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Q9HBH9 - MKNK2_HUMAN

UniProt

Q9HBH9 - MKNK2_HUMAN

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Protein

MAP kinase-interacting serine/threonine-protein kinase 2

Gene

MKNK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 As2O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 Publication
  • Zn2+Note: Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by CGP57380 and staurosporine. Activated by phosphorylation in a negative-feedback regulatory manner in response to chemotherapy (e.g. cytarabine) and thus impairs the generation of antileukemic responses.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131ATPPROSITE-ProRule annotation
Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation
Binding sitei209 – 2091Staurosporine1 Publication
Metal bindingi299 – 2991Zinc2 Publications
Metal bindingi311 – 3111Zinc2 Publications
Metal bindingi314 – 3141Zinc2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 989ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. cellular response to arsenic-containing substance Source: UniProtKB
  3. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  4. hemopoiesis Source: UniProtKB
  5. intracellular signal transduction Source: UniProtKB
  6. protein phosphorylation Source: UniProtKB
  7. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Translation regulation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9HBH9.

Names & Taxonomyi

Protein namesi
Recommended name:
MAP kinase-interacting serine/threonine-protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
MAP kinase signal-integrating kinase 2
Short name:
MAPK signal-integrating kinase 2
Short name:
Mnk2
Gene namesi
Name:MKNK2
Synonyms:GPRK7, MNK2
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:7111. MKNK2.

Subcellular locationi

Isoform 2 : Nucleus › PML body
Isoform 1 : Cytoplasm

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleolus Source: HPA
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
  5. PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281D → G: Reduced phosphorylation. 1 Publication
Mutagenesisi244 – 2441T → A: Loss of kinase activity; when associated with T-249. 1 Publication
Mutagenesisi249 – 2491T → A: Loss of kinase activity; when associated with T-244. 1 Publication
Mutagenesisi379 – 3791T → D: Constitutively active. 1 Publication

Organism-specific databases

PharmGKBiPA30830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465MAP kinase-interacting serine/threonine-protein kinase 2PRO_0000086336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei249 – 2491Phosphothreonine1 Publication
Modified residuei379 – 3791Phosphothreonine1 Publication
Modified residuei437 – 4371PhosphoserineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity
Modified residuei452 – 4521PhosphoserineBy similarity

Post-translational modificationi

Dual phosphorylation of Thr-244 and Thr-249 activates the kinase. Phosphorylation of Thr-379 activates the kinase. Phosphorylated upon arsenic trioxide As2O3 treatment. Phosphorylated by MAPK1/ERK2, MAPK11 and MAPK14. Dephosphorylated by PP2A.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HBH9.
PaxDbiQ9HBH9.
PRIDEiQ9HBH9.

PTM databases

PhosphoSiteiQ9HBH9.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissues examined. Isoform 2 is expressed at higher levels in the ovary than is isoform 1.1 Publication

Gene expression databases

BgeeiQ9HBH9.
CleanExiHS_MKNK2.
ExpressionAtlasiQ9HBH9. baseline and differential.
GenevestigatoriQ9HBH9.

Organism-specific databases

HPAiCAB037253.
HPA021875.
HPA053989.

Interactioni

Subunit structurei

Monomer. Interacts with the C-terminal regions of EIF4G1 and EIF4G2; this interaction is promoted when MAPK pathways are repressed but repressed upon ERK proteins activation. Also binds to dephosphorylated MAPK3/ERK1 and MAPK1/ERK2. Isoform 1 interaction with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects it from dephosphorylation and inactivation. Isoform 2 interacts with ESR2 and EIF4E in the nucleus.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK14Q165393EBI-2864341,EBI-73946

Protein-protein interaction databases

BioGridi109130. 12 interactions.
IntActiQ9HBH9. 6 interactions.
STRINGi9606.ENSP00000250896.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi74 – 763Combined sources
Turni79 – 813Combined sources
Beta strandi83 – 853Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi109 – 1168Combined sources
Helixi123 – 13513Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi154 – 1607Combined sources
Helixi167 – 1748Combined sources
Helixi179 – 19820Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi221 – 2244Combined sources
Helixi254 – 2563Combined sources
Helixi259 – 2646Combined sources
Helixi267 – 2726Combined sources
Helixi273 – 2753Combined sources
Helixi276 – 29015Combined sources
Helixi312 – 32413Combined sources
Helixi331 – 3344Combined sources
Helixi339 – 34810Combined sources
Turni353 – 3553Combined sources
Helixi359 – 3646Combined sources
Turni366 – 3683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AC3X-ray2.10A72-385[»]
2AC5X-ray3.20A72-385[»]
2HW7X-ray2.71A72-385[»]
ProteinModelPortaliQ9HBH9.
SMRiQ9HBH9. Positions 71-413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HBH9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 388305Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1623Staurosporine binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi60 – 667Nuclear localization signal
Motifi444 – 4485MAP kinase bindingBy similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOVERGENiHBG106949.
InParanoidiQ9HBH9.
KOiK04372.
OMAiVQKKTAE.
PhylomeDBiQ9HBH9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9HBH9-1) [UniParc]FASTAAdd to Basket

Also known as: 2a1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVQKKPAELQ GFHRSFKGQN PFELAFSLDQ PDHGDSDFGL QCSARPDMPA 
        60         70         80         90        100
SQPIDIPDAK KRGKKKKRGR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT 
       110        120        130        140        150
CINLITSQEY AVKIIEKQPG HIRSRVFREV EMLYQCQGHR NVLELIEFFE 
       160        170        180        190        200
EEDRFYLVFE KMRGGSILSH IHKRRHFNEL EASVVVQDVA SALDFLHNKG 
       210        220        230        240        250
IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS PISTPELLTP 
       260        270        280        290        300
CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGRCG 
       310        320        330        340        350
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWAHISCA AKDLISKLLV 
       360        370        380        390        400
RDAKQRLSAA QVLQHPWVQG CAPENTLPTP MVLQRNSCAK DLTSFAAEAI 
       410        420        430        440        450
AMNRQLAQHD EDLAEEEAAG QGQPVLVRAT SRCLQLSPPS QSKLAQRRQR 
       460 
ASLSSAPVVL VGDHA
Length:465
Mass (Da):51,875
Last modified:March 7, 2006 - v3
Checksum:iD6D4BE6C541012B1
GO
Isoform 21 Publication (identifier: Q9HBH9-2) [UniParc]FASTAAdd to Basket

Also known as: 2b1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     386-414: NSCAKDLTSFAAEAIAMNRQLAQHDEDLA → WDSHFLLPPHPCRIHVRPGGLVRTVTVNE
     415-465: Missing.

Show »
Length:414
Mass (Da):46,711
Checksum:iBA5E7C107CB3FD43
GO
Isoform 31 Publication (identifier: Q9HBH9-3)

Sequence is not available
Length:–
Mass (Da):–
Isoform 41 Publication (identifier: Q9HBH9-4)

Sequence is not available
Length:–
Mass (Da):–
Isoform 51 Publication (identifier: Q9HBH9-5)

Sequence is not available
Length:–
Mass (Da):–

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611V → L in AAF17226. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101Q → K.
Corresponds to variant rs3746101 [ dbSNP | Ensembl ].		VAR_051648
Natural varianti73 – 731D → N.1 Publication
Corresponds to variant rs56158214 [ dbSNP | Ensembl ].		VAR_040805
Natural varianti428 – 4281R → Q.
Corresponds to variant rs34475638 [ dbSNP | Ensembl ].		VAR_051649

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei386 – 41429NSCAK…DEDLA → WDSHFLLPPHPCRIHVRPGG LVRTVTVNE in isoform 2. 3 PublicationsVSP_007353Add
BLAST
Alternative sequencei415 – 46551Missing in isoform 2. 3 PublicationsVSP_007354Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237775 mRNA. Translation: AAG26336.1.
AF237776 mRNA. Translation: AAG26337.1.
AF125532 mRNA. Translation: AAF17226.1.
BC073140 mRNA. Translation: AAH73140.1.
CCDSiCCDS12079.1. [Q9HBH9-2]
CCDS12080.1. [Q9HBH9-1]
RefSeqiNP_060042.2. NM_017572.3. [Q9HBH9-2]
NP_951009.1. NM_199054.2. [Q9HBH9-1]
UniGeneiHs.515032.

Genome annotation databases

GeneIDi2872.
KEGGihsa:2872.
UCSCiuc002lur.2. human. [Q9HBH9-2]
uc002lus.2. human. [Q9HBH9-1]

Polymorphism databases

DMDMi90102033.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237775 mRNA. Translation: AAG26336.1.
AF237776 mRNA. Translation: AAG26337.1.
AF125532 mRNA. Translation: AAF17226.1.
BC073140 mRNA. Translation: AAH73140.1.
CCDSiCCDS12079.1. [Q9HBH9-2]
CCDS12080.1. [Q9HBH9-1]
RefSeqiNP_060042.2. NM_017572.3. [Q9HBH9-2]
NP_951009.1. NM_199054.2. [Q9HBH9-1]
UniGeneiHs.515032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AC3X-ray2.10A72-385[»]
2AC5X-ray3.20A72-385[»]
2HW7X-ray2.71A72-385[»]
ProteinModelPortaliQ9HBH9.
SMRiQ9HBH9. Positions 71-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109130. 12 interactions.
IntActiQ9HBH9. 6 interactions.
STRINGi9606.ENSP00000250896.

Chemistry

BindingDBiQ9HBH9.
ChEMBLiCHEMBL4204.
GuidetoPHARMACOLOGYi2105.

PTM databases

PhosphoSiteiQ9HBH9.

Polymorphism databases

DMDMi90102033.

Proteomic databases

MaxQBiQ9HBH9.
PaxDbiQ9HBH9.
PRIDEiQ9HBH9.

Protocols and materials databases

DNASUi2872.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2872.
KEGGihsa:2872.
UCSCiuc002lur.2. human. [Q9HBH9-2]
uc002lus.2. human. [Q9HBH9-1]

Organism-specific databases

CTDi2872.
GeneCardsiGC19M002037.
HGNCiHGNC:7111. MKNK2.
HPAiCAB037253.
HPA021875.
HPA053989.
MIMi605069. gene.
neXtProtiNX_Q9HBH9.
PharmGKBiPA30830.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOVERGENiHBG106949.
InParanoidiQ9HBH9.
KOiK04372.
OMAiVQKKTAE.
PhylomeDBiQ9HBH9.

Enzyme and pathway databases

SignaLinkiQ9HBH9.

Miscellaneous databases

ChiTaRSiMKNK2. human.
EvolutionaryTraceiQ9HBH9.
GeneWikiiMKNK2.
GenomeRNAii2872.
NextBioi11333.
PROiQ9HBH9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBH9.
CleanExiHS_MKNK2.
ExpressionAtlasiQ9HBH9. baseline and differential.
GenevestigatoriQ9HBH9.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta."
    Slentz-Kesler K., Moore J.T., Lombard M., Zhang J., Hollingsworth R., Weiner M.P.
    Genomics 69:63-71(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY, INTERACTION WITH ESR2.
    Tissue: Fetal brain.
  2. "A novel gene expressed in human adrenal gland."
    Li Y., Shi J., Huang C., Ren S., Fu S., Zhou J., Yu Y., Xu S., Wang Y., Fu G., Chen Z., Han Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adrenal gland.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  5. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
    Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
    Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS EIF4E KINASE, ENZYME REGULATION, ALTERNATIVE SPLICING, PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14, INTERACTION WITH EIF4G PROTEINS.
  6. "Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2."
    Knauf U., Tschopp C., Gram H.
    Mol. Cell. Biol. 21:5500-5511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-244; THR-249 AND THR-379, MUTAGENESIS OF THR-244; THR-249 AND THR-379.
    Tissue: Leukocyte.
  7. "The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization."
    Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B., Vertegaal A.C.O., Han Z.-G., Proud C.G.
    Mol. Cell. Biol. 23:5692-5705(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS EIF4E KINASE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH EIF4E; EIF4G1 AND EIF4G2.
  8. "The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1."
    Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., Bain J., Espel E., Proud C.G.
    Immunity 23:177-189(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS HNRNPA1 KINASE, ENZYME REGULATION.
  9. "The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha."
    Buxade M., Morrice N., Krebs D.L., Proud C.G.
    J. Biol. Chem. 283:57-65(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SFPQ/PSF KINASE.
  10. Cited for: FUNCTION IN ARSENIC TRIOXIDE SIGNALING, PHOSPHORYLATION IN RESPONSE TO ARSENIC TRIOXIDE.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Discovery of mitogen-activated protein kinase-interacting kinase 1 inhibitors by a comprehensive fragment-oriented virtual screening approach."
    Oyarzabal J., Zarich N., Albarran M.I., Palacios I., Urbano-Cuadrado M., Mateos G., Reymundo I., Rabal O., Salgado A., Corrionero A., Fominaya J., Pastor J., Bischoff J.R.
    J. Med. Chem. 53:6618-6628(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  15. "Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G interaction."
    Shveygert M., Kaiser C., Bradrick S.S., Gromeier M.
    Mol. Cell. Biol. 30:5160-5167(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS EIF4E KINASE, INTERACTION WITH EIF4G1.
  16. "Negative regulatory effects of Mnk kinases in the generation of chemotherapy-induced antileukemic responses."
    Altman J.K., Glaser H., Sassano A., Joshi S., Ueda T., Watanabe-Fukunaga R., Fukunaga R., Tallman M.S., Platanias L.C.
    Mol. Pharmacol. 78:778-784(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  17. "Protein phosphatase 2A negatively regulates eukaryotic initiation factor 4E phosphorylation and eIF4F assembly through direct dephosphorylation of Mnk and eIF4E."
    Li Y., Yue P., Deng X., Ueda T., Fukunaga R., Khuri F.R., Sun S.-Y.
    Neoplasia 12:848-855(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EIF4E PHOSPHORYLATION REGULATION, DEPHOSPHORYLATION BY PP2A, ENZYME REGULATION.
  18. "Essential role for Mnk kinases in type II interferon (IFNgamma) signaling and its suppressive effects on normal hematopoiesis."
    Joshi S., Sharma B., Kaur S., Majchrzak B., Ueda T., Fukunaga R., Verma A.K., Fish E.N., Platanias L.C.
    J. Biol. Chem. 286:6017-6026(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IFNGAMMA SIGNALING.
  19. "The Mnks: MAP kinase-interacting kinases (MAP kinase signal-integrating kinases)."
    Buxade M., Parra-Palau J.L., Proud C.G.
    Front. Biosci. 13:5359-5373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site."
    Jauch R., Jaekel S., Netter C., Schreiter K., Aicher B., Jaeckle H., Wahl M.C.
    Structure 13:1559-1568(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC, SUBUNIT.
  21. "Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment."
    Jauch R., Cho M.-K., Jaekel S., Netter C., Schreiter K., Aicher B., Zweckstetter M., Jaeckle H., Wahl M.C.
    EMBO J. 25:4020-4032(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC AND STAUROSPORINE, ENZYME REGULATION, MUTAGENESIS OF ASP-228.
  22. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-73.
+Additional computationally mapped references.

Entry informationi

Entry nameiMKNK2_HUMAN
AccessioniPrimary (citable) accession number: Q9HBH9
Secondary accession number(s): Q6GPI3
, Q9HBH8, Q9UHR0, Q9Y2N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 7, 2006
Last modified: February 4, 2015
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.