AB17B_HUMAN - dbPTM
AB17B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB17B_HUMAN
UniProt AC Q5VST6
Protein Name Alpha/beta hydrolase domain-containing protein 17B {ECO:0000305}
Gene Name ABHD17B {ECO:0000312|HGNC:HGNC:24278}
Organism Homo sapiens (Human).
Sequence Length 288
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Recycling 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 DLG4/PSD95]
Protein Sequence MNNLSFSELCCLFCCPPCPGKIASKLAFLPPDPTYTLMCDESGSRWTLHLSERADWQYSSREKDAIECFMTRTSKGNRIACMFVRCSPNAKYTLLFSHGNAVDLGQMSSFYIGLGSRINCNIFSYDYSGYGASSGKPTEKNLYADIEAAWLALRTRYGIRPENVIIYGQSIGTVPSVDLAARYESAAVILHSPLTSGMRVAFPDTKKTYCFDAFPNIDKISKITSPVLIIHGTEDEVIDFSHGLALFERCQRPVEPLWVEGAGHNDVELYGQYLERLKQFVSQELVNL
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
34PhosphorylationAFLPPDPTYTLMCDE
CCCCCCCCEEEEECC
28122231
35PhosphorylationFLPPDPTYTLMCDES
CCCCCCCEEEEECCC
28122231
36PhosphorylationLPPDPTYTLMCDESG
CCCCCCEEEEECCCC
28122231
42PhosphorylationYTLMCDESGSRWTLH
EEEEECCCCCEEEEE
28122231
44PhosphorylationLMCDESGSRWTLHLS
EEECCCCCEEEEEEH
28122231
51PhosphorylationSRWTLHLSERADWQY
CEEEEEEHHCCCCCC
24719451
63UbiquitinationWQYSSREKDAIECFM
CCCCCCCCHHHHHHE
-
136UbiquitinationGYGASSGKPTEKNLY
CCCCCCCCCCCCCCH
-
185PhosphorylationDLAARYESAAVILHS
HHHHHCCCEEEEEEC
-
192PhosphorylationSAAVILHSPLTSGMR
CEEEEEECCCCCCCE
-
206UbiquitinationRVAFPDTKKTYCFDA
EEECCCCCCEEEEEC
2190698
206 (in isoform 2)Ubiquitination-21906983
206 (in isoform 1)Ubiquitination-21906983
207UbiquitinationVAFPDTKKTYCFDAF
EECCCCCCEEEEECC
-
210S-palmitoylationPDTKKTYCFDAFPNI
CCCCCEEEEECCCCH
29575903
219UbiquitinationDAFPNIDKISKITSP
ECCCCHHHHHCCCCC
-
222UbiquitinationPNIDKISKITSPVLI
CCHHHHHCCCCCEEE
-
278UbiquitinationGQYLERLKQFVSQEL
HHHHHHHHHHHHHHH
-
282PhosphorylationERLKQFVSQELVNL-
HHHHHHHHHHHHCC-
29507054

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 AB17B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB17B_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 AB17B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AB17B_HUMAN !!

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 AB17B_HUMAN

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Related Literatures of Post-Translational Modification

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