TRI13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI13_HUMAN
• UniProt AC: O60858
• Protein Name: E3 ubiquitin-protein ligase TRIM13
• Gene Name: TRIM13
• Organism: Homo sapiens (Human).
• Sequence Length: 407
• Subcellular Localization: Endoplasmic reticulum membrane ; Single-pass membrane protein . Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
• Protein Description: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. [PubMed: 22178386 Plays also a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation]
• Protein Sequence: MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL

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
32	Ubiquitination	CSHNFCKKCLEGILE CCCCHHHHHHHHHHH	45.28	-
35 (in isoform 3)	Ubiquitination	-	54.37	-
45	Phosphorylation	LEGSVRNSLWRPAPF HHCCHHHCCCCCCCC	20.81	24719451
53	Ubiquitination	LWRPAPFKCPTCRKE CCCCCCCCCCCCCCC	37.94	-
56 (in isoform 3)	Ubiquitination	-	34.12	-
74	Phosphorylation	NSLQVNYSLKGIVEK CCCEEEEEHHHHHHH	20.57	24719451
81	Ubiquitination	SLKGIVEKYNKIKIS EHHHHHHHHHCCCCC	43.14	-
90	Ubiquitination	NKIKISPKMPVCKGH HCCCCCCCCCCCCCC	49.39	-
125	Ubiquitination	ATRGEHTKHVFCSIE CCCCCCCEEEEEEHH	39.41	-
128 (in isoform 3)	Ubiquitination	-	2.43	-
166	Phosphorylation	SRLDTLETSKRKSLQ HHHHHHHHHHHHHHH	42.53	-
167	Phosphorylation	RLDTLETSKRKSLQL HHHHHHHHHHHHHHH	22.53	-
168 (in isoform 1)	Ubiquitination	-	71.86	21906983
168	Ubiquitination	LDTLETSKRKSLQLL HHHHHHHHHHHHHHH	71.86	21906983
170	Ubiquitination	TLETSKRKSLQLLTK HHHHHHHHHHHHHHC	60.29	-
171 (in isoform 2)	Ubiquitination	-	25.94	21906983
171 (in isoform 3)	Ubiquitination	-	25.94	-
171	Phosphorylation	LETSKRKSLQLLTKD HHHHHHHHHHHHHCC	25.94	29214152
173 (in isoform 3)	Ubiquitination	-	41.33	-
174	Phosphorylation	SKRKSLQLLTKDSDK HHHHHHHHHHCCHHH	8.76	27251275
176	Phosphorylation	RKSLQLLTKDSDKVK HHHHHHHHCCHHHHH	41.20	-
183	Ubiquitination	TKDSDKVKEFFEKLQ HCCHHHHHHHHHHHH	55.32	-
186 (in isoform 3)	Ubiquitination	-	9.44	-
188	Ubiquitination	KVKEFFEKLQHTLDQ HHHHHHHHHHHHHHH	48.57	-
192	Phosphorylation	FFEKLQHTLDQKKNE HHHHHHHHHHHHHHH	21.04	29396449
196	Ubiquitination	LQHTLDQKKNEILSD HHHHHHHHHHHHHHH	58.18	-
202	Phosphorylation	QKKNEILSDFETMKL HHHHHHHHHHHHHHH	46.01	29759185
206	Phosphorylation	EILSDFETMKLAVMQ HHHHHHHHHHHHHHH	21.43	29759185
208	Ubiquitination	LSDFETMKLAVMQAY HHHHHHHHHHHHHHH	40.49	-
221 (in isoform 1)	Ubiquitination	-	49.10	21906983
221	Ubiquitination	AYDPEINKLNTILQE HHCHHHHHHHHHHHH	49.10	21906983
224 (in isoform 2)	Ubiquitination	-	33.24	21906983
224 (in isoform 3)	Ubiquitination	-	33.24	-
258	Ubiquitination	QMQEFREKIKVIKET HHHHHHHHCCHHCCC	43.50	-
270	Phosphorylation	KETPLPPSNLPASPL CCCCCCCCCCCCCCC	49.40	25002506
275	Phosphorylation	PPSNLPASPLMKNFD CCCCCCCCCCCCCCC	19.34	25850435
279	Ubiquitination	LPASPLMKNFDTSQW CCCCCCCCCCCCHHC	63.24	-
290 (in isoform 1)	Ubiquitination	-	55.57	21906983
290	Ubiquitination	TSQWEDIKLVDVDKL CHHCCCEEEEECCCC	55.57	2190698
293 (in isoform 2)	Ubiquitination	-	54.02	21906983

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM13	O60858	PMID:31744379

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRI13_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 TRI13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ROBO2_HUMAN	ROBO2	physical	21900206
GDIR1_HUMAN	ARHGDIA	physical	21900206
SQSTM_HUMAN	SQSTM1	physical	22178386
ZFYV1_HUMAN	ZFYVE1	physical	22178386
TERA_HUMAN	VCP	physical	17314412
AT2A2_HUMAN	ATP2A2	physical	17314412
OST48_HUMAN	DDOST	physical	17314412
UB2D2_HUMAN	UBE2D2	physical	17314412
TRI13_HUMAN	TRIM13	physical	17314412
NEMO_HUMAN	IKBKG	physical	25152375
GMCL1_HUMAN	GMCL1	physical	25416956
MDM2_HUMAN	MDM2	physical	21333377
AKT1_HUMAN	AKT1	physical	21333377
TRI13_HUMAN	TRIM13	physical	21333377
ELOV2_HUMAN	ELOVL2	physical	28514442
NPL4_HUMAN	NPLOC4	physical	28514442
CKAP4_HUMAN	CKAP4	physical	28514442

Drug and Disease Associations

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