ACON_HUMAN - dbPTM
ACON_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACON_HUMAN
UniProt AC Q99798
Protein Name Aconitate hydratase, mitochondrial
Gene Name ACO2
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the isomerization of citrate to isocitrate via cis-aconitate..
Protein Sequence MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
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----MAPYSLLVTRL
----CCCHHHHHHHH
11.4724043423
5Phosphorylation---MAPYSLLVTRLQ
---CCCHHHHHHHHH
17.7324043423
9PhosphorylationAPYSLLVTRLQKALG
CCHHHHHHHHHHHHC
26.1568736429
13UbiquitinationLLVTRLQKALGVRQY
HHHHHHHHHHCCCHH
50.6127667366
28Pyrrolidone_carboxylic_acidHVASVLCQRAKVAMS
HHHHHHHHHHHHHHH
44.18-
31SuccinylationSVLCQRAKVAMSHFE
HHHHHHHHHHHHCCC
32.49-
31SuccinylationSVLCQRAKVAMSHFE
HHHHHHHHHHHHCCC
32.49-
35UbiquitinationQRAKVAMSHFEPNEY
HHHHHHHHCCCCCCC
18.4523503661
42PhosphorylationSHFEPNEYIHYDLLE
HCCCCCCCCCHHHHH
10.3146157845
50AcetylationIHYDLLEKNINIVRK
CCHHHHHHHHHHHHH
64.2023954790
50SuccinylationIHYDLLEKNINIVRK
CCHHHHHHHHHHHHH
64.20-
50SuccinylationIHYDLLEKNINIVRK
CCHHHHHHHHHHHHH
64.20-
64PhosphorylationKRLNRPLTLSEKIVY
HHCCCCCCHHCHHHC
30.8123612710
66PhosphorylationLNRPLTLSEKIVYGH
CCCCCCHHCHHHCCC
31.4423612710
68UbiquitinationRPLTLSEKIVYGHLD
CCCCHHCHHHCCCCC
33.8123503661
79PhosphorylationGHLDDPASQEIERGK
CCCCCHHHHHHHHCC
33.46110757307
87PhosphorylationQEIERGKSYLRLRPD
HHHHHCCCCEECCCC
32.0246157821
102PhosphorylationRVAMQDATAQMAMLQ
HHHHHHHHHHHHHHH
26.2229978859
105UbiquitinationMQDATAQMAMLQFIS
HHHHHHHHHHHHHHH
1.8823503661
111UbiquitinationQMAMLQFISSGLSKV
HHHHHHHHHCCCCCC
1.7523503661
112PhosphorylationMAMLQFISSGLSKVA
HHHHHHHHCCCCCCC
21.4629978859
113PhosphorylationAMLQFISSGLSKVAV
HHHHHHHCCCCCCCC
38.6529978859
116PhosphorylationQFISSGLSKVAVPST
HHHHCCCCCCCCCCE
28.7128857561
138AcetylationEAQVGGEKDLRRAKD
HHHCCCHHHHHHHHH
66.3925953088
138SuccinylationEAQVGGEKDLRRAKD
HHHCCCHHHHHHHHH
66.39-
138SuccinylationEAQVGGEKDLRRAKD
HHHCCCHHHHHHHHH
66.39-
138UbiquitinationEAQVGGEKDLRRAKD
HHHCCCHHHHHHHHH
66.3923503661
1442-HydroxyisobutyrylationEKDLRRAKDINQEVY
HHHHHHHHHHCHHHH
58.28-
144AcetylationEKDLRRAKDINQEVY
HHHHHHHHHHCHHHH
58.2823749302
144SuccinylationEKDLRRAKDINQEVY
HHHHHHHHHHCHHHH
58.28-
144SuccinylationEKDLRRAKDINQEVY
HHHHHHHHHHCHHHH
58.28-
144UbiquitinationEKDLRRAKDINQEVY
HHHHHHHHHHCHHHH
58.2823503661
151NitrationKDINQEVYNFLATAG
HHHCHHHHHHHHHCC
10.23-
151PhosphorylationKDINQEVYNFLATAG
HHHCHHHHHHHHHCC
10.2331136877
156PhosphorylationEVYNFLATAGAKYGV
HHHHHHHHCCCCCCC
27.9825003641
160AcetylationFLATAGAKYGVGFWK
HHHHCCCCCCCCEEC
41.4425038526
193O-linked_GlycosylationVLLIGTDSHTPNGGG
EEEEECCCCCCCCCC
29.1528510447
212UbiquitinationCIGVGGADAVDVMAG
EEECCCCCHHHHHCC
50.8523503661
217UbiquitinationGADAVDVMAGIPWEL
CCCHHHHHCCCCCHH
2.1523503661
233AcetylationCPKVIGVKLTGSLSG
CCCEEEEEEEECCCC
34.8125038526
233SuccinylationCPKVIGVKLTGSLSG
CCCEEEEEEEECCCC
34.81-
233SuccinylationCPKVIGVKLTGSLSG
CCCEEEEEEEECCCC
34.81-
237PhosphorylationIGVKLTGSLSGWSSP
EEEEEEECCCCCCCH
17.719543159
239PhosphorylationVKLTGSLSGWSSPKD
EEEEECCCCCCCHHH
39.6628857561
242PhosphorylationTGSLSGWSSPKDVIL
EECCCCCCCHHHHHE
40.04110757319
243PhosphorylationGSLSGWSSPKDVILK
ECCCCCCCHHHHHEE
29.479543171
245UbiquitinationLSGWSSPKDVILKVA
CCCCCCHHHHHEEEE
67.5823503661
250UbiquitinationSPKDVILKVAGILTV
CHHHHHEEEEEEEEE
20.9323503661
276UbiquitinationGPGVDSISCTGMATI
CCCCCCCEECCCHHH
15.0224816145
309UbiquitinationRMKKYLSKTGREDIA
HHHHHHHHHCHHHHH
53.0224816145
310PhosphorylationMKKYLSKTGREDIAN
HHHHHHHHCHHHHHH
37.7962150913
333UbiquitinationLVPDPGCHYDQLIEI
CCCCCCCCHHHEEEE
34.8122817900
337UbiquitinationPGCHYDQLIEINLSE
CCCCHHHEEEEEHHH
3.2921890473
366UbiquitinationHPVAEVGKVAEKEGW
CCHHHHHHHHHHHCC
43.3722817900
368UbiquitinationVAEVGKVAEKEGWPL
HHHHHHHHHHHCCCC
26.1523503661
370AcetylationEVGKVAEKEGWPLDI
HHHHHHHHHCCCCEE
52.3623954790
370UbiquitinationEVGKVAEKEGWPLDI
HHHHHHHHHCCCCEE
52.3622817900
385GlutathionylationRVGLIGSCTNSSYED
EEEEEECCCCCCHHH
3.3522555962
390PhosphorylationGSCTNSSYEDMGRSA
ECCCCCCHHHHHHHH
18.7746157839
401AcetylationGRSAAVAKQALAHGL
HHHHHHHHHHHHCCC
29.5225953088
401SuccinylationGRSAAVAKQALAHGL
HHHHHHHHHHHHCCC
29.5223954790
401UbiquitinationGRSAAVAKQALAHGL
HHHHHHHHHHHHCCC
29.5223503661
409UbiquitinationQALAHGLKCKSQFTI
HHHHCCCCCEEEEEE
44.1829967540
410S-nitrosylationALAHGLKCKSQFTIT
HHHCCCCCEEEEEEC
6.5324105792
411SuccinylationLAHGLKCKSQFTITP
HHCCCCCEEEEEECC
45.78-
411SuccinylationLAHGLKCKSQFTITP
HHCCCCCEEEEEECC
45.78-
411UbiquitinationLAHGLKCKSQFTITP
HHCCCCCEEEEEECC
45.78-
432PhosphorylationATIERDGYAQILRDL
EEEECCCHHHHHHHC
10.3046157851
432UbiquitinationATIERDGYAQILRDL
EEEECCCHHHHHHHC
10.3024816145
462AcetylationWDRKDIKKGEKNTIV
CCHHHHCCCCCCEEE
73.0525953088
462UbiquitinationWDRKDIKKGEKNTIV
CCHHHHCCCCCCEEE
73.0529967540
465AcetylationKDIKKGEKNTIVTSY
HHHCCCCCCEEEEEE
68.9725953088
465UbiquitinationKDIKKGEKNTIVTSY
HHHCCCCCCEEEEEE
68.9724816145
467PhosphorylationIKKGEKNTIVTSYNR
HCCCCCCEEEEEEEC
28.0820860994
470PhosphorylationGEKNTIVTSYNRNFT
CCCCEEEEEEECCCC
22.9528152594
471PhosphorylationEKNTIVTSYNRNFTG
CCCEEEEEEECCCCC
14.9828152594
472NitrationKNTIVTSYNRNFTGR
CCEEEEEEECCCCCC
14.58-
472PhosphorylationKNTIVTSYNRNFTGR
CCEEEEEEECCCCCC
14.5828152594
474MethylationTIVTSYNRNFTGRND
EEEEEEECCCCCCCC
31.26-
477PhosphorylationTSYNRNFTGRNDANP
EEEECCCCCCCCCCC
38.497687187
487UbiquitinationNDANPETHAFVTSPE
CCCCCCCEEEECCHH
18.6023503661
488UbiquitinationDANPETHAFVTSPEI
CCCCCCEEEECCHHH
14.1823503661
513PhosphorylationKFNPETDYLTGTDGK
CCCCCCCEEECCCCC
17.37119329
515PhosphorylationNPETDYLTGTDGKKF
CCCCCEEECCCCCEE
31.63110757331
5202-HydroxyisobutyrylationYLTGTDGKKFRLEAP
EEECCCCCEEEEECC
52.10-
520AcetylationYLTGTDGKKFRLEAP
EEECCCCCEEEEECC
52.1023954790
520MalonylationYLTGTDGKKFRLEAP
EEECCCCCEEEEECC
52.1026320211
520SuccinylationYLTGTDGKKFRLEAP
EEECCCCCEEEEECC
52.1027452117
520UbiquitinationYLTGTDGKKFRLEAP
EEECCCCCEEEEECC
52.1023503661
521AcetylationLTGTDGKKFRLEAPD
EECCCCCEEEEECCC
41.047624281
521UbiquitinationLTGTDGKKFRLEAPD
EECCCCCEEEEECCC
41.0423503661
523MethylationGTDGKKFRLEAPDAD
CCCCCEEEEECCCHH
40.26-
534AcetylationPDADELPKGEFDPGQ
CCHHHCCCCCCCCCC
81.3923236377
534SuccinylationPDADELPKGEFDPGQ
CCHHHCCCCCCCCCC
81.3927452117
534UbiquitinationPDADELPKGEFDPGQ
CCHHHCCCCCCCCCC
81.3929967540
543PhosphorylationEFDPGQDTYQHPPKD
CCCCCCCCCCCCCCC
19.73110757343
544PhosphorylationFDPGQDTYQHPPKDS
CCCCCCCCCCCCCCC
17.082917121
549AcetylationDTYQHPPKDSSGQHV
CCCCCCCCCCCCCCC
74.7620167786
549MalonylationDTYQHPPKDSSGQHV
CCCCCCCCCCCCCCC
74.7626320211
549SuccinylationDTYQHPPKDSSGQHV
CCCCCCCCCCCCCCC
74.76-
549SuccinylationDTYQHPPKDSSGQHV
CCCCCCCCCCCCCCC
74.76-
551PhosphorylationYQHPPKDSSGQHVDV
CCCCCCCCCCCCCCC
42.3629396449
552PhosphorylationQHPPKDSSGQHVDVS
CCCCCCCCCCCCCCC
53.2429255136
559PhosphorylationSGQHVDVSPTSQRLQ
CCCCCCCCCHHHHHH
20.2829255136
561PhosphorylationQHVDVSPTSQRLQLL
CCCCCCCHHHHHHHC
29.9529255136
562PhosphorylationHVDVSPTSQRLQLLE
CCCCCCHHHHHHHCC
19.3825159151
5732-HydroxyisobutyrylationQLLEPFDKWDGKDLE
HHCCCCCCCCCCCHH
47.79-
573AcetylationQLLEPFDKWDGKDLE
HHCCCCCCCCCCCHH
47.7919608861
573SuccinylationQLLEPFDKWDGKDLE
HHCCCCCCCCCCCHH
47.79-
573SuccinylationQLLEPFDKWDGKDLE
HHCCCCCCCCCCCHH
47.79-
573UbiquitinationQLLEPFDKWDGKDLE
HHCCCCCCCCCCCHH
47.7919608861
577AcetylationPFDKWDGKDLEDLQI
CCCCCCCCCHHHHEE
57.5825038526
577SuccinylationPFDKWDGKDLEDLQI
CCCCCCCCCHHHHEE
57.58-
577SuccinylationPFDKWDGKDLEDLQI
CCCCCCCCCHHHHEE
57.58-
591MalonylationILIKVKGKCTTDHIS
EEEEECCEECCCCHH
23.7726320211
591SuccinylationILIKVKGKCTTDHIS
EEEEECCEECCCCHH
23.77-
591SuccinylationILIKVKGKCTTDHIS
EEEEECCEECCCCHH
23.77-
592S-nitrosocysteineLIKVKGKCTTDHISA
EEEECCEECCCCHHC
7.26-
592GlutathionylationLIKVKGKCTTDHISA
EEEECCEECCCCHHC
7.2622555962
592S-nitrosylationLIKVKGKCTTDHISA
EEEECCEECCCCHHC
7.2622178444
605AcetylationSAAGPWLKFRGHLDN
HCCCCCCEECCCHHH
29.1919608861
605MalonylationSAAGPWLKFRGHLDN
HCCCCCCEECCCHHH
29.1926320211
605SuccinylationSAAGPWLKFRGHLDN
HCCCCCCEECCCHHH
29.19-
605SuccinylationSAAGPWLKFRGHLDN
HCCCCCCEECCCHHH
29.19-
605UbiquitinationSAAGPWLKFRGHLDN
HCCCCCCEECCCHHH
29.1919608861
628AcetylationAINIENGKANSVRNA
EEEEECCCCCHHHHH
56.8525038526
628SuccinylationAINIENGKANSVRNA
EEEEECCCCCHHHHH
56.85-
628SuccinylationAINIENGKANSVRNA
EEEEECCCCCHHHHH
56.85-
646PhosphorylationEFGPVPDTARYYKKH
HCCCCCCHHHHHHHH
13.63110757355
656UbiquitinationYYKKHGIRWVVIGDE
HHHHHCCEEEEECCC
25.4027667366
665PhosphorylationVVIGDENYGEGSSRE
EEECCCCCCCCCCCC
17.952917113
667UbiquitinationIGDENYGEGSSREHA
ECCCCCCCCCCCCCC
45.6123503661
668UbiquitinationGDENYGEGSSREHAA
CCCCCCCCCCCCCCC
26.9323503661
669PhosphorylationDENYGEGSSREHAAL
CCCCCCCCCCCCCCC
23.1728857561
670PhosphorylationENYGEGSSREHAALE
CCCCCCCCCCCCCCC
53.1728857561
679MethylationEHAALEPRHLGGRAI
CCCCCCCCHHCCCEE
28.43-
684UbiquitinationEPRHLGGRAIITKSF
CCCHHCCCEEEEHHH
22.3323503661
6892-HydroxyisobutyrylationGGRAIITKSFARIHE
CCCEEEEHHHHHHHH
32.92-
689AcetylationGGRAIITKSFARIHE
CCCEEEEHHHHHHHH
32.9225825284
689SuccinylationGGRAIITKSFARIHE
CCCEEEEHHHHHHHH
32.92-
689SuccinylationGGRAIITKSFARIHE
CCCEEEEHHHHHHHH
32.92-
689UbiquitinationGGRAIITKSFARIHE
CCCEEEEHHHHHHHH
32.9227667366
690UbiquitinationGRAIITKSFARIHET
CCEEEEHHHHHHHHH
18.5823503661
697UbiquitinationSFARIHETNLKKQGL
HHHHHHHHCCHHCCC
31.5223000965
7002-HydroxyisobutyrylationRIHETNLKKQGLLPL
HHHHHCCHHCCCCCC
45.16-
700AcetylationRIHETNLKKQGLLPL
HHHHHCCHHCCCCCC
45.1625953088
700UbiquitinationRIHETNLKKQGLLPL
HHHHHCCHHCCCCCC
45.1623503661
701UbiquitinationIHETNLKKQGLLPLT
HHHHCCHHCCCCCCE
53.4123503661
703UbiquitinationETNLKKQGLLPLTFA
HHCCHHCCCCCCEEC
37.7523000965
708PhosphorylationKQGLLPLTFADPADY
HCCCCCCEECCHHHC
18.1622210691
715PhosphorylationTFADPADYNKIHPVD
EECCHHHCCCCCCCC
22.0622210691
717UbiquitinationADPADYNKIHPVDKL
CCHHHCCCCCCCCEE
35.8423503661
723AcetylationNKIHPVDKLTIQGLK
CCCCCCCEEEECCCC
48.0025038526
723SuccinylationNKIHPVDKLTIQGLK
CCCCCCCEEEECCCC
48.00-
723SuccinylationNKIHPVDKLTIQGLK
CCCCCCCEEEECCCC
48.00-
723UbiquitinationNKIHPVDKLTIQGLK
CCCCCCCEEEECCCC
48.0023503661
730AcetylationKLTIQGLKDFTPGKP
EEEECCCCCCCCCCC
58.5825038526
730MalonylationKLTIQGLKDFTPGKP
EEEECCCCCCCCCCC
58.5826320211
730SuccinylationKLTIQGLKDFTPGKP
EEEECCCCCCCCCCC
58.58-
730SuccinylationKLTIQGLKDFTPGKP
EEEECCCCCCCCCCC
58.5827452117
730UbiquitinationKLTIQGLKDFTPGKP
EEEECCCCCCCCCCC
58.5823000965
736AcetylationLKDFTPGKPLKCIIK
CCCCCCCCCEEEEEE
48.6725953088
736MalonylationLKDFTPGKPLKCIIK
CCCCCCCCCEEEEEE
48.6726320211
736SuccinylationLKDFTPGKPLKCIIK
CCCCCCCCCEEEEEE
48.6723954790
736UbiquitinationLKDFTPGKPLKCIIK
CCCCCCCCCEEEEEE
48.6723000965
739AcetylationFTPGKPLKCIIKHPN
CCCCCCEEEEEECCC
31.7325953088
739MalonylationFTPGKPLKCIIKHPN
CCCCCCEEEEEECCC
31.7326320211
743AcetylationKPLKCIIKHPNGTQE
CCEEEEEECCCCCEE
32.8526051181

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 ACON_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACON_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 ACON_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KAD3_HUMANAK3physical
22939629
THIL_HUMANACAT1physical
22939629
SIN3A_HUMANSIN3Aphysical
22939629
THIM_HUMANACAA2physical
22939629
SSDH_HUMANALDH5A1physical
26344197
ALDOA_HUMANALDOAphysical
26344197
ALDOC_HUMANALDOCphysical
26344197
AT1B1_HUMANATP1B1physical
26344197
AT5F1_HUMANATP5F1physical
26344197
ATP5J_HUMANATP5Jphysical
26344197
ESTD_HUMANESDphysical
26344197
GPDA_HUMANGPD1physical
26344197
GPD1L_HUMANGPD1Lphysical
26344197
GPDM_HUMANGPD2physical
26344197
PIPNB_HUMANPITPNBphysical
26344197
VAPA_HUMANVAPAphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614559Infantile cerebellar-retinal degeneration (ICRD)
616289Optic atrophy 8 (OPA8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACON_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-50; LYS-573 AND LYS-605, ANDMASS SPECTROMETRY.

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