dbPTM

TAB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAB3_HUMAN
UniProt AC	Q8N5C8
Protein Name	TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
Gene Name	TAB3
Organism	Homo sapiens (Human).
Sequence Length	712
Subcellular Localization
Protein Description	Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator of MAP3K7 activation, respectively in the IL1 and TNF signaling pathways. Plays a role in activation of NF-kappa-B and AP1 transcription factor. Isoform 2 may be an oncogenic factor..
Protein Sequence	MAQSSPQLDIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQESSKYLYMEYHSPDDNRMNRNRLLHINLGIHSPSSYHPGDGAQLNGGRTLVHSSSDGHIDPQHAAGKQLICLVQEPHSAPAVVAATPNYNPFFMNEQNRSAATPPSQPPQQPSSMQTGMNPSAMQGPSPPPPPPSYMHIPRYSTNPITVTVSQNLPSGQTVPRALQILPQIPSNLYGSPGSIYIRQTSQSSSGRQTPQSTPWQSSPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQSAYHSPPPSQCPSPFSSPQHQVQPSQLGHIFMPPSPSTTPPHPYQQGPPSYQKQGSHSVAYLPYTASSLSKGSMKKIEITVEPSQRPGTAINRSPSPISNQPSPRNQHSLYTATTPPSSSPSRGISSQPKPPFSVNPVYITYTQPTGPSCTPSPSPRVIPNPTTVFKITVGRATTENLLNLVDQEERSAAPEPIQPISVIPGSGGEKGSHKYQRSSSSGSDDYAYTQALLLHQRARMERLAKQLKLEKEELERLKSEVNGMEHDLMQRRLRRVSCTTAIPTPEEMTRLRSMNRQLQINVDCTLKEVDLLQSRGNFDPKAMNNFYDNIEPGPVVPPKPSKKDSSDPCTIERKARRISVTSKVQADIHDTQAAAADEHRTGSTQSPRTQPRDEDYEGAPWNCDSCTFLNHPALNRCEQCEMPRYT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQSSPQLD ------CCCCCCCHH	20.26	20068231
4	Phosphorylation	----MAQSSPQLDIQ ----CCCCCCCHHHH	34.15	28450419
5	Phosphorylation	---MAQSSPQLDIQV ---CCCCCCCHHHHH	12.46	25159151
53	Phosphorylation	LSQESSKYLYMEYHS HHHHHHHHEEEEECC	12.66	28796482
55	Phosphorylation	QESSKYLYMEYHSPD HHHHHHEEEEECCCC	5.70	28796482
58	Phosphorylation	SKYLYMEYHSPDDNR HHHEEEEECCCCCCC	7.35	28796482
60	Phosphorylation	YLYMEYHSPDDNRMN HEEEEECCCCCCCCC	29.17	25159151
80	Phosphorylation	HINLGIHSPSSYHPG EEEECCCCCCCCCCC	25.26	28450419
82	Phosphorylation	NLGIHSPSSYHPGDG EECCCCCCCCCCCCC	46.69	28450419
83	Phosphorylation	LGIHSPSSYHPGDGA ECCCCCCCCCCCCCC	30.74	28450419
84	Phosphorylation	GIHSPSSYHPGDGAQ CCCCCCCCCCCCCCC	19.17	28450419
97	Phosphorylation	AQLNGGRTLVHSSSD CCCCCCCEEEECCCC	36.09	23898821
101	Phosphorylation	GGRTLVHSSSDGHID CCCEEEECCCCCCCC	24.86	23401153
102	Phosphorylation	GRTLVHSSSDGHIDP CCEEEECCCCCCCCH	19.99	25159151
103	Phosphorylation	RTLVHSSSDGHIDPQ CEEEECCCCCCCCHH	51.10	25159151
126	Phosphorylation	CLVQEPHSAPAVVAA EEEECCCCCCEEEEE	46.81	26657352
134	Phosphorylation	APAVVAATPNYNPFF CCEEEEECCCCCCCC	11.43	28450419
137	Phosphorylation	VVAATPNYNPFFMNE EEEECCCCCCCCCCC	25.97	23898821
221	Phosphorylation	QILPQIPSNLYGSPG HHHCCCCCCCCCCCC	40.89	28122231
224	Phosphorylation	PQIPSNLYGSPGSIY CCCCCCCCCCCCEEE	21.58	22199227
226	Phosphorylation	IPSNLYGSPGSIYIR CCCCCCCCCCEEEEE	16.72	22199227
229	Phosphorylation	NLYGSPGSIYIRQTS CCCCCCCEEEEEECC	18.66	22199227
235	O-linked_Glycosylation	GSIYIRQTSQSSSGR CEEEEEECCCCCCCC	20.91	27009840
238	O-linked_Glycosylation	YIRQTSQSSSGRQTP EEEECCCCCCCCCCC	26.66	27009840
264	Methylation	PVPHYSQRPLPVYPH CCCCCCCCCCCCCCC	28.87	115918101
283	Methylation	QPSQYSPKQQQIPQS CCCCCCCCHHCCCCH	55.59	115918097
345	Phosphorylation	PSYQKQGSHSVAYLP CCCCCCCCCEEEECC	15.30	25072903
347	Phosphorylation	YQKQGSHSVAYLPYT CCCCCCCEEEECCCC	15.33	25072903
350	Phosphorylation	QGSHSVAYLPYTASS CCCCEEEECCCCHHH	13.17	25072903
353	Phosphorylation	HSVAYLPYTASSLSK CEEEECCCCHHHCCC	16.61	25072903
354	Phosphorylation	SVAYLPYTASSLSKG EEEECCCCHHHCCCC	20.37	25159151
356	Phosphorylation	AYLPYTASSLSKGSM EECCCCHHHCCCCCC	24.82	25159151
357	Phosphorylation	YLPYTASSLSKGSMK ECCCCHHHCCCCCCE	33.91	25072903
359	Phosphorylation	PYTASSLSKGSMKKI CCCHHHCCCCCCEEE	36.60	25072903
362	Phosphorylation	ASSLSKGSMKKIEIT HHHCCCCCCEEEEEE	31.03	25072903
385	Phosphorylation	TAINRSPSPISNQPS CCCCCCCCCCCCCCC	35.79	33259812
388	Phosphorylation	NRSPSPISNQPSPRN CCCCCCCCCCCCCCC	32.56	30576142
398	Phosphorylation	PSPRNQHSLYTATTP CCCCCCCCCEEECCC	17.20	22199227
400	Phosphorylation	PRNQHSLYTATTPPS CCCCCCCEEECCCCC	9.42	23186163
401	Phosphorylation	RNQHSLYTATTPPSS CCCCCCEEECCCCCC	23.87	22199227
403	Phosphorylation	QHSLYTATTPPSSSP CCCCEEECCCCCCCC	31.84	22199227
404	Phosphorylation	HSLYTATTPPSSSPS CCCEEECCCCCCCCC	30.64	23186163
407	Phosphorylation	YTATTPPSSSPSRGI EEECCCCCCCCCCCC	44.65	22199227
408	Phosphorylation	TATTPPSSSPSRGIS EECCCCCCCCCCCCC	52.63	30576142
408	O-linked_Glycosylation	TATTPPSSSPSRGIS EECCCCCCCCCCCCC	52.63	27009840
409	Phosphorylation	ATTPPSSSPSRGISS ECCCCCCCCCCCCCC	31.09	22199227
411	Phosphorylation	TPPSSSPSRGISSQP CCCCCCCCCCCCCCC	45.12	22199227
411	O-linked_Glycosylation	TPPSSSPSRGISSQP CCCCCCCCCCCCCCC	45.12	27009840
415	Phosphorylation	SSPSRGISSQPKPPF CCCCCCCCCCCCCCC	26.24	30576142
428	Phosphorylation	PFSVNPVYITYTQPT CCCCCCEEEEEECCC	6.71	27642862
431	Phosphorylation	VNPVYITYTQPTGPS CCCEEEEEECCCCCC	8.20	27642862
432	Phosphorylation	NPVYITYTQPTGPSC CCEEEEEECCCCCCC	21.30	28270605
435	Phosphorylation	YITYTQPTGPSCTPS EEEEECCCCCCCCCC	52.48	28270605
438	Phosphorylation	YTQPTGPSCTPSPSP EECCCCCCCCCCCCC	31.78	28270605
440	Phosphorylation	QPTGPSCTPSPSPRV CCCCCCCCCCCCCCC	31.01	28270605
442	Phosphorylation	TGPSCTPSPSPRVIP CCCCCCCCCCCCCCC	21.62	28270605
444	Phosphorylation	PSCTPSPSPRVIPNP CCCCCCCCCCCCCCC	29.67	28270605
492	Phosphorylation	PISVIPGSGGEKGSH CCEEECCCCCCCCCC	37.97	25159151
504	Phosphorylation	GSHKYQRSSSSGSDD CCCCCCCCCCCCCCH	21.03	23898821
505	Phosphorylation	SHKYQRSSSSGSDDY CCCCCCCCCCCCCHH	30.61	21712546
506	Phosphorylation	HKYQRSSSSGSDDYA CCCCCCCCCCCCHHH	39.71	23401153
507	Phosphorylation	KYQRSSSSGSDDYAY CCCCCCCCCCCHHHH	44.24	21712546
509	Phosphorylation	QRSSSSGSDDYAYTQ CCCCCCCCCHHHHHH	29.29	21712546
512	Phosphorylation	SSSGSDDYAYTQALL CCCCCCHHHHHHHHH	13.39	23898821
514	Phosphorylation	SGSDDYAYTQALLLH CCCCHHHHHHHHHHH	7.99	30108239
515	Phosphorylation	GSDDYAYTQALLLHQ CCCHHHHHHHHHHHH	10.13	30108239
563	Phosphorylation	QRRLRRVSCTTAIPT HHHHHHHCCCCCCCC	12.16	23312004
565	Phosphorylation	RLRRVSCTTAIPTPE HHHHHCCCCCCCCHH	16.26	23312004
566	Phosphorylation	LRRVSCTTAIPTPEE HHHHCCCCCCCCHHH	27.24	23312004
570	Phosphorylation	SCTTAIPTPEEMTRL CCCCCCCCHHHHHHH	36.90	29759185
575	Phosphorylation	IPTPEEMTRLRSMNR CCCHHHHHHHHHHHH	29.81	29759185
608 (in isoform 2)	Phosphorylation	-	16.01	25056879
613	Phosphorylation	PKAMNNFYDNIEPGP HHHHHHCCCCCCCCC	15.37	24719451
627	Phosphorylation	PVVPPKPSKKDSSDP CCCCCCCCCCCCCCC	59.47	24719451
631	Phosphorylation	PKPSKKDSSDPCTIE CCCCCCCCCCCCCHH	45.58	28270605
632	Phosphorylation	KPSKKDSSDPCTIER CCCCCCCCCCCCHHH	56.56	28270605
636	Phosphorylation	KDSSDPCTIERKARR CCCCCCCCHHHHHHH	31.12	30576142
645	Phosphorylation	ERKARRISVTSKVQA HHHHHHEECCEEEEC	19.96	28102081
647	Phosphorylation	KARRISVTSKVQADI HHHHEECCEEEECCC	18.95	20068231
648	Phosphorylation	ARRISVTSKVQADIH HHHEECCEEEECCCC	28.77	20068231
657	Phosphorylation	VQADIHDTQAAAADE EECCCCCHHHHHHHC	13.12	23312004
667	Phosphorylation	AAADEHRTGSTQSPR HHHHCCCCCCCCCCC	37.07	30624053
667	O-linked_Glycosylation	AAADEHRTGSTQSPR HHHHCCCCCCCCCCC	37.07	27009840
669	Phosphorylation	ADEHRTGSTQSPRTQ HHCCCCCCCCCCCCC	23.74	30624053
670	Phosphorylation	DEHRTGSTQSPRTQP HCCCCCCCCCCCCCC	34.12	27251275
672	O-linked_Glycosylation	HRTGSTQSPRTQPRD CCCCCCCCCCCCCCC	19.21	27009840
672	Phosphorylation	HRTGSTQSPRTQPRD CCCCCCCCCCCCCCC	19.21	27251275

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
60	S	Phosphorylation	Kinase	P38A	P47811	PSP
404	T	Phosphorylation	Kinase	P38A	P47811	PSP
506	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
506	S	Phosphorylation	Kinase	MAPKAPK3	Q16644	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	RBCK1	Q9BYM8	PMID:17449468

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
506	S	Phosphorylation		18021073
Phosphorylated at Ser-506 by MAPKAPK2 and MAPKAPK3 following IL1 treatment.

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 TAB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
M3K7_HUMAN	MAP3K7	physical	14670075
TAB1_HUMAN	TAB1	physical	14670075
TAB2_HUMAN	TAB2	physical	14633987
M3K7_HUMAN	MAP3K7	physical	14633987
TAB3_HUMAN	TAB3	physical	14633987
TRAF6_HUMAN	TRAF6	physical	14633987
TRAF2_HUMAN	TRAF2	physical	14633987
TAB1_HUMAN	TAB1	physical	21903422
TAB2_HUMAN	TAB2	physical	21903422
M3K7_HUMAN	MAP3K7	physical	21903422
M3K7_HUMAN	MAP3K7	physical	18021073
TAB1_HUMAN	TAB1	physical	18021073
TR30A_MOUSE	Trim30a	physical	18345001
BECN1_HUMAN	BECN1	physical	22081109
M3K7_HUMAN	MAP3K7	physical	22081109
UBC_HUMAN	UBC	physical	19927120
UBC_HUMAN	UBC	physical	15327770
TRAF6_HUMAN	TRAF6	physical	15327770
NEMO_HUMAN	IKBKG	physical	15327770
SMAD7_HUMAN	SMAD7	physical	17384642
M3K7_HUMAN	MAP3K7	physical	17384642
BECN1_HUMAN	BECN1	physical	21976705
ATG5_HUMAN	ATG5	physical	21976705
ATG13_HUMAN	ATG13	physical	21976705
WDR34_HUMAN	WDR34	physical	19521662
TRI38_HUMAN	TRIM38	physical	24434549
CE57L_HUMAN	CEP57L1	physical	25416956
PTPA_MYCTU	ptpA	physical	25642820
UBC_HUMAN	UBC	physical	25642820
RNF4_HUMAN	RNF4	physical	26299341
PBIP1_HUMAN	PBXIP1	physical	24488098
M3K7_HUMAN	MAP3K7	physical	27497262
IKKB_HUMAN	IKBKB	physical	27497262
TRAF6_HUMAN	TRAF6	physical	27497262
CAR11_HUMAN	CARD11	physical	27497262

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 TAB3_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-60; THR-404; SER-408 ANDSER-492, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Roles for TAB1 in regulating the IL-1-dependent phosphorylation ofthe TAB3 regulatory subunit and activity of the TAK1 complex."; Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N.,Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L.,Ghosh S., Cohen P.; Biochem. J. 409:711-722(2008). Cited for: PHOSPHORYLATION AT SER-506.	18021073 [Abstract]

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