TRIM9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRIM9_HUMAN
• UniProt AC: Q9C026
• Protein Name: E3 ubiquitin-protein ligase TRIM9
• Gene Name: TRIM9
• Organism: Homo sapiens (Human).
• Sequence Length: 710
• Subcellular Localization: Cytoplasm . Cell projection, dendrite . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle . Cell junction, synapse . Cytoplasm, cytoskeleton . Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle-associated f
• Protein Description: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation..
• Protein Sequence: MEEMEEELKCPVCGSFYREPIILPCSHNLCQACARNILVQTPESESPQSHRAAGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPATHLSPALAPVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRNMVQQIQENSVEFEACLVAQCDALIDALNRRKAQLLARVNKEHEHKLKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQWGKGTLTPRMTTDFDLSLDNSPLLQSIHQLDFVQVKASSPVPATPILQLEECCTHNNSATLSWKQPPLSTVPADGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYNARVKAFNKTGVSPYSKTLVLQTSEVAWFAFDPGSAHSDIILSNDNLTVTCSSYDDRVVLGKTGFSKGIHYWELTVDRYDNHPDPAFGVARMDVMKDVMLGKDDKAWAMYVDNNRSWFMHNNSHTNRTEGGITKGATIGVLLDLNRKNLTFFINDEQQGPIAFDNVEGLFFPAVSLNRNVQVTLHTGLPVPDFYSSRASIA

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
41	Phosphorylation	ARNILVQTPESESPQ HHHCCEECCCCCCCC	22.88	28450419
44	Phosphorylation	ILVQTPESESPQSHR CCEECCCCCCCCCCC	44.57	30266825
46	Phosphorylation	VQTPESESPQSHRAA EECCCCCCCCCCCCC	37.20	30266825
46 (in isoform 5)	Phosphorylation	-	37.20	18220336
49	Phosphorylation	PESESPQSHRAAGSG CCCCCCCCCCCCCCC	20.51	30266825
58	Phosphorylation	RAAGSGVSDYDYLDL CCCCCCCCCCCCCCH	33.70	29978859
60	Phosphorylation	AGSGVSDYDYLDLDK CCCCCCCCCCCCHHH	10.05	25884760
62	Phosphorylation	SGVSDYDYLDLDKMS CCCCCCCCCCHHHCC	8.90	29978859
69	Phosphorylation	YLDLDKMSLYSEADS CCCHHHCCCCCCCCC	29.87	30576142
76	Phosphorylation	SLYSEADSGYGSYGG CCCCCCCCCCCCCCC	40.75	-
78	Phosphorylation	YSEADSGYGSYGGFA CCCCCCCCCCCCCCC	13.57	25884760
80	Phosphorylation	EADSGYGSYGGFASA CCCCCCCCCCCCCCC	16.48	-
140	Methylation	RSLILDDRGLRGFPK CEEECCCCCCCCCCC	45.79	115918965
158	Phosphorylation	LEGVIDRYQQSKAAA HHHHHHHHHHHHHHH	13.73	28555341
161	Phosphorylation	VIDRYQQSKAAALKC HHHHHHHHHHHHHHC	14.56	28555341
230	Phosphorylation	PRKVSTCTDHELENH CCCCCCCCCCCCCCC	40.24	-
347	Phosphoglycerylation	KEHEHKLKVVRDQIS HHHHHHHHHHHHHHH	43.41	-
406	Phosphorylation	QWGKGTLTPRMTTDF CCCCCCCCCCEECCC	14.53	24719451
425	Phosphorylation	DNSPLLQSIHQLDFV CCCHHHHHHHCCCEE	23.23	-
541 (in isoform 5)	Phosphorylation	-	43.13	27732954
543 (in isoform 5)	Phosphorylation	-	39.03	27732954
611 (in isoform 4)	Sumoylation	-	59.81	-
619	Phosphorylation	DDKAWAMYVDNNRSW CCCEEEEEEECCCEE	9.26	-
625	Phosphorylation	MYVDNNRSWFMHNNS EEEECCCEEEEECCC	27.13	-

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
76	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
80	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM9	Q9C026	PMID:20085810

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRIM9_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 TRIM9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM9_HUMAN	TRIM9	physical	11331580
UB2G2_HUMAN	UBE2G2	physical	21143188
TRI46_HUMAN	TRIM46	physical	22493164
PCGF3_HUMAN	PCGF3	physical	22493164
TRI27_HUMAN	TRIM27	physical	22493164
TRIM8_HUMAN	TRIM8	physical	22493164
TRIM9_HUMAN	TRIM9	physical	24778312
SNP25_HUMAN	SNAP25	physical	24778312
DCC_MOUSE	Dcc	physical	24778312
FBW1A_HUMAN	BTRC	physical	25190485
ACTA_HUMAN	ACTA2	physical	25190485
FBW1B_HUMAN	FBXW11	physical	25190485
C19L2_HUMAN	CWF19L2	physical	25416956
ENAH_MOUSE	Enah	physical	26702829
VASP_MOUSE	Vasp	physical	26702829
TRIM9_HUMAN	TRIM9	physical	26702829
TBK1_HUMAN	TBK1	physical	26915459
TRIM9_HUMAN	TRIM9	physical	26915459

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
PubMed: 18220336