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MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)

 MAPK5_HUMAN             Reviewed;         473 AA.
Q8IW41; B3KVA5; O60491; Q86X46; Q9BVX9; Q9UG86;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 2.
07-APR-2021, entry version 176.
RecName: Full=MAP kinase-activated protein kinase 5;
Short=MAPK-activated protein kinase 5;
Short=MAPKAP kinase 5;
Short=MAPKAP-K5;
Short=MAPKAPK-5;
Short=MK-5;
Short=MK5;
EC=2.7.11.1;
AltName: Full=p38-regulated/activated protein kinase;
Short=PRAK;
Name=MAPKAPK5; Synonyms=PRAK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), MUTAGENESIS OF THR-182,
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-182, AND ACTIVITY
REGULATION.
TISSUE=Placenta;
PubMed=9628874; DOI=10.1093/emboj/17.12.3372;
New L., Jiang Y., Zhao M., Liu K., Zhu W., Flood L.J., Kato Y.,
Parry G.C.N., Han J.;
"PRAK, a novel protein kinase regulated by the p38 MAP kinase.";
EMBO J. 17:3372-3384(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix, Pancreas, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-473 (ISOFORM 2).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
INTERACTION WITH SQSTM1, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
PubMed=10708586; DOI=10.1006/bbrc.2000.2333;
Sudo T., Maruyama M., Osada H.;
"p62 functions as a p38 MAP kinase regulator.";
Biochem. Biophys. Res. Commun. 269:521-525(2000).
[7]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-212, MUTAGENESIS OF THR-182,
AND MUTAGENESIS OF LYS-51; THR-182 AND SER-212.
PubMed=12808055; DOI=10.1091/mbc.e02-08-0538;
New L., Jiang Y., Han J.;
"Regulation of PRAK subcellular location by p38 MAP kinases.";
Mol. Biol. Cell 14:2603-2616(2003).
[8]
FUNCTION IN PHOSPHORYLATION OF HSPB1, AND INTERACTION WITH YWHAE.
PubMed=17728103; DOI=10.1016/j.cellsig.2007.07.016;
Tak H., Jang E., Kim S.B., Park J., Suk J., Yoon Y.S., Ahn J.K., Lee J.H.,
Joe C.O.;
"14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin
polymerization.";
Cell. Signal. 19:2379-2387(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
FUNCTION IN PHOSPHORYLATION OF HSPB1.
PubMed=19166925; DOI=10.1016/j.cellsig.2009.01.009;
Kostenko S., Johannessen M., Moens U.;
"PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the
MAPKAP kinase MK5.";
Cell. Signal. 21:712-718(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND SER-354, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
VARIANTS [LARGE SCALE ANALYSIS] ILE-67 AND LYS-282.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[15]
FUNCTION IN PHOSPHORYLATION OF TP53.
PubMed=17254968; DOI=10.1016/j.cell.2006.11.050;
Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C., Chen J.,
Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III, Wright P.E.,
Han J.;
"PRAK is essential for ras-induced senescence and tumor suppression.";
Cell 128:295-308(2007).
[16]
FUNCTION IN PHOSPHORYLATION OF FOXO3, AUTOPHOSPHORYLATION, INDUCTION, AND
MUTAGENESIS OF THR-182 AND LEU-337.
PubMed=21329882; DOI=10.1016/j.molcel.2011.01.023;
Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M., Roepman P.,
Burgering B.M., Bushell M., Rosenwald A., Eilers M.;
"The MK5/PRAK kinase and Myc form a negative feedback loop that is
disrupted during colorectal tumorigenesis.";
Mol. Cell 41:445-457(2011).
[17]
REVIEW.
PubMed=20227494; DOI=10.1016/j.cellsig.2010.03.002;
Shiryaev A., Moens U.;
"Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: menage a trois
or menage a quatre?";
Cell. Signal. 22:1185-1192(2010).
-!- FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in
mTORC1 signaling and post-transcriptional regulation. Phosphorylates
FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as
a tumor suppressor by mediating Ras-induced senescence and
phosphorylating p53/TP53. Involved in post-transcriptional regulation
of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3
leads to promote nuclear localization of FOXO3, enabling expression of
miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind
to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a
negative regulator of mTORC1 signaling by mediating phosphorylation and
inhibition of RHEB. Part of the atypical MAPK signaling via its
interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the
complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the
complex follows a complex set of phosphorylation events: upon
interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6
(or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and
activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or
ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to
PKA/PRKACA stimulation, inducing F-actin rearrangement.
{ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17728103,
ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:21329882,
ECO:0000269|PubMed:9628874}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- ACTIVITY REGULATION: Activated following phosphorylation at Thr-182 by
p38-alpha/MAPK14, p38-beta/MAPK11, ERK2/MAPK1, ERK3/MAPK6, and
ERK4/MAPK4. Activated by stress-related extracellular stimuli; such as
H(2)O(2), arsenite, anisomycin TNF alpha and also PMA and the calcium
ionophore A23187; but to a lesser extent. In vitro, activated by
SQSTM1. Inhibited by diterpenoid alkaloid noroxoaconitine.
{ECO:0000269|PubMed:10708586, ECO:0000269|PubMed:9628874}.
-!- SUBUNIT: Interacts with ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif);
the interaction is direct (By similarity). Interacts with YWHAE; the
interaction prevents phosphorylation of HSP27/HSPB1 leading to disrupt
F-actin polymerization. Interacts with SQSTM1. {ECO:0000250,
ECO:0000269|PubMed:10708586, ECO:0000269|PubMed:17728103}.
-!- INTERACTION:
Q8IW41; Q15109: AGER; NbExp=6; IntAct=EBI-1201460, EBI-1646426;
Q8IW41; P04792: HSPB1; NbExp=2; IntAct=EBI-1201460, EBI-352682;
Q8IW41; Q16659: MAPK6; NbExp=7; IntAct=EBI-1201460, EBI-1384105;
Q8IW41; P04637: TP53; NbExp=2; IntAct=EBI-1201460, EBI-366083;
Q8IW41-2; Q16659: MAPK6; NbExp=6; IntAct=EBI-11958803, EBI-1384105;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
cytoplasm following phosphorylation and activation. Interaction with
ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the
protein kinase activity, followed by translocation to the cytoplasm.
Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IW41-1; Sequence=Displayed;
Name=2;
IsoId=Q8IW41-2; Sequence=VSP_011597;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:9628874}.
-!- INDUCTION: Directly regulated by MYC: expression is activated by MYC,
suggesting the existence of a feedback regulatory loop.
{ECO:0000269|PubMed:21329882}.
-!- PTM: Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the
regulatory phosphorylation site and is located on the T-loop/loop 12,
leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14,
p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by
PKA/PRKACA, leading to localization to the cytoplasm.
Autophosphorylated (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
protein kinase family. {ECO:0000305}.
-!- CAUTION: The role of p38 MAPK kinases is unclear in phosphorylation and
activation of MAPKAPK5. According to some reports, it interacts and is
phosphorylated by p38-alpha/MAPK14 and p38-beta/MAPK11 (PubMed:9628874
and PubMed:12808055). According to other reports, it is not activated
by p38-alpha/MAPK14 and p38-beta/MAPK11. An explanation for these
discrepancies, might be that the interaction with p38 MAPK kinases is
weak and occurs only under specific conditions. {ECO:0000305}.
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EMBL; AF032437; AAC39863.1; -; Genomic_DNA.
EMBL; AK122767; BAG53717.1; -; mRNA.
EMBL; CH471054; EAW97981.1; -; Genomic_DNA.
EMBL; BC000833; AAH00833.1; -; mRNA.
EMBL; BC041049; AAH41049.1; -; mRNA.
EMBL; BC047284; AAH47284.2; -; mRNA.
EMBL; AL110301; CAB53747.1; -; mRNA.
CCDS; CCDS44975.1; -. [Q8IW41-1]
CCDS; CCDS44976.1; -. [Q8IW41-2]
PIR; T34519; T34519.
RefSeq; NP_003659.2; NM_003668.3. [Q8IW41-2]
RefSeq; NP_620777.1; NM_139078.2. [Q8IW41-1]
SMR; Q8IW41; -.
BioGRID; 114120; 29.
CORUM; Q8IW41; -.
IntAct; Q8IW41; 22.
MINT; Q8IW41; -.
STRING; 9606.ENSP00000449381; -.
BindingDB; Q8IW41; -.
ChEMBL; CHEMBL3094; -.
DrugBank; DB12010; Fostamatinib.
GuidetoPHARMACOLOGY; 2096; -.
iPTMnet; Q8IW41; -.
PhosphoSitePlus; Q8IW41; -.
BioMuta; MAPKAPK5; -.
DMDM; 52000829; -.
EPD; Q8IW41; -.
jPOST; Q8IW41; -.
MassIVE; Q8IW41; -.
MaxQB; Q8IW41; -.
PaxDb; Q8IW41; -.
PeptideAtlas; Q8IW41; -.
PRIDE; Q8IW41; -.
ProteomicsDB; 70805; -. [Q8IW41-1]
ProteomicsDB; 70806; -. [Q8IW41-2]
Antibodypedia; 3873; 612 antibodies.
DNASU; 8550; -.
Ensembl; ENST00000550735; ENSP00000449667; ENSG00000089022. [Q8IW41-2]
Ensembl; ENST00000551404; ENSP00000449381; ENSG00000089022. [Q8IW41-1]
GeneID; 8550; -.
KEGG; hsa:8550; -.
UCSC; uc001tta.5; human. [Q8IW41-1]
CTD; 8550; -.
DisGeNET; 8550; -.
GeneCards; MAPKAPK5; -.
HGNC; HGNC:6889; MAPKAPK5.
HPA; ENSG00000089022; Low tissue specificity.
MIM; 606723; gene.
neXtProt; NX_Q8IW41; -.
OpenTargets; ENSG00000089022; -.
PharmGKB; PA30633; -.
VEuPathDB; HostDB:ENSG00000089022.13; -.
eggNOG; KOG0604; Eukaryota.
GeneTree; ENSGT00940000154089; -.
HOGENOM; CLU_000288_63_0_1; -.
InParanoid; Q8IW41; -.
OMA; GFFIHDP; -.
OrthoDB; 843707at2759; -.
PhylomeDB; Q8IW41; -.
TreeFam; TF312891; -.
PathwayCommons; Q8IW41; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q8IW41; -.
SIGNOR; Q8IW41; -.
BioGRID-ORCS; 8550; 17 hits in 1029 CRISPR screens.
ChiTaRS; MAPKAPK5; human.
GeneWiki; MAPKAPK5; -.
GenomeRNAi; 8550; -.
Pharos; Q8IW41; Tchem.
PRO; PR:Q8IW41; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; Q8IW41; protein.
Bgee; ENSG00000089022; Expressed in corpus callosum and 220 other tissues.
ExpressionAtlas; Q8IW41; baseline and differential.
Genevisible; Q8IW41; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IBA:GO_Central.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0090400; P:stress-induced premature senescence; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tumor suppressor.
CHAIN 1..473
/note="MAP kinase-activated protein kinase 5"
/id="PRO_0000086296"
DOMAIN 22..304
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 28..36
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
COILED 409..440
/evidence="ECO:0000255"
ACT_SITE 148
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 51
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 115
/note="Phosphoserine; by PKA"
/evidence="ECO:0000250|UniProtKB:O54992"
MOD_RES 182
/note="Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6
and PKA"
/evidence="ECO:0000269|PubMed:9628874,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
MOD_RES 212
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:12808055"
MOD_RES 354
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
VAR_SEQ 407..408
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
/id="VSP_011597"
VARIANT 67
/note="M -> I (in dbSNP:rs34132040)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040758"
VARIANT 282
/note="R -> K (in dbSNP:rs34843470)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040759"
MUTAGEN 51
/note="K->M: Kinase defective mutant, abolishes activity."
/evidence="ECO:0000269|PubMed:12808055"
MUTAGEN 182
/note="T->A: No p38-beta/MAPK11-induced activation."
/evidence="ECO:0000269|PubMed:12808055,
ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:9628874"
MUTAGEN 182
/note="T->D: Mimicks phosphorylation state and induces
constitutive protein kinase activity."
/evidence="ECO:0000269|PubMed:12808055,
ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:9628874"
MUTAGEN 212
/note="S->D: Mimicks phosphorylation state and displays a
slightly higher protein kinase activity."
/evidence="ECO:0000269|PubMed:12808055"
MUTAGEN 337
/note="L->G: Induces constitutive protein kinase activity."
/evidence="ECO:0000269|PubMed:21329882"
CONFLICT 273
/note="I -> T (in Ref. 5; CAB53747)"
/evidence="ECO:0000305"
CONFLICT 291
/note="E -> R (in Ref. 1; AAC39863)"
/evidence="ECO:0000305"
SEQUENCE 473 AA; 54220 MW; F3D9DDC83CC0C49D CRC64;
MSEESDMDKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL KILLDRPKAR
NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI VMEMMEGGEL FHRISQHRHF
TEKQASQVTK QIALALRHCH LLNIAHRDLK PENLLFKDNS LDAPVKLCDF GFAKIDQGDL
MTPQFTPYYV APQVLEAQRR HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP
FYSKHHSRTI PKDMRRKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK PLHSVNNPIL
RKRKLLGTKP KDSVYIHDHE NGAEDSNVAL EKLRDVIAQC ILPQAGKGEN EDEKLNEVMQ
EAWKYNRECK LLRDTLQSFS WNGRGFTDKV DRLKLAEIVK QVIEEQTTSH ESQ


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP253: Glycolysis
WP32: Translation Factors
WP1681: Pantothenate and CoA biosynthesis
WP1946: Cori Cycle
WP1703: Streptomycin biosynthesis
WP1567: Glycolysis and Gluconeogenesis
WP1844: MAP kinase cascade
WP1619: Amino sugar and nucleotide sugar metabolism
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1701: Starch and sucrose metabolism
WP1653: Galactose metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2292: Chemokine signaling pathway
WP1665: Limonene and pinene degradation
WP1713: Two-component system
WP931: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP2203: TSLP Signaling Pathway
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1909: Signal regulatory protein (SIRP) family interactions
WP1690: Propanoate metabolism
WP2324: AGE/RAGE pathway
WP1650: Fluorobenzoate degradation

Related Genes :
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[Mapkapk5] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAPK-5) (EC 2.7.11.1)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAP3K5 ASK1 MAPKKK5 MEKK5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[Map3k5 Ask1 Mekk5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk14 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[RPS6KA1 MAPKAPK1A RSK1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[Rps6ka3 Mapkapk1b Rps6ka-rs1 Rsk2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP2K5 MEK5 MKK5 PRKMK5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[MAPK7 BMK1 ERK5 PRKM7] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[mapk14a mapk14] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[Rps6ka1 Mapkapk1a Rsk1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)

Bibliography :