dbPTM

MP2K3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MP2K3_HUMAN
UniProt AC	P46734
Protein Name	Dual specificity mitogen-activated protein kinase kinase 3
Gene Name	MAP2K3
Organism	Homo sapiens (Human).
Sequence Length	347
Subcellular Localization
Protein Description	Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14..
Protein Sequence	MESPASSQPASMPQSKGKSKRKKDLRISCMSKPPAPNPTPPRNLDSRTFITIGDRNFEVEADDLVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNSQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLDKNMTIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADRFSPEFVDFTAQCLRKNPAERMSYLELMEHPFFTLHKTKKTDIAAFVKEILGEDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESPASSQ -------CCCCCCCC	11.82	22814378
3	Phosphorylation	-----MESPASSQPA -----CCCCCCCCCC	25.19	25159151
6	Phosphorylation	--MESPASSQPASMP --CCCCCCCCCCCCC	32.65	20068231
7	Phosphorylation	-MESPASSQPASMPQ -CCCCCCCCCCCCCC	42.14	20068231
10 (in isoform 2)	Phosphorylation	-	15.72	25159151
11	Phosphorylation	PASSQPASMPQSKGK CCCCCCCCCCCCCCC	37.36	20068231
15	Phosphorylation	QPASMPQSKGKSKRK CCCCCCCCCCCCCCC	37.19	25159151
28	Phosphorylation	RKKDLRISCMSKPPA CCCCCEEEECCCCCC	9.42	25159151
31	Phosphorylation	DLRISCMSKPPAPNP CCEEEECCCCCCCCC	46.46	25159151
32	Ubiquitination	LRISCMSKPPAPNPT CEEEECCCCCCCCCC	28.30	-
32	Acetylation	LRISCMSKPPAPNPT CEEEECCCCCCCCCC	28.30	25953088
37 (in isoform 3)	Ubiquitination	-	56.00	-
39	Phosphorylation	KPPAPNPTPPRNLDS CCCCCCCCCCCCCCC	53.19	25159151
46	Phosphorylation	TPPRNLDSRTFITIG CCCCCCCCCCEEEEC	36.06	20068231
80	2-Hydroxyisobutyrylation	GAYGVVEKVRHAQSG CCHHHHHHHHHCCCC	32.72	-
80	Ubiquitination	GAYGVVEKVRHAQSG CCHHHHHHHHHCCCC	32.72	-
85 (in isoform 3)	Ubiquitination	-	35.95	-
93	Ubiquitination	SGTIMAVKRIRATVN CCCEEEEEEHHHCCC	32.35	-
101	Phosphorylation	RIRATVNSQEQKRLL EHHHCCCHHHHHHHH	30.66	-
105	Ubiquitination	TVNSQEQKRLLMDLD CCCHHHHHHHHHHCC	44.24	-
117	Phosphorylation	DLDINMRTVDCFYTV HCCCCCCCCCCEEEE	15.21	27174698
122	Phosphorylation	MRTVDCFYTVTFYGA CCCCCCEEEEHHHHH	13.46	27174698
123	Phosphorylation	RTVDCFYTVTFYGAL CCCCCEEEEHHHHHH	7.88	27174698
125	Phosphorylation	VDCFYTVTFYGALFR CCCEEEEHHHHHHHC	11.88	27174698
127	Phosphorylation	CFYTVTFYGALFREG CEEEEHHHHHHHCCC	7.66	27174698
154 (in isoform 2)	Ubiquitination	-	6.55	21890473
183 (in isoform 1)	Ubiquitination	-	33.75	21890473
183	Ubiquitination	ALEHLHSKLSVIHRD HHHHHHHHHHEECCC	33.75	-
183	Acetylation	ALEHLHSKLSVIHRD HHHHHHHHHHEECCC	33.75	17881352
188 (in isoform 3)	Ubiquitination	-	20.10	21890473
192	Ubiquitination	SVIHRDVKPSNVLIN HEECCCCCHHHEEEC	47.20	-
192	Sumoylation	SVIHRDVKPSNVLIN HEECCCCCHHHEEEC	47.20	-
194	Phosphorylation	IHRDVKPSNVLINKE ECCCCCHHHEEECCC	33.58	21949786
200	Ubiquitination	PSNVLINKEGHVKMC HHHEEECCCCCEEEC	59.07	-
205 (in isoform 3)	Ubiquitination	-	28.30	-
207	Glutathionylation	KEGHVKMCDFGISGY CCCCEEECCCCCCCC	3.04	22555962
212	Phosphorylation	KMCDFGISGYLVDSV EECCCCCCCCHHHHH	23.05	22322096
214 (in isoform 2)	Ubiquitination	-	9.21	21890473
214	Phosphorylation	CDFGISGYLVDSVAK CCCCCCCCHHHHHHH	9.21	22322096
218	Phosphorylation	ISGYLVDSVAKTMDA CCCCHHHHHHHHCCC	19.25	22322096
222	Phosphorylation	LVDSVAKTMDAGCKP HHHHHHHHCCCCCCC	15.56	22322096
230	Phosphorylation	MDAGCKPYMAPERIN CCCCCCCCCCCCCCC	7.45	22322096
243 (in isoform 1)	Ubiquitination	-	63.39	21890473
243	Ubiquitination	INPELNQKGYNVKSD CCHHHHHCCCCCHHH	63.39	21890473
245	Phosphorylation	PELNQKGYNVKSDVW HHHHHCCCCCHHHHH	24.66	-
248	Ubiquitination	NQKGYNVKSDVWSLG HHCCCCCHHHHHHCC	36.98	-
248 (in isoform 3)	Ubiquitination	-	36.98	21890473
249	Phosphorylation	QKGYNVKSDVWSLGI HCCCCCHHHHHHCCC	32.87	-
250 (in isoform 2)	Ubiquitination	-	39.94	21890473
253	Phosphorylation	NVKSDVWSLGITMIE CCHHHHHHCCCEEEE	19.30	-
279	Ubiquitination	GTPFQQLKQVVEEPS CCHHHHHHHHHHCCC	36.39	2190698
279	Sumoylation	GTPFQQLKQVVEEPS CCHHHHHHHHHHCCC	36.39	-
279 (in isoform 1)	Ubiquitination	-	36.39	21890473
284 (in isoform 3)	Ubiquitination	-	39.20	21890473
305	Glutathionylation	FVDFTAQCLRKNPAE HHHHHHHHHHCCHHH	3.53	22555962
332	Ubiquitination	FTLHKTKKTDIAAFV EECCCCCHHHHHHHH	57.57	-
340	Ubiquitination	TDIAAFVKEILGEDS HHHHHHHHHHHCCCC	32.36	-

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
218	S	Phosphorylation	Kinase	MAP3K11	Q16584	GPS
218	S	Phosphorylation	Kinase	MAP3K3	Q61084	GPS
218	S	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
218	S	Phosphorylation	Kinase	MAP3K8	P41279	GPS
218	S	Phosphorylation	Kinase	MAP2K3	P46734	GPS
222	T	Phosphorylation	Kinase	MAP3K11	Q16584	GPS
222	T	Phosphorylation	Kinase	MAP2K3	P46734	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
218	S	Phosphorylation	8622669
Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity.
222	T	Phosphorylation	8622669
Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases regulates positively the kinase activity.

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 MP2K3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK03_HUMAN	MAPK3	physical	8226933
MK14_HUMAN	MAPK14	physical	11279118
MP2K6_HUMAN	MAP2K6	genetic	11562357
RL13_HUMAN	RPL13	physical	21900206
M3K4_HUMAN	MAP3K4	physical	15866172
MP2K3_HUMAN	MAP2K3	physical	9162092
MK14_HUMAN	MAPK14	physical	9162092
LRRK2_HUMAN	LRRK2	physical	20173330
JIP1_HUMAN	MAPK8IP1	physical	20173330
JIP2_HUMAN	MAPK8IP2	physical	20173330
JIP3_HUMAN	MAPK8IP3	physical	20173330
JIP4_HUMAN	SPAG9	physical	20173330
MK14_HUMAN	MAPK14	physical	20213747
A4_HUMAN	APP	physical	21832049
M3K5_HUMAN	MAP3K5	physical	16709866
MP2K6_HUMAN	MAP2K6	physical	25241761
M3K4_HUMAN	MAP3K4	physical	25241761
TAOK2_HUMAN	TAOK2	physical	25241761
MK14_HUMAN	MAPK14	physical	23904011
M3K5_HUMAN	MAP3K5	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 MP2K3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.	19413330 [Abstract]
"MKK3- and MKK6-regulated gene expression is mediated by the p38mitogen-activated protein kinase signal transduction pathway."; Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.; Mol. Cell. Biol. 16:1247-1255(1996). Cited for: PHOSPHORYLATION AT SER-218 AND THR-222, AND MUTAGENESIS OF SER-218 ANDTHR-222.	8622669 [Abstract]

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