ACO11_HUMAN - dbPTM
ACO11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACO11_HUMAN
UniProt AC Q8WXI4
Protein Name Acyl-coenzyme A thioesterase 11
Gene Name ACOT11
Organism Homo sapiens (Human).
Sequence Length 607
Subcellular Localization Cytoplasm.
Protein Description Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates..
Protein Sequence MIQNVGNHLRRGLASVFSNRTSRKSALRAGNDSAMADGEGYRNPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASEDLCSEKQWNVCKALATFVARREITKVKLKQITPRTEEEKMEHSVAAERRRMRLVYADTIKDLLANCAIQGDLESRDCSRMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKCCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVAKINSRFGYLQDT
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
15PhosphorylationHLRRGLASVFSNRTS
HHHHHHHHHHCCCCC
28.8328857561
25PhosphorylationSNRTSRKSALRAGND
CCCCCHHHHHHCCCC
31.27-
45PhosphorylationGEGYRNPTEVQMSQL
CCCCCCCCCEEEEEE
52.9546157857
80PhosphorylationIDTTACLSAERHAGC
HHHHHHHCHHHHCCC
28.1524719451
131PhosphorylationEVGIQVASEDLCSEK
CEEEEECCHHHCCHH
32.5529978859
136PhosphorylationVASEDLCSEKQWNVC
ECCHHHCCHHHHHHH
55.9429978859
367PhosphorylationLDRKYIVSCKQTEVP
CCCEEEEEEECCCCC
13.1617693683
388PhosphorylationPSNQVYLSYNNVSSL
CCCCEEEEECCCCCC
14.2350563199
444PhosphorylationAQAFLLLSDLRQRPE
HHHHHHHHHHHHCCH
34.27113136071
496MalonylationVILASRRKPCDNGDP
EEEECCCCCCCCCCC
49.2226320211
510O-linked_GlycosylationPYVIALRSVTLPTHR
CEEEEEEEEECCCCC
21.9430379171
599PhosphorylationIPVAKINSRFGYLQD
EEEEEECCCCCCCCC
32.2430576142
603PhosphorylationKINSRFGYLQDT---
EECCCCCCCCCC---
9.8530576142

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 ACO11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACO11_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 ACO11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACO11_HUMANACOT11physical
21738568
THUM3_HUMANTHUMPD3physical
26186194
THUM3_HUMANTHUMPD3physical
28514442

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 ACO11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.

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