI
CCCHHHHHHHHHHHH		3.21-
383PhosphorylationTVSPETISLNVKGPG
EECCCCEEEECCCCC		22.7024275569
387UbiquitinationETISLNVKGPGLQRM
CCEEEECCCCCCCEE		59.31-
405PhosphorylationDLPGVINTVTSGMAP
ECCCCCCHHCCCCCC		17.65-
440PhosphorylationILCIQDGSVDAERSI
EEEEECCCCCHHHHH		25.72-
474UbiquitinationTKVDLAEKNVASPSR
EEHHHHHCCCCCHHH		51.63-
478PhosphorylationLAEKNVASPSRIQQI
HHHCCCCCHHHHHHH		21.0825159151
489UbiquitinationIQQIIEGKLFPMKAL
HHHHHCCCCCCCHHC		33.88-
527UbiquitinationEEFFQNSKLLKTSML
HHHHHCCCHHHHHHH		66.44-
5302-HydroxyisobutyrylationFQNSKLLKTSMLKAH
HHCCCHHHHHHHHHH		49.33-
530UbiquitinationFQNSKLLKTSMLKAH
HHCCCHHHHHHHHHH		49.33-
535UbiquitinationLLKTSMLKAHQVTTR
HHHHHHHHHHCCHHC		34.87-
544UbiquitinationHQVTTRNLSLAVSDC
HCCHHCCHHHHHHHH		3.91-
559PhosphorylationFWKMVRESVEQQADS
HHHHHHHHHHHHHHH		22.0125367160
5682-HydroxyisobutyrylationEQQADSFKATRFNLE
HHHHHHHHHCCCCCC		53.45-
568UbiquitinationEQQADSFKATRFNLE
HHHHHHHHHCCCCCC		53.452190698
568 (in isoform 1)Ubiquitination-53.4521890473
570PhosphorylationQADSFKATRFNLETE
HHHHHHHCCCCCCHH		36.0625367160
582PhosphorylationETEWKNNYPRLRELD
CHHHHHCCHHHHHCC		10.10-
585UbiquitinationWKNNYPRLRELDRNE
HHHCCHHHHHCCHHH		4.27-
598UbiquitinationNELFEKAKNEILDEV
HHHHHHHHHHHHHHH		67.20-
605 (in isoform 2)Ubiquitination-3.4421890473
607PhosphorylationEILDEVISLSQVTPK
HHHHHHHHHHHCCHH		27.43-
612PhosphorylationVISLSQVTPKHWEEI
HHHHHHCCHHHHHHH		20.98-
623UbiquitinationWEEILQQSLWERVST
HHHHHHHHHHHHHHH		23.612190698
629PhosphorylationQSLWERVSTHVIENI
HHHHHHHHHHHHCCE		21.0120068231
630PhosphorylationSLWERVSTHVIENIY
HHHHHHHHHHHCCEE		19.8020068231
635 (in isoform 2)Ubiquitination-19.65-
637PhosphorylationTHVIENIYLPAAQTM
HHHHCCEEECHHHCC		20.4320068231
652PhosphorylationNSGTFNTTVDIKLKQ
CCCCCEEEEEEEHHH		19.7921082442
653UbiquitinationSGTFNTTVDIKLKQW
CCCCEEEEEEEHHHC		7.24-
663UbiquitinationKLKQWTDKQLPNKAV
EHHHCCCCCCCCHHH		46.49-
682PhosphorylationETLQEEFSRFMTEPK
HHHHHHHHHHHCCCC		28.08-
699UbiquitinationEHDDIFDKLKEAVKE
CCCCHHHHHHHHHHH		51.19-
708PhosphorylationKEAVKEESIKRHKWN
HHHHHHHHHHHHCCC		34.2021406692
713UbiquitinationEESIKRHKWNDFAED
HHHHHHHCCCCHHHH		52.29-
733MethylationQHNALEDRSISDKQQ
HHHHCCCCCCCHHHH		26.89115486021
734PhosphorylationHNALEDRSISDKQQW
HHHCCCCCCCHHHHH		38.4726437602
768UbiquitinationNAIENMVGPDWKKRW
HHHHHHHCCCHHHHH		12.04-
772AcetylationNMVGPDWKKRWLYWK
HHHCCCHHHHHHHCC		39.58129659
777PhosphorylationDWKKRWLYWKNRTQE
CHHHHHHHCCCCCHH		13.8426074081
782PhosphorylationWLYWKNRTQEQCVHN
HHHCCCCCHHHHHCH		45.9426074081
791PhosphorylationEQCVHNETKNELEKM
HHHHCHHCHHHHHHH		44.4826074081
792AcetylationQCVHNETKNELEKML
HHHCHHCHHHHHHHH		42.1026822725
808PhosphorylationCNEEHPAYLASDEIT
CCCCCCCCCCCCHHH		13.7824927040
815PhosphorylationYLASDEITTVRKNLE
CCCCCHHHHHHHHHH		19.72-
816PhosphorylationLASDEITTVRKNLES
CCCCHHHHHHHHHHH		24.79-
824MethylationVRKNLESRGVEVDPS
HHHHHHHCCCCCCHH		43.74115486013
831PhosphorylationRGVEVDPSLIKDTWH
CCCCCCHHHHHHHHH		37.9622673903
834AcetylationEVDPSLIKDTWHQVY
CCCHHHHHHHHHHHH		55.1623954790
834UbiquitinationEVDPSLIKDTWHQVY
CCCHHHHHHHHHHHH		55.16-
847UbiquitinationVYRRHFLKTALNHCN
HHHHHHHHHHHHHCC		30.70-
848PhosphorylationYRRHFLKTALNHCNL
HHHHHHHHHHHHCCH		38.2329083192
861PhosphorylationNLCRRGFYYYQRHFV
CHHHCCHHHHHHHCC		12.2324043423
862PhosphorylationLCRRGFYYYQRHFVD
HHHCCHHHHHHHCCC		7.2924043423
863PhosphorylationCRRGFYYYQRHFVDS
HHCCHHHHHHHCCCC		6.4124043423
889AcetylationRIQRMLAITANTLRQ
HHHHHHHHHHHHHHH		3.09-
890PhosphorylationIQRMLAITANTLRQQ
HHHHHHHHHHHHHHH		14.3018691976
893PhosphorylationMLAITANTLRQQLTN
HHHHHHHHHHHHHCH		22.3615144186
911UbiquitinationRRLEKNVKEVLEDFA
HHHHHHHHHHHHHHH		52.04-
923UbiquitinationDFAEDGEKKIKLLTG
HHHHCCHHHHHHHHC		66.39-
926AcetylationEDGEKKIKLLTGKRV
HCCHHHHHHHHCCHH		46.4562135799
929PhosphorylationEKKIKLLTGKRVQLA
HHHHHHHHCCHHHHH		51.6014729942
931AcetylationKIKLLTGKRVQLAED
HHHHHHCCHHHHHHH		44.1362135801
940UbiquitinationVQLAEDLKKVREIQE
HHHHHHHHHHHHHHH		62.64-
948UbiquitinationKVREIQEKLDAFIEA
HHHHHHHHHHHHHHH		34.98-
966UbiquitinationEK-------------
CC-------------		-
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
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:23045728
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OPA1_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 OPA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
BNIP3_HUMANBNIP3physical
20436456
GID8_HUMANGID8physical
27173435
Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
H01020 Optic atrophy (OPA)
OMIM Disease
165500Optic atrophy 1 (OPA1)
125250Dominant optic atrophy plus syndrome (DOA+)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OPA1_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-228, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-22, AND MASSSPECTROMETRY.

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