ACAD9_HUMAN - dbPTM
ACAD9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACAD9_HUMAN
UniProt AC Q9H845
Protein Name Acyl-CoA dehydrogenase family member 9, mitochondrial
Gene Name ACAD9
Organism Homo sapiens (Human).
Sequence Length 621
Subcellular Localization Mitochondrion .
Protein Description Required for mitochondrial complex I assembly. [PubMed: 20816094]
Protein Sequence MSGCGLFLRTTAAARACRGLVVSTANRRLLRTSPPVRAFAKELFLGKIKKKEVFPFPEVSQDELNEINQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRTC
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
10PhosphorylationGCGLFLRTTAAARAC
CCCHHHHHHHHHHHH		23.9620860994
11PhosphorylationCGLFLRTTAAARACR
CCHHHHHHHHHHHHH		14.0920068231
41AcetylationPPVRAFAKELFLGKI
HHHHHHHHHHHCCCC		48.7919608861
41MalonylationPPVRAFAKELFLGKI
HHHHHHHHHHHCCCC		48.7926320211
41SuccinylationPPVRAFAKELFLGKI
HHHHHHHHHHHCCCC		48.7923954790
47AcetylationAKELFLGKIKKKEVF
HHHHHCCCCCCCCCC		54.2025953088
47MalonylationAKELFLGKIKKKEVF
HHHHHCCCCCCCCCC		54.2026320211
92SuccinylationRKIDQEGKIPDETLE
HCCCCCCCCCHHHHH		50.76-
92AcetylationRKIDQEGKIPDETLE
HCCCCCCCCCHHHHH		50.7625953088
92SuccinylationRKIDQEGKIPDETLE
HCCCCCCCCCHHHHH		50.76-
100UbiquitinationIPDETLEKLKSLGLF
CCHHHHHHHHHCCCC		65.4129967540
135UbiquitinationLGEIISMDGSITVTL
HHHHCCCCCCEEEEE		40.6824816145
158PhosphorylationKGIILAGTEEQKAKY
CCEEEECCHHHHHHH		30.6421406692
185PhosphorylationFCLTEPASGSDAASI
EEECCCCCCCCHHHH		49.9328348404
187PhosphorylationLTEPASGSDAASIRS
ECCCCCCCCHHHHHH		22.9172272969
229PhosphorylationIFTVFAKTEVVDSDG
EEEEEEECEEECCCC		30.4921406692
234PhosphorylationAKTEVVDSDGSVKDK
EECEEECCCCCCCCE		32.0621406692
237PhosphorylationEVVDSDGSVKDKITA
EEECCCCCCCCEEEE		30.8621406692
239SuccinylationVDSDGSVKDKITAFI
ECCCCCCCCEEEEEE		55.8123954790
241AcetylationSDGSVKDKITAFIVE
CCCCCCCEEEEEEEE		35.9225038526
255PhosphorylationERDFGGVTNGKPEDK
EECCCCCCCCCCCCC		41.3420068231
258AcetylationFGGVTNGKPEDKLGI
CCCCCCCCCCCCCCC		47.5125038526
258UbiquitinationFGGVTNGKPEDKLGI
CCCCCCCCCCCCCCC		47.5124816145
266MethylationPEDKLGIRGSNTCEV
CCCCCCCCCCCEEEE		40.46-
279UbiquitinationEVHFENTKIPVENIL
EEEECCCCCCHHHHH		57.5029967540
297SulfoxidationGDGFKVAMNILNSGR
CCHHHHHHHHHHCCC		3.4321406390
306PhosphorylationILNSGRFSMGSVVAG
HHHCCCCCHHHHHHH		22.3720071362
309PhosphorylationSGRFSMGSVVAGLLK
CCCCCHHHHHHHHHH		12.5520071362
322PhosphorylationLKRLIEMTAEYACTR
HHHHHHHHHHHHHHH		11.9829449344
325PhosphorylationLIEMTAEYACTRKQF
HHHHHHHHHHHHHHH		12.4383331
328PhosphorylationMTAEYACTRKQFNKR
HHHHHHHHHHHHHHH		32.5029449344
337PhosphorylationKQFNKRLSEFGLIQE
HHHHHHHHHHCCHHH		34.6123312004
435PhosphorylationTNEILRMYIALTGLQ
HHHHHHHHHHHHCHH		4.0719845377
439PhosphorylationLRMYIALTGLQHAGR
HHHHHHHHCHHHHHH		27.1619845377
456AcetylationTTRIHELKQAKVSTV
HHHHHHHHHCCHHHH		45.2725953088
464SulfoxidationQAKVSTVMDTVGRRL
HCCHHHHHHHHHHHH		3.4721406390
466PhosphorylationKVSTVMDTVGRRLRD
CHHHHHHHHHHHHHH		13.5320860994
474PhosphorylationVGRRLRDSLGRTVDL
HHHHHHHHHCCEEEE		26.7023401153
478PhosphorylationLRDSLGRTVDLGLTG
HHHHHCCEEEECCCC		19.30-
521MalonylationTLLLRFGKTIMEEQL
HHHHHHCCHHHHHHH		31.9726320211
521SuccinylationTLLLRFGKTIMEEQL
HHHHHHCCHHHHHHH		31.97-
521SuccinylationTLLLRFGKTIMEEQL
HHHHHHCCHHHHHHH		31.97-
521AcetylationTLLLRFGKTIMEEQL
HHHHHHCCHHHHHHH		31.9726051181
599UbiquitinationENLDEQIKKVSQQIL
CCHHHHHHHHHHHHH		46.9823503661
600UbiquitinationNLDEQIKKVSQQILE
CHHHHHHHHHHHHHH		49.0723503661
602PhosphorylationDEQIKKVSQQILEKR
HHHHHHHHHHHHHHH		25.8328555341
608SuccinylationVSQQILEKRAYICAH
HHHHHHHHHCHHHCC		38.5923954790
608AcetylationVSQQILEKRAYICAH
HHHHHHHHHCHHHCC		38.5919608861
608UbiquitinationVSQQILEKRAYICAH
HHHHHHHHHCHHHCC		38.5919608861
611PhosphorylationQILEKRAYICAHPLD
HHHHHHCHHHCCCCC		10.687320027
619MethylationICAHPLDRTC-----
HHCCCCCCCC-----		45.75-
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 ACAD9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACAD9_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 ACAD9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDUA2_HUMANNDUFA2physical
22939629
VAMP2_HUMANVAMP2physical
22939629
SSRA_HUMANSSR1physical
22939629
RM01_HUMANMRPL1physical
22939629
ERAL1_HUMANERAL1physical
22939629
ODP2_HUMANDLATphysical
22939629
VDAC1_HUMANVDAC1physical
22939629
TIM50_HUMANTIMM50physical
22939629
ECSIT_HUMANECSITphysical
24344204
DPS1_HUMANPDSS1physical
24344204
CIA30_HUMANNDUFAF1physical
24344204
T126B_HUMANTMEM126Bphysical
24344204
RL26L_HUMANRPL26L1physical
24344204
ABCF2_HUMANABCF2physical
24344204
TIDC1_HUMANTIMMDC1physical
24344204
NDUF3_HUMANNDUFAF3physical
24344204
ODB2_HUMANDBTphysical
24344204
NU6M_HUMANND6physical
24344204
NDUS3_HUMANNDUFS3physical
24344204
NDUS2_HUMANNDUFS2physical
24344204
ECSIT_HUMANECSITphysical
20816094
CIA30_HUMANNDUFAF1physical
20816094
DLP1_HUMANPDSS2physical
28514442
CIA30_HUMANNDUFAF1physical
28514442
COA1_HUMANCOA1physical
28514442
DPS1_HUMANPDSS1physical
28514442
BPIA2_HUMANBPIFA2physical
28514442
ODB2_HUMANDBTphysical
28514442
TBB1_HUMANTUBB1physical
28514442
NFS1_HUMANNFS1physical
28514442
NDUC2_HUMANNDUFC2physical
28514442
PDK1_HUMANPDK1physical
28514442
PDK2_HUMANPDK2physical
28514442
INVO_HUMANIVLphysical
28514442
NPS3A_HUMANNIPSNAP3Aphysical
28514442
SDHA_HUMANSDHAphysical
28514442
PNPT1_HUMANPNPT1physical
28514442
PDK3_HUMANPDK3physical
28514442
PEPL_HUMANPPLphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
POF1B_HUMANPOF1Bphysical
28514442
SPB3_HUMANSERPINB3physical
28514442
SPB13_HUMANSERPINB13physical
28514442
ZG16B_HUMANZG16Bphysical
28514442
SPB5_HUMANSERPINB5physical
28514442
GLSK_HUMANGLSphysical
28514442
EVPL_HUMANEVPLphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611126Acyl-CoA dehydrogenase family, member 9, deficiency (ACAD9 deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACAD9_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-41 AND LYS-608, AND MASSSPECTROMETRY.

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