IVD_HUMAN - dbPTM
IVD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IVD_HUMAN
UniProt AC P26440
Protein Name Isovaleryl-CoA dehydrogenase, mitochondrial
Gene Name IVD
Organism Homo sapiens (Human).
Sequence Length 423
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFH
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
55AcetylationQLRQTMAKFLQEHLA
HHHHHHHHHHHHHHC		35.4725953088
55UbiquitinationQLRQTMAKFLQEHLA
HHHHHHHHHHHHHHC		35.47-
55SuccinylationQLRQTMAKFLQEHLA
HHHHHHHHHHHHHHC		35.4721890473
55SuccinylationQLRQTMAKFLQEHLA
HHHHHHHHHHHHHHC		35.47-
58UbiquitinationQTMAKFLQEHLAPKA
HHHHHHHHHHHCHHH		38.9121890473
58UbiquitinationQTMAKFLQEHLAPKA
HHHHHHHHHHHCHHH		38.91-
58SuccinylationQTMAKFLQEHLAPKA
HHHHHHHHHHHCHHH		38.91-
58AcetylationQTMAKFLQEHLAPKA
HHHHHHHHHHHCHHH		38.91-
64AcetylationLQEHLAPKAQEIDRS
HHHHHCHHHHHCCCC		58.03-
64MalonylationLQEHLAPKAQEIDRS
HHHHHCHHHHHCCCC		58.0326320211
64SuccinylationLQEHLAPKAQEIDRS
HHHHHCHHHHHCCCC		58.03-
67AcetylationHLAPKAQEIDRSNEF
HHCHHHHHCCCCHHH		52.28-
67SuccinylationHLAPKAQEIDRSNEF
HHCHHHHHCCCCHHH		52.28-
75AcetylationIDRSNEFKNLREFWK
CCCCHHHHHHHHHHH		49.2219608861
75SuccinylationIDRSNEFKNLREFWK
CCCCHHHHHHHHHHH		49.2227452117
75SuccinylationIDRSNEFKNLREFWK
CCCCHHHHHHHHHHH		49.22-
78UbiquitinationSNEFKNLREFWKQLG
CHHHHHHHHHHHHHC		46.5919608861
78SuccinylationSNEFKNLREFWKQLG
CHHHHHHHHHHHHHC		46.59-
78AcetylationSNEFKNLREFWKQLG
CHHHHHHHHHHHHHC		46.5919608861
149PhosphorylationNEAQKEKYLPKLISG
CHHHHHHHHHHHHCC		29.3628111955
152AcetylationQKEKYLPKLISGEYI
HHHHHHHHHHCCCEE		56.7225038526
155PhosphorylationKYLPKLISGEYIGAL
HHHHHHHCCCEEEEE		35.6921253578
158PhosphorylationPKLISGEYIGALAMS
HHHHCCCEEEEEEEC		14.2621253578
161PhosphorylationISGEYIGALAMSEPN
HCCCEEEEEEECCCC		5.21-
171PhosphorylationMSEPNAGSDVVSMKL
ECCCCCCCCCEEEEE		25.4829507054
211PhosphorylationVLIVYAKTDLAAVPA
EEEEEEECCHHCCCC		28.2420068231
214PhosphorylationVYAKTDLAAVPASRG
EEEECCHHCCCCCCC		14.8220068231
219PhosphorylationDLAAVPASRGITAFI
CHHCCCCCCCCEEEE		25.6020068231
222PhosphorylationAVPASRGITAFIVEK
CCCCCCCCEEEEEEC		2.1420068231
236PhosphorylationKGMPGFSTSKKLDKL
CCCCCCCCCHHHHHH		42.1620860994
238AcetylationMPGFSTSKKLDKLGM
CCCCCCCHHHHHHCC		58.4025953088
238MalonylationMPGFSTSKKLDKLGM
CCCCCCCHHHHHHCC		58.4026320211
239UbiquitinationPGFSTSKKLDKLGMR
CCCCCCHHHHHHCCC		62.78-
239AcetylationPGFSTSKKLDKLGMR
CCCCCCHHHHHHCCC		62.7824888379
241AcetylationFSTSKKLDKLGMRGS
CCCCHHHHHHCCCCC		53.68-
242UbiquitinationSTSKKLDKLGMRGSN
CCCHHHHHHCCCCCC		58.33-
259AcetylationELIFEDCKIPAANIL
HHHHCCCCCCHHHHC		65.1425038526
259SuccinylationELIFEDCKIPAANIL
HHHHCCCCCCHHHHC		65.14-
262AcetylationFEDCKIPAANILGHE
HCCCCCCHHHHCCCC		19.33-
262SuccinylationFEDCKIPAANILGHE
HCCCCCCHHHHCCCC		19.33-
274PhosphorylationGHENKGVYVLMSGLD
CCCCCCEEEEECCCC		9.13-
277PhosphorylationNKGVYVLMSGLDLER
CCCEEEEECCCCHHH		1.81-
302PhosphorylationMQAVLDHTIPYLHVR
HHHHHHCCCCCHHHH		24.2622210691
305PhosphorylationVLDHTIPYLHVREAF
HHHCCCCCHHHHHHH		12.9422210691
315SuccinylationVREAFGQKIGHFQLM
HHHHHHCCCCCHHHH		51.54-
315AcetylationVREAFGQKIGHFQLM
HHHHHHCCCCCHHHH		51.5425953088
318SuccinylationAFGQKIGHFQLMQGK
HHHCCCCCHHHHCHH		15.68-
3182-HydroxyisobutyrylationAFGQKIGHFQLMQGK
HHHCCCCCHHHHCHH		15.68-
330PhosphorylationQGKMADMYTRLMACR
CHHHHHHHHHHHHHH		6.83-
331PhosphorylationGKMADMYTRLMACRQ
HHHHHHHHHHHHHHH		15.64-
341PhosphorylationMACRQYVYNVAKACD
HHHHHHHHHHHHHCC		10.05-
345AcetylationQYVYNVAKACDEGHC
HHHHHHHHHCCCCCC		45.3126051181
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 IVD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IVD_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 IVD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ETFA_HUMANETFAphysical
27499296
ETFB_HUMANETFBphysical
27499296
IVD_HUMANIVDphysical
27499296
MPPB_HUMANPMPCBphysical
27499296
MPPA_HUMANPMPCAphysical
27499296
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
243500Isovaleric acidemia (IVA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB03147Flavin adenine dinucleotide
Regulatory Network of IVD_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-75, AND MASS SPECTROMETRY.

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