MKNK2_HUMAN - dbPTM
MKNK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MKNK2_HUMAN
UniProt AC Q9HBH9
Protein Name MAP kinase-interacting serine/threonine-protein kinase 2
Gene Name MKNK2
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Isoform 2: Nucleus, PML body.
Isoform 1: Cytoplasm.
Protein Description Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. 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. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal..
Protein Sequence MVQKKPAELQGFHRSFKGQNPFELAFSLDQPDHGDSDFGLQCSARPDMPASQPIDIPDAKKRGKKKKRGRATDSFSGRFEDVYQLQEDVLGEGAHARVQTCINLITSQEYAVKIIEKQPGHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILSHIHKRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNGDCSPISTPELLTPCGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGYPPFVGRCGSDCGWDRGEACPACQNMLFESIQEGKYEFPDKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWVQGCAPENTLPTPMVLQRNSCAKDLTSFAAEAIAMNRQLAQHDEDLAEEEAAGQGQPVLVRATSRCLQLSPPSQSKLAQRRQRASLSSAPVVLVGDHA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Sumoylation---MVQKKPAELQGF
---CCCCCHHHHCCC		32.16-
5Sumoylation---MVQKKPAELQGF
---CCCCCHHHHCCC		32.16-
15PhosphorylationELQGFHRSFKGQNPF
HHCCCCHHCCCCCCE		23.8127282143
27PhosphorylationNPFELAFSLDQPDHG
CCEEEEEEECCCCCC		25.9811154262
36PhosphorylationDQPDHGDSDFGLQCS
CCCCCCCCCCCCCCC		39.1628348404
43PhosphorylationSDFGLQCSARPDMPA
CCCCCCCCCCCCCCC		17.8528348404
51PhosphorylationARPDMPASQPIDIPD
CCCCCCCCCCCCCCC		30.5328348404
72PhosphorylationKKKRGRATDSFSGRF
CCCCCCCCCCCCCCH		30.7123312004
74PhosphorylationKRGRATDSFSGRFED
CCCCCCCCCCCCHHH		19.5629255136
76PhosphorylationGRATDSFSGRFEDVY
CCCCCCCCCCHHHHH		32.7725850435
83PhosphorylationSGRFEDVYQLQEDVL
CCCHHHHHHHHHHHH		18.8127642862
169PhosphorylationMRGGSILSHIHKRRH
CCCCCHHHHHHHHHC		20.8028348404
173UbiquitinationSILSHIHKRRHFNEL
CHHHHHHHHHCCCCC		50.99-
207SumoylationGIAHRDLKPENILCE
CCCCCCCCHHHEEEC		55.35-
207UbiquitinationGIAHRDLKPENILCE
CCCCCCCCHHHEEEC		55.35-
207SumoylationGIAHRDLKPENILCE
CCCCCCCCHHHEEEC		55.35-
220PhosphorylationCEHPNQVSPVKICDF
ECCCCCCCCEEECCE		17.7630576142
223UbiquitinationPNQVSPVKICDFDLG
CCCCCCEEECCEECC		40.79-
231PhosphorylationICDFDLGSGIKLNGD
ECCEECCCCCEECCC		44.6428348404
244PhosphorylationGDCSPISTPELLTPC
CCCCCCCCCHHHCCC		22.8511463832
249PhosphorylationISTPELLTPCGSAEY
CCCCHHHCCCCCHHH		29.2011463832
326 (in isoform 2)Ubiquitination-40.6321906983
326UbiquitinationFESIQEGKYEFPDKD
HHHHHCCCCCCCCCC		40.632190698
326 (in isoform 1)Ubiquitination-40.6321906983
342UbiquitinationAHISCAAKDLISKLL
HHHHHHHHHHHHHHH		34.24-
347UbiquitinationAAKDLISKLLVRDAK
HHHHHHHHHHHHHHH		38.56-
379PhosphorylationAPENTLPTPMVLQRN
CCCCCCCCCHHCCCC		27.4211463832
379 (in isoform 2)Phosphorylation-27.4211154262
390UbiquitinationLQRNSCAKDLTSFAA
CCCCCCHHHHHHHHH		58.56-
430PhosphorylationQPVLVRATSRCLQLS
CCEEEEEECHHHHCC		13.2122199227
431PhosphorylationPVLVRATSRCLQLSP
CEEEEEECHHHHCCC		21.7330576142
437PhosphorylationTSRCLQLSPPSQSKL
ECHHHHCCCCCHHHH		23.0825159151
440PhosphorylationCLQLSPPSQSKLAQR
HHHCCCCCHHHHHHH		50.9327794612
442PhosphorylationQLSPPSQSKLAQRRQ
HCCCCCHHHHHHHHH		33.6923403867
452PhosphorylationAQRRQRASLSSAPVV
HHHHHHHHHHCCCEE		30.8519664994
454PhosphorylationRRQRASLSSAPVVLV
HHHHHHHHCCCEEEE		23.2023927012
455PhosphorylationRQRASLSSAPVVLVG
HHHHHHHCCCEEEEC		41.7223927012
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
74SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
244TPhosphorylation

11463832
249TPhosphorylation

11463832
379TPhosphorylation

11463832
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 MKNK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4G1_HUMANEIF4G1physical
12897141
MK01_HUMANMAPK1physical
12897141
MK01_HUMANMAPK1physical
9155017
RL7A_HUMANRPL7Aphysical
20936779
RBX1_HUMANRBX1physical
16856496
VHL_HUMANVHLphysical
16856496
CUL2_HUMANCUL2physical
16856496
PFD3_HUMANVBP1physical
16856496
CSTF2_HUMANCSTF2physical
26496610
MIF_HUMANMIFphysical
26496610
RBM4_HUMANRBM4physical
26496610
VINC_HUMANVCLphysical
26496610
BAG6_HUMANBAG6physical
26496610
SYMPK_HUMANSYMPKphysical
26496610
FUBP2_HUMANKHSRPphysical
26496610
NOLC1_HUMANNOLC1physical
26496610
WDR46_HUMANWDR46physical
26496610
UBP15_HUMANUSP15physical
26496610
TRAP1_HUMANTRAP1physical
26496610
CELF1_HUMANCELF1physical
26496610
CPSF5_HUMANNUDT21physical
26496610
WWP2_HUMANWWP2physical
26496610
EXOC3_HUMANEXOC3physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
HAUS7_HUMANHAUS7physical
26496610
ADCK1_HUMANADCK1physical
26496610
RBM26_HUMANRBM26physical
26496610
BHE41_HUMANBHLHE41physical
26496610
TUT7_HUMANZCCHC6physical
26496610
ZMYM1_HUMANZMYM1physical
26496610
C99L2_HUMANCD99L2physical
26496610
RRFM_HUMANMRRFphysical
26496610
TCAM1_HUMANTICAM1physical
26496610
RICTR_HUMANRICTORphysical
26496610
MK01_HUMANMAPK1physical
10922375
MK14_HUMANMAPK14physical
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 MKNK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASSSPECTROMETRY.
"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: FUNCTION, PHOSPHORYLATION AT THR-244; THR-249 AND THR-379, ANDMUTAGENESIS OF THR-244; THR-249 AND THR-379.

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