TRI27_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI27_MOUSE
• UniProt AC: Q62158
• Protein Name: Zinc finger protein RFP
• Gene Name: Trim27
• Organism: Mus musculus (Mouse).
• Sequence Length: 513
• Subcellular Localization: Nucleus . Cytoplasm . Nucleus, PML body. Endosome. Nuclear or cytoplasmic depending on the cell type. Recruited to retromer-containing endosomes via interaction with MAGEL2 (By similarity). Colocalized with PML and EIF3S6 in nuclear bodies.
• Protein Description: E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly. Has a transcriptional repressor activity. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA..
• Protein Sequence: MASGSVAECLQQETTCPVCLQYFVEPMMLDCGHNICCACLARCWGAAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEQDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNRLDHLRRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSGLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP

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
380	Ubiquitination	WEVEVGDKAKWTIGV EEEEECCEEEEEEEE	46.03	-
473	Phosphorylation	FCGPVRPYFSLSYSG ECCCCCCCEEEEECC	8.67	26745281
475	Phosphorylation	GPVRPYFSLSYSGGK CCCCCCEEEEECCCC	15.57	26745281
477	Phosphorylation	VRPYFSLSYSGGKSA CCCCEEEEECCCCCC	18.96	26745281
478	Phosphorylation	RPYFSLSYSGGKSAA CCCEEEEECCCCCCC	19.34	26745281
479	Phosphorylation	PYFSLSYSGGKSAAP CCEEEEECCCCCCCC	37.38	26745281
493	Phosphorylation	PLIICPMSGIDGFSG CEEEEECCCCCCCCC	20.10	26643407
499	Phosphorylation	MSGIDGFSGHVGNHG CCCCCCCCCCCCCCC	33.25	26643407
508	Phosphorylation	HVGNHGHSMETSP-- CCCCCCCCCCCCC--	23.94	26643407
511	Phosphorylation	NHGHSMETSP----- CCCCCCCCCC-----	37.34	26643407
512	Phosphorylation	HGHSMETSP------ CCCCCCCCC------	18.46	26643407

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

Oops, there are no upstream regulatory protein records of TRI27_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI27_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 TRI27_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFE2_MOUSE	Tcf3	physical	16007160
ASCL1_MOUSE	Ascl1	physical	16007160
MYOD1_MOUSE	Myod1	physical	16007160

Drug and Disease Associations

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