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Protein

MAP kinase-activated protein kinase 3

Gene

MAPKAPK3

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 cytokines production, endocytosis, cell migration, chromatin remodeling 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. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair 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, such as TTP/ZFP36, leading to regulate 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 transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Activated following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited by ligand 5B (2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive inhibitors.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATPPROSITE-ProRule annotation
Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of MAPK activity Source: Reactome
  2. innate immune response Source: Reactome
  3. macropinocytosis Source: UniProtKB
  4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  6. neurotrophin TRK receptor signaling pathway Source: Reactome
  7. peptidyl-serine phosphorylation Source: BHF-UCL
  8. Ras protein signal transduction Source: Reactome
  9. response to cytokine Source: UniProtKB
  10. response to lipopolysaccharide Source: UniProtKB
  11. response to stress Source: ProtInc
  12. signal transduction Source: ProtInc
  13. stress-activated MAPK cascade Source: Reactome
  14. toll-like receptor 10 signaling pathway Source: Reactome
  15. toll-like receptor 2 signaling pathway Source: Reactome
  16. toll-like receptor 3 signaling pathway Source: Reactome
  17. toll-like receptor 4 signaling pathway Source: Reactome
  18. toll-like receptor 5 signaling pathway Source: Reactome
  19. toll-like receptor 9 signaling pathway Source: Reactome
  20. toll-like receptor signaling pathway Source: UniProtKB
  21. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  22. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  23. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_228166. VEGFA-VEGFR2 Pathway.
SignaLinkiQ16644.

Names & Taxonomyi

Protein namesi
Recommended name:
MAP kinase-activated protein kinase 3 (EC:2.7.11.1)
Short name:
MAPK-activated protein kinase 3
Short name:
MAPKAP kinase 3
Short name:
MAPKAP-K3
Short name:
MAPKAPK-3
Short name:
MK-3
Alternative name(s):
Chromosome 3p kinase
Short name:
3pK
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6888. MAPKAPK3.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Predominantly located in the nucleus, when activated it translocates to the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nuclear membrane Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731K → M: Higher affinity toward PCH2. 1 Publication

Organism-specific databases

PharmGKBiPA30632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382MAP kinase-activated protein kinase 3PRO_0000086293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei201 – 2011Phosphothreonine; by MAPK14By similarity
Modified residuei251 – 2511Phosphoserine; by MAPK14By similarity
Modified residuei307 – 3071Phosphoserine; by autocatalysisBy similarity
Modified residuei313 – 3131Phosphothreonine; by MAPK14By similarity

Post-translational modificationi

Phosphorylated and activated by MAPK1/ERK2 and MAPK3/ERK1. Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16644.
PaxDbiQ16644.
PeptideAtlasiQ16644.
PRIDEiQ16644.

PTM databases

PhosphoSiteiQ16644.

Expressioni

Tissue specificityi

Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain.2 Publications

Gene expression databases

BgeeiQ16644.
CleanExiHS_MAPKAPK3.
ExpressionAtlasiQ16644. baseline and differential.
GenevestigatoriQ16644.

Organism-specific databases

HPAiHPA049533.

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 (By similarity). Interacts with TCF3 and with polycomb proteins, such as PCH2 and BMI1/PCGF4.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279585EBI-1384657,EBI-6377335From a different organism.
HSPB1P047923EBI-1384657,EBI-352682
MAPK14Q165393EBI-1384657,EBI-73946

Protein-protein interaction databases

BioGridi113617. 20 interactions.
IntActiQ16644. 12 interactions.
MINTiMINT-3032958.
STRINGi9606.ENSP00000350639.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 413Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi56 – 638Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 7810Combined sources
Helixi79 – 9113Combined sources
Beta strandi100 – 1089Combined sources
Beta strandi111 – 1199Combined sources
Helixi126 – 1316Combined sources
Helixi140 – 15920Combined sources
Helixi169 – 1713Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi183 – 1853Combined sources
Helixi218 – 23720Combined sources
Turni267 – 2693Combined sources
Beta strandi271 – 2733Combined sources
Helixi275 – 28410Combined sources
Helixi289 – 2913Combined sources
Helixi295 – 3006Combined sources
Helixi302 – 3054Combined sources
Helixi307 – 3093Combined sources
Helixi317 – 3237Combined sources
Helixi325 – 3273Combined sources
Helixi328 – 34316Combined sources
Beta strandi344 – 3463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FHRX-ray1.90A33-349[»]
3FXWX-ray2.00A33-349[»]
3R1NX-ray2.09A33-349[»]
3SHEX-ray2.25A33-349[»]
ProteinModelPortaliQ16644.
SMRiQ16644. Positions 33-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16644.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 304261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 34337Autoinhibitory helixBy similarityAdd
BLAST
Regioni345 – 36925p38 MAPK-binding siteBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi335 – 34410Nuclear export signal (NES)By similarity
Motifi350 – 3534Bipartite nuclear localization signal 1By similarity
Motifi364 – 3685Bipartite nuclear localization signal 2By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOGENOMiHOG000233031.
HOVERGENiHBG106948.
InParanoidiQ16644.
KOiK04444.
OMAiIRMGQYG.
OrthoDBiEOG786H3M.
PhylomeDBiQ16644.
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.
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. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16644-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL
60 70 80 90 100
GLGVNGKVLE CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI
110 120 130 140 150
LDVYENMHHG KRCLLIIMEC MEGGELFSRI QERGDQAFTE REAAEIMRDI
160 170 180 190 200
GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD AVLKLTDFGF AKETTQNALQ
210 220 230 240 250
TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP PFYSNTGQAI
260 270 280 290 300
SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN
310 320 330 340 350
HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK
360 370 380
IKDLKTSNNR LLNKRRKKQA GSSSASQGCN NQ
Length:382
Mass (Da):42,987
Last modified:November 1, 1996 - v1
Checksum:i405F958B7F54E6F3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281P → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_040755
Natural varianti105 – 1051E → A in an ovarian endometrioid sample; somatic mutation. 1 Publication
VAR_040756
Natural varianti276 – 2761D → Y.1 Publication
Corresponds to variant rs56107897 [ dbSNP | Ensembl ].
VAR_040757

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43784 mRNA. Translation: AAC50428.1.
U09578 mRNA. Translation: AAD09136.1.
AB451303 mRNA. Translation: BAG70117.1.
CH471055 Genomic DNA. Translation: EAW65131.1.
BC001662 mRNA. Translation: AAH01662.1.
BC007591 mRNA. Translation: AAH07591.1.
BC010407 mRNA. Translation: AAH10407.1.
CCDSiCCDS2832.1.
PIRiJC6094.
RefSeqiNP_001230854.1. NM_001243925.1.
NP_001230855.1. NM_001243926.1.
NP_004626.1. NM_004635.4.
UniGeneiHs.234521.
Hs.735013.

Genome annotation databases

EnsembliENST00000357955; ENSP00000350639; ENSG00000114738.
ENST00000446044; ENSP00000396467; ENSG00000114738.
ENST00000621469; ENSP00000478922; ENSG00000114738.
GeneIDi7867.
KEGGihsa:7867.
UCSCiuc003day.2. human.

Polymorphism databases

DMDMi74762148.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43784 mRNA. Translation: AAC50428.1.
U09578 mRNA. Translation: AAD09136.1.
AB451303 mRNA. Translation: BAG70117.1.
CH471055 Genomic DNA. Translation: EAW65131.1.
BC001662 mRNA. Translation: AAH01662.1.
BC007591 mRNA. Translation: AAH07591.1.
BC010407 mRNA. Translation: AAH10407.1.
CCDSiCCDS2832.1.
PIRiJC6094.
RefSeqiNP_001230854.1. NM_001243925.1.
NP_001230855.1. NM_001243926.1.
NP_004626.1. NM_004635.4.
UniGeneiHs.234521.
Hs.735013.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FHRX-ray1.90A33-349[»]
3FXWX-ray2.00A33-349[»]
3R1NX-ray2.09A33-349[»]
3SHEX-ray2.25A33-349[»]
ProteinModelPortaliQ16644.
SMRiQ16644. Positions 33-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113617. 20 interactions.
IntActiQ16644. 12 interactions.
MINTiMINT-3032958.
STRINGi9606.ENSP00000350639.

Chemistry

BindingDBiQ16644.
ChEMBLiCHEMBL4670.
GuidetoPHARMACOLOGYi2095.

PTM databases

PhosphoSiteiQ16644.

Polymorphism databases

DMDMi74762148.

Proteomic databases

MaxQBiQ16644.
PaxDbiQ16644.
PeptideAtlasiQ16644.
PRIDEiQ16644.

Protocols and materials databases

DNASUi7867.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357955; ENSP00000350639; ENSG00000114738.
ENST00000446044; ENSP00000396467; ENSG00000114738.
ENST00000621469; ENSP00000478922; ENSG00000114738.
GeneIDi7867.
KEGGihsa:7867.
UCSCiuc003day.2. human.

Organism-specific databases

CTDi7867.
GeneCardsiGC03P050648.
HGNCiHGNC:6888. MAPKAPK3.
HPAiHPA049533.
MIMi602130. gene.
neXtProtiNX_Q16644.
PharmGKBiPA30632.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOGENOMiHOG000233031.
HOVERGENiHBG106948.
InParanoidiQ16644.
KOiK04444.
OMAiIRMGQYG.
OrthoDBiEOG786H3M.
PhylomeDBiQ16644.
TreeFamiTF312891.

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_228166. VEGFA-VEGFR2 Pathway.
SignaLinkiQ16644.

Miscellaneous databases

ChiTaRSiMAPKAPK3. human.
EvolutionaryTraceiQ16644.
GeneWikiiMAPKAPK3.
GenomeRNAii7867.
NextBioi30313.
PROiQ16644.
SOURCEiSearch...

Gene expression databases

BgeeiQ16644.
CleanExiHS_MAPKAPK3.
ExpressionAtlasiQ16644. baseline and differential.
GenevestigatoriQ16644.

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.
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. 1 hit.
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. "Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase."
    McLaughlin M.M., Kumar S., McDonnell P.C., Van Horn S., Lee J.C., Livi G.P., Young P.R.
    J. Biol. Chem. 271:8488-8492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  2. "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region."
    Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G.
    , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.
    Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION BY MAPK1/ERK2 AND MAPK3/ERK1.
    Tissue: Heart.
  3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Colon and Skin.
  6. "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress."
    Clifton A.D., Young P.R., Cohen P.
    FEBS Lett. 392:209-214(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF HSPB1.
  7. "Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation."
    Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.
    J. Biol. Chem. 274:18947-18956(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
  8. "Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity."
    Neufeld B., Grosse-Wilde A., Hoffmeyer A., Jordan B.W., Chen P., Dinev D., Ludwig S., Rapp U.R.
    J. Biol. Chem. 275:20239-20242(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TCF3.
  9. "Mitogen-activated 3p kinase is active in the nucleus."
    Zakowski V., Keramas G., Kilian K., Rapp U.R., Ludwig S.
    Exp. Cell Res. 299:101-109(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1."
    Voncken J.W., Niessen H., Neufeld B., Rennefahrt U., Dahlmans V., Kubben N., Holzer B., Ludwig S., Rapp U.R.
    J. Biol. Chem. 280:5178-5187(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-73, INTERACTION WITH PHC2 AND BMI1.
  11. "Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex."
    Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P.
    Biochem. J. 409:711-722(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TAB3.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin."
    Ronkina N., Menon M.B., Schwermann J., Tiedje C., Hitti E., Kotlyarov A., Gaestel M.
    Biochem. Pharmacol. 80:1915-1920(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: REVIEW.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand."
    Cheng R., Felicetti B., Palan S., Toogood-Johnson I., Scheich C., Barker J., Whittaker M., Hesterkamp T.
    Protein Sci. 19:168-173(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR P4O.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR 5B.
  19. "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] SER-28; ALA-105 AND TYR-276.

Entry informationi

Entry nameiMAPK3_HUMAN
AccessioniPrimary (citable) accession number: Q16644
Secondary accession number(s): B5BU67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 131 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 3
    Human chromosome 3: 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.