TRI11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI11_MOUSE
• UniProt AC: Q99PQ2
• Protein Name: E3 ubiquitin-protein ligase TRIM11
• Gene Name: Trim11
• Organism: Mus musculus (Mouse).
• Sequence Length: 467
• Subcellular Localization: Cytoplasm . Nucleus . In the nucleus, colocalizes with PAX6.
• Protein Description: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle..
• Protein Sequence: MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ

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
85	Phosphorylation	ARRLHPPSPVPQGVC HHHHCCCCCCCCCCC	42.87	25159016
100	Phosphorylation	AAHREPLTTFCGDDL CCCCCCCCCCCCCCH	28.65	-
260 (in isoform 2)	Acetylation	-	29.29	-
442	Phosphorylation	GTLRPLFSPLSSSPT CCCCCCCCCCCCCCC	32.39	30635358
445	Phosphorylation	RPLFSPLSSSPTPMT CCCCCCCCCCCCCCH	31.96	30635358
446	Phosphorylation	PLFSPLSSSPTPMTI CCCCCCCCCCCCCHH	48.28	30635358
447	Phosphorylation	LFSPLSSSPTPMTIC CCCCCCCCCCCCHHH	29.44	30635358
449	Phosphorylation	SPLSSSPTPMTICRL CCCCCCCCCCHHHHH	27.86	30635358

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TRI11_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI11_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRI11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAX6_MOUSE	Pax6	physical	18628401
TBK1_HUMAN	TBK1	physical	23675467

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.