dbPTM

MKNK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MKNK1_HUMAN
UniProt AC	Q9BUB5
Protein Name	MAP kinase-interacting serine/threonine-protein kinase 1
Gene Name	MKNK1
Organism	Homo sapiens (Human).
Sequence Length	465
Subcellular Localization	Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Nucleus.
Protein Description	May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap..
Protein Sequence	MVSSQKLEKPIEMGSSEPLPIADGDRRRKKKRRGRATDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKDKVSLCHLGWSAMAPSGLTAAPTSLGSSDPPTSASQVAGTTGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPEKGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEPEALADGLCSMKLSPPCKSRLARRRALAQAGRGEDRSPPTAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Phosphorylation	KKRRGRATDSLPGKF HHHCCCCCCCCCCCH	25.43	28450419
39	Phosphorylation	RRGRATDSLPGKFED HCCCCCCCCCCCHHH	31.91	29255136
48	Phosphorylation	PGKFEDMYKLTSELL CCCHHHHHHHHHHHH	18.37	28060719
60	Phosphorylation	ELLGEGAYAKVQGAV HHHCCCCCEEEEEEE	20.15	25159151
68	Phosphorylation	AKVQGAVSLQNGKEY EEEEEEEEEECCCEE	24.57	24719451
148	Phosphorylation	HFNEREASRVVRDVA CCCHHHHHHHHHHHH	22.36	21659604
164 (in isoform 2)	Ubiquitination	-	44.82	-
191	Phosphorylation	AAPTSLGSSDPPTSA CCCCCCCCCCCCCCH	36.54	16162500
221	Phosphorylation	PENILCESPEKVSPV HHHCEECCCCCCCCC	37.04	23401153
226	Phosphorylation	CESPEKVSPVKICDF ECCCCCCCCCEECEE	34.74	29255136
237	Phosphorylation	ICDFDLGSGMKLNNS ECEEECCCCCEECCC	42.91	-
239	Sulfoxidation	DFDLGSGMKLNNSCT EEECCCCCEECCCCC	4.83	21406390
249	Phosphorylation	NNSCTPITTPELTTP CCCCCCCCCCCCCCC	37.19	26074081
250	Phosphorylation	NSCTPITTPELTTPC CCCCCCCCCCCCCCC	18.58	16982703
254	Phosphorylation	PITTPELTTPCGSAE CCCCCCCCCCCCCCH	27.34	27251275
255	Phosphorylation	ITTPELTTPCGSAEY CCCCCCCCCCCCCHH	29.25	16982703
286	Phosphorylation	DKRCDLWSLGVVLYI CCCHHHHHHHHHHHH	23.65	22210691
296	Phosphorylation	VVLYIMLSGYPPFVG HHHHHHHHCCCCCCC	20.92	22210691
332	Ubiquitination	FESIQEGKYEFPDKD HHHHHCCCCCCCCCC	40.63	-
338	Ubiquitination	GKYEFPDKDWAHISS CCCCCCCCCCHHHCH	56.24	-
353	Ubiquitination	EAKDLISKLLVRDAK HHHHHHHHHHHHHHH	38.56	-
385	Phosphorylation	APEKGLPTPQVLQRN CCCCCCCCHHHHHCC	31.25	28555341
393	Phosphorylation	PQVLQRNSSTMDLTL HHHHHCCCCHHHHHH	29.40	27251275
394	Phosphorylation	QVLQRNSSTMDLTLF HHHHCCCCHHHHHHH	31.16	28348404
395	Phosphorylation	VLQRNSSTMDLTLFA HHHCCCCHHHHHHHH	17.96	28348404
413	Phosphorylation	IALNRQLSQHEENEL HHHHHHHHHHHHHHH	22.58	26657352
433	Phosphorylation	ALADGLCSMKLSPPC HHHHCHHHCCCCHHH	24.80	28450419
437	Phosphorylation	GLCSMKLSPPCKSRL CHHHCCCCHHHHHHH	22.68	22617229
455	Methylation	RALAQAGRGEDRSPP HHHHHCCCCCCCCCC	48.63	54557395
459	Methylation	QAGRGEDRSPPTAL- HCCCCCCCCCCCCC-	46.92	115388429
460	Phosphorylation	AGRGEDRSPPTAL-- CCCCCCCCCCCCC--	47.77	23401153
463	Phosphorylation	GEDRSPPTAL----- CCCCCCCCCC-----	43.93	28450419

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
209	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
214	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
250	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
255	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
255	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
353	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
353	S	Phosphorylation	Kinase	SGK1	O00141	PSP
385	T	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
250	T	Phosphorylation	11463832
Dual phosphorylation of Thr-250 and Thr-255 activates the kinase.
255	T	Phosphorylation	11463832
Dual phosphorylation of Thr-250 and Thr-255 activates the kinase.
385	T	Phosphorylation	11463832
Phosphorylation of Thr-385 activates the kinase.

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 MKNK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK01_HUMAN	MAPK1	physical	9155017
IF4E_HUMAN	EIF4E	physical	9878069
IF4G1_HUMAN	EIF4G1	physical	9878069
IF4G2_HUMAN	EIF4G2	physical	9878069
CBP_HUMAN	CREBBP	physical	20936779
HS90B_HUMAN	HSP90AB1	physical	20936779
PRKDC_HUMAN	PRKDC	physical	20936779
DNJC7_HUMAN	DNAJC7	physical	20936779
IF4G3_HUMAN	EIF4G3	physical	21900206
DDAH2_HUMAN	DDAH2	physical	21900206
ATX3_HUMAN	ATXN3	physical	21900206
UB2D1_HUMAN	UBE2D1	physical	21900206
PHAX_HUMAN	PHAX	physical	21900206
SPY2_HUMAN	SPRY2	physical	16479008
A4_HUMAN	APP	physical	21832049
RCN3_HUMAN	RCN3	physical	21988832
TNIP2_HUMAN	TNIP2	physical	21988832
PAK2_HUMAN	PAK2	physical	25241761
MK01_HUMAN	MAPK1	physical	10922375
MK14_HUMAN	MAPK14	physical	10922375

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 MKNK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-460, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Negative regulation of protein translation by mitogen-activatedprotein kinase-interacting kinases 1 and 2."; Knauf U., Tschopp C., Gram H.; Mol. Cell. Biol. 21:5500-5511(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION ATTHR-250; THR-255 AND THR-385, AND MUTAGENESIS OF LYS-78; ASP-232;THR-250; THR-255 AND THR-385.	11463832 [Abstract]

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