TRIM8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRIM8_HUMAN
• UniProt AC: Q9BZR9
• Protein Name: E3 ubiquitin-protein ligase TRIM8
• Gene Name: TRIM8
• Organism: Homo sapiens (Human).
• Sequence Length: 551
• Subcellular Localization: Cytoplasm . Nucleus . Nucleo-cytoplasmic translocation is involved in regulation of NF-kappa-B.
• Protein Description: E3 ubiquitin-protein ligase which plays different roles in immune pathways. Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1. [PubMed: 12163497 Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'lys-63' polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B]
• Protein Sequence: MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSLSPTKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVSSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASGEGQSGQPLGPCSSTQHLVALPGGAQPVHSSPVFPPSQYPNGSAAQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQSLPSLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS

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
45	Ubiquitination	CIGEAWAKDSGLVRC CCCHHHHCCCCCEEC	41.55	-
70	Ubiquitination	PGLEKNLKLTNIVEK CCHHHHHHHHHHHHH	63.76	29967540
195	Ubiquitination	EIRKMLMKQQDRLEE HHHHHHHHHHHHHHH	40.63	-
213	Ubiquitination	DIEDQLYKLESDKRL HHHHHHHHHHHCHHH	55.13	29967540
224	Ubiquitination	DKRLVEEKVNQLKEE CHHHHHHHHHHHHHH	32.74	29967540
229	Ubiquitination	EEKVNQLKEEVRLQY HHHHHHHHHHHHHHH	41.90	29967540
238	Ubiquitination	EVRLQYEKLHQLLDE HHHHHHHHHHHHCCH	46.46	29967540
256	Ubiquitination	QTVEVLDKAQAKFCS HHHHHHHHHHHHHCC	37.93	29967540
300	Ubiquitination	TEDVSFMKNTKSVKI CCCCCHHCCCCCEEE	60.50	29967540
316	Phosphorylation	MDRTQTCTSSSLSPT ECCCCCCCCCCCCCC	34.72	28450419
317	Phosphorylation	DRTQTCTSSSLSPTK CCCCCCCCCCCCCCC	21.78	28450419
318	Phosphorylation	RTQTCTSSSLSPTKI CCCCCCCCCCCCCCH	19.69	28450419
319	Phosphorylation	TQTCTSSSLSPTKIG CCCCCCCCCCCCCHH	32.41	28450419
321	Phosphorylation	TCTSSSLSPTKIGHL CCCCCCCCCCCHHHH	32.26	25159151
323	Phosphorylation	TSSSLSPTKIGHLNS CCCCCCCCCHHHHCC	31.73	21815630
331	Ubiquitination	KIGHLNSKLFLNEVA CHHHHCCHHHHHHHH	42.03	29967540
339	Ubiquitination	LFLNEVAKKEKQLRK HHHHHHHHHHHHHHH	67.64	29967540
370	Phosphorylation	PLYPCGVSSSGAEKR CCCCCCCCCCHHHHC	12.22	-
371	Phosphorylation	LYPCGVSSSGAEKRK CCCCCCCCCHHHHCC	30.31	-

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

Oops, there are no upstream regulatory protein records of TRIM8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRIM8_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRIM8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM8_HUMAN	TRIM8	physical	11331580
PIAS3_HUMAN	PIAS3	physical	20516148
M3K7_HUMAN	MAP3K7	physical	22084099
HS90B_HUMAN	HSP90AB1	physical	21689689
UB2D2_HUMAN	UBE2D2	physical	22084099
R113A_HUMAN	RNF113A	physical	22493164
UHRF2_HUMAN	UHRF2	physical	22493164
TRIM8_HUMAN	TRIM8	physical	22493164
TRIM2_HUMAN	TRIM2	physical	22493164
MKRN3_HUMAN	MKRN3	physical	22493164
RN111_HUMAN	RNF111	physical	22493164
TRAF5_HUMAN	TRAF5	physical	22493164
RBX2_HUMAN	RNF7	physical	22493164
RNF41_HUMAN	RNF41	physical	22493164
TRI39_HUMAN	TRIM39	physical	22493164
UBP7_HUMAN	USP7	physical	21988832
M3K7_HUMAN	MAP3K7	physical	27956576
M3K7_HUMAN	MAP3K7	physical	27981609

Drug and Disease Associations

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