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Q16644 (MAPK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAP kinase-activated protein kinase 3

Short name=MAPK-activated protein kinase 3
Short name=MAPKAP kinase 3
Short name=MAPKAP-K3
Short name=MAPKAPK-3
Short name=MK-3
EC=2.7.11.1
Alternative name(s):
Chromosome 3p kinase
Short name=3pK
Gene names
Name:MAPKAPK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.7

Enzyme regulation

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.

Subunit structure

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. Ref.9 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly located in the nucleus, when activated it translocates to the cytoplasm. Ref.10

Tissue specificity

Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain. Ref.1 Ref.2

Post-translational modification

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. Ref.1 Ref.2

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Ras protein signal transduction

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

macropinocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 15850461. Source: BHF-UCL

response to cytokine

Inferred from direct assay Ref.7. Source: UniProtKB

response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: UniProtKB

response to stress

Traceable author statement Ref.1. Source: ProtInc

signal transduction

Traceable author statement Ref.1. Source: ProtInc

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.9. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Traceable author statement Ref.9. Source: ProtInc

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279585EBI-1384657,EBI-6377335From a different organism.
HSPB1P047922EBI-1384657,EBI-352682

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382MAP kinase-activated protein kinase 3
PRO_0000086293

Regions

Domain44 – 304261Protein kinase
Nucleotide binding50 – 589ATP By similarity
Region307 – 34337Autoinhibitory helix By similarity
Region345 – 36925p38 MAPK-binding site By similarity
Motif335 – 34410Nuclear export signal (NES) By similarity
Motif350 – 3534Bipartite nuclear localization signal 1 By similarity
Motif364 – 3685Bipartite nuclear localization signal 2 By similarity

Sites

Active site1661Proton acceptor By similarity
Binding site731ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13 Ref.17
Modified residue2011Phosphothreonine; by MAPK14 By similarity
Modified residue2511Phosphoserine; by MAPK14 By similarity
Modified residue3071Phosphoserine; by autocatalysis By similarity
Modified residue3131Phosphothreonine; by MAPK14 By similarity

Natural variations

Natural variant281P → S in a glioblastoma multiforme sample; somatic mutation. Ref.20
VAR_040755
Natural variant1051E → A in an ovarian endometrioid sample; somatic mutation. Ref.20
VAR_040756
Natural variant2761D → Y. Ref.20
Corresponds to variant rs56107897 [ dbSNP | Ensembl ].
VAR_040757

Experimental info

Mutagenesis731K → M: Higher affinity toward PCH2. Ref.11

Secondary structure

.............................................. 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16644 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 405F958B7F54E6F3

FASTA38242,987
        10         20         30         40         50         60 
MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL GLGVNGKVLE 

        70         80         90        100        110        120 
CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI LDVYENMHHG KRCLLIIMEC 

       130        140        150        160        170        180 
MEGGELFSRI QERGDQAFTE REAAEIMRDI GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD 

       190        200        210        220        230        240 
AVLKLTDFGF AKETTQNALQ TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP 

       250        260        270        280        290        300 
PFYSNTGQAI SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN 

       310        320        330        340        350        360 
HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK IKDLKTSNNR 

       370        380 
LLNKRRKKQA GSSSASQGCN NQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Erratum
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. expand/collapse author list , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.
Mol. Cell. Biol. 16:1880-1880(1996)
[4]"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. expand/collapse author list , 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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Skin.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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].
[14]"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.
[15]"MK2 and MK3--a pair of isoenzymes?"
Ronkina N., Kotlyarov A., Gaestel M.
Front. Biosci. 13:5511-5521(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
[19]"Structure-based lead identification of ATP-competitive MK2 inhibitors."
Barf T., Kaptein A., de Wilde S., van der Heijden R., van Someren R., Demont D., Schultz-Fademrecht C., Versteegh J., van Zeeland M., Seegers N., Kazemier B., van de Kar B., van Hoek M., de Roos J., Klop H., Smeets R., Hofstra C., Hornberg J., Oubrie A.
Bioorg. Med. Chem. Lett. 21:3818-3822(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 33-349 IN COMPLEX WITH INHIBITOR 5B.
[20]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2832.1.
PIRJC6094.
RefSeqNP_001230854.1. NM_001243925.1.
NP_001230855.1. NM_001243926.1.
NP_004626.1. NM_004635.4.
UniGeneHs.234521.
Hs.735013.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FHRX-ray1.90A33-349[»]
3FXWX-ray2.00A33-349[»]
3R1NX-ray2.09A33-349[»]
3SHEX-ray2.25A33-349[»]
ProteinModelPortalQ16644.
SMRQ16644. Positions 33-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113617. 19 interactions.
IntActQ16644. 10 interactions.
MINTMINT-3032958.
STRING9606.ENSP00000350639.

Chemistry

BindingDBQ16644.
ChEMBLCHEMBL4670.
GuidetoPHARMACOLOGY2095.

PTM databases

PhosphoSiteQ16644.

Polymorphism databases

DMDM74762148.

Proteomic databases

MaxQBQ16644.
PaxDbQ16644.
PeptideAtlasQ16644.
PRIDEQ16644.

Protocols and materials databases

DNASU7867.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357955; ENSP00000350639; ENSG00000114738.
ENST00000446044; ENSP00000396467; ENSG00000114738.
GeneID7867.
KEGGhsa:7867.
UCSCuc003day.2. human.

Organism-specific databases

CTD7867.
GeneCardsGC03P050648.
HGNCHGNC:6888. MAPKAPK3.
HPAHPA049533.
MIM602130. gene.
neXtProtNX_Q16644.
PharmGKBPA30632.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233031.
HOVERGENHBG106948.
InParanoidQ16644.
KOK04444.
OMAIRMGQYG.
OrthoDBEOG786H3M.
PhylomeDBQ16644.
TreeFamTF312891.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ16644.

Gene expression databases

ArrayExpressQ16644.
BgeeQ16644.
CleanExHS_MAPKAPK3.
GenevestigatorQ16644.

Family and domain databases

Gene3D4.10.1170.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPKAPK3. human.
EvolutionaryTraceQ16644.
GeneWikiMAPKAPK3.
GenomeRNAi7867.
NextBio30313.
PROQ16644.
SOURCESearch...

Entry information

Entry nameMAPK3_HUMAN
AccessionPrimary (citable) accession number: Q16644
Secondary accession number(s): B5BU67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM