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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
15 | Phosphorylation | HLRRGLASVFSNRTS HHHHHHHHHHCCCCC | 28.83 | 28857561 | |
25 | Phosphorylation | SNRTSRKSALRAGND CCCCCHHHHHHCCCC | 31.27 | - | |
45 | Phosphorylation | GEGYRNPTEVQMSQL CCCCCCCCCEEEEEE | 52.95 | 46157857 | |
80 | Phosphorylation | IDTTACLSAERHAGC HHHHHHHCHHHHCCC | 28.15 | 24719451 | |
131 | Phosphorylation | EVGIQVASEDLCSEK CEEEEECCHHHCCHH | 32.55 | 29978859 | |
136 | Phosphorylation | VASEDLCSEKQWNVC ECCHHHCCHHHHHHH | 55.94 | 29978859 | |
367 | Phosphorylation | LDRKYIVSCKQTEVP CCCEEEEEEECCCCC | 13.16 | 17693683 | |
388 | Phosphorylation | PSNQVYLSYNNVSSL CCCCEEEEECCCCCC | 14.23 | 50563199 | |
444 | Phosphorylation | AQAFLLLSDLRQRPE HHHHHHHHHHHHCCH | 34.27 | 113136071 | |
496 | Malonylation | VILASRRKPCDNGDP EEEECCCCCCCCCCC | 49.22 | 26320211 | |
510 | O-linked_Glycosylation | PYVIALRSVTLPTHR CEEEEEEEEECCCCC | 21.94 | 30379171 | |
599 | Phosphorylation | IPVAKINSRFGYLQD EEEEEECCCCCCCCC | 32.24 | 30576142 | |
603 | Phosphorylation | KINSRFGYLQDT--- EECCCCCCCCCC--- | 9.85 | 30576142 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACO11_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ACO11_HUMAN | ACOT11 | physical | 21738568 | |
THUM3_HUMAN | THUMPD3 | physical | 26186194 | |
THUM3_HUMAN | THUMPD3 | physical | 28514442 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |