ECHA_MOUSE - dbPTM
ECHA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECHA_MOUSE
UniProt AC Q8BMS1
Protein Name Trifunctional enzyme subunit alpha, mitochondrial
Gene Name Hadha
Organism Mus musculus (Mouse).
Sequence Length 763
Subcellular Localization Mitochondrion matrix.
Protein Description Bifunctional subunit..
Protein Sequence MVASRAIGSLSRFSAFRILRSRGCICRSFTTSSALLTRTHINYGVKGDVAVIRINSPNSKVNTLNKEVQSEFIEVMNEIWANDQIRSAVLISSKPGCFVAGADINMLSSCTTPQEATRISQEGQRMFEKLEKSPKPVVAAISGSCLGGGLELAIACQYRIATKDRKTVLGVPEVLLGILPGAGGTQRLPKMVGVPAAFDMMLTGRNIRADRAKKMGLVDQLVEPLGPGIKSPEERTIEYLEEVAVNFAKGLADRKVSAKQSKGLVEKLTTYAMTVPFVRQQVYKTVEEKVKKQTKGLYPAPLKIIDAVKAGLEQGSDAGYLAESQKFGELALTKESKALMGLYNGQVLCKKNKFGAPQKNVQQLAILGAGLMGAGIAQVSVDKGLKTLLKDTTVTGLGRGQQQVFKGLNDKVKKKALTSFERDSIFSNLIGQLDYKGFEKADMVIEAVFEDLGVKHKVLKEVESVTPEHCIFASNTSALPINQIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTDKTSKDTTASAVAVGLRQGKVIIVVKDGPGFYTTRCLAPMMSEVMRILQEGVDPKKLDALTTGFGFPVGAATLADEVGVDVAQHVAEDLGKAFGERFGGGSVELLKQMVSKGFLGRKSGKGFYIYQEGSKNKSLNSEMDNILANLRLPAKPEVSSDEDVQYRVITRFVNEAVLCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKVVDRLRKYESAYGTQFTPCQLLLDHANNSSKKFYQ
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
46AcetylationTHINYGVKGDVAVIR
CEECCCCCCCEEEEE
45.0623576753
46SuccinylationTHINYGVKGDVAVIR
CEECCCCCCCEEEEE
45.06-
46SuccinylationTHINYGVKGDVAVIR
CEECCCCCCCEEEEE
45.0623806337
46UbiquitinationTHINYGVKGDVAVIR
CEECCCCCCCEEEEE
45.06-
60AcetylationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.2623806337
60GlutarylationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.2624703693
60MalonylationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.2626073543
60SuccinylationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.26-
60SuccinylationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.2623806337
60UbiquitinationRINSPNSKVNTLNKE
EECCCCHHHCCCCHH
46.2627667366
66AcetylationSKVNTLNKEVQSEFI
HHHCCCCHHHHHHHH
63.4822733758
120PhosphorylationPQEATRISQEGQRMF
HHHHHHHCHHHHHHH
20.9130482847
129AcetylationEGQRMFEKLEKSPKP
HHHHHHHHHHCCCCC
51.1623576753
129SuccinylationEGQRMFEKLEKSPKP
HHHHHHHHHHCCCCC
51.1623806337
163AcetylationCQYRIATKDRKTVLG
HCEEECCCCCCCCCC
46.6523864654
163SuccinylationCQYRIATKDRKTVLG
HCEEECCCCCCCCCC
46.6526388266
166AcetylationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.7923576753
166GlutarylationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.7924703693
166MalonylationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.7926320211
166SuccinylationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.79-
166SuccinylationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.7923806337
166UbiquitinationRIATKDRKTVLGVPE
EECCCCCCCCCCCCH
53.79-
167PhosphorylationIATKDRKTVLGVPEV
ECCCCCCCCCCCCHH
23.1223984901
185PhosphorylationILPGAGGTQRLPKMV
CCCCCCCCCCCCHHH
15.0329233185
190UbiquitinationGGTQRLPKMVGVPAA
CCCCCCCHHHCCCHH
51.3022790023
203PhosphorylationAAFDMMLTGRNIRAD
HHHHHHHHCCCCCHH
19.0529119230
213AcetylationNIRADRAKKMGLVDQ
CCCHHHHHHCCHHHH
44.1623806337
213SuccinylationNIRADRAKKMGLVDQ
CCCHHHHHHCCHHHH
44.16-
213SuccinylationNIRADRAKKMGLVDQ
CCCHHHHHHCCHHHH
44.1623806337
214AcetylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.9023576753
214GlutarylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.9024703693
214MalonylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.9026320211
214PhosphoglycerylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.90-
214SuccinylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.90-
214SuccinylationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.9023806337
214UbiquitinationIRADRAKKMGLVDQL
CCHHHHHHCCHHHHH
36.90-
230AcetylationEPLGPGIKSPEERTI
CCCCCCCCCHHHHHH
66.9123806337
230SuccinylationEPLGPGIKSPEERTI
CCCCCCCCCHHHHHH
66.91-
230SuccinylationEPLGPGIKSPEERTI
CCCCCCCCCHHHHHH
66.9123806337
231PhosphorylationPLGPGIKSPEERTIE
CCCCCCCCHHHHHHH
35.3126824392
249AcetylationEVAVNFAKGLADRKV
HHHHHHHHHHHCCCC
50.7723576753
249SuccinylationEVAVNFAKGLADRKV
HHHHHHHHHHHCCCC
50.77-
249SuccinylationEVAVNFAKGLADRKV
HHHHHHHHHHHCCCC
50.7723806337
255AcetylationAKGLADRKVSAKQSK
HHHHHCCCCCHHHCC
40.886269753
255SuccinylationAKGLADRKVSAKQSK
HHHHHCCCCCHHHCC
40.8826388266
259AcetylationADRKVSAKQSKGLVE
HCCCCCHHHCCCHHH
47.822393849
259SuccinylationADRKVSAKQSKGLVE
HCCCCCHHHCCCHHH
47.8226388266
262AcetylationKVSAKQSKGLVEKLT
CCCHHHCCCHHHHHH
54.492393857
262SuccinylationKVSAKQSKGLVEKLT
CCCHHHCCCHHHHHH
54.4926388266
267AcetylationQSKGLVEKLTTYAMT
HCCCHHHHHHHHHHH
43.5923576753
283PhosphorylationPFVRQQVYKTVEEKV
HHHHHHHHHHHHHHH
9.1520495213
284AcetylationFVRQQVYKTVEEKVK
HHHHHHHHHHHHHHH
47.4323954790
284SuccinylationFVRQQVYKTVEEKVK
HHHHHHHHHHHHHHH
47.4326388266
289AcetylationVYKTVEEKVKKQTKG
HHHHHHHHHHHHCCC
45.9423576753
289SuccinylationVYKTVEEKVKKQTKG
HHHHHHHHHHHHCCC
45.9426388266
291AcetylationKTVEEKVKKQTKGLY
HHHHHHHHHHCCCCC
50.6723576753
291SuccinylationKTVEEKVKKQTKGLY
HHHHHHHHHHCCCCC
50.6726388266
292AcetylationTVEEKVKKQTKGLYP
HHHHHHHHHCCCCCC
67.212393881
292GlutarylationTVEEKVKKQTKGLYP
HHHHHHHHHCCCCCC
67.2124703693
292SuccinylationTVEEKVKKQTKGLYP
HHHHHHHHHCCCCCC
67.2126388266
295AcetylationEKVKKQTKGLYPAPL
HHHHHHCCCCCCCCH
44.4123864654
295GlutarylationEKVKKQTKGLYPAPL
HHHHHHCCCCCCCCH
44.4124703693
295MalonylationEKVKKQTKGLYPAPL
HHHHHHCCCCCCCCH
44.4126320211
295SuccinylationEKVKKQTKGLYPAPL
HHHHHHCCCCCCCCH
44.41-
295UbiquitinationEKVKKQTKGLYPAPL
HHHHHHCCCCCCCCH
44.41-
303AcetylationGLYPAPLKIIDAVKA
CCCCCCHHHHHHHHH
36.2323576753
303GlutarylationGLYPAPLKIIDAVKA
CCCCCCHHHHHHHHH
36.2324703693
303SuccinylationGLYPAPLKIIDAVKA
CCCCCCHHHHHHHHH
36.23-
303SuccinylationGLYPAPLKIIDAVKA
CCCCCCHHHHHHHHH
36.2323806337
303UbiquitinationGLYPAPLKIIDAVKA
CCCCCCHHHHHHHHH
36.23-
309AcetylationLKIIDAVKAGLEQGS
HHHHHHHHHHHHCCC
38.1623576753
309SuccinylationLKIIDAVKAGLEQGS
HHHHHHHHHHHHCCC
38.1626388266
309UbiquitinationLKIIDAVKAGLEQGS
HHHHHHHHHHHHCCC
38.16-
316PhosphorylationKAGLEQGSDAGYLAE
HHHHHCCCCCHHHHH
24.7925521595
320PhosphorylationEQGSDAGYLAESQKF
HCCCCCHHHHHHHCC
12.4027742792
326AcetylationGYLAESQKFGELALT
HHHHHHHCCCCEECC
65.6923576753
326SuccinylationGYLAESQKFGELALT
HHHHHHHCCCCEECC
65.69-
326SuccinylationGYLAESQKFGELALT
HHHHHHHCCCCEECC
65.6923806337
326UbiquitinationGYLAESQKFGELALT
HHHHHHHCCCCEECC
65.69-
333PhosphorylationKFGELALTKESKALM
CCCCEECCHHHHHHH
27.4521183079
334AcetylationFGELALTKESKALMG
CCCEECCHHHHHHHH
61.9223576753
334GlutarylationFGELALTKESKALMG
CCCEECCHHHHHHHH
61.9224703693
334SuccinylationFGELALTKESKALMG
CCCEECCHHHHHHHH
61.92-
334SuccinylationFGELALTKESKALMG
CCCEECCHHHHHHHH
61.9223806337
337AcetylationLALTKESKALMGLYN
EECCHHHHHHHHHHC
46.7823864654
349S-nitrosocysteineLYNGQVLCKKNKFGA
HHCCEEEECCCCCCC
6.57-
349S-nitrosylationLYNGQVLCKKNKFGA
HHCCEEEECCCCCCC
6.5721278135
349S-palmitoylationLYNGQVLCKKNKFGA
HHCCEEEECCCCCCC
6.5728526873
350AcetylationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.0423576753
350GlutarylationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.0424703693
350MalonylationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.0426320211
350SuccinylationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.04-
350SuccinylationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.0423806337
350UbiquitinationYNGQVLCKKNKFGAP
HCCEEEECCCCCCCC
56.04-
351AcetylationNGQVLCKKNKFGAPQ
CCEEEECCCCCCCCC
65.4623201123
351SuccinylationNGQVLCKKNKFGAPQ
CCEEEECCCCCCCCC
65.4626388266
353AcetylationQVLCKKNKFGAPQKN
EEEECCCCCCCCCCC
54.8023576753
353SuccinylationQVLCKKNKFGAPQKN
EEEECCCCCCCCCCC
54.8023806337
383SuccinylationIAQVSVDKGLKTLLK
EEEEECCCHHHHHHH
65.0826388266
386AcetylationVSVDKGLKTLLKDTT
EECCCHHHHHHHCCC
45.8823864654
390AcetylationKGLKTLLKDTTVTGL
CHHHHHHHCCCCCCC
57.0223864654
390SuccinylationKGLKTLLKDTTVTGL
CHHHHHHHCCCCCCC
57.0223806337
390UbiquitinationKGLKTLLKDTTVTGL
CHHHHHHHCCCCCCC
57.02-
393PhosphorylationKTLLKDTTVTGLGRG
HHHHHCCCCCCCCHH
26.6323737553
395PhosphorylationLLKDTTVTGLGRGQQ
HHHCCCCCCCCHHHH
25.2923737553
399MethylationTTVTGLGRGQQQVFK
CCCCCCCHHHHHHHH
44.8024129315
406AcetylationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.7323806337
406GlutarylationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.7324703693
406MalonylationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.7326073543
406SuccinylationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.73-
406SuccinylationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.7323806337
406UbiquitinationRGQQQVFKGLNDKVK
HHHHHHHHCCCHHHH
64.73-
411AcetylationVFKGLNDKVKKKALT
HHHCCCHHHHHHHCH
55.6823576753
411MalonylationVFKGLNDKVKKKALT
HHHCCCHHHHHHHCH
55.6826320211
411SuccinylationVFKGLNDKVKKKALT
HHHCCCHHHHHHHCH
55.68-
411SuccinylationVFKGLNDKVKKKALT
HHHCCCHHHHHHHCH
55.6823806337
413AcetylationKGLNDKVKKKALTSF
HCCCHHHHHHHCHHH
55.0623864654
413MalonylationKGLNDKVKKKALTSF
HCCCHHHHHHHCHHH
55.0626073543
413SuccinylationKGLNDKVKKKALTSF
HCCCHHHHHHHCHHH
55.0624315375
414AcetylationGLNDKVKKKALTSFE
CCCHHHHHHHCHHHH
46.3924062335
414SuccinylationGLNDKVKKKALTSFE
CCCHHHHHHHCHHHH
46.3923806337
415AcetylationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.8023806337
415GlutarylationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.8024703693
415MalonylationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.8026320211
415SuccinylationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.80-
415SuccinylationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.8023806337
415UbiquitinationLNDKVKKKALTSFER
CCHHHHHHHCHHHHH
42.80-
418PhosphorylationKVKKKALTSFERDSI
HHHHHHCHHHHHHHH
35.9127742792
419PhosphorylationVKKKALTSFERDSIF
HHHHHCHHHHHHHHH
26.4323737553
424PhosphorylationLTSFERDSIFSNLIG
CHHHHHHHHHHHHHH
31.5823984901
427PhosphorylationFERDSIFSNLIGQLD
HHHHHHHHHHHHHCC
29.1123984901
436AcetylationLIGQLDYKGFEKADM
HHHHCCCCCHHHHHH
57.7123576753
436SuccinylationLIGQLDYKGFEKADM
HHHHCCCCCHHHHHH
57.71-
436SuccinylationLIGQLDYKGFEKADM
HHHHCCCCCHHHHHH
57.7123806337
440AcetylationLDYKGFEKADMVIEA
CCCCCHHHHHHHHHH
47.6423806337
440SuccinylationLDYKGFEKADMVIEA
CCCCCHHHHHHHHHH
47.64-
440SuccinylationLDYKGFEKADMVIEA
CCCCCHHHHHHHHHH
47.6423806337
455UbiquitinationVFEDLGVKHKVLKEV
HHHHHCCCHHHHHHC
35.5922790023
457AcetylationEDLGVKHKVLKEVES
HHHCCCHHHHHHCCC
43.4724062335
460AcetylationGVKHKVLKEVESVTP
CCCHHHHHHCCCCCH
63.8023576753
460SuccinylationGVKHKVLKEVESVTP
CCCHHHHHHCCCCCH
63.80-
460SuccinylationGVKHKVLKEVESVTP
CCCHHHHHHCCCCCH
63.8023806337
470S-nitrosocysteineESVTPEHCIFASNTS
CCCCHHHEEECCCCC
2.33-
470S-nitrosylationESVTPEHCIFASNTS
CCCCHHHEEECCCCC
2.3321278135
470S-palmitoylationESVTPEHCIFASNTS
CCCCHHHEEECCCCC
2.3328526873
489SuccinylationNQIAAVSKRPEKVIG
HHHHHHCCCCHHEEE
66.4324315375
493AcetylationAVSKRPEKVIGMHYF
HHCCCCHHEEEEEEC
41.6624062335
505AcetylationHYFSPVDKMQLLEII
EECCCCCHHHEEEEH
28.8723576753
505MalonylationHYFSPVDKMQLLEII
EECCCCCHHHEEEEH
28.8726073543
505SuccinylationHYFSPVDKMQLLEII
EECCCCCHHHEEEEH
28.87-
505SuccinylationHYFSPVDKMQLLEII
EECCCCCHHHEEEEH
28.8723806337
516AcetylationLEIITTDKTSKDTTA
EEEHHCCCCCCCCCH
53.2423864654
516SuccinylationLEIITTDKTSKDTTA
EEEHHCCCCCCCCCH
53.2423806337
519AcetylationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.4123576753
519GlutarylationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.4124703693
519MalonylationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.4126073543
519SuccinylationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.41-
519SuccinylationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.4123806337
519UbiquitinationITTDKTSKDTTASAV
HHCCCCCCCCCHHHH
65.41-
540AcetylationGKVIIVVKDGPGFYT
CEEEEEEECCCCCCH
46.1823576753
540SuccinylationGKVIIVVKDGPGFYT
CEEEEEEECCCCCCH
46.1826388266
540UbiquitinationGKVIIVVKDGPGFYT
CEEEEEEECCCCCCH
46.18-
550S-nitrosocysteinePGFYTTRCLAPMMSE
CCCCHHHHHHHHHHH
3.40-
550S-nitrosylationPGFYTTRCLAPMMSE
CCCCHHHHHHHHHHH
3.4021278135
556PhosphorylationRCLAPMMSEVMRILQ
HHHHHHHHHHHHHHH
22.3127566939
569AcetylationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.6023576753
569GlutarylationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.6024703693
569MalonylationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.6026073543
569SuccinylationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.60-
569SuccinylationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.6023806337
569UbiquitinationLQEGVDPKKLDALTT
HHCCCCHHHCHHHHC
62.60-
570AcetylationQEGVDPKKLDALTTG
HCCCCHHHCHHHHCC
57.9224062335
570SuccinylationQEGVDPKKLDALTTG
HCCCCHHHCHHHHCC
57.9224315375
575PhosphorylationPKKLDALTTGFGFPV
HHHCHHHHCCCCCCC
26.9620495213
576PhosphorylationKKLDALTTGFGFPVG
HHCHHHHCCCCCCCC
31.2220495213
586PhosphorylationGFPVGAATLADEVGV
CCCCCHHHHHHHHCC
23.1920495213
615PhosphorylationGERFGGGSVELLKQM
HHHHCCCHHHHHHHH
18.7219060867
620AcetylationGGSVELLKQMVSKGF
CCHHHHHHHHHHCCC
49.3123806337
620SuccinylationGGSVELLKQMVSKGF
CCHHHHHHHHHHCCC
49.31-
620SuccinylationGGSVELLKQMVSKGF
CCHHHHHHHHHHCCC
49.3123806337
620UbiquitinationGGSVELLKQMVSKGF
CCHHHHHHHHHHCCC
49.31-
625AcetylationLLKQMVSKGFLGRKS
HHHHHHHCCCCCCCC
42.1224062335
631AcetylationSKGFLGRKSGKGFYI
HCCCCCCCCCCCEEE
62.862393941
632PhosphorylationKGFLGRKSGKGFYIY
CCCCCCCCCCCEEEE
44.3626643407
634AcetylationFLGRKSGKGFYIYQE
CCCCCCCCCEEEEEC
53.6023806337
634SuccinylationFLGRKSGKGFYIYQE
CCCCCCCCCEEEEEC
53.60-
634SuccinylationFLGRKSGKGFYIYQE
CCCCCCCCCEEEEEC
53.6023806337
637PhosphorylationRKSGKGFYIYQEGSK
CCCCCCEEEEECCCC
13.8526643407
639PhosphorylationSGKGFYIYQEGSKNK
CCCCEEEEECCCCCC
6.8026643407
643PhosphorylationFYIYQEGSKNKSLNS
EEEEECCCCCCCCCH
32.1023737553
644AcetylationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.3023576753
644GlutarylationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.3024703693
644MalonylationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.3026073543
644SuccinylationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.30-
644SuccinylationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.3023806337
644UbiquitinationYIYQEGSKNKSLNSE
EEEECCCCCCCCCHH
78.30-
646AcetylationYQEGSKNKSLNSEMD
EECCCCCCCCCHHHH
61.1223806337
646SuccinylationYQEGSKNKSLNSEMD
EECCCCCCCCCHHHH
61.12-
646SuccinylationYQEGSKNKSLNSEMD
EECCCCCCCCCHHHH
61.1223806337
646UbiquitinationYQEGSKNKSLNSEMD
EECCCCCCCCCHHHH
61.12-
647PhosphorylationQEGSKNKSLNSEMDN
ECCCCCCCCCHHHHH
42.0223737553
650PhosphorylationSKNKSLNSEMDNILA
CCCCCCCHHHHHHHH
39.3223737553
664AcetylationANLRLPAKPEVSSDE
HHCCCCCCCCCCCCC
39.5123576753
664GlutarylationANLRLPAKPEVSSDE
HHCCCCCCCCCCCCC
39.5124703693
664SuccinylationANLRLPAKPEVSSDE
HHCCCCCCCCCCCCC
39.51-
664SuccinylationANLRLPAKPEVSSDE
HHCCCCCCCCCCCCC
39.5123806337
664UbiquitinationANLRLPAKPEVSSDE
HHCCCCCCCCCCCCC
39.51-
668PhosphorylationLPAKPEVSSDEDVQY
CCCCCCCCCCCCHHH
30.3426525534
669PhosphorylationPAKPEVSSDEDVQYR
CCCCCCCCCCCHHHH
50.6326525534
675PhosphorylationSSDEDVQYRVITRFV
CCCCCHHHHHHHHHH
13.4926032504
724PhosphorylationPFRFVDLYGAQKVVD
CEEEEHHHCHHHHHH
13.1217242355
728AcetylationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.6323576753
728GlutarylationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.6324703693
728MalonylationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.6326320211
728SuccinylationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.63-
728SuccinylationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.6323806337
728UbiquitinationVDLYGAQKVVDRLRK
EHHHCHHHHHHHHHH
43.63-
735AcetylationKVVDRLRKYESAYGT
HHHHHHHHHHHHHCC
58.9423576753
735UbiquitinationKVVDRLRKYESAYGT
HHHHHHHHHHHHHCC
58.9422790023
745PhosphorylationSAYGTQFTPCQLLLD
HHHCCCCCHHHHHHH
17.2127742792
747S-nitrosocysteineYGTQFTPCQLLLDHA
HCCCCCHHHHHHHCC
3.96-
747S-nitrosylationYGTQFTPCQLLLDHA
HCCCCCHHHHHHHCC
3.9621278135
747S-palmitoylationYGTQFTPCQLLLDHA
HCCCCCHHHHHHHCC
3.9628526873
757PhosphorylationLLDHANNSSKKFYQ-
HHHCCCCCCCCCCC-
43.2627742792
758PhosphorylationLDHANNSSKKFYQ--
HHCCCCCCCCCCC--
41.8227742792
759AcetylationDHANNSSKKFYQ---
HCCCCCCCCCCC---
46.8823576753
759SuccinylationDHANNSSKKFYQ---
HCCCCCCCCCCC---
46.88-
759SuccinylationDHANNSSKKFYQ---
HCCCCCCCCCCC---
46.8823806337
759UbiquitinationDHANNSSKKFYQ---
HCCCCCCCCCCC---
46.88-
760AcetylationHANNSSKKFYQ----
CCCCCCCCCCC----
51.78155825
760SuccinylationHANNSSKKFYQ----
CCCCCCCCCCC----
51.7826388266

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 ECHA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
569KAcetylation

23806337
728KAcetylation

23806337

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 ECHA_MOUSE !!

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

Oops, there are no PPI records of ECHA_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129; LYS-326; LYS-350;LYS-569 AND LYS-728, AND MASS SPECTROMETRY.

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