dbPTM

TNIP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TNIP2_HUMAN
UniProt AC	Q8NFZ5
Protein Name	TNFAIP3-interacting protein 2
Gene Name	TNIP2 {ECO:0000312\|EMBL:EAW82514.1}
Organism	Homo sapiens (Human).
Sequence Length	429
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Inhibits NF-kappa-B activation by blocking the interaction of RIPK1 with its downstream effector NEMO/IKBKG. Forms a ternary complex with NFKB1 and MAP3K8 but appears to function upstream of MAP3K8 in the TLR4 signaling pathway that regulates MAP3K8 activation. Involved in activation of the MEK/ERK signaling pathway during innate immune response; this function seems to be stimulus- and cell type specific. Required for stability of MAP3K8. Involved in regulation of apoptosis in endothelial cells; promotes TEK agonist-stimulated endothelial survival. May act as transcriptional coactivator when translocated to the nucleus. Enhances CHUK-mediated NF-kappa-B activation involving NF-kappa-B p50-p65 and p50-c-Rel complexes..
Protein Sequence	MSRDPGSGGWEEAPRAAAALCTLYHEAGQRLRRLQDQLAARDALIARLRARLAALEGDAAPSLVDALLEQVARFREQLRRQEGGAAEAQMRQEIERLTERLEEKEREMQQLLSQPQHEREKEVVLLRRSMAEGERARAASDVLCRSLANETHQLRRTLTATAHMCQHLAKCLDERQHAQRNVGERSPDQSEHTDGHTSVQSVIEKLQEENRLLKQKVTHVEDLNAKWQRYNASRDEYVRGLHAQLRGLQIPHEPELMRKEISRLNRQLEEKINDCAEVKQELAASRTARDAALERVQMLEQQILAYKDDFMSERADRERAQSRIQELEEKVASLLHQVSWRQDSREPDAGRIHAGSKTAKYLAADALELMVPGGWRPGTGSQQPEPPAEGGHPGAAQRGQGDLQCPHCLQCFSDEQGEELLRHVAECCQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRDPGSGG ------CCCCCCCCC	45.45	-
7	Phosphorylation	-MSRDPGSGGWEEAP -CCCCCCCCCCCHHH	39.25	23401153
22	Phosphorylation	RAAAALCTLYHEAGQ HHHHHHHHHHHHHHH	31.07	21712546
24	Phosphorylation	AAALCTLYHEAGQRL HHHHHHHHHHHHHHH	4.58	21712546
62	Phosphorylation	LEGDAAPSLVDALLE HHCCCCHHHHHHHHH	35.98	30108239
113	Phosphorylation	REMQQLLSQPQHERE HHHHHHHCCCHHHHH	48.70	24043423
121	Ubiquitination	QPQHEREKEVVLLRR CCHHHHHHHHHHHHH	63.13	-
129	Phosphorylation	EVVLLRRSMAEGERA HHHHHHHHHHHHHHH	18.86	-
140	Phosphorylation	GERARAASDVLCRSL HHHHHHHHHHHHHHH	27.54	27251275
146	Phosphorylation	ASDVLCRSLANETHQ HHHHHHHHHHHHHHH	30.73	30108239
170	Ubiquitination	HMCQHLAKCLDERQH HHHHHHHHHHHHHHH	41.51	-
186	Phosphorylation	QRNVGERSPDQSEHT HHCCCCCCCCCCCCC	28.64	23401153
190	Phosphorylation	GERSPDQSEHTDGHT CCCCCCCCCCCCCCC	38.43	23663014
193	Phosphorylation	SPDQSEHTDGHTSVQ CCCCCCCCCCCCHHH	39.36	23663014
197	Phosphorylation	SEHTDGHTSVQSVIE CCCCCCCCHHHHHHH	35.80	29255136
198	Phosphorylation	EHTDGHTSVQSVIEK CCCCCCCHHHHHHHH	16.69	29255136
201	Phosphorylation	DGHTSVQSVIEKLQE CCCCHHHHHHHHHHH	23.94	29255136
205	Ubiquitination	SVQSVIEKLQEENRL HHHHHHHHHHHHCHH	44.33	-
279	Ubiquitination	INDCAEVKQELAASR HHHHHHHHHHHHHHH	29.56	-
330	Ubiquitination	RIQELEEKVASLLHQ HHHHHHHHHHHHHHH	33.45	-
333	Phosphorylation	ELEEKVASLLHQVSW HHHHHHHHHHHHHHC	34.16	30108239
339	Phosphorylation	ASLLHQVSWRQDSRE HHHHHHHHCCCCCCC	15.24	27273156
344	Phosphorylation	QVSWRQDSREPDAGR HHHCCCCCCCCCCCC	30.15	26699800
356	Phosphorylation	AGRIHAGSKTAKYLA CCCCCCCHHHHHHHH	27.84	27273156
357	Ubiquitination	GRIHAGSKTAKYLAA CCCCCCHHHHHHHHH	52.14	-
361	Phosphorylation	AGSKTAKYLAADALE CCHHHHHHHHHHHHH	10.10	27642862
413	Phosphorylation	PHCLQCFSDEQGEEL CCHHHHCCHHHHHHH	48.11	30108239

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	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TNIP2_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 TNIP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNAP3_HUMAN	TNFAIP3	physical	21266526
M3K8_HUMAN	MAP3K8	physical	15169888
NFKB1_HUMAN	NFKB1	physical	15169888
NEMO_HUMAN	IKBKG	physical	14653779
IKKA_HUMAN	CHUK	physical	21784860
IKKB_HUMAN	IKBKB	physical	21784860
SMRD1_HUMAN	SMARCD1	physical	12753905
TIE2_HUMAN	TEK	physical	12609966
STK11_HUMAN	STK11	physical	12595760
A4_HUMAN	APP	physical	21832049
UBC_HUMAN	UBC	physical	19373254
UBC_HUMAN	UBC	physical	27916521
UBP35_HUMAN	USP35	physical	26348204

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 TNIP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.	18691976 [Abstract]