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Protein

MAP kinase-interacting serine/threonine-protein kinase 2

Gene

Mknk2

Organism
Mus musculus (Mouse)
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. Enhances the formation of EIF4F complex in pachytene spermatocytes, thus promoting mRNA translation during spermatogenesis. Displays a high basal 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.7 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 Publication
  • Zn2+By similarityNote: Binds 1 zinc ion per monomer.By similarity

Enzyme regulationi

Inhibited by CGP57380 and staurosporine.2 Publications

Sites

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

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • cellular response to arsenic-containing substance Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • hemopoiesis Source: MGI
  • intracellular signal transduction Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • 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

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:Mnk2
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:894279. Mknk2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi238 – 2381D → A: Loss of activity. 1 Publication
Mutagenesisi438 – 4381L → A: Reduced phosphorylation. 1 Publication
Mutagenesisi440 – 4401Q → R: Reduced MAPK3/ERK1 and MAPK1/ERK2-binding. 1 Publication
Mutagenesisi446 – 4461S → A or D: Normal MAPK3/ERK1 and MAPK1/ERK2-binding. 1 Publication
Mutagenesisi448 – 4481S → A: Normal MAPK3/ERK1 and MAPK1/ER2K-binding. 1 Publication
Mutagenesisi448 – 4481S → D: Reduced MAPK3/ERK1 and MAPK1/ER2K-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459MAP kinase-interacting serine/threonine-protein kinase 2PRO_0000086337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineCombined sources1 Publication
Modified residuei244 – 2441PhosphothreonineBy similarity
Modified residuei249 – 2491PhosphothreonineBy similarity
Modified residuei379 – 3791PhosphothreonineBy similarity
Modified residuei431 – 4311Phosphoserine1 Publication
Modified residuei434 – 4341Phosphoserine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication
Modified residuei450 – 4501Phosphothreonine1 Publication

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 (By similarity). Dephosphorylated by PP2A.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CDB0.
PaxDbiQ8CDB0.
PRIDEiQ8CDB0.

PTM databases

iPTMnetiQ8CDB0.
PhosphoSiteiQ8CDB0.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissues examined, with high levels in skeletal muscle and low levels in brain.1 Publication

Gene expression databases

BgeeiQ8CDB0.
CleanExiMM_MKNK2.
ExpressionAtlasiQ8CDB0. baseline and differential.
GenevisibleiQ8CDB0. MM.

Interactioni

Subunit structurei

Interacts with ESR2 and EIF4E in the nucleus (By similarity). 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. Interaction with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects it from dephosphorylation and inactivation.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk1P6308523EBI-646209,EBI-397697
Traf2P394293EBI-646209,EBI-520016

Protein-protein interaction databases

BioGridi201432. 2 interactions.
IntActiQ8CDB0. 3 interactions.
MINTiMINT-1524069.
STRINGi10090.ENSMUSP00000003433.

Structurei

3D structure databases

ProteinModelPortaliQ8CDB0.
SMRiQ8CDB0. Positions 71-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 368285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi60 – 667Nuclear localization signalBy similarity
Motifi438 – 4425MAP kinase binding

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0607. Eukaryota.
ENOG410XQA9. LUCA.
GeneTreeiENSGT00830000128274.
HOGENOMiHOG000231140.
HOVERGENiHBG106949.
InParanoidiQ8CDB0.
KOiK04372.
OMAiVQKKTAE.
OrthoDBiEOG7SV0VB.
PhylomeDBiQ8CDB0.
TreeFamiTF314050.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q8CDB0-1) [UniParc]FASTAAdd to basket

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
MVQKRTAELQ GFHRSFKGQN PFELAFSLDL AQHRDSDFSP QCEARPDMPS
60 70 80 90 100
SQPIDIPDAK KRGRKKKRCR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT
110 120 130 140 150
CVNLITNQEY AVKIIEKQLG HIRSRVFREV EMLYQCQGHR NVLELIEFFE
160 170 180 190 200
EEDRFYLVFE KMRGGSILSH IHRRRHFNEL EASVVVQDVA SALDFLHNKG
210 220 230 240 250
IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS PISTPELLTP
260 270 280 290 300
CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGHCG
310 320 330 340 350
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWSHISFA AKDLISKLLV
360 370 380 390 400
RDAKQRLSAA QVLQHPWVQG CAPENTLPTP LVLQRNSCAK DLTSFAAEAI
410 420 430 440 450
AMNRQLAQCE EDAGQDQPVV IRATSRCLQL SPPSQSKLAQ RRQRASLSAT

PVVLVGDRA
Length:459
Mass (Da):51,633
Last modified:March 7, 2006 - v3
Checksum:i5252C711AD99729A
GO
Isoform 2 (identifier: Q8CDB0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-256: Missing.

Note: No experimental confirmation available.
Show »
Length:250
Mass (Da):27,770
Checksum:iF0B92AE4C5841C85
GO

Sequence cautioni

The sequence AAH10256.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB25570.2 differs from that shown. Reason: Frameshift at position 439. Curated
The sequence CAA71966.1 differs from that shown. Reason: Frameshift at position 31. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561Y → D in BAB25570 (PubMed:16141072).Curated
Sequence conflicti349 – 3491L → P in BAB25570 (PubMed:16141072).Curated
Sequence conflicti454 – 4541L → I in BAB25570 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 256209Missing in isoform 2. 1 PublicationVSP_007355Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB164081 mRNA. Translation: BAD18852.1.
AK008277 mRNA. Translation: BAB25570.2. Frameshift.
AK030830 mRNA. Translation: BAC27151.2.
AK154235 mRNA. Translation: BAE32453.1.
Y11092 mRNA. Translation: CAA71966.1. Frameshift.
BC010256 mRNA. Translation: AAH10256.1. Different initiation.
CCDSiCCDS24030.2. [Q8CDB0-1]
RefSeqiNP_067437.2. NM_021462.4. [Q8CDB0-1]
XP_006513379.1. XM_006513316.1. [Q8CDB0-1]
UniGeneiMm.42126.
Mm.486332.

Genome annotation databases

EnsembliENSMUST00000200082; ENSMUSP00000143508; ENSMUSG00000020190. [Q8CDB0-1]
GeneIDi17347.
KEGGimmu:17347.
UCSCiuc007gef.3. mouse. [Q8CDB0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB164081 mRNA. Translation: BAD18852.1.
AK008277 mRNA. Translation: BAB25570.2. Frameshift.
AK030830 mRNA. Translation: BAC27151.2.
AK154235 mRNA. Translation: BAE32453.1.
Y11092 mRNA. Translation: CAA71966.1. Frameshift.
BC010256 mRNA. Translation: AAH10256.1. Different initiation.
CCDSiCCDS24030.2. [Q8CDB0-1]
RefSeqiNP_067437.2. NM_021462.4. [Q8CDB0-1]
XP_006513379.1. XM_006513316.1. [Q8CDB0-1]
UniGeneiMm.42126.
Mm.486332.

3D structure databases

ProteinModelPortaliQ8CDB0.
SMRiQ8CDB0. Positions 71-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201432. 2 interactions.
IntActiQ8CDB0. 3 interactions.
MINTiMINT-1524069.
STRINGi10090.ENSMUSP00000003433.

PTM databases

iPTMnetiQ8CDB0.
PhosphoSiteiQ8CDB0.

Proteomic databases

EPDiQ8CDB0.
PaxDbiQ8CDB0.
PRIDEiQ8CDB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000200082; ENSMUSP00000143508; ENSMUSG00000020190. [Q8CDB0-1]
GeneIDi17347.
KEGGimmu:17347.
UCSCiuc007gef.3. mouse. [Q8CDB0-1]

Organism-specific databases

CTDi2872.
MGIiMGI:894279. Mknk2.

Phylogenomic databases

eggNOGiKOG0607. Eukaryota.
ENOG410XQA9. LUCA.
GeneTreeiENSGT00830000128274.
HOGENOMiHOG000231140.
HOVERGENiHBG106949.
InParanoidiQ8CDB0.
KOiK04372.
OMAiVQKKTAE.
OrthoDBiEOG7SV0VB.
PhylomeDBiQ8CDB0.
TreeFamiTF314050.

Miscellaneous databases

ChiTaRSiMknk2. mouse.
PROiQ8CDB0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CDB0.
CleanExiMM_MKNK2.
ExpressionAtlasiQ8CDB0. baseline and differential.
GenevisibleiQ8CDB0. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. "Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development."
    Ueda T., Watanabe-Fukunaga R., Fukuyama H., Nagata S., Fukunaga R.
    Mol. Cell. Biol. 24:6539-6549(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell, Small intestine and Thymus.
  3. "Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2."
    Waskiewicz A.J., Flynn A., Proud C.G., Cooper J.A.
    EMBO J. 16:1909-1920(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-459 (ISOFORM 1), FUNCTION, INTERACTION WITH MAPK3 AND MAPK1.
    Tissue: Embryo.
  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] OF 31-459 (ISOFORM 1).
    Strain: NMRI.
    Tissue: Mammary gland.
  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, PHOSPHORYLATION AT SER-74; SER-431; SER-434; SER-446 AND THR-450, PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14, INTERACTION WITH EIF4G PROTEINS.
  6. "Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties."
    Parra J.L., Buxade M., Proud C.G.
    J. Biol. Chem. 280:37623-37633(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK3/ERK1 AND MAPK1/ERK2, MUTAGENESIS OF ASP-238; LEU-438; GLN-440; SER-446 AND SER-448.
  7. "Loss of MNK function sensitizes fibroblasts to serum-withdrawal induced apoptosis."
    Chrestensen C.A., Eschenroeder A., Ross W.G., Ueda T., Watanabe-Fukunaga R., Fukunaga R., Sturgill T.W.
    Genes Cells 12:1133-1140(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SERUM-WITHDRAWAL INDUCED APOPTOSIS, ENZYME REGULATION.
  8. "Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation."
    Shenberger J.S., Zhang L., Hughlock M.K., Ueda T., Watanabe-Fukunaga R., Fukunaga R.
    Int. J. Biochem. Cell Biol. 39:1828-1842(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS EIF4E KINASE.
  9. "Differential contribution of the MTOR and MNK pathways to the regulation of mRNA translation in meiotic and postmeiotic mouse male germ cells."
    Messina V., Di Sauro A., Pedrotti S., Adesso L., Latina A., Geremia R., Rossi P., Sette C.
    Biol. Reprod. 83:607-615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA TRANSLATION REGULATION DURING SPERMATOGENESIS.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue.
  11. "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.
  12. "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.

Entry informationi

Entry nameiMKNK2_MOUSE
AccessioniPrimary (citable) accession number: Q8CDB0
Secondary accession number(s): O08606, Q75PY0, Q9D893
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 7, 2006
Last modified: June 8, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.