Q9HBH9 (MKNK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MKNK2
Synonyms:	GPRK7, MNK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Evidence 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: Nucleus › PML 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 process	Apoptosis Translation regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell 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 regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 465

465

MAP kinase-interacting serine/threonine-protein kinase 2

PRO_0000086336

Regions

Domain

84 – 388

305

Protein kinase

Nucleotide binding

90 – 98

9

ATP By similarity

Region

160 – 162

3

Staurosporine binding

Motif

60 – 66

7

Nuclear localization signal

Motif

444 – 448

5

MAP kinase binding By similarity

Sites

Active site

205

1

Proton acceptor By similarity

Metal binding

299

1

Zinc

Metal binding

311

1

Zinc

Metal binding

314

1

Zinc

Binding site

113

1

ATP By similarity

Binding site

209

1

Staurosporine

Amino acid modifications

Modified residue

74

1

Phosphoserine By similarity

Modified residue

244

1

Phosphothreonine Ref.6

Modified residue

249

1

Phosphothreonine Ref.6

Modified residue

379

1

Phosphothreonine Ref.6

Modified residue

437

1

Phosphoserine By similarity

Modified residue

440

1

Phosphoserine By similarity

Natural variations

Alternative sequence

386 – 414

29

NSCAK…DEDLA → WDSHFLLPPHPCRIHVRPGG LVRTVTVNE in isoform 2.

VSP_007353

Alternative sequence

415 – 465

51

Missing in isoform 2.

VSP_007354

Natural variant

10

1

Q → K.
Corresponds to variant rs3746101 [ dbSNP | Ensembl ].

VAR_051648

Natural variant

73

1

D → N. Ref.22
Corresponds to variant rs56158214 [ dbSNP | Ensembl ].

VAR_040805

Natural variant

428

1

R → Q.
Corresponds to variant rs34475638 [ dbSNP | Ensembl ].

VAR_051649

Experimental info

Mutagenesis

228

1

D → G: Reduced phosphorylation. Ref.21

Mutagenesis

244

1

T → A: Loss of kinase activity; when associated with T-249. Ref.6

Mutagenesis

249

1

T → A: Loss of kinase activity; when associated with T-244. Ref.6

Mutagenesis

379

1

T → D: Constitutively active. Ref.6

Sequence conflict

261

1

V → L in AAF17226. Ref.2

Secondary structure

1

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465

Helix Strand Turn

Details...

Beta strand

74 – 76

3

Turn

79 – 81

3

Beta strand

83 – 85

3

Beta strand

94 – 102

9

Beta strand

104 – 106

3

Beta strand

109 – 116

8

Helix

123 – 135

13

Beta strand

145 – 151

7

Beta strand

154 – 160

7

Helix

167 – 174

8

Helix

179 – 198

20

Helix

208 – 210

3

Beta strand

211 – 214

4

Beta strand

216 – 219

4

Beta strand

221 – 224

4

Helix

254 – 256

3

Helix

259 – 264

6

Helix

267 – 272

6

Helix

273 – 275

3

Helix

276 – 290

15

Helix

312 – 324

13

Helix

331 – 334

4

Helix

339 – 348

10

Turn

353 – 355

3

Helix

359 – 364

6

Turn

366 – 368

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (2a) [UniParc]. Last modified March 7, 2006. Version 3. Checksum: D6D4BE6C541012B1	FASTA	465	51,875
	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
	Isoform 2 (2b) [UniParc]. Checksum: BA5E7C107CB3FD43	FASTA	414	46,711
	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 QVLQHPWVQG CAPENTLPTP MVLQRWDSHF LLPPHPCRIH VRPGGLVRTV TVNE
	Isoform 3 (Sequence not available).		–	–
	Isoform 4 (Sequence not available).		–	–
	Isoform 5 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

RefSeq

NP_060042.2. NM_017572.3.
NP_951009.1. NM_199054.2.

UniGene

Hs.515032.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AC3	X-ray	2.10	A	72-385	[»]
2AC5	X-ray	3.20	A	72-385	[»]
2HW7	X-ray	2.71	A	72-385	[»]

ProteinModelPortal

Q9HBH9.

SMR

Q9HBH9. Positions 71-369.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

109130. 13 interactions.

IntAct

Q9HBH9. 5 interactions.

STRING

9606.ENSP00000250896.

Chemistry

BindingDB

Q9HBH9.

ChEMBL

CHEMBL4204.

GuidetoPHARMACOLOGY

2105.

PTM databases

PhosphoSite

Q9HBH9.

Polymorphism databases

DMDM

90102033.

Proteomic databases

PaxDb

Q9HBH9.

PRIDE

Q9HBH9.

Protocols and materials databases

DNASU

2872.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250896; ENSP00000250896; ENSG00000099875.
ENST00000309340; ENSP00000309485; ENSG00000099875.
ENST00000591601; ENSP00000467811; ENSG00000099875.

GeneID

2872.

KEGG

hsa:2872.

UCSC

uc002lus.2. human.

Organism-specific databases

CTD

2872.

GeneCards

GC19M002037.

HGNC

HGNC:7111. MKNK2.

HPA

CAB037253.
HPA021875.
HPA053989.

MIM

605069. gene.

neXtProt

NX_Q9HBH9.

PharmGKB

PA30830.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG106949.

InParanoid

Q9HBH9.

KO

K04372.

OMA

EPCHTCQ.

PhylomeDB

Q9HBH9.

Enzyme and pathway databases

SignaLink

Q9HBH9.

Gene expression databases

ArrayExpress

Q9HBH9.

Bgee

Q9HBH9.

CleanEx

HS_MKNK2.

Genevestigator

Q9HBH9.

Family and domain databases

InterPro

IPR011009. 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]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. SSF56112. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9HBH9.

GeneWiki

MKNK2.

GenomeRNAi

2872.

NextBio

11333.

PRO

Q9HBH9.

SOURCE

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Entry information

Entry name

MKNK2_HUMAN

Accession

Primary (citable) accession number: Q9HBH9
Secondary accession number(s): Q6GPI3 , Q9HBH8, Q9UHR0, Q9Y2N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 7, 2006
Last modified:	February 19, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.