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Q9HBH9 (MKNK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MKNK2
Synonyms:GPRK7, MNK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15 Ref.17 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.6

Cofactor

Magnesium. Ref.6

Binds 1 zinc ion per subunit.

Enzyme regulation

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. Ref.5 Ref.8 Ref.14 Ref.16 Ref.17 Ref.21

Subunit structure

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. Ref.1 Ref.5 Ref.7 Ref.15 Ref.20

Subcellular location

Isoform 2: NucleusPML body Ref.7.

Isoform 1: Cytoplasm Ref.7.

Tissue specificity

Ubiquitously expressed in all tissues examined. Isoform 2 is expressed at higher levels in the ovary than is isoform 1. Ref.1

Post-translational modification

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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.17

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Translation regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement PubMed 8415712. Source: ProtInc

cellular response to arsenic-containing substance

Inferred from direct assay Ref.10. Source: UniProtKB

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Inferred from direct assay Ref.18. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.6. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from direct assay Ref.6. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9HBH9-1)

Also known as: 2a;

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.
Isoform 2 Ref.1 (identifier: Q9HBH9-2)

Also known as: 2b;

The sequence of this isoform differs from the canonical sequence as follows:
     386-414: NSCAKDLTSFAAEAIAMNRQLAQHDEDLA → WDSHFLLPPHPCRIHVRPGGLVRTVTVNE
     415-465: Missing.
Isoform 3 Ref.1 (identifier: Q9HBH9-3)

The sequence of this isoform is not available.
Isoform 4 Ref.1 (identifier: Q9HBH9-4)

The sequence of this isoform is not available.
Isoform 5 Ref.1 (identifier: Q9HBH9-5)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465MAP kinase-interacting serine/threonine-protein kinase 2
PRO_0000086336

Regions

Domain84 – 388305Protein kinase
Nucleotide binding90 – 989ATP By similarity
Region160 – 1623Staurosporine binding
Motif60 – 667Nuclear localization signal
Motif444 – 4485MAP kinase binding By similarity

Sites

Active site2051Proton acceptor By similarity
Metal binding2991Zinc
Metal binding3111Zinc
Metal binding3141Zinc
Binding site1131ATP By similarity
Binding site2091Staurosporine

Amino acid modifications

Modified residue741Phosphoserine By similarity
Modified residue2441Phosphothreonine Ref.6
Modified residue2491Phosphothreonine Ref.6
Modified residue3791Phosphothreonine Ref.6
Modified residue4371Phosphoserine By similarity
Modified residue4401Phosphoserine By similarity
Modified residue4521Phosphoserine By similarity

Natural variations

Alternative sequence386 – 41429NSCAK…DEDLA → WDSHFLLPPHPCRIHVRPGG LVRTVTVNE in isoform 2.
VSP_007353
Alternative sequence415 – 46551Missing in isoform 2.
VSP_007354
Natural variant101Q → K.
Corresponds to variant rs3746101 [ dbSNP | Ensembl ].
VAR_051648
Natural variant731D → N. Ref.22
Corresponds to variant rs56158214 [ dbSNP | Ensembl ].
VAR_040805
Natural variant4281R → Q.
Corresponds to variant rs34475638 [ dbSNP | Ensembl ].
VAR_051649

Experimental info

Mutagenesis2281D → G: Reduced phosphorylation. Ref.21
Mutagenesis2441T → A: Loss of kinase activity; when associated with T-249. Ref.6
Mutagenesis2491T → A: Loss of kinase activity; when associated with T-244. Ref.6
Mutagenesis3791T → D: Constitutively active. Ref.6
Sequence conflict2611V → L in AAF17226. Ref.2

Secondary structure

.................................................. 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (2a) [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: D6D4BE6C541012B1

FASTA46551,875
        10         20         30         40         50         60 
MVQKKPAELQ GFHRSFKGQN PFELAFSLDQ PDHGDSDFGL QCSARPDMPA SQPIDIPDAK 

        70         80         90        100        110        120 
KRGKKKKRGR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT CINLITSQEY AVKIIEKQPG 

       130        140        150        160        170        180 
HIRSRVFREV EMLYQCQGHR NVLELIEFFE EEDRFYLVFE KMRGGSILSH IHKRRHFNEL 

       190        200        210        220        230        240 
EASVVVQDVA SALDFLHNKG IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS 

       250        260        270        280        290        300 
PISTPELLTP CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGRCG 

       310        320        330        340        350        360 
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWAHISCA AKDLISKLLV RDAKQRLSAA 

       370        380        390        400        410        420 
QVLQHPWVQG CAPENTLPTP MVLQRNSCAK DLTSFAAEAI AMNRQLAQHD EDLAEEEAAG 

       430        440        450        460 
QGQPVLVRAT SRCLQLSPPS QSKLAQRRQR ASLSSAPVVL VGDHA 

« Hide

Isoform 2 (2b) [UniParc].

Checksum: BA5E7C107CB3FD43
Show »

FASTA41446,711
Isoform 3 (Sequence not available).
Isoform 4 (Sequence not available).
Isoform 5 (Sequence not available).

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Regulation of arsenic trioxide-induced cellular responses by Mnk1 and Mnk2."
Dolniak B., Katsoulidis E., Carayol N., Altman J.K., Redig A.J., Tallman M.S., Ueda T., Watanabe-Fukunaga R., Fukunaga R., Platanias L.C.
J. Biol. Chem. 283:12034-12042(2008) [PubMed] [Europe PMC] [Abstract]
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]"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) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237775 mRNA. Translation: AAG26336.1.
AF237776 mRNA. Translation: AAG26337.1.
AF125532 mRNA. Translation: AAF17226.1.
BC073140 mRNA. Translation: AAH73140.1.
RefSeqNP_060042.2. NM_017572.3.
NP_951009.1. NM_199054.2.
UniGeneHs.515032.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AC3X-ray2.10A72-385[»]
2AC5X-ray3.20A72-385[»]
2HW7X-ray2.71A72-385[»]
ProteinModelPortalQ9HBH9.
SMRQ9HBH9. Positions 71-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109130. 13 interactions.
IntActQ9HBH9. 5 interactions.
STRING9606.ENSP00000250896.

Chemistry

BindingDBQ9HBH9.
ChEMBLCHEMBL4204.
GuidetoPHARMACOLOGY2105.

PTM databases

PhosphoSiteQ9HBH9.

Polymorphism databases

DMDM90102033.

Proteomic databases

PaxDbQ9HBH9.
PRIDEQ9HBH9.

Protocols and materials databases

DNASU2872.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250896; ENSP00000250896; ENSG00000099875. [Q9HBH9-1]
ENST00000309340; ENSP00000309485; ENSG00000099875. [Q9HBH9-2]
ENST00000591601; ENSP00000467811; ENSG00000099875. [Q9HBH9-1]
GeneID2872.
KEGGhsa:2872.
UCSCuc002lur.2. human. [Q9HBH9-2]
uc002lus.2. human. [Q9HBH9-1]

Organism-specific databases

CTD2872.
GeneCardsGC19M002037.
HGNCHGNC:7111. MKNK2.
HPACAB037253.
HPA021875.
HPA053989.
MIM605069. gene.
neXtProtNX_Q9HBH9.
PharmGKBPA30830.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG106949.
InParanoidQ9HBH9.
KOK04372.
OMAEPCHTCQ.
PhylomeDBQ9HBH9.

Enzyme and pathway databases

SignaLinkQ9HBH9.

Gene expression databases

ArrayExpressQ9HBH9.
BgeeQ9HBH9.
CleanExHS_MKNK2.
GenevestigatorQ9HBH9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9HBH9.
GeneWikiMKNK2.
GenomeRNAi2872.
NextBio11333.
PROQ9HBH9.
SOURCESearch...

Entry information

Entry nameMKNK2_HUMAN
AccessionPrimary (citable) accession number: Q9HBH9
Secondary accession number(s): Q6GPI3 expand/collapse secondary AC list , Q9HBH8, Q9UHR0, Q9Y2N6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM