Q9BUB5 (MKNK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
MAP kinase-interacting serine/threonine-protein kinase 1
EC=2.7.11.1

Alternative name(s):
MAP kinase signal-integrating kinase 1
Short name=MAPK signal-integrating kinase 1
Short name=Mnk1

Gene names

Name:	MKNK1
Synonyms:	MNK1

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › 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	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. Ref.1 Ref.2 Ref.3 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2
Cofactor	Magnesium. Ref.1 Ref.2
Enzyme regulation	Phosphorylated and activated by the p38 kinases and kinases in the Erk pathway. Ref.1
Subunit structure	Interacts with the C-terminal regions of EIF4G1 and EIF4G2. Also binds to dephosphorylated ERK1 and ERK2, and to the p38 kinases. Ref.7 UniProtKB O08605
Subcellular location	Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Nucleus Ref.3.
Tissue specificity	Ubiquitous. Ref.3
Post-translational modification	Dual phosphorylation of Thr-250 and Thr-255 activates the kinase. Phosphorylation of Thr-385 activates the kinase. MAPK3/ERK1 is one of the kinases which activate MKNK1/MNK1. Phosphorylation by PAK2 leads to a reduced phosphorylation of EIF4G1.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome intracellular protein kinase cascade Inferred from direct assay Ref.1. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay PubMed 17130135. Source: BHF-UCL regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4E	P06730	2	EBI-73837,EBI-73440
EIF4G1	Q04637	2	EBI-73837,EBI-73711

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.2 (identifier: Q9BUB5-1)

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: Q9BUB5-2)

Also known as: MNK1a;

The sequence of this isoform differs from the canonical sequence as follows:
     165-205: Missing.

Isoform 3 (identifier: Q9BUB5-3)

Also known as: MNK1b;

The sequence of this isoform differs from the canonical sequence as follows:
     165-205: Missing.
     377-465: QAPEKGLPTP...GEDRSPPTAL → EQQHNGPDALRS

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 1

PRO_0000086334

Regions

Domain

49 – 374

326

Protein kinase

Nucleotide binding

55 – 63

9

ATP By similarity UniProtKB P49137

Sites

Active site

211

1

Proton acceptor By similarity UniProtKB P49137

Binding site

78

1

ATP Ref.2

Amino acid modifications

Modified residue

39

1

Phosphoserine; by PAK2 By similarity

Modified residue

250

1

Phosphothreonine Ref.2

Modified residue

255

1

Phosphothreonine Ref.2

Modified residue

385

1

Phosphothreonine Ref.2

Modified residue

460

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

165 – 205

41

Missing in isoform 2 and isoform 3.

VSP_007352

Alternative sequence

377 – 465

89

QAPEK…PPTAL → EQQHNGPDALRS in isoform 3.

VSP_017515

Natural variant

49

1

K → Q. Ref.10
Corresponds to variant rs56351860 [ dbSNP | Ensembl ].

VAR_040801

Natural variant

158

1

L → V. Ref.10
Corresponds to variant rs56408722 [ dbSNP | Ensembl ].

VAR_040802

Natural variant

308

1

D → N. Ref.10
Corresponds to variant rs55791614 [ dbSNP | Ensembl ].

VAR_040803

Natural variant

446

1

R → Q. Ref.10
Corresponds to variant rs34881418 [ dbSNP | Ensembl ].

VAR_040804

Experimental info

Mutagenesis

78

1

K → M: Loss of kinase activity; when associated with D-232. Ref.2

Mutagenesis

232

1

D → A: Loss of kinase activity; when associated with K-78. Ref.2

Mutagenesis

250

1

T → A: Loss of kinase activity; when associated with T-255. Ref.2

Mutagenesis

255

1

T → A: Loss of kinase activity; when associated with T-250. Ref.2

Mutagenesis

385

1

T → D: Constitutively active. Ref.2

Secondary structure

1

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465

Helix Strand Turn

Details...

Helix

44 – 46

3

Beta strand

48 – 57

10

Beta strand

59 – 68

10

Turn

69 – 71

3

Beta strand

74 – 81

8

Helix

87 – 101

15

Beta strand

110 – 115

6

Beta strand

117 – 125

9

Helix

132 – 139

8

Helix

144 – 163

20

Helix

214 – 216

3

Beta strand

217 – 220

4

Beta strand

227 – 230

4

Beta strand

271 – 274

4

Helix

277 – 296

20

Helix

337 – 340

4

Helix

345 – 354

10

Turn

359 – 361

3

Helix

365 – 370

6

Turn

372 – 375

4

Helix

439 – 441

3

Helix

443 – 449

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: CAE225C35DCB2B43	FASTA	465	51,342
	10 20 30 40 50 60 MVSSQKLEKP IEMGSSEPLP IADGDRRRKK KRRGRATDSL PGKFEDMYKL TSELLGEGAY 70 80 90 100 110 120 AKVQGAVSLQ NGKEYAVKII EKQAGHSRSR VFREVETLYQ CQGNKNILEL IEFFEDDTRF 130 140 150 160 170 180 YLVFEKLQGG SILAHIQKQK HFNEREASRV VRDVAAALDF LHTKDKVSLC HLGWSAMAPS 190 200 210 220 230 240 GLTAAPTSLG SSDPPTSASQ VAGTTGIAHR DLKPENILCE SPEKVSPVKI CDFDLGSGMK 250 260 270 280 290 300 LNNSCTPITT PELTTPCGSA EYMAPEVVEV FTDQATFYDK RCDLWSLGVV LYIMLSGYPP 310 320 330 340 350 360 FVGHCGADCG WDRGEVCRVC QNKLFESIQE GKYEFPDKDW AHISSEAKDL ISKLLVRDAK 370 380 390 400 410 420 QRLSAAQVLQ HPWVQGQAPE KGLPTPQVLQ RNSSTMDLTL FAAEAIALNR QLSQHEENEL 430 440 450 460 AEEPEALADG LCSMKLSPPC KSRLARRRAL AQAGRGEDRS PPTAL
	Isoform 2 (MNK1a) [UniParc]. Checksum: DB39E49EC0BED990	FASTA	424	47,402
	10 20 30 40 50 60 MVSSQKLEKP IEMGSSEPLP IADGDRRRKK KRRGRATDSL PGKFEDMYKL TSELLGEGAY 70 80 90 100 110 120 AKVQGAVSLQ NGKEYAVKII EKQAGHSRSR VFREVETLYQ CQGNKNILEL IEFFEDDTRF 130 140 150 160 170 180 YLVFEKLQGG SILAHIQKQK HFNEREASRV VRDVAAALDF LHTKGIAHRD LKPENILCES 190 200 210 220 230 240 PEKVSPVKIC DFDLGSGMKL NNSCTPITTP ELTTPCGSAE YMAPEVVEVF TDQATFYDKR 250 260 270 280 290 300 CDLWSLGVVL YIMLSGYPPF VGHCGADCGW DRGEVCRVCQ NKLFESIQEG KYEFPDKDWA 310 320 330 340 350 360 HISSEAKDLI SKLLVRDAKQ RLSAAQVLQH PWVQGQAPEK GLPTPQVLQR NSSTMDLTLF 370 380 390 400 410 420 AAEAIALNRQ LSQHEENELA EEPEALADGL CSMKLSPPCK SRLARRRALA QAGRGEDRSP PTAL
	Isoform 3 (MNK1b) [UniParc]. Checksum: 1CCA03B12D39641F	FASTA	347	39,104
	10 20 30 40 50 60 MVSSQKLEKP IEMGSSEPLP IADGDRRRKK KRRGRATDSL PGKFEDMYKL TSELLGEGAY 70 80 90 100 110 120 AKVQGAVSLQ NGKEYAVKII EKQAGHSRSR VFREVETLYQ CQGNKNILEL IEFFEDDTRF 130 140 150 160 170 180 YLVFEKLQGG SILAHIQKQK HFNEREASRV VRDVAAALDF LHTKGIAHRD LKPENILCES 190 200 210 220 230 240 PEKVSPVKIC DFDLGSGMKL NNSCTPITTP ELTTPCGSAE YMAPEVVEVF TDQATFYDKR 250 260 270 280 290 300 CDLWSLGVVL YIMLSGYPPF VGHCGADCGW DRGEVCRVCQ NKLFESIQEG KYEFPDKDWA 310 320 330 340 HISSEAKDLI SKLLVRDAKQ RLSAAQVLQH PWVQGEQQHN GPDALRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates." Fukunaga R., Hunter T. EMBO J. 16:1921-1933(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION BY MAPK3/ERK1, ENZYME REGULATION. Tissue: Cervix carcinoma.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION AT THR-250; THR-255 AND THR-385, MUTAGENESIS OF LYS-78; ASP-232; THR-250; THR-255 AND THR-385. Tissue: T-cell.
[3]	"Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1." O'Loghlen A., Gonzalez V.M., Pineiro D., Perez-Morgado M.I., Salinas M., Martin M.E. Exp. Cell Res. 299:343-355(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 1). Tissue: Placenta.
[7]	"Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E." Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N. EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF4G1 AND EIF4G2.
[8]	"Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk." Orton K.C., Ling J., Waskiewicz A.J., Cooper J.A., Merrick W.C., Korneeva N.L., Rhoads R.E., Sonenberg N., Traugh J.A. J. Biol. Chem. 279:38649-38657(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PAK2.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: VARIANTS [LARGE SCALE ANALYSIS] GLN-49; VAL-158; ASN-308 AND GLN-446.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB000409 mRNA. Translation: BAA19885.1.
AY355461 mRNA. Translation: AAQ84219.1.
AL136373 Genomic DNA. Translation: CAI14764.1.
AL136373 Genomic DNA. Translation: CAI14765.1.
CH471059 Genomic DNA. Translation: EAX06900.1.
CH471059 Genomic DNA. Translation: EAX06902.1.
CH471059 Genomic DNA. Translation: EAX06904.1.
CH471059 Genomic DNA. Translation: EAX06905.1.
BC002755 mRNA. Translation: AAH02755.1.

IPI

IPI00187091.
IPI00304048.
IPI00412417.

RefSeq

NP_001129025.1. NM_001135553.2.
NP_003675.2. NM_003684.5.
NP_945324.1. NM_198973.3.

UniGene

Hs.371594.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HW6	X-ray	2.50	A/B	37-382	[»]
2Y9Q	X-ray	1.55	B	434-451	[»]

ProteinModelPortal

Q9BUB5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BUB5. 11 interactions.

MINT

MINT-85533.

STRING

9606.ENSP00000361014.

PTM databases

PhosphoSite

Q9BUB5.

Polymorphism databases

DMDM

30316115.

Proteomic databases

PaxDb

Q9BUB5.

PRIDE

Q9BUB5.

Protocols and materials databases

DNASU

8569.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341183; ENSP00000339573; ENSG00000079277.
ENST00000371945; ENSP00000361013; ENSG00000079277.
ENST00000371946; ENSP00000361014; ENSG00000079277.
ENST00000428112; ENSP00000411135; ENSG00000079277.

GeneID

8569.

KEGG

hsa:8569.

UCSC

uc001cqb.3. human.
uc001cqc.3. human.
uc009vyi.3. human.

Organism-specific databases

CTD

8569.

GeneCards

GC01M047023.

HGNC

HGNC:7110. MKNK1.

MIM

606724. gene.

neXtProt

NX_Q9BUB5.

PharmGKB

PA30829.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG106949.

InParanoid

Q9BUB5.

KO

K04372.

OMA

ILTHIQK.

OrthoDB

EOG4GTKD2.

PhylomeDB

Q9BUB5.

Enzyme and pathway databases

Pathway_Interaction_DB

mtor_4pathway. mTOR signaling pathway.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q9BUB5.

Bgee

Q9BUB5.

CleanEx

HS_MKNK1.

Genevestigator

Q9BUB5.

GermOnline

ENSG00000079277. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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. Kinase_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

Q9BUB5.

ChEMBL

CHEMBL4718.

EvolutionaryTrace

Q9BUB5.

GenomeRNAi

8569.

NextBio

32143.

SOURCE

Search...

Entry information

Entry name

MKNK1_HUMAN

Accession

Primary (citable) accession number: Q9BUB5
Secondary accession number(s): D3DQ20 , D3DQ21, O00312, Q5TC06, Q5TC07, Q6V0N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 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.