UD19_HUMAN - dbPTM
UD19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UD19_HUMAN
UniProt AC O60656
Protein Name UDP-glucuronosyltransferase 1-9
Gene Name UGT1A9
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Microsome. Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1..
Protein Sequence MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLFFSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVTEYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
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
69PhosphorylationVSWQLGRSLNCTVKT
HHHHHCCCCCCEEEE		23.3328787133
71N-linked_GlycosylationWQLGRSLNCTVKTYS
HHHCCCCCCEEEEEE		22.2119951703
80PhosphorylationTVKTYSTSYTLEDLD
EEEEEECCEEHHHHH		15.3528787133
99SuccinylationAFAHAQWKAQVRSIY
HHHHHHHHHHHHHHH		19.50-
99SuccinylationAFAHAQWKAQVRSIY
HHHHHHHHHHHHHHH		19.50-
126PhosphorylationLFFSNCRSLFKDKKL
HHHHCHHHHCCCHHH		40.1224719451
202PhosphorylationLGFSDAMTFKERVRN
HCCCCCCCHHHHHHH		33.02-
292N-linked_GlycosylationMEFEAYINASGEHGI
CEEEEEEECCCCCEE		18.5119951703
329PhosphorylationALGKIPQTVLWRYTG
HHCCCCHHHHHHCCC		16.5323403867
334PhosphorylationPQTVLWRYTGTRPSN
CHHHHHHCCCCCCCH		9.65-
337PhosphorylationVLWRYTGTRPSNLAN
HHHHCCCCCCCHHCC		31.4423403867
340PhosphorylationRYTGTRPSNLANNTI
HCCCCCCCHHCCCEE		40.9823403867
344N-linked_GlycosylationTRPSNLANNTILVKW
CCCCHHCCCEEEEEE		49.7119951703
346PhosphorylationPSNLANNTILVKWLP
CCHHCCCEEEEEECC		18.5923403867
363PhosphorylationDLLGHPMTRAFITHA
CCCCCCCHHHHHHCC		24.2423403867
432PhosphorylationKAVINDKSYKENIMR
HHHHCCHHHHHHHHH		44.2815845768
434AcetylationVINDKSYKENIMRLS
HHCCHHHHHHHHHHH		51.9118530249
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 UD19_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UD19_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 UD19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UD110_HUMANUGT1A10physical
28514442
UD17_HUMANUGT1A7physical
28514442
ESYT1_HUMANESYT1physical
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
D01854 Mitiglinide calcium hydrate (JAN); Mitiglinide calcium dihydrate; Glufast (TN)
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D08524 Sorafenib (USAN/INN)
DrugBank
DB00316Acetaminophen
DB00921Buprenorphine
DB08907Canagliflozin
DB06695Dabigatran etexilate
DB06292Dapagliflozin
DB00494Entacapone
DB00749Etodolac
DB04953Ezogabine
DB00712Flurbiprofen
DB00502Haloperidol
DB00062Human Serum Albumin
DB00327Hydromorphone
DB01050Ibuprofen
DB00328Indomethacin
DB00762Irinotecan
DB06738Ketobemidone
DB01283Lumiracoxib
DB00688Mycophenolate mofetil
DB01024Mycophenolic acid
DB00731Nateglinide
DB04552Niflumic Acid
DB00842Oxazepam
DB00818Propofol
DB08896Regorafenib
DB00398Sorafenib
DB01015Sulfamethoxazole
DB06204Tapentadol
DB00313Valproic Acid
DB00744Zileuton
Regulatory Network of UD19_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"N-Glycosylation plays a role in protein folding of human UGT1A9.";
Nakajima M., Koga T., Sakai H., Yamanaka H., Fujiwara R., Yokoi T.;
Biochem. Pharmacol. 79:1165-1172(2010).
Cited for: GLYCOSYLATION AT ASN-71; ASN-292 AND ASN-344.

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