RNF11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RNF11_MOUSE
• UniProt AC: Q9QYK7
• Protein Name: RING finger protein 11
• Gene Name: Rnf11
• Organism: Mus musculus (Mouse).
• Sequence Length: 154
• Subcellular Localization: Early endosome. Recycling endosome. Cytoplasm. Nucleus. Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1..
• Protein Description: Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome..
• Protein Sequence: MGNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPIYHPTPSQTRLATQLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHIYHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN

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
2	Myristoylation	------MGNCLKSPT ------CCCCCCCCC	33.29	-
4	S-palmitoylation	----MGNCLKSPTSD ----CCCCCCCCCCC	4.13	-
7	Phosphorylation	-MGNCLKSPTSDDIS -CCCCCCCCCCCCCH	22.06	20415495
9	Phosphorylation	GNCLKSPTSDDISLL CCCCCCCCCCCCHHH	52.45	27742792
10	Phosphorylation	NCLKSPTSDDISLLH CCCCCCCCCCCHHHC	36.35	27742792
14	Phosphorylation	SPTSDDISLLHESQS CCCCCCCHHHCHHHC	31.69	26824392
19	Phosphorylation	DISLLHESQSDRASF CCHHHCHHHCCHHCC	25.00	27742792
21	Phosphorylation	SLLHESQSDRASFGE HHHCHHHCCHHCCCC	38.04	27742792
25	Phosphorylation	ESQSDRASFGEGTEP HHHCCHHCCCCCCCC	34.38	23684622
30	Phosphorylation	RASFGEGTEPDQEPP HHCCCCCCCCCCCCC	39.79	29472430
49	Phosphorylation	EQVPVPIYHPTPSQT CCCCCCCCCCCHHHH	8.83	25293948
52	Phosphorylation	PVPIYHPTPSQTRLA CCCCCCCCHHHHCHH	23.43	25293948
54	Phosphorylation	PIYHPTPSQTRLATQ CCCCCCHHHHCHHHC	46.81	23684622
56	Phosphorylation	YHPTPSQTRLATQLT CCCCHHHHCHHHCCC	31.80	25293948
63	Phosphorylation	TRLATQLTEEEQIRI HCHHHCCCHHHHHHH	31.37	-
82	Ubiquitination	GLIQHLPKGVYDPGR CHHHHCCCCCCCCCC	68.33	22790023
135	Phosphorylation	DWLMRSFTCPSCMEP HHHHHHCCCCCCCCC	25.42	-

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
135	T	Phosphorylation	Kinase	AKT1	P31750	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RNF11_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 RNF11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AXIN1_MOUSE	Axin1	physical	16601693
ITCH_MOUSE	Itch	physical	21765415
TNAP3_MOUSE	Tnfaip3	physical	21765415
RIPK1_MOUSE	Ripk1	physical	21765415
TAXB1_MOUSE	Tax1bp1	physical	21765415
TRAF6_MOUSE	Traf6	physical	21765415
NEDD4_MOUSE	Nedd4	physical	11042109
TNAP3_MOUSE	Tnfaip3	physical	22975135

Drug and Disease Associations

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