dbPTM

MK04_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK04_HUMAN
UniProt AC	P31152
Protein Name	Mitogen-activated protein kinase 4
Gene Name	MAPK4
Organism	Homo sapiens (Human).
Sequence Length	587
Subcellular Localization	Cytoplasm. Nucleus. Translocates to the cytoplasm following interaction with MAPKAPK5..
Protein Description	Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity)..
Protein Sequence	MAEKGDCIASVYGYDLGGRFVDFQPLGFGVNGLVLSAVDSRACRKVAVKKIALSDARSMKHALREIKIIRRLDHDNIVKVYEVLGPKGTDLQGELFKFSVAYIVQEYMETDLARLLEQGTLAEEHAKLFMYQLLRGLKYIHSANVLHRDLKPANIFISTEDLVLKIGDFGLARIVDQHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFVSSTWEVKRPLRKLLPEVNSEAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAANQSQLSNWDTCSSRYPVSLSSDLEWRPDRCQDASEVQRDPRAGSAPLAEDVQVDPRKDSHSSSERFLEQSHSSMERAFEADYGRSCDYKVGSPSYLDKLLWRDNKPHHYSEPKLILDLSHWKQAAGAPPTATGLADTGAREDEPASLFLEIAQWVKSTQGGPEHASPPADDPERRLSASPPGRPAPVDGGASPQFDLDVFISRALKLCTKPEDLPDNKLGDLNGACIPEHPGDLVQTEAFSKERW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
50	Ubiquitination	CRKVAVKKIALSDAR HHHHHHHHHHCCCHH	26.98	-
58	Phosphorylation	IALSDARSMKHALRE HHCCCHHHHHHHHHH	33.62	-
87	Ubiquitination	VYEVLGPKGTDLQGE EEEECCCCCCCCCHH	73.05	-
138	Ubiquitination	YQLLRGLKYIHSANV HHHHHHHHHHHHCCE	45.01	-
142	Phosphorylation	RGLKYIHSANVLHRD HHHHHHHHCCEECCC	16.39	-
182	Ubiquitination	VDQHYSHKGYLSEGL HHCCCCCCCCCCCCC	43.22	-
184	Phosphorylation	QHYSHKGYLSEGLVT CCCCCCCCCCCCCCC	16.32	27251275
186	Phosphorylation	YSHKGYLSEGLVTKW CCCCCCCCCCCCCCC	22.57	25159151
191	Phosphorylation	YLSEGLVTKWYRSPR CCCCCCCCCCCCCCC	22.39	27251275
196	Phosphorylation	LVTKWYRSPRLLLSP CCCCCCCCCCEEECC	9.93	1319925
206	Phosphorylation	LLLSPNNYTKAIDMW EEECCCCHHHHHHHH	19.09	25690035
207	Phosphorylation	LLSPNNYTKAIDMWA EECCCCHHHHHHHHH	19.00	25690035
276	Ubiquitination	EVKRPLRKLLPEVNS HCCHHHHHHCHHCCH	63.16	-
294	Phosphorylation	DFLEKILTFNPMDRL HHHHHHHHCCHHHHH	25.49	-
316	Phosphorylation	HPYMSPYSCPEDEPT CCCCCCCCCCCCCCC	26.95	-
360	Phosphorylation	CSSRYPVSLSSDLEW CCCCCCCCCCCCCCC	20.30	22210691
362	Phosphorylation	SRYPVSLSSDLEWRP CCCCCCCCCCCCCCC	17.82	22210691
363	Phosphorylation	RYPVSLSSDLEWRPD CCCCCCCCCCCCCCC	52.05	28348404
386	Phosphorylation	QRDPRAGSAPLAEDV HCCCCCCCCCCCCCC	26.23	30576142
412	Phosphorylation	SERFLEQSHSSMERA HHHHHHHHHHHHHHH	18.89	22617229
414	Phosphorylation	RFLEQSHSSMERAFE HHHHHHHHHHHHHHH	36.31	22617229
415	Phosphorylation	FLEQSHSSMERAFEA HHHHHHHHHHHHHHC	21.17	22617229
424	Phosphorylation	ERAFEADYGRSCDYK HHHHHCCCCCCCCCC	22.83	-
427	Phosphorylation	FEADYGRSCDYKVGS HHCCCCCCCCCCCCC	13.64	28348404
431	Ubiquitination	YGRSCDYKVGSPSYL CCCCCCCCCCCHHHH	27.20	-
434	Phosphorylation	SCDYKVGSPSYLDKL CCCCCCCCHHHHHHH	17.41	29116813
436	Phosphorylation	DYKVGSPSYLDKLLW CCCCCCHHHHHHHHH	39.77	25072903
437	Phosphorylation	YKVGSPSYLDKLLWR CCCCCHHHHHHHHHC	23.46	25072903
447	Ubiquitination	KLLWRDNKPHHYSEP HHHHCCCCCCCCCCC	50.44	-
451	Phosphorylation	RDNKPHHYSEPKLIL CCCCCCCCCCCEEEE	16.22	29083192
452	Phosphorylation	DNKPHHYSEPKLILD CCCCCCCCCCEEEEE	42.96	29083192
472	Phosphorylation	QAAGAPPTATGLADT HHCCCCCCCCCCCCC	35.47	-
479	Phosphorylation	TATGLADTGAREDEP CCCCCCCCCCCCCCC	27.42	-
508	Phosphorylation	QGGPEHASPPADDPE CCCCCCCCCCCCCHH	33.07	29116813
519	Phosphorylation	DDPERRLSASPPGRP CCHHHCCCCCCCCCC	25.53	29116813
521	Phosphorylation	PERRLSASPPGRPAP HHHCCCCCCCCCCCC	28.40	22210691
548	Ubiquitination	VFISRALKLCTKPED HHHHHHHHHCCCHHH	40.30	-
560	Ubiquitination	PEDLPDNKLGDLNGA HHHCCCCCCCCCCCC	62.32	-

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
186	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
186	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
186	S	Phosphorylation	Kinase	PAK3	O75914	Uniprot
186	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
196	S	Phosphorylation	Kinase	MAPK4	P31152	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
186	S	Phosphorylation		18669648
Phosphorylated at Ser-186 by PAK1, PAK2 and PAK3 resulting in catalytic activation.

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 MK04_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAPK5_HUMAN	MAPKAPK5	physical	23602568
RB6I2_HUMAN	ERC1	physical	23602568
TECR_HUMAN	TECR	physical	23602568
FAKD5_HUMAN	FASTKD5	physical	23602568
FA57A_HUMAN	FAM57A	physical	23602568
PFKAP_HUMAN	PFKP	physical	23602568
PSA7_HUMAN	PSMA7	physical	23602568
SFXN2_HUMAN	SFXN2	physical	23602568
ACSL3_HUMAN	ACSL3	physical	23602568
AT1A1_HUMAN	ATP1A1	physical	23602568

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 MK04_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Activation loop phosphorylation of ERK3/ERK4 by group I p21-activatedkinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated proteinkinase 5 signaling pathway."; Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L.,Thibault P., Meloche S.; J. Biol. Chem. 286:6470-6478(2011). Cited for: PHOSPHORYLATION AT SER-186.	21177870 [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-186, AND MASSSPECTROMETRY.	18669648 [Abstract]

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