ECHD1_HUMAN - dbPTM
ECHD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECHD1_HUMAN
UniProt AC Q9NTX5
Protein Name Ethylmalonyl-CoA decarboxylase
Gene Name ECHDC1
Organism Homo sapiens (Human).
Sequence Length 307
Subcellular Localization Cytoplasm, cytosol.
Protein Description Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level..
Protein Sequence MALKQEMAKSLLKTASLSGRTKLLHQTGLSLYSTSHGFYEEEVKKTLQQFPGGSIDLQKEDNGIGILTLNNPSRMNAFSGVMMLQLLEKVIELENWTEGKGLIVRGAKNTFSSGSDLNAVKSLGTPEDGMAVCMFMQNTLTRFMRLPLISVALVQGWALGGGAEFTTACDFRLMTPESKIRFVHKEMGIIPSWGGTTRLVEIIGSRQALKVLSGALKLDSKNALNIGMVEEVLQSSDETKSLEEAQEWLKQFIQGPPEVIRALKKSVCSGRELYLEEALQNERDLLGTVWGGPANLEAIAKKGKFNK
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
2 (in isoform 2)Acetylation-24.3822814378
2 (in isoform 5)Acetylation-24.3822814378
2 (in isoform 6)Acetylation-24.3822814378
7Ubiquitination-MALKQEMAKSLLKT
-CCHHHHHHHHHHHH		5.4327667366
9UbiquitinationALKQEMAKSLLKTAS
CHHHHHHHHHHHHHH		40.08-
10PhosphorylationLKQEMAKSLLKTASL
HHHHHHHHHHHHHHH		29.4224719451
13UbiquitinationEMAKSLLKTASLSGR
HHHHHHHHHHHHCCC		47.5427667366
14PhosphorylationMAKSLLKTASLSGRT
HHHHHHHHHHHCCCC		22.8126437602
16PhosphorylationKSLLKTASLSGRTKL
HHHHHHHHHCCCCHH		28.4433259812
18PhosphorylationLLKTASLSGRTKLLH
HHHHHHHCCCCHHHH		24.5927794612
19UbiquitinationLKTASLSGRTKLLHQ
HHHHHHCCCCHHHHH		46.7123503661
27UbiquitinationRTKLLHQTGLSLYST
CCHHHHHHCCCEECC		29.3727667366
30PhosphorylationLLHQTGLSLYSTSHG
HHHHHCCCEECCCCC		26.9728857561
34PhosphorylationTGLSLYSTSHGFYEE
HCCCEECCCCCCCHH		15.9326657352
38UbiquitinationLYSTSHGFYEEEVKK
EECCCCCCCHHHHHH		6.0923000965
39UbiquitinationYSTSHGFYEEEVKKT
ECCCCCCCHHHHHHH		27.3321890473
39PhosphorylationYSTSHGFYEEEVKKT
ECCCCCCCHHHHHHH		27.3329496907
39UbiquitinationYSTSHGFYEEEVKKT
ECCCCCCCHHHHHHH		27.3321890473
39 (in isoform 2)Ubiquitination-27.3321890473
39UbiquitinationYSTSHGFYEEEVKKT
ECCCCCCCHHHHHHH		27.3321890473
39UbiquitinationYSTSHGFYEEEVKKT
ECCCCCCCHHHHHHH		27.3321890473
40 (in isoform 4)Ubiquitination-45.48-
40UbiquitinationSTSHGFYEEEVKKTL
CCCCCCCHHHHHHHH		45.4829967540
44UbiquitinationGFYEEEVKKTLQQFP
CCCHHHHHHHHHHCC		43.2323000965
45UbiquitinationFYEEEVKKTLQQFPG
CCHHHHHHHHHHCCC		60.6923000965
45 (in isoform 1)Ubiquitination-60.6921890473
53UbiquitinationTLQQFPGGSIDLQKE
HHHHCCCCCCEEECC		22.9723503661
53 (in isoform 2)Ubiquitination-22.9721890473
54PhosphorylationLQQFPGGSIDLQKED
HHHCCCCCCEEECCC		20.8825159151
56 (in isoform 4)Phosphorylation-44.75-
59 (in isoform 1)Ubiquitination-74.4721890473
59UbiquitinationGGSIDLQKEDNGIGI
CCCCEEECCCCCEEE		74.4721906983
92UbiquitinationQLLEKVIELENWTEG
HHHHHHHHHCCCCCC		53.6821890473
94UbiquitinationLEKVIELENWTEGKG
HHHHHHHCCCCCCCC		37.6223503661
94 (in isoform 2)Ubiquitination-37.6221890473
99UbiquitinationELENWTEGKGLIVRG
HHCCCCCCCCEEEEC		23.1923503661
100 (in isoform 1)Ubiquitination-44.2921890473
100UbiquitinationLENWTEGKGLIVRGA
HCCCCCCCCEEEECC		44.2921906983
102 (in isoform 2)Ubiquitination-3.5921890473
102UbiquitinationNWTEGKGLIVRGAKN
CCCCCCCEEEECCCC		3.5927667366
103UbiquitinationWTEGKGLIVRGAKNT
CCCCCCEEEECCCCC		2.4323503661
108UbiquitinationGLIVRGAKNTFSSGS
CEEEECCCCCCCCCC		60.3821906983
108 (in isoform 1)Ubiquitination-60.3821890473
110PhosphorylationIVRGAKNTFSSGSDL
EEECCCCCCCCCCCH		24.96-
115UbiquitinationKNTFSSGSDLNAVKS
CCCCCCCCCHHHHHH		40.6529967540
129UbiquitinationSLGTPEDGMAVCMFM
HHCCCCCHHHHHHHH		12.3221890473
129UbiquitinationSLGTPEDGMAVCMFM
HHCCCCCHHHHHHHH		12.3221890473
129UbiquitinationSLGTPEDGMAVCMFM
HHCCCCCHHHHHHHH		12.3221890473
131 (in isoform 5)Phosphorylation-9.26-
132UbiquitinationTPEDGMAVCMFMQNT
CCCCHHHHHHHHHHH		1.4823503661
136UbiquitinationGMAVCMFMQNTLTRF
HHHHHHHHHHHHHHH		0.8923503661
140UbiquitinationCMFMQNTLTRFMRLP
HHHHHHHHHHHHHHH		4.1923503661
147UbiquitinationLTRFMRLPLISVALV
HHHHHHHHHHHHHHH		19.7924816145
159UbiquitinationALVQGWALGGGAEFT
HHHHCCCCCCCCEEE		5.4429967540
169UbiquitinationGAEFTTACDFRLMTP
CCEEEECCCEEECCC		4.8323503661
173 (in isoform 2)Ubiquitination-4.5321890473
175PhosphorylationACDFRLMTPESKIRF
CCCEEECCCHHHHHE		28.61-
179AcetylationRLMTPESKIRFVHKE
EECCCHHHHHEHHHH		35.9226822725
179UbiquitinationRLMTPESKIRFVHKE
EECCCHHHHHEHHHH		35.92-
179MalonylationRLMTPESKIRFVHKE
EECCCHHHHHEHHHH		35.9226320211
179 (in isoform 1)Ubiquitination-35.9221890473
184UbiquitinationESKIRFVHKEMGIIP
HHHHHEHHHHHCCCC		20.0424816145
185MalonylationSKIRFVHKEMGIIPS
HHHHEHHHHHCCCCC		44.0626320211
189UbiquitinationFVHKEMGIIPSWGGT
EHHHHHCCCCCCCCH		3.9521890473
204 (in isoform 2)Ubiquitination-23.5721890473
204UbiquitinationTRLVEIIGSRQALKV
HHHHHHHCCHHHHHH		23.5721890473
204UbiquitinationTRLVEIIGSRQALKV
HHHHHHHCCHHHHHH		23.5721890473
205O-linked_GlycosylationRLVEIIGSRQALKVL
HHHHHHCCHHHHHHH		15.7130379171
205PhosphorylationRLVEIIGSRQALKVL
HHHHHHCCHHHHHHH		15.7122496350
210 (in isoform 1)Ubiquitination-44.1121890473
210UbiquitinationIGSRQALKVLSGALK
HCCHHHHHHHHHCCC		44.1121890473
211UbiquitinationGSRQALKVLSGALKL
CCHHHHHHHHHCCCC		5.5223503661
215 (in isoform 2)Ubiquitination-9.7221890473
215UbiquitinationALKVLSGALKLDSKN
HHHHHHHCCCCCCCC		9.7223503661
217SuccinylationKVLSGALKLDSKNAL
HHHHHCCCCCCCCCC		50.1127452117
217AcetylationKVLSGALKLDSKNAL
HHHHHCCCCCCCCCC		50.1123749302
217SuccinylationKVLSGALKLDSKNAL
HHHHHCCCCCCCCCC		50.11-
217MalonylationKVLSGALKLDSKNAL
HHHHHCCCCCCCCCC		50.1126320211
217UbiquitinationKVLSGALKLDSKNAL
HHHHHCCCCCCCCCC		50.1123503661
220UbiquitinationSGALKLDSKNALNIG
HHCCCCCCCCCCCCH		37.9429967540
221UbiquitinationGALKLDSKNALNIGM
HCCCCCCCCCCCCHH		46.0021906983
221 (in isoform 1)Ubiquitination-46.0021890473
234UbiquitinationGMVEEVLQSSDETKS
HHHHHHHHCCHHHCC		46.1729967540
235PhosphorylationMVEEVLQSSDETKSL
HHHHHHHCCHHHCCH		35.28-
236PhosphorylationVEEVLQSSDETKSLE
HHHHHHCCHHHCCHH		26.89-
240UbiquitinationLQSSDETKSLEEAQE
HHCCHHHCCHHHHHH		51.5029967540
244 (in isoform 2)Ubiquitination-62.03-
244UbiquitinationDETKSLEEAQEWLKQ
HHHCCHHHHHHHHHH		62.0323503661
250UbiquitinationEEAQEWLKQFIQGPP
HHHHHHHHHHHHCCH		44.2123503661
259UbiquitinationFIQGPPEVIRALKKS
HHHCCHHHHHHHHHH		4.4124816145
265UbiquitinationEVIRALKKSVCSGRE
HHHHHHHHHHCCCCH		49.3124816145
295UbiquitinationTVWGGPANLEAIAKK
CHHCCHHHHHHHHHH		41.3629967540
295 (in isoform 2)Ubiquitination-41.3621890473
301AcetylationANLEAIAKKGKFNK-
HHHHHHHHHCCCCC-		56.8125953088
301SuccinylationANLEAIAKKGKFNK-
HHHHHHHHHCCCCC-		56.8121906983
301UbiquitinationANLEAIAKKGKFNK-
HHHHHHHHHCCCCC-		56.8129967540
301 (in isoform 1)Ubiquitination-56.8121890473
301SuccinylationANLEAIAKKGKFNK-
HHHHHHHHHCCCCC-		56.81-
302UbiquitinationNLEAIAKKGKFNK--
HHHHHHHHCCCCC--		59.31-
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 ECHD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECHD1_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 ECHD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PNPH_HUMANPNPphysical
26344197
RMD1_HUMANRMDN1physical
26344197
SNP47_HUMANSNAP47physical
27173435
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 ECHD1_HUMAN

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Related Literatures of Post-Translational Modification

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