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Protein

MAP kinase-activated protein kinase 2

Gene

MAPKAPK2

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

Functioni

Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.17 Publications

Catalytic activityi

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

Enzyme regulationi

Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited following sumoylation. Specifically inhibited by pyrrolopyridine inhibitors.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei93ATPPROSITE-ProRule annotation1
Active sitei186Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi70 – 78ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein serine/threonine kinase activity Source: GO_Central
  • calmodulin binding Source: GO_Central
  • calmodulin-dependent protein kinase activity Source: GO_Central
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: UniProtKB
  • signal transducer activity Source: ProtInc

GO - Biological processi

  • 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  • activation of MAPK activity Source: Reactome
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • G2 DNA damage checkpoint Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • inner ear development Source: Ensembl
  • leukotriene metabolic process Source: Reactome
  • macropinocytosis Source: UniProtKB
  • MAPK cascade Source: ProtInc
  • p38MAPK cascade Source: Ensembl
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  • protein autophosphorylation Source: GO_Central
  • protein phosphorylation Source: ProtInc
  • Ras protein signal transduction Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of interleukin-6 production Source: UniProtKB
  • regulation of mRNA stability Source: Reactome
  • regulation of tumor necrosis factor production Source: UniProtKB
  • response to cytokine Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • response to stress Source: UniProtKB
  • toll-like receptor signaling pathway Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08751-MONOMER.
ZFISH:HS08751-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-171007. p38MAPK events.
R-HSA-199920. CREB phosphorylation.
R-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLinkiP49137.
SIGNORiP49137.

Names & Taxonomyi

Protein namesi
Recommended name:
MAP kinase-activated protein kinase 2 (EC:2.7.11.1)
Short name:
MAPK-activated protein kinase 2
Short name:
MAPKAP kinase 2
Short name:
MAPKAP-K2
Short name:
MAPKAPK-2
Short name:
MK-2
Short name:
MK2
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6887. MAPKAPK2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HPA
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi93K → R: Kinase defective mutant, abolishes activity. 1 Publication1
Mutagenesisi207D → A: Kinase defective mutant, abolishes activity. 1 Publication1
Mutagenesisi222T → A: Strong decrease in kinase activity. 3 Publications1
Mutagenesisi222T → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 3 Publications1
Mutagenesisi222T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-334. 3 Publications1
Mutagenesisi272S → A: Strong decrease in kinase activity. 1 Publication1
Mutagenesisi272S → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 1 Publication1
Mutagenesisi334T → A: Slight decrease in kinase activity. 3 Publications1
Mutagenesisi334T → D or E: Mimicks phosphorylation state, leading to elevated basal kinase activity. 3 Publications1
Mutagenesisi334T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-222. 3 Publications1
Mutagenesisi353K → R: Induces decreased sumoylation and increase in protein kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi9261.
OpenTargetsiENSG00000162889.
PharmGKBiPA30631.

Chemistry databases

ChEMBLiCHEMBL2208.
GuidetoPHARMACOLOGYi2094.

Polymorphism and mutation databases

BioMutaiMAPKAPK2.
DMDMi1346538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000862881 – 400MAP kinase-activated protein kinase 2Add BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphoserine1 Publication1
Modified residuei25Phosphothreonine1 Publication1
Modified residuei222Phosphothreonine; by MAPK141 Publication1
Modified residuei272Phosphoserine; by MAPK141 Publication1
Modified residuei328Phosphoserine; by autocatalysisBy similarity1
Modified residuei334Phosphothreonine; by MAPK14Combined sources1 Publication1
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylation inhibits the protein kinase activity.1 Publication
Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-222, Ser-272 and Thr-334.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49137.
MaxQBiP49137.
PaxDbiP49137.
PeptideAtlasiP49137.
PRIDEiP49137.

PTM databases

iPTMnetiP49137.
PhosphoSitePlusiP49137.

Expressioni

Tissue specificityi

Expressed in all tissues examined.

Gene expression databases

BgeeiENSG00000162889.
CleanExiHS_MAPKAPK2.
GenevisibleiP49137. HS.

Organism-specific databases

HPAiCAB010297.
HPA045556.

Interactioni

Subunit structurei

Heterodimer with p38-alpha/MAPK14. The heterodimer with p38-alpha/MAPK14 forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface. Interacts with PHC2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSF1Q006135EBI-993299,EBI-719620
HSPB1P047923EBI-993299,EBI-352682
MAPK14Q165397EBI-993299,EBI-73946
Phc2Q9QWH12EBI-993299,EBI-642357From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114683. 41 interactors.
DIPiDIP-35671N.
IntActiP49137. 14 interactors.
MINTiMINT-1539725.
STRINGi9606.ENSP00000356070.

Chemistry databases

BindingDBiP49137.

Structurei

Secondary structure

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 47Combined sources3
Beta strandi48 – 50Combined sources3
Helixi59 – 61Combined sources3
Beta strandi63 – 73Combined sources11
Beta strandi76 – 83Combined sources8
Turni84 – 86Combined sources3
Beta strandi89 – 96Combined sources8
Helixi99 – 111Combined sources13
Beta strandi114 – 117Combined sources4
Beta strandi120 – 128Combined sources9
Beta strandi131 – 138Combined sources8
Beta strandi143 – 145Combined sources3
Helixi146 – 152Combined sources7
Helixi160 – 179Combined sources20
Helixi189 – 191Combined sources3
Beta strandi192 – 198Combined sources7
Beta strandi203 – 205Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi228 – 230Combined sources3
Helixi232 – 234Combined sources3
Helixi239 – 242Combined sources4
Helixi243 – 258Combined sources16
Beta strandi264 – 266Combined sources3
Beta strandi267 – 269Combined sources3
Helixi275 – 281Combined sources7
Beta strandi283 – 285Combined sources3
Helixi288 – 291Combined sources4
Helixi296 – 305Combined sources10
Turni310 – 312Combined sources3
Helixi316 – 320Combined sources5
Helixi323 – 326Combined sources4
Helixi328 – 330Combined sources3
Beta strandi335 – 337Combined sources3
Helixi338 – 344Combined sources7
Helixi346 – 348Combined sources3
Helixi349 – 363Combined sources15
Turni375 – 377Combined sources3
Helixi381 – 389Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KWPX-ray2.80A/B1-400[»]
1NXKX-ray2.70A/B/C/D1-400[»]
1NY3X-ray3.00A1-400[»]
2JBOX-ray3.10A41-364[»]
2JBPX-ray3.31A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
2OKRX-ray2.00C/F370-393[»]
2ONLX-ray4.00C/D1-400[»]
2OZAX-ray2.70A47-400[»]
2P3GX-ray3.80X45-371[»]
2PZYX-ray2.90A/B/C/D41-364[»]
3A2CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3FPMX-ray3.30A41-364[»]
3FYJX-ray3.80X45-371[»]
3FYKX-ray3.50X45-371[»]
3GOKX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KA0X-ray2.90A47-366[»]
3KC3X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KGAX-ray2.55A47-364[»]
3M2WX-ray2.41A47-364[»]
3M42X-ray2.68A47-364[»]
3R2BX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L47-364[»]
3R2YX-ray3.00A46-364[»]
3R30X-ray3.20A46-364[»]
3WI6X-ray2.99A/B/C/D/E/F41-364[»]
4TYHX-ray3.00A51-400[»]
ProteinModelPortaliP49137.
SMRiP49137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49137.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni139 – 141Staurosporine binding3
Regioni328 – 364Autoinhibitory helixBy similarityAdd BLAST37
Regioni366 – 390p38 MAPK-binding siteAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi356 – 365Nuclear export signal (NES)10
Motifi371 – 374Bipartite nuclear localization signal 14
Motifi385 – 389Bipartite nuclear localization signal 25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi10 – 40Pro-richAdd BLAST31
Compositional biasi35 – 40Poly-Pro6

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0604. Eukaryota.
ENOG410XP8F. LUCA.
GeneTreeiENSGT00830000128274.
HOGENOMiHOG000233031.
HOVERGENiHBG106948.
InParanoidiP49137.
KOiK04443.
OMAiLQMLQDC.
OrthoDBiEOG091G14PL.
PhylomeDBiP49137.
TreeFamiTF312891.

Family and domain databases

Gene3Di4.10.1170.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49137-1) [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
MLSNSQGQSP PVPFPAPAPP PQPPTPALPH PPAQPPPPPP QQFPQFHVKS
60 70 80 90 100
GLQIKKNAII DDYKVTSQVL GLGINGKVLQ IFNKRTQEKF ALKMLQDCPK
110 120 130 140 150
ARREVELHWR ASQCPHIVRI VDVYENLYAG RKCLLIVMEC LDGGELFSRI
160 170 180 190 200
QDRGDQAFTE REASEIMKSI GEAIQYLHSI NIAHRDVKPE NLLYTSKRPN
210 220 230 240 250
AILKLTDFGF AKETTSHNSL TTPCYTPYYV APEVLGPEKY DKSCDMWSLG
260 270 280 290 300
VIMYILLCGY PPFYSNHGLA ISPGMKTRIR MGQYEFPNPE WSEVSEEVKM
310 320 330 340 350
LIRNLLKTEP TQRMTITEFM NHPWIMQSTK VPQTPLHTSR VLKEDKERWE
360 370 380 390 400
DVKEEMTSAL ATMRVDYEQI KIKKIEDASN PLLLKRRKKA RALEAAALAH
Note: Has a nuclear localization signal.
Length:400
Mass (Da):45,568
Last modified:February 1, 1996 - v1
Checksum:iE4EFFF11CCF288DC
GO
Isoform 2 (identifier: P49137-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     354-400: EEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH → GCLHDKNSDQATWLTRL

Show »
Length:370
Mass (Da):42,203
Checksum:iFF09AD93D4F73BDB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116H → D in CAA53094 (PubMed:8280084).Curated1
Sequence conflicti247 – 248WS → LV in CAA53094 (PubMed:8280084).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040753173A → G.1 PublicationCorresponds to variant rs35671930dbSNPEnsembl.1
Natural variantiVAR_040754361A → S.1 PublicationCorresponds to variant rs55894011dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004910354 – 400EEMTS…AALAH → GCLHDKNSDQATWLTRL in isoform 2. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12779 mRNA. Translation: AAA20851.1.
AL591846 Genomic DNA. Translation: CAI13543.1.
AL591846 Genomic DNA. Translation: CAI13544.1.
CH471100 Genomic DNA. Translation: EAW93526.1.
CH471100 Genomic DNA. Translation: EAW93529.1.
BC036060 mRNA. Translation: AAH36060.2.
BC052584 mRNA. Translation: AAH52584.1.
X75346 mRNA. Translation: CAA53094.1.
CCDSiCCDS1466.1. [P49137-2]
CCDS31001.1. [P49137-1]
PIRiJC2204.
S39793.
RefSeqiNP_004750.1. NM_004759.4. [P49137-2]
NP_116584.2. NM_032960.3. [P49137-1]
UniGeneiHs.643566.
Hs.713747.

Genome annotation databases

EnsembliENST00000294981; ENSP00000294981; ENSG00000162889. [P49137-2]
ENST00000367103; ENSP00000356070; ENSG00000162889. [P49137-1]
GeneIDi9261.
KEGGihsa:9261.
UCSCiuc001hel.3. human. [P49137-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12779 mRNA. Translation: AAA20851.1.
AL591846 Genomic DNA. Translation: CAI13543.1.
AL591846 Genomic DNA. Translation: CAI13544.1.
CH471100 Genomic DNA. Translation: EAW93526.1.
CH471100 Genomic DNA. Translation: EAW93529.1.
BC036060 mRNA. Translation: AAH36060.2.
BC052584 mRNA. Translation: AAH52584.1.
X75346 mRNA. Translation: CAA53094.1.
CCDSiCCDS1466.1. [P49137-2]
CCDS31001.1. [P49137-1]
PIRiJC2204.
S39793.
RefSeqiNP_004750.1. NM_004759.4. [P49137-2]
NP_116584.2. NM_032960.3. [P49137-1]
UniGeneiHs.643566.
Hs.713747.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KWPX-ray2.80A/B1-400[»]
1NXKX-ray2.70A/B/C/D1-400[»]
1NY3X-ray3.00A1-400[»]
2JBOX-ray3.10A41-364[»]
2JBPX-ray3.31A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
2OKRX-ray2.00C/F370-393[»]
2ONLX-ray4.00C/D1-400[»]
2OZAX-ray2.70A47-400[»]
2P3GX-ray3.80X45-371[»]
2PZYX-ray2.90A/B/C/D41-364[»]
3A2CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3FPMX-ray3.30A41-364[»]
3FYJX-ray3.80X45-371[»]
3FYKX-ray3.50X45-371[»]
3GOKX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KA0X-ray2.90A47-366[»]
3KC3X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KGAX-ray2.55A47-364[»]
3M2WX-ray2.41A47-364[»]
3M42X-ray2.68A47-364[»]
3R2BX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L47-364[»]
3R2YX-ray3.00A46-364[»]
3R30X-ray3.20A46-364[»]
3WI6X-ray2.99A/B/C/D/E/F41-364[»]
4TYHX-ray3.00A51-400[»]
ProteinModelPortaliP49137.
SMRiP49137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114683. 41 interactors.
DIPiDIP-35671N.
IntActiP49137. 14 interactors.
MINTiMINT-1539725.
STRINGi9606.ENSP00000356070.

Chemistry databases

BindingDBiP49137.
ChEMBLiCHEMBL2208.
GuidetoPHARMACOLOGYi2094.

PTM databases

iPTMnetiP49137.
PhosphoSitePlusiP49137.

Polymorphism and mutation databases

BioMutaiMAPKAPK2.
DMDMi1346538.

Proteomic databases

EPDiP49137.
MaxQBiP49137.
PaxDbiP49137.
PeptideAtlasiP49137.
PRIDEiP49137.

Protocols and materials databases

DNASUi9261.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294981; ENSP00000294981; ENSG00000162889. [P49137-2]
ENST00000367103; ENSP00000356070; ENSG00000162889. [P49137-1]
GeneIDi9261.
KEGGihsa:9261.
UCSCiuc001hel.3. human. [P49137-1]

Organism-specific databases

CTDi9261.
DisGeNETi9261.
GeneCardsiMAPKAPK2.
HGNCiHGNC:6887. MAPKAPK2.
HPAiCAB010297.
HPA045556.
MIMi602006. gene.
neXtProtiNX_P49137.
OpenTargetsiENSG00000162889.
PharmGKBiPA30631.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0604. Eukaryota.
ENOG410XP8F. LUCA.
GeneTreeiENSGT00830000128274.
HOGENOMiHOG000233031.
HOVERGENiHBG106948.
InParanoidiP49137.
KOiK04443.
OMAiLQMLQDC.
OrthoDBiEOG091G14PL.
PhylomeDBiP49137.
TreeFamiTF312891.

Enzyme and pathway databases

BioCyciMetaCyc:HS08751-MONOMER.
ZFISH:HS08751-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-171007. p38MAPK events.
R-HSA-199920. CREB phosphorylation.
R-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-HSA-450513. Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
SignaLinkiP49137.
SIGNORiP49137.

Miscellaneous databases

ChiTaRSiMAPKAPK2. human.
EvolutionaryTraceiP49137.
GeneWikiiMAPKAPK2.
GenomeRNAii9261.
PROiP49137.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162889.
CleanExiHS_MAPKAPK2.
GenevisibleiP49137. HS.

Family and domain databases

Gene3Di4.10.1170.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAPK2_HUMAN
AccessioniPrimary (citable) accession number: P49137
Secondary accession number(s): Q5SY30, Q5SY41, Q8IYD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 177 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

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 one 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.