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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931ATPPROSITE-ProRule annotation
Active sitei186 – 1861Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi70 – 789ATPPROSITE-ProRule annotation

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931K → R: Kinase defective mutant, abolishes activity. 1 Publication
Mutagenesisi207 – 2071D → A: Kinase defective mutant, abolishes activity. 1 Publication
Mutagenesisi222 – 2221T → A: Strong decrease in kinase activity. 3 Publications
Mutagenesisi222 – 2221T → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 3 Publications
Mutagenesisi222 – 2221T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-334. 3 Publications
Mutagenesisi272 – 2721S → A: Strong decrease in kinase activity. 1 Publication
Mutagenesisi272 – 2721S → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 1 Publication
Mutagenesisi334 – 3341T → A: Slight decrease in kinase activity. 3 Publications
Mutagenesisi334 – 3341T → D or E: Mimicks phosphorylation state, leading to elevated basal kinase activity. 3 Publications
Mutagenesisi334 – 3341T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-222. 3 Publications
Mutagenesisi353 – 3531K → R: Induces decreased sumoylation and increase in protein kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA30631.

Chemistry

ChEMBLiCHEMBL2208.
GuidetoPHARMACOLOGYi2094.

Polymorphism and mutation databases

BioMutaiMAPKAPK2.
DMDMi1346538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400MAP kinase-activated protein kinase 2PRO_0000086288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei25 – 251Phosphothreonine1 Publication
Modified residuei222 – 2221Phosphothreonine; by MAPK141 Publication
Modified residuei272 – 2721Phosphoserine; by MAPK141 Publication
Modified residuei328 – 3281Phosphoserine; by autocatalysisBy similarity
Modified residuei334 – 3341Phosphothreonine; by MAPK14Combined sources1 Publication
Cross-linki353 – 353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

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.
PhosphoSiteiP49137.

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 interactions.
DIPiDIP-35671N.
IntActiP49137. 14 interactions.
MINTiMINT-1539725.
STRINGi9606.ENSP00000356070.

Chemistry

BindingDBiP49137.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 473Combined sources
Beta strandi48 – 503Combined sources
Helixi59 – 613Combined sources
Beta strandi63 – 7311Combined sources
Beta strandi76 – 838Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 968Combined sources
Helixi99 – 11113Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi120 – 1289Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi143 – 1453Combined sources
Helixi146 – 1527Combined sources
Helixi160 – 17920Combined sources
Helixi189 – 1913Combined sources
Beta strandi192 – 1987Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi228 – 2303Combined sources
Helixi232 – 2343Combined sources
Helixi239 – 2424Combined sources
Helixi243 – 25816Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi267 – 2693Combined sources
Helixi275 – 2817Combined sources
Beta strandi283 – 2853Combined sources
Helixi288 – 2914Combined sources
Helixi296 – 30510Combined sources
Turni310 – 3123Combined sources
Helixi316 – 3205Combined sources
Helixi323 – 3264Combined sources
Helixi328 – 3303Combined sources
Beta strandi335 – 3373Combined sources
Helixi338 – 3447Combined sources
Helixi346 – 3483Combined sources
Helixi349 – 36315Combined sources
Turni375 – 3773Combined sources
Helixi381 – 3899Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 51-390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49137.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 325262Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1413Staurosporine binding
Regioni328 – 36437Autoinhibitory helixBy similarityAdd
BLAST
Regioni366 – 39025p38 MAPK-binding siteAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi356 – 36510Nuclear export signal (NES)
Motifi371 – 3744Bipartite nuclear localization signal 1
Motifi385 – 3895Bipartite nuclear localization signal 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 4031Pro-richAdd
BLAST
Compositional biasi35 – 406Poly-Pro

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161H → D in CAA53094 (PubMed:8280084).Curated
Sequence conflicti247 – 2482WS → LV in CAA53094 (PubMed:8280084).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731A → G.1 Publication
Corresponds to variant rs35671930 [ dbSNP | Ensembl ].
VAR_040753
Natural varianti361 – 3611A → S.1 Publication
Corresponds to variant rs55894011 [ dbSNP | Ensembl ].
VAR_040754

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei354 – 40047EEMTS…AALAH → GCLHDKNSDQATWLTRL in isoform 2. 1 PublicationVSP_004910Add
BLAST

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
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. Positions 51-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP49137.
ChEMBLiCHEMBL2208.
GuidetoPHARMACOLOGYi2094.

PTM databases

iPTMnetiP49137.
PhosphoSiteiP49137.

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

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc: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: September 7, 2016
This is version 175 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.