HOIL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HOIL1_MOUSE
• UniProt AC: Q9WUB0
• Protein Name: RanBP-type and C3HC4-type zinc finger-containing protein 1
• Gene Name: Rbck1
• Organism: Mus musculus (Mouse).
• Sequence Length: 508
• Protein Description: E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types (By similarity)..
• Protein Sequence: MDEKTKKAEEMALSLARAVAGGDEQAAIKYATWLAEQRVPLRVQVKPEVSPTQDIRLCVSVEDAYMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPSLQQWVVGQRLARDQETLHSHGIRRNGDGAYLYLLSARNTSLNPQELQRQRQLRMLEDLGFKDLTLQSRGPLEPVLPKPRTNQEPGQPDAAPESPPVGWQCPGCTFINKPTRPGCEMCCRARPETYQIPASYQPDEEERARLAGEEEALRQYQQRKQQQQEGNYLQHVQLEQRSLVLNTEPTECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVACPFIDSTYSCPGKLLEREIRALLSPEDYQRFLDLGVSIAENRSTLSYHCKTPDCRGWCFFEDDVNEFTCPVCTRVNCLLCKAIHEHMNCREYQDDLALRAQNDVAARQTTEMLKVMLQQGEAMHCPQCRIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH

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
1	Acetylation	-------MDEKTKKA -------CCHHHHHH	15.76	-
14	Phosphorylation	KAEEMALSLARAVAG HHHHHHHHHHHHHHC	15.50	27149854
50	Phosphorylation	VQVKPEVSPTQDIRL EEECCCCCCCCCEEE	22.14	26824392
52	Phosphorylation	VKPEVSPTQDIRLCV ECCCCCCCCCEEEEE	31.22	28066266
113	Phosphorylation	RLARDQETLHSHGIR HHHCCHHHHHHCCCC	24.92	25159016
116	Phosphorylation	RDQETLHSHGIRRNG CCHHHHHHCCCCCCC	26.90	25159016
158	Ubiquitination	MLEDLGFKDLTLQSR HHHHCCCCCCEECCC	50.45	22790023
190	Phosphorylation	QPDAAPESPPVGWQC CCCCCCCCCCCCCCC	33.18	25266776
248	Phosphorylation	EEEALRQYQQRKQQQ HHHHHHHHHHHHHHH	10.52	29514104
251	Ubiquitination	ALRQYQQRKQQQQEG HHHHHHHHHHHHHHC	24.19	27667366
252	Ubiquitination	LRQYQQRKQQQQEGN HHHHHHHHHHHHHCC	48.39	22790023
260	Phosphorylation	QQQQEGNYLQHVQLE HHHHHCCHHHHHEEH	20.70	29514104
270	Phosphorylation	HVQLEQRSLVLNTEP HHEEHHCEEEECCCC	23.64	30352176
326	Phosphorylation	VACPFIDSTYSCPGK EECCCCCCCCCCCCH	25.16	25367039
327	Phosphorylation	ACPFIDSTYSCPGKL ECCCCCCCCCCCCHH	18.73	22817900
328	Phosphorylation	CPFIDSTYSCPGKLL CCCCCCCCCCCCHHH	16.54	18034455
329	Phosphorylation	PFIDSTYSCPGKLLE CCCCCCCCCCCHHHH	17.58	25367039
344	Phosphorylation	REIRALLSPEDYQRF HHHHHHCCHHHHHHH	27.39	22817900

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

Oops, there are no upstream regulatory protein records of HOIL1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HOIL1_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 HOIL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EYA1_MOUSE	Eya1	physical	20956555
RNF31_MOUSE	Rnf31	physical	21455181
SHRPN_MOUSE	Sharpin	physical	21455181
RNF31_MOUSE	Rnf31	physical	19136968
NEMO_MOUSE	Ikbkg	physical	19136968
IKKA_MOUSE	Chuk	physical	19136968
IKKB_MOUSE	Ikbkb	physical	19136968

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, AND MASSSPECTROMETRY.
PubMed: 18034455

"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, AND MASSSPECTROMETRY.
PubMed: 17947660