HOIL1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HOIL1_RAT
• UniProt AC: Q62921
• Protein Name: RanBP-type and C3HC4-type zinc finger-containing protein 1
• Gene Name: Rbck1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 508
• Protein Description: 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). 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..
• Protein Sequence: MDEKTKKAEEMALSLARAVTGGDEQAAIKYATWLAEQKVPLRVQVKPEVSPTQDIRLCVSVEDAYMHTVTIWLTVRPDMTVASLKDMVFLDYGFPPSLQQWVVGQRLARDQETLHSHGIRRNGDSAYLYLLSARNTSLNPQELQRQRQLRMLEDLGFKDLTLQPRGPLEPVLPKPRTHQETGQPDAAPESPPVGWQCPGCTFINKPTRPGCEMCCRARPEAYQIPASYQPDEEERARLAGEEEALRQYEQRKQQQQEGNYLQHVQLEQRSLVLNTEPAECPVCYSVLAPGEAVVLRECLHTFCRECLQGTIRNSQEAEVSCPFIDNTYSCPGKLLEREIRALLSPEDYQRFLDLGVSIAENRSTLSYHCKTPDCRGWCFFEDDVNEFTCPVCTRVNCLLCKAIHERMNCREYQDDLAHRARNDVAAQQTTEMLRVMLQQGEAMYCPQCRIVVQKKDGCDWIRCTVCHTEICWVTKGPRWGPGGPGDTSGGCRCRVNGIPCHPSCQNCH

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	-
50	Phosphorylation	VQVKPEVSPTQDIRL EEECCCCCCCCCEEE	22.14	30181290
52	Phosphorylation	VKPEVSPTQDIRLCV ECCCCCCCCCEEEEE	31.22	30181290
137	Phosphorylation	LLSARNTSLNPQELQ HHHHCCCCCCHHHHH	29.69	18303026
161	Phosphorylation	DLGFKDLTLQPRGPL HCCCCCCCCCCCCCC	33.22	18303026
207	Phosphorylation	CTFINKPTRPGCEMC CEEECCCCCCCCHHC	51.62	18303026
270	Phosphorylation	HVQLEQRSLVLNTEP HHHHHHCEEEECCCC	23.64	18303026
275	Phosphorylation	QRSLVLNTEPAECPV HCEEEECCCCCCCCC	38.90	18303026
285	Phosphorylation	AECPVCYSVLAPGEA CCCCCEEEEECCCCC	12.91	18303026
328	Phosphorylation	CPFIDNTYSCPGKLL CCCCCCCCCCCCHHH	17.96	-

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
137	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
161	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
207	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
270	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
275	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
285	S	Phosphorylation	Kinase	PRKCB	P05771	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HOIL1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPCZ_RAT	Prkcz	physical	9514928
KPCB_RAT	Prkcb	physical	9514928

Drug and Disease Associations

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