AB17A_HUMAN - dbPTM
AB17A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB17A_HUMAN
UniProt AC Q96GS6
Protein Name Alpha/beta hydrolase domain-containing protein 17A {ECO:0000305}
Gene Name ABHD17A {ECO:0000312|HGNC:HGNC:28756}
Organism Homo sapiens (Human).
Sequence Length 310
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Endosome membrane
Lipid-anchor
Cytoplasmic side . Cell projection, dendritic spine . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density .
Protein Description Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. [PubMed: 26701913 Has depalmitoylating activity towards NRAS]
Protein Sequence MNGLSLSELCCLFCCPPCPGRIAAKLAFLPPEATYSLVPEPEPGPGGAGAAPLGTLRASSGAPGRWKLHLTERADFQYSQRELDTIEVFPTKSARGNRVSCMYVRCVPGARYTVLFSHGNAVDLGQMSSFYIGLGSRLHCNIFSYDYSGYGASSGRPSERNLYADIDAAWQALRTRYGISPDSIILYGQSIGTVPTVDLASRYECAAVVLHSPLTSGMRVAFPDTKKTYCFDAFPNIEKVSKITSPVLIIHGTEDEVIDFSHGLALYERCPKAVEPLWVEGAGHNDIELYSQYLERLRRFISQELPSQRA
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
5Phosphorylation---MNGLSLSELCCL
---CCCCCHHHCHHH
46208651
7Phosphorylation-MNGLSLSELCCLFC
-CCCCCHHHCHHHHH
46208655
35PhosphorylationFLPPEATYSLVPEPE
CCCCCCEEEECCCCC
18083107
55PhosphorylationAGAAPLGTLRASSGA
CCCCCCCCEEECCCC
46208659
67 (in isoform 2)Ubiquitination--
67UbiquitinationSGAPGRWKLHLTERA
CCCCCCEEEEEEECC
-
78UbiquitinationTERADFQYSQRELDT
EECCCCCCCCCCCCE
22817900
79UbiquitinationERADFQYSQRELDTI
ECCCCCCCCCCCCEE
22817900
92UbiquitinationTIEVFPTKSARGNRV
EEEEEECCCCCCCEE
23000965
92 (in isoform 2)Ubiquitination--
226 (in isoform 3)Ubiquitination-21906983
226 (in isoform 1)Ubiquitination-21906983
226UbiquitinationRVAFPDTKKTYCFDA
EEECCCCCCEEEECC
27667366
227UbiquitinationVAFPDTKKTYCFDAF
EECCCCCCEEEECCC
22817900
277UbiquitinationCPKAVEPLWVEGAGH
CCCCCCCEEECCCCC
27667366
277 (in isoform 2)Ubiquitination-21906983
278UbiquitinationPKAVEPLWVEGAGHN
CCCCCCEEECCCCCC
22817900
278 (in isoform 2)Ubiquitination--
302PhosphorylationERLRRFISQELPSQR
HHHHHHHHHHCCCCC
-
307PhosphorylationFISQELPSQRA----
HHHHHCCCCCC----
26701913

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 AB17A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB17A_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 AB17A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS28_HUMANVPS28physical
26186194
TC1D2_HUMANTCTEX1D2physical
26186194
RGS20_HUMANRGS20physical
21516116
PNMA1_HUMANPNMA1physical
21516116
TC1D2_HUMANTCTEX1D2physical
28514442
VPS28_HUMANVPS28physical
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 AB17A_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP