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Protein

MAP kinase-interacting serine/threonine-protein kinase 1

Gene

MKNK1

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

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

Phosphorylated and activated by the p38 kinases and kinases in the Erk pathway.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781ATP1 PublicationPROSITE-ProRule annotation
Active sitei211 – 2111Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi55 – 639ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  2. fibroblast growth factor receptor signaling pathway Source: Reactome
  3. intracellular signal transduction Source: UniProtKB
  4. peptidyl-serine phosphorylation Source: BHF-UCL
  5. protein phosphorylation Source: UniProtKB
  6. regulation of translational initiation Source: Ensembl
  7. response to salt stress Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_111080. Spry regulation of FGF signaling.
SignaLinkiQ9BUB5.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MKNK1
Synonyms:MNK1
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:7110. MKNK1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781K → M: Loss of kinase activity; when associated with D-232. 1 Publication
Mutagenesisi232 – 2321D → A: Loss of kinase activity; when associated with K-78. 1 Publication
Mutagenesisi250 – 2501T → A: Loss of kinase activity; when associated with T-255. 1 Publication
Mutagenesisi255 – 2551T → A: Loss of kinase activity; when associated with T-250. 1 Publication
Mutagenesisi385 – 3851T → D: Constitutively active. 1 Publication

Organism-specific databases

PharmGKBiPA30829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465MAP kinase-interacting serine/threonine-protein kinase 1PRO_0000086334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391Phosphoserine; by PAK2By similarity
Modified residuei250 – 2501Phosphothreonine1 Publication
Modified residuei255 – 2551Phosphothreonine1 Publication
Modified residuei385 – 3851Phosphothreonine1 Publication
Modified residuei460 – 4601Phosphoserine1 Publication

Post-translational modificationi

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 EIF4G1.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BUB5.
PaxDbiQ9BUB5.
PRIDEiQ9BUB5.

PTM databases

PhosphoSiteiQ9BUB5.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9BUB5.
CleanExiHS_MKNK1.
ExpressionAtlasiQ9BUB5. baseline and differential.
GenevestigatoriQ9BUB5.

Interactioni

Subunit structurei

Interacts with the C-terminal regions of EIF4G1 and EIF4G2. Also binds to dephosphorylated ERK1 and ERK2, and to the p38 kinases.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK14Q165393EBI-73837,EBI-73946

Protein-protein interaction databases

BioGridi114138. 24 interactions.
IntActiQ9BUB5. 17 interactions.
MINTiMINT-85533.
STRINGi9606.ENSP00000361014.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 463Combined sources
Beta strandi48 – 5710Combined sources
Beta strandi59 – 6810Combined sources
Turni69 – 713Combined sources
Beta strandi74 – 818Combined sources
Helixi87 – 10115Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi117 – 1259Combined sources
Helixi132 – 1398Combined sources
Helixi144 – 16320Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi271 – 2744Combined sources
Helixi277 – 29620Combined sources
Helixi337 – 3404Combined sources
Helixi345 – 35410Combined sources
Turni359 – 3613Combined sources
Helixi365 – 3706Combined sources
Turni372 – 3754Combined sources
Helixi439 – 4413Combined sources
Helixi443 – 4497Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HW6X-ray2.50A/B37-382[»]
2Y9QX-ray1.55B434-451[»]
ProteinModelPortaliQ9BUB5.
SMRiQ9BUB5. Positions 39-409.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BUB5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 374326Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOVERGENiHBG106949.
InParanoidiQ9BUB5.
KOiK04372.
OMAiASFYDKR.
PhylomeDBiQ9BUB5.
TreeFamiTF314050.

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. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q9BUB5-1) [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
MVSSQKLEKP IEMGSSEPLP IADGDRRRKK KRRGRATDSL PGKFEDMYKL
60 70 80 90 100
TSELLGEGAY AKVQGAVSLQ NGKEYAVKII EKQAGHSRSR VFREVETLYQ
110 120 130 140 150
CQGNKNILEL IEFFEDDTRF YLVFEKLQGG SILAHIQKQK HFNEREASRV
160 170 180 190 200
VRDVAAALDF LHTKDKVSLC HLGWSAMAPS GLTAAPTSLG SSDPPTSASQ
210 220 230 240 250
VAGTTGIAHR DLKPENILCE SPEKVSPVKI CDFDLGSGMK LNNSCTPITT
260 270 280 290 300
PELTTPCGSA EYMAPEVVEV FTDQATFYDK RCDLWSLGVV LYIMLSGYPP
310 320 330 340 350
FVGHCGADCG WDRGEVCRVC QNKLFESIQE GKYEFPDKDW AHISSEAKDL
360 370 380 390 400
ISKLLVRDAK QRLSAAQVLQ HPWVQGQAPE KGLPTPQVLQ RNSSTMDLTL
410 420 430 440 450
FAAEAIALNR QLSQHEENEL AEEPEALADG LCSMKLSPPC KSRLARRRAL
460
AQAGRGEDRS PPTAL
Length:465
Mass (Da):51,342
Last modified:June 1, 2001 - v1
Checksum:iCAE225C35DCB2B43
GO
Isoform 21 Publication (identifier: Q9BUB5-2) [UniParc]FASTAAdd to basket

Also known as: MNK1a

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

Show »
Length:424
Mass (Da):47,402
Checksum:iDB39E49EC0BED990
GO
Isoform 3 (identifier: Q9BUB5-3) [UniParc]FASTAAdd to basket

Also known as: MNK1b

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

Show »
Length:347
Mass (Da):39,104
Checksum:i1CCA03B12D39641F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491K → Q.1 Publication
Corresponds to variant rs56351860 [ dbSNP | Ensembl ].
VAR_040801
Natural varianti158 – 1581L → V.1 Publication
Corresponds to variant rs56408722 [ dbSNP | Ensembl ].
VAR_040802
Natural varianti308 – 3081D → N.1 Publication
Corresponds to variant rs55791614 [ dbSNP | Ensembl ].
VAR_040803
Natural varianti446 – 4461R → Q.1 Publication
Corresponds to variant rs34881418 [ dbSNP | Ensembl ].
VAR_040804

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 20541Missing in isoform 2 and isoform 3. 2 PublicationsVSP_007352Add
BLAST
Alternative sequencei377 – 46589QAPEK…PPTAL → EQQHNGPDALRS in isoform 3. 1 PublicationVSP_017515Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30705.1. [Q9BUB5-3]
CCDS44134.1. [Q9BUB5-2]
CCDS538.1. [Q9BUB5-1]
RefSeqiNP_001129025.1. NM_001135553.2. [Q9BUB5-2]
NP_003675.2. NM_003684.5. [Q9BUB5-1]
NP_945324.1. NM_198973.3. [Q9BUB5-3]
XP_006711063.1. XM_006711000.1. [Q9BUB5-2]
XP_006711075.1. XM_006711012.1. [Q9BUB5-3]
UniGeneiHs.371594.

Genome annotation databases

GeneIDi8569.
KEGGihsa:8569.
UCSCiuc001cqb.4. human. [Q9BUB5-1]
uc001cqc.4. human. [Q9BUB5-2]
uc009vyi.4. human. [Q9BUB5-3]

Polymorphism databases

DMDMi30316115.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30705.1. [Q9BUB5-3]
CCDS44134.1. [Q9BUB5-2]
CCDS538.1. [Q9BUB5-1]
RefSeqiNP_001129025.1. NM_001135553.2. [Q9BUB5-2]
NP_003675.2. NM_003684.5. [Q9BUB5-1]
NP_945324.1. NM_198973.3. [Q9BUB5-3]
XP_006711063.1. XM_006711000.1. [Q9BUB5-2]
XP_006711075.1. XM_006711012.1. [Q9BUB5-3]
UniGeneiHs.371594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HW6X-ray2.50A/B37-382[»]
2Y9QX-ray1.55B434-451[»]
ProteinModelPortaliQ9BUB5.
SMRiQ9BUB5. Positions 39-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114138. 24 interactions.
IntActiQ9BUB5. 17 interactions.
MINTiMINT-85533.
STRINGi9606.ENSP00000361014.

Chemistry

BindingDBiQ9BUB5.
ChEMBLiCHEMBL4718.
GuidetoPHARMACOLOGYi2104.

PTM databases

PhosphoSiteiQ9BUB5.

Polymorphism databases

DMDMi30316115.

Proteomic databases

MaxQBiQ9BUB5.
PaxDbiQ9BUB5.
PRIDEiQ9BUB5.

Protocols and materials databases

DNASUi8569.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8569.
KEGGihsa:8569.
UCSCiuc001cqb.4. human. [Q9BUB5-1]
uc001cqc.4. human. [Q9BUB5-2]
uc009vyi.4. human. [Q9BUB5-3]

Organism-specific databases

CTDi8569.
GeneCardsiGC01M047023.
HGNCiHGNC:7110. MKNK1.
MIMi606724. gene.
neXtProtiNX_Q9BUB5.
PharmGKBiPA30829.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOVERGENiHBG106949.
InParanoidiQ9BUB5.
KOiK04372.
OMAiASFYDKR.
PhylomeDBiQ9BUB5.
TreeFamiTF314050.

Enzyme and pathway databases

ReactomeiREACT_111080. Spry regulation of FGF signaling.
SignaLinkiQ9BUB5.

Miscellaneous databases

EvolutionaryTraceiQ9BUB5.
GeneWikiiMKNK1.
GenomeRNAii8569.
NextBioi32143.
PROiQ9BUB5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BUB5.
CleanExiHS_MKNK1.
ExpressionAtlasiQ9BUB5. baseline and differential.
GenevestigatoriQ9BUB5.

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. 2 hits.
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. "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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiMKNK1_HUMAN
AccessioniPrimary (citable) accession number: Q9BUB5
Secondary accession number(s): D3DQ20
, D3DQ21, O00312, Q5TC06, Q5TC07, Q6V0N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 141 of the entry and version 1 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 1
    Human chromosome 1: 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.