dbPTM

TRI29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRI29_HUMAN
UniProt AC	Q14134
Protein Name	Tripartite motif-containing protein 29
Gene Name	TRIM29
Organism	Homo sapiens (Human).
Sequence Length	588
Subcellular Localization	Cytoplasm . Lysosome . Colocalizes with intermediate filaments.
Protein Description	Plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in the lysosome where it induces its 'Lys-48' ubiquitination and subsequent degradation. In turn, the expression of type I interferons and the production of proinflammatory cytokines are inhibited. Additionally, induces the 'Lys-48' ubiquitination of TMEM173/STING in a similar way, leading to its degradation..
Protein Sequence	MEAADASRSNGSSPEARDARSPSGPSGSLENGTKADGKDAKTTNGHGGEAAEGKSLGSALKPGEGRSALFAGNEWRRPIIQFVESGDDKNSNYFSMDSMEGKRSPYAGLQLGAAKKPPVTFAEKGELRKSIFSESRKPTVSIMEPGETRRNSYPRADTGLFSRSKSGSEEVLCDSCIGNKQKAVKSCLVCQASFCELHLKPHLEGAAFRDHQLLEPIRDFEARKCPVHGKTMELFCQTDQTCICYLCMFQEHKNHSTVTVEEAKAEKETELSLQKEQLQLKIIEIEDEAEKWQKEKDRIKSFTTNEKAILEQNFRDLVRDLEKQKEEVRAALEQREQDAVDQVKVIMDALDERAKVLHEDKQTREQLHSISDSVLFLQEFGALMSNYSLPPPLPTYHVLLEGEGLGQSLGNFKDDLLNVCMRHVEKMCKADLSRNFIERNHMENGGDHRYVNNYTNSFGGEWSAPDTMKRYSMYLTPKGGVRTSYQPSSPGRFTKETTQKNFNNLYGTKGNYTSRVWEYSSSIQNSDNDLPVVQGSSSFSLKGYPSLMRSQSPKAQPQTWKSGKQTMLSHYRPFYVNKGNGIGSNEAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MEAADASRSNGSSP -CCHHHHHHCCCCCH	36.47	25159151
9	Phosphorylation	EAADASRSNGSSPEA CHHHHHHCCCCCHHH	42.94	25159151
12	Phosphorylation	DASRSNGSSPEARDA HHHHCCCCCHHHHHC	47.15	25159151
13	Phosphorylation	ASRSNGSSPEARDAR HHHCCCCCHHHHHCC	28.32	25159151
21	Phosphorylation	PEARDARSPSGPSGS HHHHHCCCCCCCCCC	25.74	28355574
23	Phosphorylation	ARDARSPSGPSGSLE HHHCCCCCCCCCCCC	65.66	23927012
26	Phosphorylation	ARSPSGPSGSLENGT CCCCCCCCCCCCCCC	44.53	23927012
28	Phosphorylation	SPSGPSGSLENGTKA CCCCCCCCCCCCCCC	36.53	28355574
33	Phosphorylation	SGSLENGTKADGKDA CCCCCCCCCCCCCCC	34.34	24732914
34	Acetylation	GSLENGTKADGKDAK CCCCCCCCCCCCCCC	45.97	7987767
38	Acetylation	NGTKADGKDAKTTNG CCCCCCCCCCCCCCC	55.87	7987777
42	Phosphorylation	ADGKDAKTTNGHGGE CCCCCCCCCCCCCCC	27.49	24702127
43	Phosphorylation	DGKDAKTTNGHGGEA CCCCCCCCCCCCCCC	38.20	24702127
54	Ubiquitination	GGEAAEGKSLGSALK CCCCCCCCCCCCCCC	33.73	-
58	Phosphorylation	AEGKSLGSALKPGEG CCCCCCCCCCCCCCC	35.40	25159151
61	Ubiquitination	KSLGSALKPGEGRSA CCCCCCCCCCCCCCC	51.17	-
67	Phosphorylation	LKPGEGRSALFAGNE CCCCCCCCCEECCCC	39.93	23312004
85	Phosphorylation	PIIQFVESGDDKNSN CEEEHHHCCCCCCCC	42.07	22617229
91	Phosphorylation	ESGDDKNSNYFSMDS HCCCCCCCCCCCCCC	38.35	21945579
93	Phosphorylation	GDDKNSNYFSMDSME CCCCCCCCCCCCCCC	9.24	21945579
95	Phosphorylation	DKNSNYFSMDSMEGK CCCCCCCCCCCCCCC	16.00	21945579
98	Phosphorylation	SNYFSMDSMEGKRSP CCCCCCCCCCCCCCC	15.30	21945579
102	Acetylation	SMDSMEGKRSPYAGL CCCCCCCCCCCCCCC	36.07	20368352
102	Ubiquitination	SMDSMEGKRSPYAGL CCCCCCCCCCCCCCC	36.07	-
104	Phosphorylation	DSMEGKRSPYAGLQL CCCCCCCCCCCCCCC	26.25	21945579
106	Phosphorylation	MEGKRSPYAGLQLGA CCCCCCCCCCCCCCC	17.97	21945579
115	Ubiquitination	GLQLGAAKKPPVTFA CCCCCCCCCCCCCEE	66.34	-
116	Acetylation	LQLGAAKKPPVTFAE CCCCCCCCCCCCEEC	50.23	20368352
116	Ubiquitination	LQLGAAKKPPVTFAE CCCCCCCCCCCCEEC	50.23	-
120	O-linked_Glycosylation	AAKKPPVTFAEKGEL CCCCCCCCEECCCHH	23.93	30059200
124	Ubiquitination	PPVTFAEKGELRKSI CCCCEECCCHHHHHH	55.01	-
129	Ubiquitination	AEKGELRKSIFSESR ECCCHHHHHHCCCCC	61.60	-
130	Phosphorylation	EKGELRKSIFSESRK CCCHHHHHHCCCCCC	23.56	23090842
133	Phosphorylation	ELRKSIFSESRKPTV HHHHHHCCCCCCCCE	32.75	21815630
135	Phosphorylation	RKSIFSESRKPTVSI HHHHCCCCCCCCEEE	44.39	23090842
137	Ubiquitination	SIFSESRKPTVSIME HHCCCCCCCCEEECC	55.08	-
139	Phosphorylation	FSESRKPTVSIMEPG CCCCCCCCEEECCCC	29.89	24114839
141	Phosphorylation	ESRKPTVSIMEPGET CCCCCCEEECCCCCC	20.78	24114839
148	Phosphorylation	SIMEPGETRRNSYPR EECCCCCCCCCCCCC	40.62	23090842
152	Phosphorylation	PGETRRNSYPRADTG CCCCCCCCCCCCCCC	34.40	25394399
153	Phosphorylation	GETRRNSYPRADTGL CCCCCCCCCCCCCCC	10.57	24732914
158	Phosphorylation	NSYPRADTGLFSRSK CCCCCCCCCCCCCCC	34.50	24732914
162	Phosphorylation	RADTGLFSRSKSGSE CCCCCCCCCCCCCCC	40.46	24732914
164	Phosphorylation	DTGLFSRSKSGSEEV CCCCCCCCCCCCCEE	29.94	23663014
165	Ubiquitination	TGLFSRSKSGSEEVL CCCCCCCCCCCCEEE	58.70	-
166	Phosphorylation	GLFSRSKSGSEEVLC CCCCCCCCCCCEEEC	49.12	23927012
168	Phosphorylation	FSRSKSGSEEVLCDS CCCCCCCCCEEECHH	37.36	23927012
175	Phosphorylation	SEEVLCDSCIGNKQK CCEEECHHHCCCHHH	13.46	23927012
180	Ubiquitination	CDSCIGNKQKAVKSC CHHHCCCHHHHHHHH	48.22	-
256	Phosphorylation	FQEHKNHSTVTVEEA HHHCCCCCEEEHHHH	33.69	25056879
264	Ubiquitination	TVTVEEAKAEKETEL EEEHHHHHHHHHHHH	61.43	-
272	Phosphorylation	AEKETELSLQKEQLQ HHHHHHHHHHHHHHH	23.63	24719451
275	Acetylation	ETELSLQKEQLQLKI HHHHHHHHHHHHEEE	53.36	20368352
275	Ubiquitination	ETELSLQKEQLQLKI HHHHHHHHHHHHEEE	53.36	-
281	Ubiquitination	QKEQLQLKIIEIEDE HHHHHHEEEEEEHHH	28.77	-
291	Acetylation	EIEDEAEKWQKEKDR EEHHHHHHHHHHHHH	63.07	20368352
291	Ubiquitination	EIEDEAEKWQKEKDR EEHHHHHHHHHHHHH	63.07	-
300	Acetylation	QKEKDRIKSFTTNEK HHHHHHHHHHCCCHH	40.17	20368352
300	Ubiquitination	QKEKDRIKSFTTNEK HHHHHHHHHHCCCHH	40.17	-
301	Phosphorylation	KEKDRIKSFTTNEKA HHHHHHHHHCCCHHH	26.00	27794612
303	Phosphorylation	KDRIKSFTTNEKAIL HHHHHHHCCCHHHHH	35.48	27794612
304	Phosphorylation	DRIKSFTTNEKAILE HHHHHHCCCHHHHHH	39.09	27794612
307	Ubiquitination	KSFTTNEKAILEQNF HHHCCCHHHHHHHHH	42.68	-
323	Ubiquitination	DLVRDLEKQKEEVRA HHHHHHHHHHHHHHH	74.17	-
325	Ubiquitination	VRDLEKQKEEVRAAL HHHHHHHHHHHHHHH	67.90	-
344	Ubiquitination	QDAVDQVKVIMDALD HHHHHHHHHHHHHHH	22.02	-
361	Acetylation	AKVLHEDKQTREQLH HHHHHCCHHHHHHHH	51.05	20368352
361	Ubiquitination	AKVLHEDKQTREQLH HHHHHCCHHHHHHHH	51.05	-
429	Ubiquitination	RHVEKMCKADLSRNF HHHHHHHHHHHHHCH	41.24	-
450	Phosphorylation	ENGGDHRYVNNYTNS HCCCCCCCCCCCCCC	12.24	21945579
454	Phosphorylation	DHRYVNNYTNSFGGE CCCCCCCCCCCCCCC	11.33	21945579
455	Phosphorylation	HRYVNNYTNSFGGEW CCCCCCCCCCCCCCC	26.89	21945579
457	Phosphorylation	YVNNYTNSFGGEWSA CCCCCCCCCCCCCCC	19.91	21945579
467	Phosphorylation	GEWSAPDTMKRYSMY CCCCCCCHHHEEEEE	24.43	-
469	Methylation	WSAPDTMKRYSMYLT CCCCCHHHEEEEEEE	50.72	115979497
469	Ubiquitination	WSAPDTMKRYSMYLT CCCCCHHHEEEEEEE	50.72	-
471	Phosphorylation	APDTMKRYSMYLTPK CCCHHHEEEEEEECC	7.71	21945579
472	Phosphorylation	PDTMKRYSMYLTPKG CCHHHEEEEEEECCC	12.65	26657352
474	Phosphorylation	TMKRYSMYLTPKGGV HHHEEEEEEECCCCC	11.07	21945579
476	Phosphorylation	KRYSMYLTPKGGVRT HEEEEEEECCCCCCC	12.88	21945579
478	Acetylation	YSMYLTPKGGVRTSY EEEEEECCCCCCCCC	64.16	20368352
483	Phosphorylation	TPKGGVRTSYQPSSP ECCCCCCCCCCCCCC	29.40	24732914
484	Phosphorylation	PKGGVRTSYQPSSPG CCCCCCCCCCCCCCC	15.94	24732914
485	Phosphorylation	KGGVRTSYQPSSPGR CCCCCCCCCCCCCCC	24.67	24732914
488	Phosphorylation	VRTSYQPSSPGRFTK CCCCCCCCCCCCCCH	33.37	22617229
489	Phosphorylation	RTSYQPSSPGRFTKE CCCCCCCCCCCCCHH	37.75	25159151
494	Phosphorylation	PSSPGRFTKETTQKN CCCCCCCCHHHCCHH	26.98	24732914
495	Acetylation	SSPGRFTKETTQKNF CCCCCCCHHHCCHHH	50.80	20368352
495	Ubiquitination	SSPGRFTKETTQKNF CCCCCCCHHHCCHHH	50.80	-
497	Phosphorylation	PGRFTKETTQKNFNN CCCCCHHHCCHHHHH	35.76	25072903
498	Phosphorylation	GRFTKETTQKNFNNL CCCCHHHCCHHHHHH	38.34	25072903
500	Ubiquitination	FTKETTQKNFNNLYG CCHHHCCHHHHHHCC	62.51	-
506	Phosphorylation	QKNFNNLYGTKGNYT CHHHHHHCCCCCCCC	25.52	25394399
508	Phosphorylation	NFNNLYGTKGNYTSR HHHHHCCCCCCCCHH	23.40	26356563
509	Methylation	FNNLYGTKGNYTSRV HHHHCCCCCCCCHHC	40.57	115979505
509	Ubiquitination	FNNLYGTKGNYTSRV HHHHCCCCCCCCHHC	40.57	-
512	Phosphorylation	LYGTKGNYTSRVWEY HCCCCCCCCHHCEEE	18.11	25072903
513	Phosphorylation	YGTKGNYTSRVWEYS CCCCCCCCHHCEEEC	17.66	25072903
514	Phosphorylation	GTKGNYTSRVWEYSS CCCCCCCHHCEEECC	17.93	25072903
536	Phosphorylation	DLPVVQGSSSFSLKG CCCEEECCCCCCCCC	13.01	23090842
537	Phosphorylation	LPVVQGSSSFSLKGY CCEEECCCCCCCCCC	42.08	23090842
538	Phosphorylation	PVVQGSSSFSLKGYP CEEECCCCCCCCCCH	22.13	23090842
540	Phosphorylation	VQGSSSFSLKGYPSL EECCCCCCCCCCHHH	30.99	25056879
544	Phosphorylation	SSFSLKGYPSLMRSQ CCCCCCCCHHHHHCC	6.51	23090842
546	Phosphorylation	FSLKGYPSLMRSQSP CCCCCCHHHHHCCCC	26.72	24719451
550	Phosphorylation	GYPSLMRSQSPKAQP CCHHHHHCCCCCCCC	22.50	24732914
552	Phosphorylation	PSLMRSQSPKAQPQT HHHHHCCCCCCCCCC	29.61	24732914
554	Acetylation	LMRSQSPKAQPQTWK HHHCCCCCCCCCCCC	65.97	20368352
554	Ubiquitination	LMRSQSPKAQPQTWK HHHCCCCCCCCCCCC	65.97	-
561	Methylation	KAQPQTWKSGKQTML CCCCCCCCCCCCHHH	53.36	115979513
561	Ubiquitination	KAQPQTWKSGKQTML CCCCCCCCCCCCHHH	53.36	-
564	Ubiquitination	PQTWKSGKQTMLSHY CCCCCCCCCHHHHHC	50.08	-
566	Phosphorylation	TWKSGKQTMLSHYRP CCCCCCCHHHHHCCC	24.46	24719451
571	Phosphorylation	KQTMLSHYRPFYVNK CCHHHHHCCCEEEEC	19.33	23917254
575	Phosphorylation	LSHYRPFYVNKGNGI HHHCCCEEEECCCCC	13.04	26356563
584	Phosphorylation	NKGNGIGSNEAP--- ECCCCCCCCCCC---	29.58	24719451

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
550	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
552	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRI29_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 TRI29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EFC4B_HUMAN	CRACR2A	physical	16189514
TSG10_HUMAN	TSGA10	physical	16189514
LZTS2_HUMAN	LZTS2	physical	16189514
GCC1_HUMAN	GCC1	physical	16189514
CEP70_HUMAN	CEP70	physical	16189514
FBF1_HUMAN	FBF1	physical	16189514
TRI29_HUMAN	TRIM29	physical	16189514
TRI29_HUMAN	TRIM29	physical	11331580
TRI23_HUMAN	TRIM23	physical	11331580
TRIM1_HUMAN	MID2	physical	11331580
TRI11_HUMAN	TRIM11	physical	11331580
TRI27_HUMAN	TRIM27	physical	11331580
TX1B3_HUMAN	TAX1BP3	physical	20211142
FXL19_HUMAN	FBXL19	physical	20211142
KAT5_HUMAN	KAT5	physical	21463657
CARD9_HUMAN	CARD9	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
GOGA2_HUMAN	GOLGA2	physical	21516116
PYR1_HUMAN	CAD	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
DCTN1_HUMAN	DCTN1	physical	26496610
TRI27_HUMAN	TRIM27	physical	26496610
SC16A_HUMAN	SEC16A	physical	26496610
SYNE1_HUMAN	SYNE1	physical	26496610
SACS_HUMAN	SACS	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
MIC19_HUMAN	CHCHD3	physical	26496610
ACTL8_HUMAN	ACTL8	physical	26496610
KLH13_HUMAN	KLHL13	physical	26496610
TBB5_HUMAN	TUBB	physical	26496610
H12_HUMAN	HIST1H1C	physical	26381412
YBOX3_HUMAN	YBX3	physical	26381412
PHB2_HUMAN	PHB2	physical	26381412
RNF8_HUMAN	RNF8	physical	26381412
VIME_HUMAN	VIM	physical	26381412
RL13_HUMAN	RPL13	physical	26381412
RS19_HUMAN	RPS19	physical	26381412
BASP1_HUMAN	BASP1	physical	26381412
GRP78_HUMAN	HSPA5	physical	26381412
RS4X_HUMAN	RPS4X	physical	26381412
RS18_HUMAN	RPS18	physical	26381412
H1X_HUMAN	H1FX	physical	26381412
PAIRB_HUMAN	SERBP1	physical	26381412
RS10_HUMAN	RPS10	physical	26381412
C1QBP_HUMAN	C1QBP	physical	26381412
HMGA1_HUMAN	HMGA1	physical	26381412
MARCS_HUMAN	MARCKS	physical	26381412
HNRPU_HUMAN	HNRNPU	physical	26381412
RL26_HUMAN	RPL26	physical	26381412
EF1A1_HUMAN	EEF1A1	physical	26381412
PARP1_HUMAN	PARP1	physical	26381412
RUVB2_HUMAN	RUVBL2	physical	26381412
H10_MOUSE	H1f0	physical	26381412
DVL2_HUMAN	DVL2	physical	24469230
NEMO_HUMAN	IKBKG	physical	27695001
UB2R1_HUMAN	CDC34	physical	27695001
UB2E1_HUMAN	UBE2E1	physical	27695001
UBE2C_HUMAN	UBE2C	physical	27695001

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 TRI29_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-21; SER-104; THR-476 ANDSER-489, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-21; SER-23 AND SER-104,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-489, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-106 AND TYR-474, ANDMASS SPECTROMETRY.	19534553 [Abstract]