dbPTM

M3K5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	M3K5_HUMAN
UniProt AC	Q99683
Protein Name	Mitogen-activated protein kinase kinase kinase 5
Gene Name	MAP3K5
Organism	Homo sapiens (Human).
Sequence Length	1374
Subcellular Localization	Cytoplasm. Endoplasmic reticulum. Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region.
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 signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). 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 MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1)..
Protein Sequence	MSTEADEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGEGEEHQLPPPPPGSFWNVESAAAPGIGCPAATSSSSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDLLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKVDPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKIVRNLMESLAQGAEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQAVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSSGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
82	Phosphorylation	SATRGRGSSVGGGSR CCCCCCCCCCCCCCC	22.08	-
83	Phosphorylation	ATRGRGSSVGGGSRR CCCCCCCCCCCCCCC	27.83	16532036
89	Methylation	SSVGGGSRRTTVAYV CCCCCCCCCEEEEEE	43.15	-
95	Phosphorylation	SRRTTVAYVINEASQ CCCEEEEEEEECCCC	9.49	23025827
101	Phosphorylation	AYVINEASQGQLVVA EEEEECCCCCCEEEE	28.76	27251275
115	Phosphorylation	AESEALQSLREACET ECHHHHHHHHHHHHH	30.19	23025827
140	Phosphorylation	GKLDFGETTVLDRFY CCCCCCCCCCHHHHC	23.68	23312004
141	Phosphorylation	KLDFGETTVLDRFYN CCCCCCCCCHHHHCC	18.12	23312004
267	Phosphorylation	LLKVAQASSSQYFRE HHHHHHHCCCHHHHH	20.60	23312004
268	Phosphorylation	LKVAQASSSQYFRES HHHHHHCCCHHHHHH	25.20	23312004
269	Phosphorylation	KVAQASSSQYFRESI HHHHHCCCHHHHHHH	26.80	28857561
271	Phosphorylation	AQASSSQYFRESILN HHHCCCHHHHHHHHH	13.42	23312004
461	Phosphorylation	KVGVKLSSLLGKKGN HHHHHHHHHHCCCCC	37.74	-
465	Ubiquitination	KLSSLLGKKGNLEKL HHHHHHCCCCCHHHH	58.43	32015554
528	Phosphorylation	YKHFVKLTTEQPVAK HHHHHHCCCCCCCHH	23.67	-
535	Sumoylation	TTEQPVAKQELVDFW CCCCCCHHHHHHHHH	44.53	-
535	Sumoylation	TTEQPVAKQELVDFW CCCCCCHHHHHHHHH	44.53	-
570	Phosphorylation	ILEPTKIYQPSYLSI EECCCCCCCCCEECC	18.87	-
574	Phosphorylation	TKIYQPSYLSINNEV CCCCCCCEECCCCCE	15.91	-
611	Ubiquitination	FSASSVRGVSISKFE CCCCCCCCCCHHHHH	18.50	22817900
613	Phosphorylation	ASSVRGVSISKFEER CCCCCCCCHHHHHHH	24.78	26434776
615	Phosphorylation	SVRGVSISKFEERCC CCCCCCHHHHHHHEE	24.64	26434776
654	Phosphorylation	FEMVNTITEEKGRST HHHHHHHHHHCCCCC	35.73	22468782
709	Ubiquitination	NQVRIAIKEIPERDS CCEEEEEECCCCCCC	40.34	24448648
718	Phosphorylation	IPERDSRYSQPLHEE CCCCCCCCCCCHHHH	18.66	28851738
719	Phosphorylation	PERDSRYSQPLHEEI CCCCCCCCCCHHHHH	24.98	28851738
730	Ubiquitination	HEEIALHKHLKHKNI HHHHHHHHHHCCCCH	52.03	29967540
761	Phosphorylation	MEQVPGGSLSALLRS EEECCCCCHHHHHHH	25.68	22210691
763	Phosphorylation	QVPGGSLSALLRSKW ECCCCCHHHHHHHCC	20.68	22210691
785	Ubiquitination	QTIGFYTKQILEGLK CEEHHHHHHHHHHHH	24.78	29967540
805	Ubiquitination	QIVHRDIKGDNVLIN CEEECCCCCCCEEEE	65.58	22817900
813	Phosphorylation	GDNVLINTYSGVLKI CCCEEEEEECCEEEH	16.45	17937911
814	Phosphorylation	DNVLINTYSGVLKIS CCEEEEEECCEEEHH	10.03	18083107
821	Phosphorylation	YSGVLKISDFGTSKR ECCEEEHHHCCCCCC	25.87	-
825	Phosphorylation	LKISDFGTSKRLAGI EEHHHCCCCCCCCCC	30.94	-
827	Ubiquitination	ISDFGTSKRLAGINP HHHCCCCCCCCCCCC	51.79	-
836	Phosphorylation	LAGINPCTETFTGTL CCCCCCCCCCCCCCH	39.04	28857561
838	Phosphorylation	GINPCTETFTGTLQY CCCCCCCCCCCCHHH	14.35	17210579
840	Phosphorylation	NPCTETFTGTLQYMA CCCCCCCCCCHHHHC	36.35	28857561
842	Dephosphorylation	CTETFTGTLQYMAPE CCCCCCCCHHHHCHH	13.97	11689443
842	Phosphorylation	CTETFTGTLQYMAPE CCCCCCCCHHHHCHH	13.97	17937911
869	S-nitrosocysteine	ADIWSLGCTIIEMAT HHHHHCCCEEEHHHH	2.75	-
869	S-nitrosylation	ADIWSLGCTIIEMAT HHHHHCCCEEEHHHH	2.75	22178444
878	Ubiquitination	IIEMATGKPPFYELG EEHHHHCCCCCCCCC	45.20	22817900
906	Phosphorylation	VHPEIPESMSAEAKA ECCCCCCCCCHHHHH	16.81	30206219
908	Phosphorylation	PEIPESMSAEAKAFI CCCCCCCCHHHHHHH	32.03	30206219
914	Ubiquitination	MSAEAKAFILKCFEP CCHHHHHHHHHHHCC	7.10	22817900
946	Acetylation	KVSSKKKKTQPKLSA HHCCCCCCCCCCHHH	62.36	7974837
952	Phosphorylation	KKTQPKLSALSAGSN CCCCCCHHHHCCCCC	33.03	29759185
955	Phosphorylation	QPKLSALSAGSNEYL CCCHHHHCCCCCHHH	30.24	26657352
958	Phosphorylation	LSALSAGSNEYLRSI HHHHCCCCCHHHHHC	26.63	25159151
961	Phosphorylation	LSAGSNEYLRSISLP HCCCCCHHHHHCCCC	16.21	29978859
964	Phosphorylation	GSNEYLRSISLPVPV CCCHHHHHCCCCCCE	17.59	28060719
966	Phosphorylation	NEYLRSISLPVPVLV CHHHHHCCCCCCEEE	28.06	17671211
976	Phosphorylation	VPVLVEDTSSSSEYG CCEEEECCCCCCCCC	19.59	28060719
977	Phosphorylation	PVLVEDTSSSSEYGS CEEEECCCCCCCCCC	40.31	28060719
978	Phosphorylation	VLVEDTSSSSEYGSV EEEECCCCCCCCCCC	39.72	28060719
979	Phosphorylation	LVEDTSSSSEYGSVS EEECCCCCCCCCCCC	27.27	28060719
980	Phosphorylation	VEDTSSSSEYGSVSP EECCCCCCCCCCCCC	36.46	28060719
982	Phosphorylation	DTSSSSEYGSVSPDT CCCCCCCCCCCCCCC	19.35	28060719
984	Phosphorylation	SSSSEYGSVSPDTEL CCCCCCCCCCCCCCC	20.65	26657352
986	Phosphorylation	SSEYGSVSPDTELKV CCCCCCCCCCCCCEE	20.82	26074081
989	Phosphorylation	YGSVSPDTELKVDPF CCCCCCCCCCEECCC	46.75	26074081
997	Phosphorylation	ELKVDPFSFKTRAKS CCEECCCCHHHHHHH	31.08	24719451
1015	Phosphorylation	RDVKGIRTLFLGIPD CCCCCHHEEEECCCC	21.68	20873877
1029	Phosphorylation	DENFEDHSAPPSPEE CCCCCCCCCCCCHHH	55.59	25463755
1033	Phosphorylation	EDHSAPPSPEEKDSG CCCCCCCCHHHCCCC	43.83	25159151
1039	Phosphorylation	PSPEEKDSGFFMLRK CCHHHCCCCCEEEEC	48.87	26074081
1059	Phosphorylation	ATLHRILTEDQDKIV HHHHHHHCCCHHHHH	34.83	28857561
1064	Ubiquitination	ILTEDQDKIVRNLME HHCCCHHHHHHHHHH	37.15	30230243
1072	Phosphorylation	IVRNLMESLAQGAEE HHHHHHHHHHCCCCC	18.29	28857561
1083	Sumoylation	GAEEPKLKWEHITTL CCCCCCCCHHHHHHH	57.57	-
1083	Sumoylation	GAEEPKLKWEHITTL CCCCCCCCHHHHHHH	57.57	-
1108	Phosphorylation	TDRKIIATTLSKLKL CCHHHHHHHHHHCCE	20.19	23403867
1109	Phosphorylation	DRKIIATTLSKLKLE CHHHHHHHHHHCCEE	21.73	23403867
1111	Phosphorylation	KIIATTLSKLKLELD HHHHHHHHHCCEEEC	33.57	23403867
1114	Sumoylation	ATTLSKLKLELDFDS HHHHHHCCEEECCCC	43.59	-
1114	Sumoylation	ATTLSKLKLELDFDS HHHHHHCCEEECCCC	43.59	-
1157	Phosphorylation	HWMFALDSIIRKAVQ HHHHHHHHHHHHHHH	22.29	24719451
1220	Phosphorylation	VIEDAVATSGVSTLS HHCHHHHCCCCCHHC	21.29	28270605
1221	Phosphorylation	IEDAVATSGVSTLSS HCHHHHCCCCCHHCE	27.71	28270605
1224	Phosphorylation	AVATSGVSTLSSTVS HHHCCCCCHHCEECC	27.44	28270605
1225	Phosphorylation	VATSGVSTLSSTVSH HHCCCCCHHCEECCC	28.40	28270605
1227	Phosphorylation	TSGVSTLSSTVSHDS CCCCCHHCEECCCCC	24.85	28270605
1228	Phosphorylation	SGVSTLSSTVSHDSQ CCCCHHCEECCCCCC	35.62	28270605
1229	Phosphorylation	GVSTLSSTVSHDSQS CCCHHCEECCCCCCH	23.74	28270605
1231	Phosphorylation	STLSSTVSHDSQSAH CHHCEECCCCCCHHH	22.97	28270605
1234	Phosphorylation	SSTVSHDSQSAHRSL CEECCCCCCHHHHHH	22.17	28270605
1236	Phosphorylation	TVSHDSQSAHRSLNV ECCCCCCHHHHHHHH	29.96	28270605
1240	Phosphorylation	DSQSAHRSLNVQLGR CCCHHHHHHHHHHCC	17.90	29743597
1326	Phosphorylation	VNGADEDTISRFLAE HCCCCHHHHHHHHHC	20.85	-

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
83	S	Phosphorylation	Kinase	AKT2	P31751	Uniprot
83	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
83	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
83	S	Phosphorylation	Kinase	PIM1	P11309	Uniprot
83	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
83	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
718	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
718	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
813	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
825	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
838	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
838	T	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
838	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
838	T	Phosphorylation	Kinase	MELK	Q14680	Uniprot
838	T	Phosphorylation	Kinase	MAP3K6	O95382	Uniprot
838	T	Phosphorylation	Kinase	PRKD1	Q15139	PSP
838	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
842	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
966	S	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
966	S	Phosphorylation	Kinase	PDPK1	O15530	GPS
1109	T	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
1326	T	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:17220297
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:16038411

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
83	S	Phosphorylation	11154276
Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2.
838	T	Phosphorylation	11689443
Phosphorylated at Thr-838 through autophosphorylation and by MAP3K6/ASK2 which leads to activation.
838	T	Phosphorylation	11689443
Thr-838 is dephosphorylated by PPP5C.
966	S	Oxidation	10411906
Phosphorylation at Ser-966 in response to oxidative stress is negatively regulated by PPIA/CYPA.
966	S	Phosphorylation	10411906
Phosphorylated at Ser-966 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity.
966	S	Phosphorylation	10411906
Phosphorylation at Ser-966 in response to oxidative stress is negatively regulated by PPIA/CYPA.
1033	S	Phosphorylation	15094778
Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2.

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 M3K5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDCD6_HUMAN	PDCD6	physical	12372597
SYQ_HUMAN	QARS	physical	11096076
M3K5_HUMAN	MAP3K5	physical	11416155
MPIP1_HUMAN	CDC25A	physical	11416155
DUS19_HUMAN	DUSP19	genetic	11959862
TRAF5_HUMAN	TRAF5	physical	10523862
TRAF6_HUMAN	TRAF6	physical	10523862
TRAF2_HUMAN	TRAF2	physical	10523862
MP2K6_HUMAN	MAP2K6	physical	12820963
RBCC1_HUMAN	RB1CC1	physical	17015619
RBCC1_MOUSE	Rb1cc1	physical	17015619
1433Z_HUMAN	YWHAZ	physical	10411906
GSTM1_MOUSE	Gstm1	physical	11278289
RAF1_HUMAN	RAF1	physical	11427728
E2AK2_HUMAN	EIF2AK2	physical	12473108
JIP3_HUMAN	MAPK8IP3	physical	12189133
M3K5_HUMAN	MAP3K5	physical	11689443
PPP5_HUMAN	PPP5C	physical	11689443
M3K6_HUMAN	MAP3K6	physical	11689443
MP2K6_HUMAN	MAP2K6	physical	11689443
PPP5_HUMAN	PPP5C	genetic	11689443
THIO_HUMAN	TXN	physical	9564042
M3K5_HUMAN	MAP3K5	physical	11920685
M3K7_HUMAN	MAP3K7	physical	10921914
DAXX_HUMAN	DAXX	physical	9743501
GNA13_HUMAN	GNA13	physical	17595347
SOCS1_HUMAN	SOCS1	physical	16407264
SOCS3_HUMAN	SOCS3	physical	16407264
CBP_HUMAN	CREBBP	physical	20936779
DMD_HUMAN	DMD	physical	20936779
EP300_HUMAN	EP300	physical	20936779
USP9X_HUMAN	USP9X	physical	20005844
SMN_HUMAN	SMN1	physical	21496457
TNAP3_HUMAN	TNFAIP3	physical	20448643
HSP74_HUMAN	HSPA4	physical	20349136
CHIP_HUMAN	STUB1	physical	20349136
PRS7_HUMAN	PSMC2	physical	20843792
PRS4_HUMAN	PSMC1	physical	20843792
PRS6B_HUMAN	PSMC4	physical	20843792
PRS6A_HUMAN	PSMC3	physical	20843792
PRS8_HUMAN	PSMC5	physical	20843792
SOCS1_HUMAN	SOCS1	physical	18776134
M3K7_HUMAN	MAP3K7	physical	22167179
THIO_HUMAN	TXN	physical	17724081
TRAF2_HUMAN	TRAF2	physical	17724081
TRAF6_HUMAN	TRAF6	physical	17724081
M3K5_HUMAN	MAP3K5	physical	17724081
DAXX_HUMAN	DAXX	physical	11495919
DAB2P_HUMAN	DAB2IP	physical	17389591
MP2K4_HUMAN	MAP2K4	physical	15258908
JIP3_HUMAN	MAPK8IP3	physical	15258908
PTN11_HUMAN	PTPN11	physical	19287004
PARK7_HUMAN	PARK7	physical	19293155
MBP_HUMAN	MBP	physical	19293155
THIO_HUMAN	TXN	physical	17331951
DYR1A_HUMAN	DYRK1A	physical	22110360
THIO_HUMAN	TXN	physical	20385180
MP2K6_HUMAN	MAP2K6	physical	20213747
PARK7_HUMAN	PARK7	physical	20213747
M3K5_HUMAN	MAP3K5	physical	20213747
MBP_MOUSE	Mbp	physical	10843682
AKT2_HUMAN	AKT2	physical	12697749
ARRB2_HUMAN	ARRB2	physical	19782076
MP2K3_HUMAN	MAP2K3	physical	16709866
GEMI5_HUMAN	GEMIN5	physical	17541429
M3K5_HUMAN	MAP3K5	physical	17541429
MP2K4_HUMAN	MAP2K4	physical	17541429
DAB2P_HUMAN	DAB2IP	physical	19903888
P85A_HUMAN	PIK3R1	physical	19903888
THIOM_HUMAN	TXN2	physical	23291592
THIO_HUMAN	TXN	physical	23291592
THIO_HUMAN	TXN	physical	15696199
ATD3A_HUMAN	ATAD3A	physical	25852190
NACC1_HUMAN	NACC1	physical	25852190
M3K6_HUMAN	MAP3K6	physical	25852190
1433Z_HUMAN	YWHAZ	physical	25852190
SIAH1_HUMAN	SIAH1	physical	25391652
MP2K4_HUMAN	MAP2K4	physical	15310755
DAB2P_HUMAN	DAB2IP	physical	15310755
TNR6_HUMAN	FAS	physical	25241761
A4_HUMAN	APP	physical	25241761
DAXX_HUMAN	DAXX	physical	25241761
ERN1_HUMAN	ERN1	physical	25241761
VIF_HV1B1	vif	physical	25901786
VIF_HV1BR	vif	physical	25901786
VIF_HV1H2	vif	physical	25901786
M3K5_HUMAN	MAP3K5	physical	12624112
TRAF2_HUMAN	TRAF2	physical	25098452
M3K5_HUMAN	MAP3K5	physical	25098452
THIO_HUMAN	TXN	physical	25098452
MP2K6_HUMAN	MAP2K6	physical	25098452
CIB1_HUMAN	CIB1	physical	19805025
THIO_HUMAN	TXN	physical	19805025
M3K5_HUMAN	MAP3K5	physical	19805025
TRAF2_HUMAN	TRAF2	physical	19805025
MP2K3_HUMAN	MAP2K3	physical	19805025

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 M3K5_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-836; THR-838; SER-958;THR-976; SER-977; SER-978; SER-979; SER-984; SER-986; THR-989 ANDSER-1033, AND MASS SPECTROMETRY.	19369195 [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-1029 AND SER-1033, ANDMASS SPECTROMETRY.	18669648 [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-1029 AND SER-1033, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"PIM1 phosphorylates and negatively regulates ASK1-mediatedapoptosis."; Gu J.J., Wang Z., Reeves R., Magnuson N.S.; Oncogene 28:4261-4271(2009). Cited for: PHOSPHORYLATION AT SER-83 BY PIM1, AND INTERACTION WITH PIM1.	19749799 [Abstract]
"Negative control of apoptosis signal-regulating kinase 1 throughphosphorylation of Ser-1034."; Fujii K., Goldman E.H., Park H.R., Zhang L., Chen J., Fu H.; Oncogene 23:5099-5104(2004). Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-966 AND SER-1033,MUTAGENESIS OF SER-966 AND SER-1033, AND INTERACTION WITH YWHAG.	15094778 [Abstract]
"Activation of apoptosis signal-regulating kinase 1 by reactive oxygenspecies through dephosphorylation at serine 967 and 14-3-3dissociation."; Goldman E.H., Chen L., Fu H.; J. Biol. Chem. 279:10442-10449(2004). Cited for: PHOSPHORYLATION AT SER-966, ENZYME REGULATION, AND FUNCTION.	14688258 [Abstract]
"AKT2 inhibition of cisplatin-induced JNK/p38 and Bax activation byphosphorylation of ASK1: implication of AKT2 in chemoresistance."; Yuan Z.Q., Feldman R.I., Sussman G.E., Coppola D., Nicosia S.V.,Cheng J.Q.; J. Biol. Chem. 278:23432-23440(2003). Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, AND FUNCTION.	12697749 [Abstract]
"Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1."; Kim A.H., Khursigara G., Sun X., Franke T.F., Chao M.V.; Mol. Cell. Biol. 21:893-901(2001). Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, AND FUNCTION.	11154276 [Abstract]
"Structural and functional characterization of the human proteinkinase ASK1."; Bunkoczi G., Salah E., Filippakopoulos P., Fedorov O., Muller S.,Sobott F., Parker S.A., Zhang H., Min W., Turk B.E., Knapp S.; Structure 15:1215-1226(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-951, AND PHOSPHORYLATIONAT THR-813; THR-838 AND THR-842.	17937911 [Abstract]
"Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr 838 phosphorylation."; Jung H., Seong H.A., Ha H.; J. Biol. Chem. 283:34541-34553(2008). Cited for: PHOSPHORYLATION AT THR-838.	18948261 [Abstract]
"Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-activated protein kinase kinase kinase in a heteromeric complex withASK1."; Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I.,Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.; J. Biol. Chem. 282:7522-7531(2007). Cited for: ENZYME REGULATION, INTERACTION WITH MAP3K5, PHOSPHORYLATION ATTHR-838, AND MUTAGENESIS OF LYS-709.	17210579 [Abstract]
"Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer."; Tobiume K., Saitoh M., Ichijo H.; J. Cell. Physiol. 191:95-104(2002). Cited for: FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, AND PHOSPHORYLATION ATTHR-838.	11920685 [Abstract]
"Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5)in response to oxidative stress."; Morita K., Saitoh M., Tobiume K., Matsuura H., Enomoto S.,Nishitoh H., Ichijo H.; EMBO J. 20:6028-6036(2001). Cited for: INTERACTION WITH PPP5C, DEPHOSPHORYLATION AT THR-838, SUBCELLULARLOCATION, ENZYME REGULATION, AND FUNCTION.	11689443 [Abstract]
"SOCS1 inhibits tumor necrosis factor-induced activation of ASK1-JNKinflammatory signaling by mediating ASK1 degradation."; He Y., Zhang W., Zhang R., Zhang H., Min W.; J. Biol. Chem. 281:5559-5566(2006). Cited for: PHOSPHORYLATION AT TYR-718, INTERACTION WITH SOCS1, AND ENZYMEREGULATION.	16407264 [Abstract]

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