dbPTM

TRBP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRBP2_HUMAN
UniProt AC	Q15633
Protein Name	RISC-loading complex subunit TARBP2 {ECO:0000255\|HAMAP-Rule:MF_03034}
Gene Name	TARBP2 {ECO:0000255\|HAMAP-Rule:MF_03034}
Organism	Homo sapiens (Human).
Sequence Length	366
Subcellular Localization	Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
Protein Description	Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1, and stimulates translation of TAR-containing RNAs. This is achieved in part at least by binding to and inhibiting EIF2AK2/PKR, thereby reducing phosphorylation and inhibition of EIF2S1/eIF-2-alpha. May also promote translation of TAR-containing RNAs independently of EIF2AK2/PKR..
Protein Sequence	MSEEEQGSGTTTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPVFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEVEPDDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCRVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCHGSATTREAARGEAARRALQYLKIMAGSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEEEQGSG ------CCHHHCCCC	54.43	28348404
8	Phosphorylation	MSEEEQGSGTTTGCG CCHHHCCCCCCCCCC	32.43	28348404
9	Phosphorylation	SEEEQGSGTTTGCGL CHHHCCCCCCCCCCC	33.63	24719451
10	Phosphorylation	EEEQGSGTTTGCGLP HHHCCCCCCCCCCCC	23.92	28348404
11	Phosphorylation	EEQGSGTTTGCGLPS HHCCCCCCCCCCCCC	25.39	28348404
12	Phosphorylation	EQGSGTTTGCGLPSI HCCCCCCCCCCCCCH	30.25	28348404
30	Phosphorylation	LAANPGKTPISLLQE HHHCCCCCCHHHHHH	31.60	25159151
38	Phosphorylation	PISLLQEYGTRIGKT CHHHHHHHHCCCCCC	15.73	27642862
48	Phosphorylation	RIGKTPVYDLLKAEG CCCCCCHHHHHHHCC	11.32	27642862
52	Sumoylation	TPVYDLLKAEGQAHQ CCHHHHHHHCCCCCC	52.25	-
52	Sumoylation	TPVYDLLKAEGQAHQ CCHHHHHHHCCCCCC	52.25	-
71	Phosphorylation	FRVTVGDTSCTGQGP EEEEECCCCCCCCCC	21.55	-
79	Phosphorylation	SCTGQGPSKKAAKHK CCCCCCCCHHHHHHH	54.32	-
80	Acetylation	CTGQGPSKKAAKHKA CCCCCCCHHHHHHHH	49.95	26051181
93	Acetylation	KAAEVALKHLKGGSM HHHHHHHHHCCCCCC	36.83	25953088
108	Phosphorylation	LEPALEDSSSFSPLD CCHHHCCCCCCCCCC	20.64	28348404
109	Phosphorylation	EPALEDSSSFSPLDS CHHHCCCCCCCCCCC	47.96	28348404
110	Phosphorylation	PALEDSSSFSPLDSS HHHCCCCCCCCCCCC	33.42	28348404
112	Phosphorylation	LEDSSSFSPLDSSLP HCCCCCCCCCCCCCC	26.88	28348404
116	Phosphorylation	SSFSPLDSSLPEDIP CCCCCCCCCCCCCCC	41.27	28348404
117	Phosphorylation	SFSPLDSSLPEDIPV CCCCCCCCCCCCCCC	47.84	28348404
126	Phosphorylation	PEDIPVFTAAAAATP CCCCCCCCHHHCCCC	18.67	29496963
142	Phosphorylation	PSVVLTRSPPMELQP CEEEEECCCCCCCCC	28.28	30278072
152	Phosphorylation	MELQPPVSPQQSECN CCCCCCCCCCCCCCC	23.82	30278072
156	Phosphorylation	PPVSPQQSECNPVGA CCCCCCCCCCCCCHH	38.58	30278072
178	Phosphorylation	KGWRLPEYTVTQESG CCCCCCEEEEEECCC	12.45	27642862
179	Phosphorylation	GWRLPEYTVTQESGP CCCCCEEEEEECCCC	18.53	-
181	Phosphorylation	RLPEYTVTQESGPAH CCCEEEEEECCCCCC	20.86	-
184	Phosphorylation	EYTVTQESGPAHRKE EEEEEECCCCCCCCE	40.01	28555341
206	Phosphorylation	ERFIEIGSGTSKKLA EEEEECCCCCCHHHH	44.55	25159151
208	Phosphorylation	FIEIGSGTSKKLAKR EEECCCCCCHHHHHH	38.79	21406692
209	Phosphorylation	IEIGSGTSKKLAKRN EECCCCCCHHHHHHH	31.17	21406692
246	Phosphorylation	EPDDDHFSIGVGSRL CCCCCCEECCCCHHH	18.27	23401153
251	Phosphorylation	HFSIGVGSRLDGLRN CEECCCCHHHHCHHC	27.54	27251275
262	Phosphorylation	GLRNRGPGCTWDSLR CHHCCCCCCCHHHHH	25.06	24719451
275	Ubiquitination	LRNSVGEKILSLRSC HHHHHHHHHHHHCCC	42.91	-
275	Acetylation	LRNSVGEKILSLRSC HHHHHHHHHHHHCCC	42.91	26051181
281	Phosphorylation	EKILSLRSCSLGSLG HHHHHHCCCCCCHHH	17.22	29978859
283	Phosphorylation	ILSLRSCSLGSLGAL HHHHCCCCCCHHHHH	36.69	29978859
286	Phosphorylation	LRSCSLGSLGALGPA HCCCCCCHHHHHHHH	28.99	29978859
360	Ubiquitination	RRALQYLKIMAGSK- HHHHHHHHHHHCCC-	26.04	-

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
283	S	Phosphorylation	Kinase	AKT1	P31749	PSP
283	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
283	S	Phosphorylation	Kinase	RPS6KB2	Q9UBS0	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRBP2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TRBP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRBP2_HUMAN	TARBP2	physical	11438532
RBM14_HUMAN	RBM14	physical	11443112
TRBP2_HUMAN	TARBP2	physical	7568151
E2AK2_HUMAN	EIF2AK2	physical	7568151
E2AK2_HUMAN	EIF2AK2	physical	11438532
NEMO_HUMAN	IKBKG	physical	20211142
MED21_HUMAN	MED21	physical	20211142
CSEN_HUMAN	KCNIP3	physical	20211142
TGIF2_HUMAN	TGIF2	physical	20211142
A4_HUMAN	APP	physical	21832049
AGO2_HUMAN	AGO2	physical	24778252
TRM1_HUMAN	TRMT1	physical	24778252
AK17A_HUMAN	AKAP17A	physical	24778252
SRP54_HUMAN	SRP54	physical	24778252
CEBPZ_HUMAN	CEBPZ	physical	24778252
DDX27_HUMAN	DDX27	physical	24778252
DDX50_HUMAN	DDX50	physical	24778252
DICER_HUMAN	DICER1	physical	24778252
HP1B3_HUMAN	HP1BP3	physical	24778252
MMTA2_HUMAN	C1orf35	physical	24778252
NOC3L_HUMAN	NOC3L	physical	24778252
POP1_HUMAN	POP1	physical	24778252
PRKRA_HUMAN	PRKRA	physical	24778252
TCOF_HUMAN	TCOF1	physical	24778252
SRP72_HUMAN	SRP72	physical	24778252
SDA1_HUMAN	SDAD1	physical	24778252
RBM28_HUMAN	RBM28	physical	24778252
RRP12_HUMAN	RRP12	physical	24778252
RRP1B_HUMAN	RRP1B	physical	24778252
SRPRA_HUMAN	SRPR	physical	24778252
TSR1_HUMAN	TSR1	physical	24778252
U3IP2_HUMAN	RRP9	physical	24778252
TRBP2_HUMAN	TARBP2	physical	25416956
PRKRA_HUMAN	PRKRA	physical	25416956
ZN346_HUMAN	ZNF346	physical	25416956
STRBP_HUMAN	STRBP	physical	25416956
TEANC_HUMAN	TCEANC	physical	25416956

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.

Regulatory Network of TRBP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASSSPECTROMETRY.	18669648 [Abstract]