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Q15759

- MK11_HUMAN

UniProt

Q15759 - MK11_HUMAN

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Protein

Mitogen-activated protein kinase 11

Gene

MAPK11

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

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 functions are mostly redundant with those of MAPK14. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Additional examples of p38 MAPK substrates are the FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by phosphorylation on threonine and tyrosine by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 induced by environmental stress. HDAC3 interacts directly and selectively with MAPK11 to repress ATF2 transcriptional activity, and regulate TNF gene expression in LPS-stimulated cells. Inhibited by SB203580 and pyridinyl-imidazole related compounds.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Binding sitei71 – 711Nilotinib
Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  1. activation of MAPK activity Source: Reactome
  2. gene expression Source: Reactome
  3. innate immune response Source: Reactome
  4. intracellular signal transduction Source: UniProtKB
  5. mRNA metabolic process Source: Reactome
  6. muscle cell differentiation Source: Reactome
  7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. positive regulation of muscle cell differentiation Source: Reactome
  11. Ras protein signal transduction Source: Reactome
  12. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  13. response to stress Source: UniProtKB
  14. RNA metabolic process Source: Reactome
  15. signal transduction Source: ProtInc
  16. stress-activated MAPK cascade Source: Reactome
  17. toll-like receptor 10 signaling pathway Source: Reactome
  18. toll-like receptor 2 signaling pathway Source: Reactome
  19. toll-like receptor 3 signaling pathway Source: Reactome
  20. toll-like receptor 4 signaling pathway Source: Reactome
  21. toll-like receptor 5 signaling pathway Source: Reactome
  22. toll-like receptor 9 signaling pathway Source: Reactome
  23. toll-like receptor signaling pathway Source: Reactome
  24. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  25. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  26. transcription, DNA-templated Source: UniProtKB-KW
  27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 2681.
ReactomeiREACT_12065. p38MAPK events.
REACT_12599. ERK/MAPK targets.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25042. KSRP destabilizes mRNA.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiQ15759.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 11 (EC:2.7.11.24)
Short name:
MAP kinase 11
Short name:
MAPK 11
Alternative name(s):
Mitogen-activated protein kinase p38 beta
Short name:
MAP kinase p38 beta
Short name:
p38b
Stress-activated protein kinase 2b
Short name:
SAPK2b
p38-2
Gene namesi
Name:MAPK11
Synonyms:PRKM11, SAPK2, SAPK2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6873. MAPK11.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801T → A: Inactivation.
Mutagenesisi182 – 1821Y → F: Inactivation.

Organism-specific databases

PharmGKBiPA30618.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Mitogen-activated protein kinase 11PRO_0000186280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K61 Publication
Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K61 Publication
Modified residuei323 – 3231Phosphotyrosine; by ZAP70By similarity

Post-translational modificationi

Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6, which activates the enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ15759.
PRIDEiQ15759.

PTM databases

PhosphoSiteiQ15759.

Expressioni

Tissue specificityi

Highest levels in the brain and heart. Also expressed in the placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiQ15759.
CleanExiHS_MAPK11.
ExpressionAtlasiQ15759. baseline and differential.
GenevestigatoriQ15759.

Organism-specific databases

HPAiCAB012961.

Interactioni

Subunit structurei

Interacts with HDAC3 and DUSP16.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046372EBI-298304,EBI-366083
ZNHIT1O432572EBI-298304,EBI-347522

Protein-protein interaction databases

BioGridi111586. 28 interactions.
IntActiQ15759. 21 interactions.
MINTiMINT-3032032.
STRINGi9606.ENSP00000333685.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Beta strandi17 – 215Combined sources
Beta strandi24 – 296Combined sources
Beta strandi31 – 333Combined sources
Turni34 – 374Combined sources
Beta strandi38 – 436Combined sources
Turni44 – 474Combined sources
Beta strandi48 – 547Combined sources
Helixi62 – 7716Combined sources
Beta strandi86 – 905Combined sources
Helixi96 – 983Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi110 – 1123Combined sources
Helixi113 – 1197Combined sources
Helixi124 – 14320Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi164 – 1663Combined sources
Helixi179 – 1824Combined sources
Helixi185 – 1884Combined sources
Helixi191 – 1944Combined sources
Helixi203 – 21816Combined sources
Helixi228 – 23912Combined sources
Helixi244 – 2496Combined sources
Turni253 – 2553Combined sources
Helixi256 – 2605Combined sources
Helixi270 – 2734Combined sources
Turni274 – 2763Combined sources
Helixi279 – 2857Combined sources
Turni286 – 2883Combined sources
Helixi293 – 2953Combined sources
Helixi299 – 3024Combined sources
Helixi306 – 3083Combined sources
Turni309 – 3113Combined sources
Helixi314 – 3163Combined sources
Helixi326 – 3294Combined sources
Helixi334 – 34714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GC8X-ray2.40A/B1-364[»]
3GC9X-ray2.05A/B1-364[»]
3GP0X-ray1.90A5-350[»]
ProteinModelPortaliQ15759.
SMRiQ15759. Positions 3-349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 308285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1105Inhibitor-binding
Regioni168 – 1692Inhibitor-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1823TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ15759.
KOiK04441.
OMAiETIGGCE.
OrthoDBiEOG7PCJGV.
PhylomeDBiQ15759.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15759-1) [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
MSGPRAGFYR QELNKTVWEV PQRLQGLRPV GSGAYGSVCS AYDARLRQKV
60 70 80 90 100
AVKKLSRPFQ SLIHARRTYR ELRLLKHLKH ENVIGLLDVF TPATSIEDFS
110 120 130 140 150
EVYLVTTLMG ADLNNIVKCQ ALSDEHVQFL VYQLLRGLKY IHSAGIIHRD
160 170 180 190 200
LKPSNVAVNE DCELRILDFG LARQADEEMT GYVATRWYRA PEIMLNWMHY
210 220 230 240 250
NQTVDIWSVG CIMAELLQGK ALFPGSDYID QLKRIMEVVG TPSPEVLAKI
260 270 280 290 300
SSEHARTYIQ SLPPMPQKDL SSIFRGANPL AIDLLGRMLV LDSDQRVSAA
310 320 330 340 350
EALAHAYFSQ YHDPEDEPEA EPYDESVEAK ERTLEEWKEL TYQEVLSFKP
360
PEPPKPPGSL EIEQ
Length:364
Mass (Da):41,357
Last modified:March 20, 2007 - v2
Checksum:i68DA4C7B7C721475
GO
Isoform 2 (identifier: Q15759-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
     204-321: VDIWSVGCIM...HDPEDEPEAE → GAGGRPWGDE...GYLVRGLHHG
     322-364: Missing.

Note: No experimental confirmation available.

Show »
Length:213
Mass (Da):23,603
Checksum:iE3466E25BE1D27A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981D → V in BAF84534. (PubMed:14702039)Curated
Sequence conflicti122 – 1232LS → GAHQGARLAL in AAB05036. (PubMed:8663524)Curated
Sequence conflicti326 – 3261S → G in AAB66313. (PubMed:9235954)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211A → V in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_042264
Natural varianti275 – 2751R → H.2 Publications
Corresponds to variant rs33932986 [ dbSNP | Ensembl ].
VAR_025176

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_055221Add
BLAST
Alternative sequencei204 – 321118VDIWS…EPEAE → GAGGRPWGDEGQGPRLALDW LCMPGLRGQARSPRMWDPHS KVALQRPLEHDGCWPPLAVQ LWTSPCLGGLGMAEEGVCPS WGLDVTVGLLEEGRGVGTLM EVPSPSHSGYLVRGLHHG in isoform 2. 1 PublicationVSP_055222Add
BLAST
Alternative sequencei322 – 36443Missing in isoform 2. 1 PublicationVSP_055223Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53442 mRNA. Translation: AAB05036.1.
AF001008 mRNA. Translation: AAC51250.1.
AF001174 mRNA. Translation: AAC51373.1.
AF031135 mRNA. Translation: AAC12714.1.
Y14440 mRNA. Translation: CAA74792.1.
U92268 mRNA. Translation: AAB66313.1.
CR456514 mRNA. Translation: CAG30400.1.
DQ279722 Genomic DNA. Translation: ABB72677.1.
AK291845 mRNA. Translation: BAF84534.1.
AK299745 mRNA. Translation: BAH13116.1.
EU332851 Genomic DNA. Translation: ABY87540.1.
JX512451 Genomic DNA. Translation: AGC09598.1.
AL022328 Genomic DNA. No translation available.
CH471138 Genomic DNA. Translation: EAW73524.1.
CH471138 Genomic DNA. Translation: EAW73525.1.
CH471138 Genomic DNA. Translation: EAW73526.1.
BC027933 mRNA. Translation: AAH27933.1.
CCDSiCCDS14090.1. [Q15759-1]
PIRiG02524.
JC5529.
RefSeqiNP_002742.3. NM_002751.6. [Q15759-1]
UniGeneiHs.57732.

Genome annotation databases

EnsembliENST00000330651; ENSP00000333685; ENSG00000185386. [Q15759-1]
ENST00000395764; ENSP00000379113; ENSG00000185386. [Q15759-1]
GeneIDi5600.
KEGGihsa:5600.
UCSCiuc003bkr.3. human. [Q15759-1]

Polymorphism databases

DMDMi134047835.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53442 mRNA. Translation: AAB05036.1 .
AF001008 mRNA. Translation: AAC51250.1 .
AF001174 mRNA. Translation: AAC51373.1 .
AF031135 mRNA. Translation: AAC12714.1 .
Y14440 mRNA. Translation: CAA74792.1 .
U92268 mRNA. Translation: AAB66313.1 .
CR456514 mRNA. Translation: CAG30400.1 .
DQ279722 Genomic DNA. Translation: ABB72677.1 .
AK291845 mRNA. Translation: BAF84534.1 .
AK299745 mRNA. Translation: BAH13116.1 .
EU332851 Genomic DNA. Translation: ABY87540.1 .
JX512451 Genomic DNA. Translation: AGC09598.1 .
AL022328 Genomic DNA. No translation available.
CH471138 Genomic DNA. Translation: EAW73524.1 .
CH471138 Genomic DNA. Translation: EAW73525.1 .
CH471138 Genomic DNA. Translation: EAW73526.1 .
BC027933 mRNA. Translation: AAH27933.1 .
CCDSi CCDS14090.1. [Q15759-1 ]
PIRi G02524.
JC5529.
RefSeqi NP_002742.3. NM_002751.6. [Q15759-1 ]
UniGenei Hs.57732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GC8 X-ray 2.40 A/B 1-364 [» ]
3GC9 X-ray 2.05 A/B 1-364 [» ]
3GP0 X-ray 1.90 A 5-350 [» ]
ProteinModelPortali Q15759.
SMRi Q15759. Positions 3-349.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111586. 28 interactions.
IntActi Q15759. 21 interactions.
MINTi MINT-3032032.
STRINGi 9606.ENSP00000333685.

Chemistry

BindingDBi Q15759.
ChEMBLi CHEMBL3961.
DrugBanki DB08896. Regorafenib.
GuidetoPHARMACOLOGYi 1500.

PTM databases

PhosphoSitei Q15759.

Polymorphism databases

DMDMi 134047835.

Proteomic databases

PaxDbi Q15759.
PRIDEi Q15759.

Protocols and materials databases

DNASUi 5600.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330651 ; ENSP00000333685 ; ENSG00000185386 . [Q15759-1 ]
ENST00000395764 ; ENSP00000379113 ; ENSG00000185386 . [Q15759-1 ]
GeneIDi 5600.
KEGGi hsa:5600.
UCSCi uc003bkr.3. human. [Q15759-1 ]

Organism-specific databases

CTDi 5600.
GeneCardsi GC22M050702.
HGNCi HGNC:6873. MAPK11.
HPAi CAB012961.
MIMi 602898. gene.
neXtProti NX_Q15759.
PharmGKBi PA30618.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi Q15759.
KOi K04441.
OMAi ETIGGCE.
OrthoDBi EOG7PCJGV.
PhylomeDBi Q15759.
TreeFami TF105100.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 2681.
Reactomei REACT_12065. p38MAPK events.
REACT_12599. ERK/MAPK targets.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25042. KSRP destabilizes mRNA.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki Q15759.

Miscellaneous databases

EvolutionaryTracei Q15759.
GeneWikii MAPK11.
GenomeRNAii 5600.
NextBioi 21748.
PROi Q15759.
SOURCEi Search...

Gene expression databases

Bgeei Q15759.
CleanExi HS_MAPK11.
ExpressionAtlasi Q15759. baseline and differential.
Genevestigatori Q15759.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)."
    Jiang Y., Chen C., Li Z., Guo W., Gegner J.A., Lin S., Han J.
    J. Biol. Chem. 271:17920-17926(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. Jiang Y., Han J.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles."
    Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.
    Biochem. Biophys. Res. Commun. 235:533-538(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
    Enslen H., Raingeaud J., Davis R.J.
    J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, ENZYME REGULATION.
    Tissue: Brain.
  5. "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases."
    Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.
    EMBO J. 16:3563-3571(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION.
  6. "p38-2, a novel mitogen-activated protein kinase with distinct properties."
    Stein B., Yang M.X., Young D.B., Janknecht R., Hunter T., Murray B.W., Barbosa M.S.
    J. Biol. Chem. 272:19509-19517(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  9. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-275.
  10. NHLBI resequencing and genotyping service (RS&G)
    Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "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: Brain.
  14. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
  15. "Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors."
    Yang S.-H., Galanis A., Sharrocks A.D.
    Mol. Cell. Biol. 19:4028-4038(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
  16. "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs."
    Tanoue T., Yamamoto T., Maeda R., Nishida E.
    J. Biol. Chem. 276:26629-26639(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP16, ENZYME REGULATION.
  17. "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 MKNK2 KINASE.
  18. "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression."
    Mahlknecht U., Will J., Varin A., Hoelzer D., Herbein G.
    J. Immunol. 173:3979-3990(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC3, PHOSPHORYLATION, ENZYME REGULATION, FUNCTION IN ATF2 ACTIVATION.
  19. "In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance."
    Shi Y., Gaestel M.
    Biol. Chem. 383:1519-1536(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Mechanisms and functions of p38 MAPK signalling."
    Cuadrado A., Nebreda A.R.
    Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  22. "The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha."
    Patel S.B., Cameron P.M., O'Keefe S.J., Frantz-Wattley B., Thompson J., O'Neill E.A., Tennis T., Liu L., Becker J.W., Scapin G.
    Acta Crystallogr. D 65:777-785(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  23. "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] VAL-221 AND HIS-275.

Entry informationi

Entry nameiMK11_HUMAN
AccessioniPrimary (citable) accession number: Q15759
Secondary accession number(s): A8K730
, B0LPG1, B7Z630, E7ETQ1, L7RT27, O00284, O15472, Q2XNF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 20, 2007
Last modified: November 26, 2014
This is version 161 of the entry and version 2 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 22
    Human chromosome 22: 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