ACD11_HUMAN - dbPTM
ACD11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACD11_HUMAN
UniProt AC Q709F0
Protein Name Acyl-CoA dehydrogenase family member 11
Gene Name ACAD11
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization Peroxisome. Mitochondrion . Has been detected associated with mitochondrial membrane, but no matrix, in kidney and cerebellum, as well as in a neuroblastoma cell line, but not in skin fibroblasts, where it is observed in cytoplasmic vesicles (PubMed:
Protein Description Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA..
Protein Sequence MKPGATGESDLAEVLPQHKFDSKSLEAYLNQHLSGFGAEREATLTIAQYRAGKSNPTFYLQKGFQTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFYVMEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLRSLNIQSLQLEGYGIGAGYCKRQVSTWTKQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPKECRVIAVLDWELSTIGHPLSDLAHFSLFYFWPRTVPMINQGSYSENSGIPSMEELISIYCRCRGINSILPNWNFFLALSYFKMAGIAQGVYSRYLLGNNSSEDSFLFANIVQPLAETGLQLSKRTFSTVLPQIDTTGQLFVQTRKGQEVLIKVKHFMKQHILPAEKEVTEFYVQNENSVDKWGKPLVIDKLKEMAKVEGLWNLFLPAVSGLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVINGKKWWSSGAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNFHGGHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQAKRLTAKI
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
6Phosphorylation--MKPGATGESDLAE
--CCCCCCCCCCHHH		47.6124114839
9PhosphorylationKPGATGESDLAEVLP
CCCCCCCCCHHHHCC		38.9980535845
28PhosphorylationDSKSLEAYLNQHLSG
CHHHHHHHHHHHHCC		9.2318452278
34PhosphorylationAYLNQHLSGFGAERE
HHHHHHHCCCCCCHH		29.9218452278
54PhosphorylationAQYRAGKSNPTFYLQ
EEHHCCCCCCEEEEC		47.3159151847
59PhosphorylationGKSNPTFYLQKGFQT
CCCCCEEEECCCCEE		15.6568729205
76PhosphorylationLRKKPPGSLLPKAHQ
EECCCCCCCCCCHHH		32.2946157353
86MethylationPKAHQIDREFKVQKA
CCHHHCCCHHHHHHH		53.53-
107PhosphorylationPVPKPILYCSDTSVI
CCCCCEEEEECCCEE		7.22141975
177AcetylationGIGAGYCKRQVSTWT
CCCCCCCHHHHHHHH		37.06-
324PhosphorylationAGIAQGVYSRYLLGN
HCCCHHCHHHHHCCC		8.3427259358
325PhosphorylationGIAQGVYSRYLLGNN
CCCHHCHHHHHCCCC		16.4326356563
358PhosphorylationGLQLSKRTFSTVLPQ
CCCCCCCCHHCCCCE		26.1925867546
360PhosphorylationQLSKRTFSTVLPQID
CCCCCCHHCCCCEEC		19.5925867546
361PhosphorylationLSKRTFSTVLPQIDT
CCCCCHHCCCCEECC		23.1325867546
368PhosphorylationTVLPQIDTTGQLFVQ
CCCCEECCCCCEEEE		34.1625867546
369PhosphorylationVLPQIDTTGQLFVQT
CCCEECCCCCEEEEE		21.1225867546
376PhosphorylationTGQLFVQTRKGQEVL
CCCEEEEECCCCEEE		29.1025867546
378AcetylationQLFVQTRKGQEVLIK
CEEEEECCCCEEEEE		69.22130183
385AcetylationKGQEVLIKVKHFMKQ
CCCEEEEEEHHHHHH		40.86130187
391SuccinylationIKVKHFMKQHILPAE
EEEHHHHHHHCCCCC		37.47-
391SuccinylationIKVKHFMKQHILPAE
EEEHHHHHHHCCCCC		37.47-
4232-HydroxyisobutyrylationGKPLVIDKLKEMAKV
CCCCHHHHHHHHHHH		50.78-
482PhosphorylationNMEVLHLYGSEEQKK
CEEEEEEECCHHHHH		14.0927732954
484PhosphorylationEVLHLYGSEEQKKQW
EEEEEECCHHHHHHH		25.1427732954
547S-nitrosylationSGAGNPKCKIAIVLG
CCCCCCCEEEEEEEC		3.9824105792
562PhosphorylationRTQNTSLSRHKQHSM
CCCCCCCCCCCCCEE		31.9122798277
576PhosphorylationMILVPMNTPGVKIIR
EEEEECCCCCCEEEE		18.3746157359
619MethylationNLILGEGRGFEISQG
EEEEECCCCCEECCC		42.18-
663AcetylationQRIAFKKKLYAHEVV
HHHHHHHHHHHHHHH		47.5226051181
683AcetylationESRIAIEKIRLLTLK
HHHHHHHHHHHHHHH		27.3220167786
683MalonylationESRIAIEKIRLLTLK
HHHHHHHHHHHHHHH		27.3226320211
690MethylationKIRLLTLKAAHSMDT
HHHHHHHHHHHCCCC		37.99-
704AcetylationTLGSAGAKKEIAMIK
CCCCCCCHHHEEEEE		50.4426051181
762PhosphorylationGPDEVHLSAIATMEL
CCCCEEHHHEEHHHH		11.6225867546
766PhosphorylationVHLSAIATMELRDQA
EEHHHEEHHHHHHHH		12.6925867546
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 ACD11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACD11_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 ACD11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
UBXN7_HUMANUBXN7physical
26389662
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 ACD11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-324, AND MASSSPECTROMETRY.

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