UD110_HUMAN - dbPTM
UD110_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UD110_HUMAN
UniProt AC Q9HAW8
Protein Name UDP-glucuronosyltransferase 1-10
Gene Name UGT1A10
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. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1..
Protein Sequence MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEGAQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
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
71N-linked_GlycosylationWQLERSLNCTVKTYS
HHHHHHHCCEEEEEE		22.21UniProtKB CARBOHYD
104PhosphorylationQWKAQAQSIFSLLMS
HHHHHHHHHHHHHHH		28.7222210691
114PhosphorylationSLLMSSSSGFLDLFF
HHHHHCCCHHHHHHH		35.2022210691
292N-linked_GlycosylationMEFEAYINASGEHGI
CEEEEEEECCCCCEE		18.51UniProtKB CARBOHYD
329PhosphorylationALGKIPQTVLWRYTG
HHCCCCHHHHHHCCC		16.5323403867
334PhosphorylationPQTVLWRYTGTRPSN
CHHHHHHCCCCCCCH		9.65-
337PhosphorylationVLWRYTGTRPSNLAN
HHHHCCCCCCCHHCC		31.4423403867
340PhosphorylationRYTGTRPSNLANNTI
HCCCCCCCHHCCCEE		40.9823403867
344N-linked_GlycosylationTRPSNLANNTILVKW
CCCCHHCCCEEEEEE		49.71UniProtKB CARBOHYD
346PhosphorylationPSNLANNTILVKWLP
CCHHCCCEEEEEECC		18.5923403867
363PhosphorylationDLLGHPMTRAFITHA
CCCCCCCHHHHHHCC		24.2423403867
432PhosphorylationKAVINDKSYKENIMR
HHHHCCHHHHHHHHH		44.2815845768
434AcetylationVINDKSYKENIMRLS
HHCCHHHHHHHHHHH		51.9118530755
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 UD110_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UD110_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 UD110_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ANXA1_HUMANANXA1physical
26186194
PEPL_HUMANPPLphysical
26186194
CALL5_HUMANCALML5physical
26186194
UD17_HUMANUGT1A7physical
26186194
OS9_HUMANOS9physical
26186194
SPB5_HUMANSERPINB5physical
26186194
NGAL_HUMANLCN2physical
26186194
SPB4_HUMANSERPINB4physical
26186194
S1A7A_HUMANS100A7Aphysical
26186194
INVO_HUMANIVLphysical
26186194
MANEA_HUMANMANEAphysical
26186194
KLK10_HUMANKLK10physical
26186194
EVPL_HUMANEVPLphysical
26186194
RABP2_HUMANCRABP2physical
26186194
UD17_HUMANUGT1A7physical
28514442
S1A7A_HUMANS100A7Aphysical
28514442
SPB4_HUMANSERPINB4physical
28514442
NGAL_HUMANLCN2physical
28514442
RABP2_HUMANCRABP2physical
28514442
CALL5_HUMANCALML5physical
28514442
KLK10_HUMANKLK10physical
28514442
PEPL_HUMANPPLphysical
28514442
MANEA_HUMANMANEAphysical
28514442
OS9_HUMANOS9physical
28514442
INVO_HUMANIVLphysical
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
There are no disease associations of PTM sites.
DrugBank
DB00316Acetaminophen
DB00749Etodolac
DB00678Losartan
DB00688Mycophenolate mofetil
DB00313Valproic Acid
Regulatory Network of UD110_HUMAN

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Related Literatures of Post-Translational Modification

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