dbPTM

M3K14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	M3K14_HUMAN
UniProt AC	Q99558
Protein Name	Mitogen-activated protein kinase kinase kinase 14
Gene Name	MAP3K14
Organism	Homo sapiens (Human).
Sequence Length	947
Subcellular Localization	Cytoplasm.
Protein Description	Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner..
Protein Sequence	MAVMEMACPGAPGSAVGQQKELPKAKEKTPPLGKKQSSVYKLEAVEKSPVFCGKWEILNDVITKGTAKEGSEAGPAAISIIAQAECENSQEFSPTFSERIFIAGSKQYSQSESLDQIPNNVAHATEGKMARVCWKGKRRSKARKKRKKKSSKSLAHAGVALAKPLPRTPEQESCTIPVQEDESPLGAPYVRNTPQFTKPLKEPGLGQLCFKQLGEGLRPALPRSELHKLISPLQCLNHVWKLHHPQDGGPLPLPTHPFPYSRLPHPFPFHPLQPWKPHPLESFLGKLACVDSQKPLPDPHLSKLACVDSPKPLPGPHLEPSCLSRGAHEKFSVEEYLVHALQGSVSSGQAHSLTSLAKTWAARGSRSREPSPKTEDNEGVLLTEKLKPVDYEYREEVHWATHQLRLGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTSPRIVPLYGAVREGPWVNIFMELLEGGSLGQLVKEQGCLPEDRALYYLGQALEGLEYLHSRRILHGDVKADNVLLSSDGSHAALCDFGHAVCLQPDGLGKSLLTGDYIPGTETHMAPEVVLGRSCDAKVDVWSSCCMMLHMLNGCHPWTQFFRGPLCLKIASEPPPVREIPPSCAPLTAQAIQEGLRKEPIHRVSAAELGGKVNRALQQVGGLKSPWRGEYKEPRHPPPNQANYHQTLHAQPRELSPRAPGPRPAEETTGRAPKLQPPLPPEPPEPNKSPPLTLSKEESGMWEPLPLSSLEPAPARNPSSPERKATVPEQELQQLEIELFLNSLSQPFSLEEQEQILSCLSIDSLSLSDDSEKNPSKASQSSRDTLSSGVHSWSSQAEARSSSWNMVLARGRPTDTPSYFNGVKVQIQSLNGEHLHIREFHRVKVGDIATGISSQIPAAAFSLVTKDGQPVRYDMEVPDSGIDLQCTLAPDGSFAWSWRVKHGQLENRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Ubiquitination	GSAVGQQKELPKAKE CCCCCCCCCCCCHHH	54.02	-
29	Phosphorylation	LPKAKEKTPPLGKKQ CCCHHHCCCCCCCCC	31.09	23532336
37	Phosphorylation	PPLGKKQSSVYKLEA CCCCCCCCCEEEEEE	30.56	28796482
38	Phosphorylation	PLGKKQSSVYKLEAV CCCCCCCCEEEEEEE	27.29	28796482
40	Phosphorylation	GKKQSSVYKLEAVEK CCCCCCEEEEEEECC	16.29	28796482
41	Ubiquitination	KKQSSVYKLEAVEKS CCCCCEEEEEEECCC	37.38	-
47	Ubiquitination	YKLEAVEKSPVFCGK EEEEEECCCCCCCCC	54.16	-
54	Ubiquitination	KSPVFCGKWEILNDV CCCCCCCCHHHHHCH	42.72	-
64	Ubiquitination	ILNDVITKGTAKEGS HHHCHHCCCCCCCCC	43.04	-
106	Ubiquitination	RIFIAGSKQYSQSES EEEEECCCCCCCCCC	52.95	21906983
125	Phosphorylation	PNNVAHATEGKMARV CCCHHHHCCCCCHHH	35.09	-
128	Ubiquitination	VAHATEGKMARVCWK HHHHCCCCCHHHHHC	24.13	21906983
163	Ubiquitination	HAGVALAKPLPRTPE HHHHHHCCCCCCCCC	48.19	21906983
198	Ubiquitination	RNTPQFTKPLKEPGL CCCCCCCCCCCCCCH	50.03	-
201	Ubiquitination	PQFTKPLKEPGLGQL CCCCCCCCCCCHHHH	71.09	-
241	Ubiquitination	QCLNHVWKLHHPQDG HHHHHHHHCCCCCCC	36.53	-
261	Phosphorylation	PTHPFPYSRLPHPFP CCCCCCCCCCCCCCC	27.81	-
276	Ubiquitination	FHPLQPWKPHPLESF CCCCCCCCCCCHHHH	39.88	-
294	Ubiquitination	LACVDSQKPLPDPHL HHCCCCCCCCCCCCH	53.10	21906983
352	Phosphorylation	VSSGQAHSLTSLAKT CCCCCCHHHHHHHHH	36.04	22210691
354	Phosphorylation	SGQAHSLTSLAKTWA CCCCHHHHHHHHHHH	25.39	-
365	Phosphorylation	KTWAARGSRSREPSP HHHHHCCCCCCCCCC	22.87	20068231
367	Phosphorylation	WAARGSRSREPSPKT HHHCCCCCCCCCCCC	42.57	20068231
385	Ubiquitination	EGVLLTEKLKPVDYE CCCEEEEECCCCCCH	57.48	-
387	Ubiquitination	VLLTEKLKPVDYEYR CEEEEECCCCCCHHH	54.80	-
410	Phosphorylation	QLRLGRGSFGEVHRM CCCCCCCCCCCEECC	28.81	27251275
429	Ubiquitination	TGFQCAVKKVRLEVF CCCCCEEEEHHEEEE	27.33	PubMed
549	Phosphorylation	QPDGLGKSLLTGDYI CCCCCCHHHCCCCCC	27.15	29759185
552	Phosphorylation	GLGKSLLTGDYIPGT CCCHHHCCCCCCCCC	33.04	29759185
559	Phosphorylation	TGDYIPGTETHMAPE CCCCCCCCCCCCCCC	32.15	29759185
561	Phosphorylation	DYIPGTETHMAPEVV CCCCCCCCCCCCCHH	19.45	29759185
643	Phosphorylation	KEPIHRVSAAELGGK CCCCCCCCHHHHHHH	23.01	-
682	Phosphorylation	PPPNQANYHQTLHAQ CCCCCCCCCHHHCCC	9.79	-
814	Phosphorylation	DDSEKNPSKASQSSR CCCCCCCCHHCHHHH	50.69	-
817	Phosphorylation	EKNPSKASQSSRDTL CCCCCHHCHHHHHHH	34.04	-
820	Phosphorylation	PSKASQSSRDTLSSG CCHHCHHHHHHHHHC	26.91	-
823	Phosphorylation	ASQSSRDTLSSGVHS HCHHHHHHHHHCCCC	27.68	30576142
825	Phosphorylation	QSSRDTLSSGVHSWS HHHHHHHHHCCCCCC	27.43	30576142
830	Phosphorylation	TLSSGVHSWSSQAEA HHHHCCCCCCCHHHH	26.67	30576142
882	Ubiquitination	IREFHRVKVGDIATG EEEEEEEEHHHHCCC	40.22	21906983

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
814	S	Phosphorylation	Kinase	IKKA	O15111	PSP
817	S	Phosphorylation	Kinase	IKKA	O15111	PSP
820	S	Phosphorylation	Kinase	IKKA	O15111	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	ZFP91	Q96JP5	PMID:20682767
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF3	Q13114	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF1	Q13077	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC3	Q13489	PMID:18022362
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:18022362
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF2	Q12933	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
48	K	ubiquitylation	-
Undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
559	T	Phosphorylation	20682767
Phosphorylation at Thr-559 is required to activates its kinase activity and 'Lys-63'-linked polyubiquitination.
559	T	ubiquitylation	20682767
Phosphorylation at Thr-559 is required to activates its kinase activity and 'Lys-63'-linked polyubiquitination.

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 M3K14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IKKA_HUMAN	CHUK	physical	9244310
M3K8_HUMAN	MAP3K8	physical	10072079
M3K14_HUMAN	MAP3K14	physical	10887201
NFKB2_HUMAN	NFKB2	physical	11239468
RIPK1_HUMAN	RIPK1	physical	11116146
TRAF1_HUMAN	TRAF1	physical	11278268
TRAF2_HUMAN	TRAF2	physical	11278268
TRAF3_HUMAN	TRAF3	physical	11278268
TRAF6_MOUSE	Traf6	physical	11278268
IKKA_HUMAN	CHUK	physical	11278268
IKKB_HUMAN	IKBKB	physical	11278268
TRAF2_HUMAN	TRAF2	physical	9020361
M3K14_HUMAN	MAP3K14	physical	9020361
M3K7_HUMAN	MAP3K7	physical	10094049
IKKA_HUMAN	CHUK	physical	10094049
TRAF6_HUMAN	TRAF6	physical	10921914
PEBP1_RAT	Pebp1	physical	11585904
PEBP1_RAT	Pebp1	genetic	11585904
BIRC2_HUMAN	BIRC2	physical	18022362
ZFP91_HUMAN	ZFP91	physical	20682767
EF1A1_HUMAN	EEF1A1	physical	21900206
TRAF3_HUMAN	TRAF3	physical	20348096
UBC_HUMAN	UBC	physical	20348096
IKKA_HUMAN	CHUK	physical	20348096
BIRC2_HUMAN	BIRC2	physical	20184394
TRAF2_HUMAN	TRAF2	physical	20184394
TANK_HUMAN	TANK	physical	20184394
TRAF2_HUMAN	TRAF2	physical	20385093
TRAF1_HUMAN	TRAF1	physical	20385093
TRAF3_HUMAN	TRAF3	physical	15208311
IKKA_HUMAN	CHUK	physical	15208311
PELI3_HUMAN	PELI3	physical	12874243
TRAF3_HUMAN	TRAF3	physical	15084608
TRAF1_HUMAN	TRAF1	physical	15084608
TRAF2_HUMAN	TRAF2	physical	15084608
IKKA_HUMAN	CHUK	physical	15084608
IKKA_HUMAN	CHUK	physical	16286467
IKKB_HUMAN	IKBKB	physical	16286467
TRAF1_HUMAN	TRAF1	physical	23543740
TRAF3_HUMAN	TRAF3	physical	23543740
BIRC2_HUMAN	BIRC2	physical	25246529
TRAF2_HUMAN	TRAF2	physical	25246529
TRAF3_HUMAN	TRAF3	physical	25246529
BRCA1_HUMAN	BRCA1	physical	25184681
SL9A1_HUMAN	SLC9A1	physical	11369779
TRAF6_HUMAN	TRAF6	physical	25241761
IKKA_HUMAN	CHUK	physical	25241761
CASP3_HUMAN	CASP3	physical	25241761
IKKA_HUMAN	CHUK	physical	28514442
IKKB_HUMAN	IKBKB	physical	28514442
NEMO_HUMAN	IKBKG	physical	28514442
TRAF3_HUMAN	TRAF3	physical	28514442
NAV1_HUMAN	NAV1	physical	28514442

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 M3K14_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"An atypical E3 ligase zinc finger protein 91 stabilizes and activatesNF-kappaB-inducing kinase via Lys63-linked ubiquitination."; Jin X., Jin H.R., Jung H.S., Lee S.J., Lee J.H., Lee J.J.; J. Biol. Chem. 285:30539-30547(2010). Cited for: PHOSPHORYLATION AT THR-559, UBIQUITINATION, INTERACTION WITH ZFP91,AND MUTAGENESIS OF 429-LYS-LYS-430 AND THR-559.	20682767 [Abstract]

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