TRIM7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRIM7_HUMAN
• UniProt AC: Q9C029
• Protein Name: E3 ubiquitin-protein ligase TRIM7 {ECO:0000305}
• Gene Name: TRIM7
• Organism: Homo sapiens (Human).
• Sequence Length: 511
• Protein Description: E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation..
• Protein Sequence: MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP

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 (in isoform 4)	Phosphorylation	-	15.74	24043423
5 (in isoform 4)	Phosphorylation	-	10.97	24043423
68	Ubiquitination	GAGSVGAATRAPPFP CCCCCCCCCCCCCCC	7.53	29967540
78	Ubiquitination	APPFPLPCPQCREPA CCCCCCCCCCCCCCC	4.85	29967540
94	Ubiquitination	PSQLRPNRQLAAVAT HHHCCCHHHHHHHHH	35.26	29967540
102	Ubiquitination	QLAAVATLLRRFSLP HHHHHHHHHHHCCCC	2.23	29967540
104	Ubiquitination	AAVATLLRRFSLPAA HHHHHHHHHCCCCCC	40.48	29967540
107	Phosphorylation	ATLLRRFSLPAAAPG HHHHHHCCCCCCCCC	31.47	23927012
118	Phosphorylation	AAPGEHGSQAAAARA CCCCCCHHHHHHHHH	20.67	-
128	Ubiquitination	AAARAAAARCGQHGE HHHHHHHHHHCCCCC	11.54	29967540
133	Ubiquitination	AAARCGQHGEPFKLY HHHHHCCCCCCEEEE	28.06	29967540
138	Methylation	GQHGEPFKLYCQDDG CCCCCCEEEEECCCC	49.62	115979491
159	Ubiquitination	CDRAREHREHAVLPL CCCHHHHHHCCCCCH	32.42	29967540
174	Ubiquitination	DEAVQEAKELLESRL HHHHHHHHHHHHHHH	48.41	29967540
186	Ubiquitination	SRLRVLKKELEDCEV HHHHHHHHHHHHCHH	64.47	29967540
261	Phosphorylation	AQLGVEITQLSKLSS HHHCHHHHHHHHHHH	15.22	22210691
264	Phosphorylation	GVEITQLSKLSSQIQ CHHHHHHHHHHHHHH	23.02	22210691
267	Phosphorylation	ITQLSKLSSQIQETA HHHHHHHHHHHHHHH	24.75	22673903
268	Phosphorylation	TQLSKLSSQIQETAQ HHHHHHHHHHHHHHC	41.56	22673903
273	Phosphorylation	LSSQIQETAQKPDLD HHHHHHHHHCCCCCH	20.29	22210691
276	Ubiquitination	QIQETAQKPDLDFLQ HHHHHHCCCCCHHHH	37.73	29967540
286	Ubiquitination	LDFLQEFKSTLSRCS CHHHHHHHHHHHHHC	41.60	29967540
287	Phosphorylation	DFLQEFKSTLSRCSN HHHHHHHHHHHHHCC	39.64	18785766
288	Phosphorylation	FLQEFKSTLSRCSNV HHHHHHHHHHHHCCC	29.37	18785766
310	Ubiquitination	VSSEMKNKVWNVSLK CCHHHHHCHHCCHHH	43.01	29967540
341	Ubiquitination	GELEKEEKVELTLDP CCCCCHHCEEEEECC	41.94	29967540

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
107	S	Phosphorylation	Kinase	RPS6KA5	O75582	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
107	S	Phosphorylation	Phosphorylated at Ser-107 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity.	25851810
107	S	ubiquitylation	Phosphorylated at Ser-107 by RPS6KA5/MSK1, which stimulates the ubiquitin ligase activity.	25851810

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TRIM7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GLYG_HUMAN	GYG1	physical	11916970
UB2D1_HUMAN	UBE2D1	physical	21143188
UB2D2_HUMAN	UBE2D2	physical	21143188
UB2D3_HUMAN	UBE2D3	physical	21143188
UB2E1_HUMAN	UBE2E1	physical	21143188
TRIM7_HUMAN	TRIM7	physical	14984203

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.