THEM4_HUMAN - dbPTM
THEM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THEM4_HUMAN
UniProt AC Q5T1C6
Protein Name Acyl-coenzyme A thioesterase THEM4
Gene Name THEM4
Organism Homo sapiens (Human).
Sequence Length 240
Subcellular Localization Cell membrane . Cell projection, ruffle membrane . Cytoplasm . Mitochondrion . Mitochondrion inner membrane
Peripheral membrane protein . Mitochondrion intermembrane space . Released from the mitochondria into the cytosol in response to apoptotic st
Protein Description Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays an role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane..
Protein Sequence MLRSCAARLRTLGALCLPPVGRRLPGSEPRPELRSFSSEEVILKDCSVPNPSWNKDLRLLFDQFMKKCEDGSWKRLPSYKRTPTEWIQDFKTHFLDPKLMKEEQMSQAQLFTRSFDDGLGFEYVMFYNDIEKRMVCLFQGGPYLEGPPGFIHGGAIATMIDATVGMCAMMAGGIVMTANLNINYKRPIPLCSVVMINSQLDKVEGRKFFVSCNVQSVDEKTLYSEATSLFIKLNPAKSLT
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
37PhosphorylationRPELRSFSSEEVILK
CHHHHCCCCCEEEEE
37.7822817900
38PhosphorylationPELRSFSSEEVILKD
HHHHCCCCCEEEEEC
35.4522817900
55SuccinylationVPNPSWNKDLRLLFD
CCCCCCCHHHHHHHH
52.46-
55SuccinylationVPNPSWNKDLRLLFD
CCCCCCCHHHHHHHH
52.46-
66SuccinylationLLFDQFMKKCEDGSW
HHHHHHHHHCCCCCC
56.41-
66SuccinylationLLFDQFMKKCEDGSW
HHHHHHHHHCCCCCC
56.41-
74AcetylationKCEDGSWKRLPSYKR
HCCCCCCCCCCCCCC
45.84-
74UbiquitinationKCEDGSWKRLPSYKR
HCCCCCCCCCCCCCC
45.84-
80UbiquitinationWKRLPSYKRTPTEWI
CCCCCCCCCCCCHHH
54.88-
98SuccinylationKTHFLDPKLMKEEQM
HHHCCCHHHCCHHHH
61.96-
98SuccinylationKTHFLDPKLMKEEQM
HHHCCCHHHCCHHHH
61.96-
192PhosphorylationKRPIPLCSVVMINSQ
CCCCCEEEEEEECCC
25.9820068231
198PhosphorylationCSVVMINSQLDKVEG
EEEEEECCCEEECCC
22.6120068231
207MalonylationLDKVEGRKFFVSCNV
EEECCCCEEEEEEEC
54.7526320211
207SuccinylationLDKVEGRKFFVSCNV
EEECCCCEEEEEEEC
54.75-
207SuccinylationLDKVEGRKFFVSCNV
EEECCCCEEEEEEEC
54.75-
221PhosphorylationVQSVDEKTLYSEATS
CCCCCCCCCCCCHHH
28.9620068231
223PhosphorylationSVDEKTLYSEATSLF
CCCCCCCCCCHHHHH
15.0820068231
224PhosphorylationVDEKTLYSEATSLFI
CCCCCCCCCHHHHHH
24.7020068231
227PhosphorylationKTLYSEATSLFIKLN
CCCCCCHHHHHHHCC
23.1620068231
228PhosphorylationTLYSEATSLFIKLNP
CCCCCHHHHHHHCCC
28.4720068231

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 THEM4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THEM4_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 THEM4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKT1_HUMANAKT1physical
11598301
ALAT2_HUMANGPT2physical
28514442
GSTT2_HUMANGSTT2physical
28514442
DPS1_HUMANPDSS1physical
28514442
HEM1_HUMANALAS1physical
28514442
DLP1_HUMANPDSS2physical
28514442
ODB2_HUMANDBTphysical
28514442
FOLC_HUMANFPGSphysical
28514442
SIR5_HUMANSIRT5physical
28514442
MRRP3_HUMANKIAA0391physical
28514442
CARD9_HUMANCARD9physical
28514442
KLC2_HUMANKLC2physical
28514442
TOP3A_HUMANTOP3Aphysical
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 THEM4_HUMAN

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Related Literatures of Post-Translational Modification

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