dbPTM

M3K7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	M3K7_HUMAN
UniProt AC	O43318
Protein Name	Mitogen-activated protein kinase kinase kinase 7
Gene Name	MAP3K7
Organism	Homo sapiens (Human).
Sequence Length	606
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein Cytoplasmic side . Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane.
Protein Description	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity..
Protein Sequence	MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Ubiquitination	APSQVLNFEEIDYKE CCHHEECHHHCCCCE	8.56	22817900
63	Ubiquitination	RAKDVAIKQIESESE HHHHEEEHHCCCHHH	35.17	24816145
67	Phosphorylation	VAIKQIESESERKAF EEEHHCCCHHHHHHH	48.31	20068231
69	Phosphorylation	IKQIESESERKAFIV EHHCCCHHHHHHHHH	52.56	20068231
69 (in isoform 2)	Phosphorylation	-	52.56	-
69 (in isoform 3)	Phosphorylation	-	52.56	-
69 (in isoform 4)	Phosphorylation	-	52.56	-
72	Ubiquitination	IESESERKAFIVELR CCCHHHHHHHHHHHH	43.53	-
79	Ubiquitination	KAFIVELRQLSRVNH HHHHHHHHHHHCCCC	23.14	22817900
158	Ubiquitination	ALIHRDLKPPNLLLV EEECCCCCCCCEEEE	63.82	22817900
169	Phosphorylation	LLLVAGGTVLKICDF EEEEECCEEEEECCC	23.03	28258704
178	Phosphorylation	LKICDFGTACDIQTH EEECCCCCCCEEEHH	24.89	22817900
184	Acetylation	GTACDIQTHMTNNKG CCCCEEEHHCCCCCC	17.59	22802624
184	Phosphorylation	GTACDIQTHMTNNKG CCCCEEEHHCCCCCC	17.59	22817900
184 (in isoform 2)	Phosphorylation	-	17.59	-
184 (in isoform 3)	Phosphorylation	-	17.59	-
184 (in isoform 4)	Phosphorylation	-	17.59	-
187	Acetylation	CDIQTHMTNNKGSAA CEEEHHCCCCCCCCE	28.21	22802624
187	Phosphorylation	CDIQTHMTNNKGSAA CEEEHHCCCCCCCCE	28.21	21512573
187 (in isoform 2)	Phosphorylation	-	28.21	-
187 (in isoform 3)	Phosphorylation	-	28.21	-
187 (in isoform 4)	Phosphorylation	-	28.21	-
192	Phosphorylation	HMTNNKGSAAWMAPE HCCCCCCCCEEECCC	19.20	15590691
192 (in isoform 2)	Phosphorylation	-	19.20	-
192 (in isoform 3)	Phosphorylation	-	19.20	-
192 (in isoform 4)	Phosphorylation	-	19.20	-
206	Phosphorylation	EVFEGSNYSEKCDVF CHHCCCCCHHCCCHH	21.65	-
209	Ubiquitination	EGSNYSEKCDVFSWG CCCCCHHCCCHHHHH	29.78	22817900
216	Ubiquitination	KCDVFSWGIILWEVI CCCHHHHHHHHHHHH	8.89	22817900
221	Ubiquitination	SWGIILWEVITRRKP HHHHHHHHHHHCCCC	22.16	22817900
228	Ubiquitination	EVITRRKPFDEIGGP HHHHCCCCCCCCCCH	39.86	24816145
269	Ubiquitination	LMTRCWSKDPSQRPS HHHHHHCCCHHHCCC	49.51	29967540
304	Phosphorylation	PLQYPCQYSDEGQSN CCCCCCCCCCCCCCC	25.47	28348404
305	Phosphorylation	LQYPCQYSDEGQSNS CCCCCCCCCCCCCCC	11.87	28348404
310	Phosphorylation	QYSDEGQSNSATSTG CCCCCCCCCCCCCCC	43.54	28348404
312	Phosphorylation	SDEGQSNSATSTGSF CCCCCCCCCCCCCCE	37.86	28348404
314	Phosphorylation	EGQSNSATSTGSFMD CCCCCCCCCCCCEEC	27.00	28348404
315	Phosphorylation	GQSNSATSTGSFMDI CCCCCCCCCCCEECH	30.41	28348404
316	Phosphorylation	QSNSATSTGSFMDIA CCCCCCCCCCEECHH	32.27	28348404
318	Phosphorylation	NSATSTGSFMDIAST CCCCCCCCEECHHCC	19.93	28348404
331	Phosphorylation	STNTSNKSDTNMEQV CCCCCCCCCCCHHHC	54.65	25849741
333	Phosphorylation	NTSNKSDTNMEQVPA CCCCCCCCCHHHCCC	43.48	25849741
335	Sulfoxidation	SNKSDTNMEQVPATN CCCCCCCHHHCCCCH	4.07	21406390
341	Acetylation	NMEQVPATNDTIKRL CHHHCCCCHHHHHHH	27.79	22520462
341	Phosphorylation	NMEQVPATNDTIKRL CHHHCCCCHHHHHHH	27.79	30576142
344	Phosphorylation	QVPATNDTIKRLESK HCCCCHHHHHHHHHH	30.39	30576142
346	Ubiquitination	PATNDTIKRLESKLL CCCHHHHHHHHHHHH	53.69	21906983
346 (in isoform 1)	Ubiquitination	-	53.69	21890473
346 (in isoform 2)	Ubiquitination	-	53.69	21890473
346 (in isoform 3)	Ubiquitination	-	53.69	21906983
351	Ubiquitination	TIKRLESKLLKNQAK HHHHHHHHHHHHHHH	48.76	22817900
354	Ubiquitination	RLESKLLKNQAKQQS HHHHHHHHHHHHHHC	58.41	-
358	Ubiquitination	KLLKNQAKQQSESGR HHHHHHHHHHCCCCC	38.82	24816145
361	Phosphorylation	KNQAKQQSESGRLSL HHHHHHHCCCCCCCC	31.10	30266825
363	Phosphorylation	QAKQQSESGRLSLGA HHHHHCCCCCCCCCC	34.16	30266825
367	Phosphorylation	QSESGRLSLGASRGS HCCCCCCCCCCCCCC	24.32	30266825
371	Phosphorylation	GRLSLGASRGSSVES CCCCCCCCCCCCCCC	35.06	30266825
374	Phosphorylation	SLGASRGSSVESLPP CCCCCCCCCCCCCCC	30.05	28450419
375	Phosphorylation	LGASRGSSVESLPPT CCCCCCCCCCCCCCC	32.50	25159151
378	Phosphorylation	SRGSSVESLPPTSEG CCCCCCCCCCCCCCC	43.98	28450419
382	Phosphorylation	SVESLPPTSEGKRMS CCCCCCCCCCCCCCC	37.15	23090842
383	O-linked_Glycosylation	VESLPPTSEGKRMSA CCCCCCCCCCCCCCC	50.56	30059200
383	Phosphorylation	VESLPPTSEGKRMSA CCCCCCCCCCCCCCC	50.56	23090842
386	Acetylation	LPPTSEGKRMSADMS CCCCCCCCCCCCCHH	40.66	30592829
389	Phosphorylation	TSEGKRMSADMSEIE CCCCCCCCCCHHHHH	25.75	29255136
389 (in isoform 2)	Phosphorylation	-	25.75	25849741
389 (in isoform 3)	Phosphorylation	-	25.75	-
389 (in isoform 4)	Phosphorylation	-	25.75	25849741
393	Phosphorylation	KRMSADMSEIEARIA CCCCCCHHHHHHHHH	35.65	23927012
393 (in isoform 2)	Phosphorylation	-	35.65	23322592
393 (in isoform 4)	Phosphorylation	-	35.65	23322592
402	Phosphorylation	IEARIAATTAYSKPK HHHHHHHHHCCCCCC	11.70	28258704
402	Ubiquitination	IEARIAATTAYSKPK HHHHHHHHHCCCCCC	11.70	24816145
402 (in isoform 2)	Phosphorylation	-	11.70	23322592
402 (in isoform 4)	Phosphorylation	-	11.70	23322592
403	Phosphorylation	EARIAATTAYSKPKR HHHHHHHHCCCCCCC	20.90	28258704
403 (in isoform 3)	Phosphorylation	-	20.90	-
405	Phosphorylation	RIAATTAYSKPKRGH HHHHHHCCCCCCCCC	18.35	28152594
406	Phosphorylation	IAATTAYSKPKRGHR HHHHHCCCCCCCCCC	39.76	28152594
406 (in isoform 3)	Phosphorylation	-	39.76	-
412	Phosphorylation	YSKPKRGHRKTASFG CCCCCCCCCCCCCCC	31.90	32142685
412 (in isoform 2)	Phosphorylation	-	31.90	25849741
412 (in isoform 4)	Phosphorylation	-	31.90	25849741
415	Phosphorylation	PKRGHRKTASFGNIL CCCCCCCCCCCCCCC	27.73	30278072
417	Phosphorylation	RGHRKTASFGNILDV CCCCCCCCCCCCCCC	38.63	30278072
417 (in isoform 2)	Phosphorylation	-	38.63	25849741
417 (in isoform 4)	Phosphorylation	-	38.63	25849741
419 (in isoform 2)	Phosphorylation	-	20.13	-
419 (in isoform 4)	Phosphorylation	-	20.13	-
427	Phosphorylation	NILDVPEIVISGNGQ CCCCCCEEEECCCCC	2.46	32142685
427 (in isoform 2)	Phosphorylation	-	2.46	-
427 (in isoform 4)	Phosphorylation	-	2.46	-
428 (in isoform 2)	Phosphorylation	-	2.44	-
428 (in isoform 4)	Phosphorylation	-	2.44	-
429	Ubiquitination	LDVPEIVISGNGQPR CCCCEEEECCCCCCC	5.54	24816145
430	Phosphorylation	DVPEIVISGNGQPRR CCCEEEECCCCCCCC	18.47	23186163
432	Ubiquitination	PEIVISGNGQPRRRS CEEEECCCCCCCCCC	38.85	23000965
433	Ubiquitination	EIVISGNGQPRRRSI EEEECCCCCCCCCCE	42.25	21890473
439	Phosphorylation	NGQPRRRSIQDLTVT CCCCCCCCEEEEEEE	23.84	19664994
439 (in isoform 3)	Phosphorylation	-	23.84	-
444	Acetylation	RRSIQDLTVTGTEPG CCCEEEEEEECCCCC	25.06	22520462
444	Phosphorylation	RRSIQDLTVTGTEPG CCCEEEEEEECCCCC	25.06	29255136
446	Acetylation	SIQDLTVTGTEPGQV CEEEEEEECCCCCCC	32.90	22520462
446	Phosphorylation	SIQDLTVTGTEPGQV CEEEEEEECCCCCCC	32.90	23927012
446 (in isoform 3)	Phosphorylation	-	32.90	-
447	Ubiquitination	IQDLTVTGTEPGQVS EEEEEEECCCCCCCC	24.60	29967540
448	Acetylation	QDLTVTGTEPGQVSS EEEEEECCCCCCCCC	29.64	22520462
448	O-linked_Glycosylation	QDLTVTGTEPGQVSS EEEEEECCCCCCCCC	29.64	30059200
448	Phosphorylation	QDLTVTGTEPGQVSS EEEEEECCCCCCCCC	29.64	23927012
454	Phosphorylation	GTEPGQVSSRSSSPS CCCCCCCCCCCCCCC	16.49	29255136
454 (in isoform 3)	Phosphorylation	-	16.49	-
455	Phosphorylation	TEPGQVSSRSSSPSV CCCCCCCCCCCCCCE	37.01	29255136
455 (in isoform 3)	Phosphorylation	-	37.01	-
457	Phosphorylation	PGQVSSRSSSPSVRM CCCCCCCCCCCCEEE	36.80	30576142
458	Phosphorylation	GQVSSRSSSPSVRMI CCCCCCCCCCCEEEE	45.20	28450419
459	Phosphorylation	QVSSRSSSPSVRMIT CCCCCCCCCCEEEEE	23.57	30576142
459	Ubiquitination	QVSSRSSSPSVRMIT CCCCCCCCCCEEEEE	23.57	23000965
460	Ubiquitination	VSSRSSSPSVRMITT CCCCCCCCCEEEEEC	38.50	21890473
461	Phosphorylation	SSRSSSPSVRMITTS CCCCCCCCEEEEECC	25.05	28450419
466	Phosphorylation	SPSVRMITTSGPTSE CCCEEEEECCCCCCC	12.93	23312004
467	Acetylation	PSVRMITTSGPTSEK CCEEEEECCCCCCCC	22.29	22520462
467	Phosphorylation	PSVRMITTSGPTSEK CCEEEEECCCCCCCC	22.29	23312004
468	Phosphorylation	SVRMITTSGPTSEKP CEEEEECCCCCCCCC	33.84	23312004
471	Phosphorylation	MITTSGPTSEKPTRS EEECCCCCCCCCCCC	53.71	28857561
472	Phosphorylation	ITTSGPTSEKPTRSH EECCCCCCCCCCCCC	46.91	25159151
474	Acetylation	TSGPTSEKPTRSHPW CCCCCCCCCCCCCCC	52.00	25953088
474	Ubiquitination	TSGPTSEKPTRSHPW CCCCCCCCCCCCCCC	52.00	29967540
476	Phosphorylation	GPTSEKPTRSHPWTP CCCCCCCCCCCCCCC	56.74	23312004
520	Ubiquitination	CPNSKESMAVFEQHC CCCCHHHHHHHHHHH	3.75	29967540
532	Ubiquitination	QHCKMAQEYMKVQTE HHHHHHHHHHHHHHH	37.75	24816145
538	Phosphorylation	QEYMKVQTEIALLLQ HHHHHHHHHHHHHHH	32.14	-
547	Ubiquitination	IALLLQRKQELVAEL HHHHHHHHHHHHHHH	34.85	29967540
552	Ubiquitination	QRKQELVAELDQDEK HHHHHHHHHHCCCHH	25.02	32015554
559	Ubiquitination	AELDQDEKDQQNTSR HHHCCCHHHHHHHHH	69.95	24816145
562	Ubiquitination	DQDEKDQQNTSRLVQ CCCHHHHHHHHHHHH	66.36	23000965
563	Ubiquitination	QDEKDQQNTSRLVQE CCHHHHHHHHHHHHH	34.10	23000965
563 (in isoform 2)	Ubiquitination	-	34.10	21890473
572	2-Hydroxyisobutyrylation	SRLVQEHKKLLDENK HHHHHHHHHHHHHCC	44.35	-
573	Acetylation	RLVQEHKKLLDENKS HHHHHHHHHHHHCCC	57.07	7662889
579	Ubiquitination	KKLLDENKSLSTYYQ HHHHHHCCCHHHHHH	51.21	32015554
584	Phosphorylation	ENKSLSTYYQQCKKQ HCCCHHHHHHHHHHH	8.90	-
585	Phosphorylation	NKSLSTYYQQCKKQL CCCHHHHHHHHHHHH	7.69	-
589	Ubiquitination	STYYQQCKKQLEVIR HHHHHHHHHHHHHHH	38.94	23000965
590	Ubiquitination	TYYQQCKKQLEVIRS HHHHHHHHHHHHHHH	68.68	23000965
590 (in isoform 1)	Ubiquitination	-	68.68	21890473

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
178	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS
184	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS
187	T	Phosphorylation	Kinase	M3K7	O43318	PhosphoELM
187	T	Phosphorylation	Kinase	MAP3K7	Q62073	GPS
192	S	Phosphorylation	Kinase	MAP3K7	O43318	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM8	Q9BZR9	PMID:22084099
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF3	Q13114	PMID:26882989
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:15492226
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
63	K	Phosphorylation	12589052
Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7.
63	K	ubiquitylation	12589052
Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7.
72	K	ubiquitylation	22406003
'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation.
184	T	Acetylation	10838074
(Microbial infection) Acetylation of Thr-184 and Thr-187 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.
184	T	Phosphorylation	10838074
(Microbial infection) Acetylation of Thr-184 and Thr-187 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.
187	T	Acetylation	10838074
(Microbial infection) Acetylation of Thr-184 and Thr-187 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.
187	T	Phosphorylation	10838074
(Microbial infection) Acetylation of Thr-184 and Thr-187 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway.
187	T	Phosphorylation	10838074
Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation.
192	S	Phosphorylation	10838074
Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation.
192	S	Phosphorylation	10838074
Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation.

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 M3K7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAB1_HUMAN	TAB1	physical	14670075
TAB2_HUMAN	TAB2	physical	14670075
TAB3_HUMAN	TAB3	physical	14670075
TAB3_HUMAN	TAB3	physical	14633987
MP2K6_HUMAN	MAP2K6	physical	14633987
IKKA_HUMAN	CHUK	physical	10187861
MP2K6_HUMAN	MAP2K6	physical	11460167
M3K7_HUMAN	MAP3K7	physical	9556573
SMAD6_HUMAN	SMAD6	physical	10748100
XIAP_HUMAN	XIAP	physical	12048196
STRAB_HUMAN	STRADB	physical	12048196
HGS_HUMAN	HGS	physical	11397816
TRAF6_HUMAN	TRAF6	physical	11259596
TAB1_HUMAN	TAB1	genetic	10094049
TAB2_HUMAN	TAB2	physical	11259596
MP2K6_HUMAN	MAP2K6	physical	10094049
TRAF6_HUMAN	TRAF6	physical	10921914
M3K5_HUMAN	MAP3K5	physical	10921914
TAB1_HUMAN	TAB1	physical	10838074
MP2K6_HUMAN	MAP2K6	physical	10838074
CYLD_HUMAN	CYLD	physical	18332137
CSN5_HUMAN	COPS5	physical	20936779
HIPK2_HUMAN	HIPK2	physical	15082531
TRAF6_HUMAN	TRAF6	physical	14633987
TAB2_HUMAN	TAB2	physical	14633987
TRAF2_HUMAN	TRAF2	physical	14633987
NEMO_HUMAN	IKBKG	physical	19531477
M3K7_HUMAN	MAP3K7	physical	9742107
IKKA_HUMAN	CHUK	physical	9742107
MIB2_HUMAN	MIB2	physical	21896478
MP2K6_HUMAN	MAP2K6	physical	20932476
IKKB_HUMAN	IKBKB	physical	20932476
RB6I2_HUMAN	ERC1	physical	20932476
PPP6_HUMAN	PPP6C	physical	19955178
TAB2_HUMAN	TAB2	physical	19955178
MP2K6_HUMAN	MAP2K6	physical	19675569
KPCT_HUMAN	PRKCQ	physical	20164171
FYB1_HUMAN	FYB	physical	20164171
CAR11_HUMAN	CARD11	physical	20164171
HS90A_HUMAN	HSP90AA1	physical	19026643
CDC37_HUMAN	CDC37	physical	19026643
TAB1_HUMAN	TAB1	physical	19026643
TAB2_HUMAN	TAB2	physical	19026643
IRAK1_HUMAN	IRAK1	physical	19026643
DAAM1_HUMAN	DAAM1	physical	21903422
TAB1_HUMAN	TAB1	physical	21903422
TAB2_HUMAN	TAB2	physical	21903422
TAB3_HUMAN	TAB3	physical	21903422
ZN593_HUMAN	ZNF593	physical	21900206
BBS10_HUMAN	BBS10	physical	21900206
RN19A_HUMAN	RNF19A	physical	21900206
PPP5_HUMAN	PPP5C	physical	21900206
RBX1_HUMAN	RBX1	physical	21900206
ZN746_HUMAN	ZNF746	physical	21900206
NDUS6_HUMAN	NDUFS6	physical	21900206
EZH2_HUMAN	EZH2	physical	21900206
E2AK2_HUMAN	EIF2AK2	physical	12609980
TAB2_HUMAN	TAB2	physical	12609980
TRAF6_HUMAN	TRAF6	physical	12609980
MP2K6_HUMAN	MAP2K6	physical	12609980
TR30A_MOUSE	Trim30a	physical	18345001
IKKA_HUMAN	CHUK	physical	20200282
TAB2_HUMAN	TAB2	physical	20200282
TAB1_HUMAN	TAB1	physical	20200282
MP2K6_HUMAN	MAP2K6	physical	15590691
TAB1_HUMAN	TAB1	physical	15590691
TAB1_HUMAN	TAB1	physical	18456659
IKKB_HUMAN	IKBKB	physical	18456659
NEMO_HUMAN	IKBKG	physical	21606198
RIPK1_HUMAN	RIPK1	physical	21606198
ATM_HUMAN	ATM	physical	21606198
XIAP_HUMAN	XIAP	physical	19584092
SIVA_HUMAN	SIVA1	physical	19584092
UBP4_HUMAN	USP4	physical	21331078
IKKB_HUMAN	IKBKB	physical	21331078
M3K5_HUMAN	MAP3K5	physical	22167179
TAB1_HUMAN	TAB1	physical	22167179
TAB2_HUMAN	TAB2	physical	22167179
TRAF6_HUMAN	TRAF6	physical	19843958
M3K3_HUMAN	MAP3K3	physical	19843958
IRAK1_HUMAN	IRAK1	physical	12242293
TRAF6_HUMAN	TRAF6	physical	12242293
TAB1_HUMAN	TAB1	physical	12242293
TAB2_HUMAN	TAB2	physical	12242293
MP2K6_HUMAN	MAP2K6	physical	12242293
TRIM8_HUMAN	TRIM8	physical	22084099
TRAF6_HUMAN	TRAF6	physical	22851693
MP2K6_HUMAN	MAP2K6	physical	17384642
TRAF5_HUMAN	TRAF5	physical	17384642
PELI3_HUMAN	PELI3	physical	12874243
MAVS_HUMAN	MAVS	physical	16153868
YETS2_HUMAN	YEATS2	physical	18838386
KAT2A_HUMAN	KAT2A	physical	18838386
TADA3_HUMAN	TADA3	physical	18838386
SGF29_HUMAN	CCDC101	physical	18838386
NC2B_HUMAN	DR1	physical	18838386
TAB1_HUMAN	TAB1	physical	8638164
TAB2_HUMAN	TAB2	physical	8638164
STAT3_HUMAN	STAT3	physical	15764709
MP2K6_HUMAN	MAP2K6	physical	15764709
TAB1_HUMAN	TAB1	physical	19232515
TAB2_HUMAN	TAB2	physical	19232515
TAB3_HUMAN	TAB3	physical	19232515
FBXW5_HUMAN	FBXW5	physical	19232515
TRAF6_HUMAN	TRAF6	physical	19232515
M3K7_HUMAN	MAP3K7	physical	19232515
ROR2_HUMAN	ROR2	physical	18762249
DAZP2_HUMAN	DAZAP2	physical	18762249
TAB1_HUMAN	TAB1	physical	20538596
TAB2_HUMAN	TAB2	physical	20538596
AAPK1_HUMAN	PRKAA1	physical	20538596
AAKB1_HUMAN	PRKAB1	physical	20538596
M3K7_HUMAN	MAP3K7	physical	20538596
TGFR2_HUMAN	TGFBR2	physical	19556242
TGFR1_HUMAN	TGFBR1	physical	19556242
TAB1_HUMAN	TAB1	physical	19556242
TAB2_HUMAN	TAB2	physical	19556242
IKKB_HUMAN	IKBKB	physical	18316610
CAR11_HUMAN	CARD11	physical	18625728
RIPK2_HUMAN	RIPK2	physical	17965022
TRAF6_HUMAN	TRAF6	physical	19521662
WDR34_HUMAN	WDR34	physical	19521662
BCL10_HUMAN	BCL10	physical	17189706
MP2K6_HUMAN	MAP2K6	physical	16893890
TAOK2_HUMAN	TAOK2	physical	16893890
TAOK1_HUMAN	TAOK1	physical	16893890
RIPK2_HUMAN	RIPK2	physical	17947236
MP2K6_HUMAN	MAP2K6	physical	17079228
PPP6_HUMAN	PPP6C	physical	17079228
PINK1_HUMAN	PINK1	physical	22643835
TRAF6_HUMAN	TRAF6	physical	22643835
BST2_HUMAN	BST2	physical	23221546
IRAK1_HUMAN	IRAK1	physical	23244239
NOD2_HUMAN	NOD2	physical	15075345
UBP2_HUMAN	USP2	physical	23264041
SKIL_HUMAN	SKIL	physical	17276978
TAB1_HUMAN	TAB1	physical	12429732
MP2K4_HUMAN	MAP2K4	physical	12429732
M3K3_HUMAN	MAP3K3	physical	16260783
PPM1L_HUMAN	PPM1L	physical	12556533
MP2K6_HUMAN	MAP2K6	physical	17363973
IKKB_HUMAN	IKBKB	physical	17363973
IKKB_HUMAN	IKBKB	physical	17363905
MP2K6_HUMAN	MAP2K6	physical	17363905
RIPK2_HUMAN	RIPK2	physical	17348859
TAB1_HUMAN	TAB1	physical	10702308
MP2K6_HUMAN	MAP2K6	physical	10702308
M3K7_HUMAN	MAP3K7	physical	10702308
IRAK1_HUMAN	IRAK1	physical	17197697
TRAF6_HUMAN	TRAF6	physical	16517750
SASH1_HUMAN	SASH1	physical	23776175
SIK3_HUMAN	SIK3	physical	24061540
TAB2_HUMAN	TAB2	physical	24061540
SIK1_HUMAN	SIK1	physical	24061540
IKKB_HUMAN	IKBKB	physical	24270572
MP2K6_HUMAN	MAP2K6	physical	23606331
M3K7_HUMAN	MAP3K7	physical	21817100
MAGD1_HUMAN	MAGED1	physical	24947323
IKBA_HUMAN	NFKBIA	physical	15327770
ECSIT_HUMAN	ECSIT	physical	25371197
TAB1_HUMAN	TAB1	physical	24912525
TAB2_HUMAN	TAB2	physical	24912525
TAB3_HUMAN	TAB3	physical	24912525
M3K14_HUMAN	MAP3K14	physical	10807933
NFIP1_HUMAN	NDFIP1	physical	25632008
ITCH_HUMAN	ITCH	physical	25632008
IKKA_HUMAN	CHUK	physical	25241761
CLH1_HUMAN	CLTC	physical	25241761
RUVB1_HUMAN	RUVBL1	physical	25241761
HS71L_HUMAN	HSPA1L	physical	25241761
NLK_HUMAN	NLK	physical	25241761
MP2K7_HUMAN	MAP2K7	physical	25241761
SMAD3_HUMAN	SMAD3	physical	25241761
TF65_HUMAN	RELA	physical	25241761
TAB1_HUMAN	TAB1	physical	25241761
I17RD_HUMAN	IL17RD	physical	23770285
PDPK1_HUMAN	PDPK1	physical	26432169
TAB1_HUMAN	TAB1	physical	26432169
TAB2_HUMAN	TAB2	physical	26432169
IKKB_HUMAN	IKBKB	physical	25946971
RNF4_HUMAN	RNF4	physical	26299341
UBP18_HUMAN	USP18	physical	26240016
RACK1_HUMAN	GNB2L1	physical	26038599
MP2K6_HUMAN	MAP2K6	physical	26038599
TRAF3_HUMAN	TRAF3	physical	26882989
MP2K6_HUMAN	MAP2K6	physical	23825189
AAPK1_HUMAN	PRKAA1	physical	20615388
M3K7_HUMAN	MAP3K7	physical	12624112
MP2K6_HUMAN	MAP2K6	physical	12624112
TAB1_HUMAN	TAB1	physical	12624112
CRBN_HUMAN	CRBN	physical	27468689
TAB1_HUMAN	TAB1	physical	27468689
TAB2_HUMAN	TAB2	physical	27468689
TRIM8_HUMAN	TRIM8	physical	27956576
TRIM8_HUMAN	TRIM8	physical	27981609
TRAF6_HUMAN	TRAF6	physical	27249171
M3K7_HUMAN	MAP3K7	physical	27497262
CAR11_HUMAN	CARD11	physical	27497262
IKKB_HUMAN	IKBKB	physical	26334375
UBP18_HUMAN	USP18	physical	28718215

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 M3K7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389; SER-439 ANDTHR-444, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-455, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-389 AND SER-439, ANDMASS 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-439, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASSSPECTROMETRY.	17081983 [Abstract]
"TAK1 mitogen-activated protein kinase kinase kinase is activated byautophosphorylation within its activation loop."; Kishimoto K., Matsumoto K., Ninomiya-Tsuji J.; J. Biol. Chem. 275:7359-7364(2000). Cited for: PHOSPHORYLATION AT SER-192, AND ENZYME REGULATION.	10702308 [Abstract]
"Phosphorylation-dependent activation of TAK1 mitogen-activatedprotein kinase kinase kinase by TAB1."; Sakurai H., Miyoshi H., Mizukami J., Sugita T.; FEBS Lett. 474:141-145(2000). Cited for: INTERACTION WITH TAB1, PHOSPHORYLATION AT THR-184; THR-187 ANDSER-192, AND ACTIVATION.	10838074 [Abstract]
"Protein phosphatase 6 down-regulates TAK1 kinase activation in theIL-1 signaling pathway."; Kajino T., Ren H., Iemura S., Natsume T., Stefansson B.,Brautigan D.L., Matsumoto K., Ninomiya-Tsuji J.; J. Biol. Chem. 281:39891-39896(2006). Cited for: INTERACTION WITH PP2A AND PPP6C, AND DEPHOSPHORYLATION AT THR-187 BYPP2A AND PPP6C.	17079228 [Abstract]
"The Yersinia enterocolitica effector YopP inhibits host cellsignalling by inactivating the protein kinase TAK1 in the IL-1signalling pathway."; Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K.,Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K.,Kracht M.; EMBO Rep. 7:838-844(2006). Cited for: UBIQUITINATION, PHOSPHORYLATION AT THR-187 BY AUTOCATALYSIS, SUBUNIT,AND FUNCTION.	16845370 [Abstract]

show

show

show

show

show

show

show

show

show

show