UD3A2_HUMAN - dbPTM
UD3A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UD3A2_HUMAN
UniProt AC Q3SY77
Protein Name UDP-glucuronosyltransferase 3A2
Gene Name UGT3A2
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity)..
Protein Sequence MAGQRVLLLVGFLLPGVLLSEAAKILTISTVGGSHYLLMDRVSQILQDHGHNVTMLNHKRGPFMPDFKKEEKSYQVISWLAPEDHQREFKKSFDFFLEETLGGRGKFENLLNVLEYLALQCSHFLNRKDIMDSLKNENFDMVIVETFDYCPFLIAEKLGKPFVAILSTSFGSLEFGLPIPLSYVPVFRSLLTDHMDFWGRVKNFLMFFSFCRRQQHMQSTFDNTIKEHFTEGSRPVLSHLLLKAELWFINSDFAFDFARPLLPNTVYVGGLMEKPIKPVPQDLENFIAKFGDSGFVLVTLGSMVNTCQNPEIFKEMNNAFAHLPQGVIWKCQCSHWPKDVHLAANVKIVDWLPQSDLLAHPSIRLFVTHGGQNSIMEAIQHGVPMVGIPLFGDQPENMVRVEAKKFGVSIQLKKLKAETLALKMKQIMEDKRYKSAAVAASVILRSHPLSPTQRLVGWIDHVLQTGGATHLKPYVFQQPWHEQYLLDVFVFLLGLTLGTLWLCGKLLGMAVWWLRGARKVKET
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
27 (in isoform 2)Phosphorylation-19.1630631047
29 (in isoform 2)Phosphorylation-16.2930631047
30 (in isoform 2)Phosphorylation-21.2230631047
36PhosphorylationSTVGGSHYLLMDRVS
ECCCCHHHHHHHHHH
11.83-
43PhosphorylationYLLMDRVSQILQDHG
HHHHHHHHHHHHHCC
16.64-
52N-linked_GlycosylationILQDHGHNVTMLNHK
HHHHCCCCEEEECCC
35.23UniProtKB CARBOHYD
128AcetylationCSHFLNRKDIMDSLK
HHHHCCHHHHHHHHH
51.007824087
135AcetylationKDIMDSLKNENFDMV
HHHHHHHHCCCCCEE
67.197824097
362PhosphorylationSDLLAHPSIRLFVTH
HHHHCCCEEEEEEEC
15.5224719451
425UbiquitinationETLALKMKQIMEDKR
HHHHHHHHHHHCCCC
34.78-
433PhosphorylationQIMEDKRYKSAAVAA
HHHCCCCHHHHHHHH
18.2927251275
435PhosphorylationMEDKRYKSAAVAASV
HCCCCHHHHHHHHHH
16.7227251275
441PhosphorylationKSAAVAASVILRSHP
HHHHHHHHHHHHHCC
10.4328176443
446PhosphorylationAASVILRSHPLSPTQ
HHHHHHHHCCCCHHH
26.4728176443
450PhosphorylationILRSHPLSPTQRLVG
HHHHCCCCHHHHHHH
30.2828176443
452PhosphorylationRSHPLSPTQRLVGWI
HHCCCCHHHHHHHHH
23.9728176443

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 UD3A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UD3A2_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 UD3A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIL_HUMANACAT1physical
26344197

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UD3A2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP