ABHDB_HUMAN - dbPTM
ABHDB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABHDB_HUMAN
UniProt AC Q8NFV4
Protein Name Protein ABHD11 {ECO:0000305}
Gene Name ABHD11 {ECO:0000312|HGNC:HGNC:16407}
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization
Protein Description
Protein Sequence MRAGQQLASMLRWTRAWRLPREGLGPHGPSFARVPVAPSSSSGGRGGAEPRPLPLSYRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTGVSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVRQHLLTNLVEVDGRFVWRVNLDALTQHLDKILAFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFLV
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
9PhosphorylationRAGQQLASMLRWTRA
CHHHHHHHHHHHHHH
27.2646157015
39PhosphorylationARVPVAPSSSSGGRG
CCCCCCCCCCCCCCC
32.8721406692
40PhosphorylationRVPVAPSSSSGGRGG
CCCCCCCCCCCCCCC
27.7121406692
41PhosphorylationVPVAPSSSSGGRGGA
CCCCCCCCCCCCCCC
37.0221406692
42PhosphorylationPVAPSSSSGGRGGAE
CCCCCCCCCCCCCCC
47.4121406692
57PhosphorylationPRPLPLSYRLLDGEA
CCCCCCEEEECCCCC
16.98113327985
80 (in isoform 5)Ubiquitination-46.9021890473
80 (in isoform 4)Ubiquitination-46.9021890473
80UbiquitinationHGLFGSKTNFNSIAK
HHHHCCCCCHHHHHH
46.9019608861
80AcetylationHGLFGSKTNFNSIAK
HHHHCCCCCHHHHHH
46.9019608861
80 (in isoform 5)Acetylation-46.90-
80 (in isoform 4)Acetylation-46.90-
87 (in isoform 3)Acetylation-36.26-
87 (in isoform 2)Acetylation-36.26-
87SuccinylationTNFNSIAKILAQQTG
CCHHHHHHHHHHHHC
36.2619608861
87UbiquitinationTNFNSIAKILAQQTG
CCHHHHHHHHHHHHC
36.2621890473
87 (in isoform 1)Ubiquitination-36.2621890473
87 (in isoform 2)Ubiquitination-36.2621890473
87 (in isoform 3)Ubiquitination-36.2621890473
87SuccinylationTNFNSIAKILAQQTG
CCHHHHHHHHHHHHC
36.26-
87AcetylationTNFNSIAKILAQQTG
CCHHHHHHHHHHHHC
36.2619608861
193 (in isoform 4)Ubiquitination-4.3721890473
196PhosphorylationIADELPRSRARKLAD
HHHHCCHHHHHHHHH
28.4924825855
200UbiquitinationLPRSRARKLADEQLS
CCHHHHHHHHHHHHH
47.222190698
200 (in isoform 1)Ubiquitination-47.2221890473
221PhosphorylationAVRQHLLTNLVEVDG
HHHHHHHHHHEEECC
32.6368730483

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 ABHDB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABHDB_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 ABHDB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PGM1_HUMANPGM1physical
26344197
NDKM_HUMANNME4physical
27499296
ABHDB_HUMANABHD11physical
27499296
BOLA3_HUMANBOLA3physical
27499296
DHRS4_HUMANDHRS4physical
27499296
HOGA1_HUMANHOGA1physical
27499296
BOLA1_HUMANBOLA1physical
27499296
ACAD8_HUMANACAD8physical
27499296
ECH1_HUMANECH1physical
27499296
MIA40_HUMANCHCHD4physical
27499296
C1QBP_HUMANC1QBPphysical
27499296

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 ABHDB_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87, AND MASS SPECTROMETRY.

TOP