ABHEB_HUMAN - dbPTM
ABHEB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABHEB_HUMAN
UniProt AC Q96IU4
Protein Name Protein ABHD14B {ECO:0000305}
Gene Name ABHD14B {ECO:0000312|HGNC:HGNC:28235}
Organism Homo sapiens (Human).
Sequence Length 210
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic.
Protein Description Has hydrolase activity towards p-nitrophenyl butyrate (in vitro). May activate transcription..
Protein Sequence MAASVEQREGTIQVQGQALFFREALPGSGQARFSVLLLHGIRFSSETWQNLGTLHRLAQAGYRAVAIDLPGLGHSKEAAAPAPIGELAPGSFLAAVVDALELGPPVVISPSLSGMYSLPFLTAPGSQLPGFVPVAPICTDKINAANYASVKTPALIVYGDQDPMGQTSFEHLKQLPNHRVLIMKGAGHPCYLDKPEEWHTGLLDFLQGLQ
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
2Acetylation------MAASVEQRE
------CCCCCCCCC
14.4022814378
4Phosphorylation----MAASVEQREGT
----CCCCCCCCCCE
19.3528857561
34PhosphorylationGSGQARFSVLLLHGI
CCCCHHHHHEEEECC
13.3028857561
44PhosphorylationLLHGIRFSSETWQNL
EEECCCCCHHHHHHH
19.8820068231
45PhosphorylationLHGIRFSSETWQNLG
EECCCCCHHHHHHHH
36.0120068231
47PhosphorylationGIRFSSETWQNLGTL
CCCCCHHHHHHHHHH
34.0120068231
53PhosphorylationETWQNLGTLHRLAQA
HHHHHHHHHHHHHHC
23.6620068231
91PhosphorylationIGELAPGSFLAAVVD
CCCCCCCCHHHHHHH
18.9414702039
147PhosphorylationDKINAANYASVKTPA
CCCCHHHCCCCCCCE
8.7725884760
149PhosphorylationINAANYASVKTPALI
CCHHHCCCCCCCEEE
17.4924114839
151UbiquitinationAANYASVKTPALIVY
HHHCCCCCCCEEEEE
46.42-
152PhosphorylationANYASVKTPALIVYG
HHCCCCCCCEEEEEC
16.1927174698
158PhosphorylationKTPALIVYGDQDPMG
CCCEEEEECCCCCCC
14.1627174698
164SulfoxidationVYGDQDPMGQTSFEH
EECCCCCCCCCCHHH
9.2728183972
167PhosphorylationDQDPMGQTSFEHLKQ
CCCCCCCCCHHHHHC
29.6527174698
168PhosphorylationQDPMGQTSFEHLKQL
CCCCCCCCHHHHHCC
22.2827174698
173UbiquitinationQTSFEHLKQLPNHRV
CCCHHHHHCCCCCCE
52.26-

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 ABHEB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABHEB_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 ABHEB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TKT_HUMANTKTphysical
26344197

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 ABHEB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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