Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

MAP kinase-activated protein kinase 2 (MAPK-activated protein kinase 2) (MAPKAP kinase 2) (MAPKAP-K2) (MAPKAPK-2) (MK-2) (MK2) (EC 2.7.11.1) (P45-54 HSP27 kinase) (Fragment)

 MAPK2_CRILO             Reviewed;         329 AA.
P49136;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 92.
RecName: Full=MAP kinase-activated protein kinase 2;
Short=MAPK-activated protein kinase 2;
Short=MAPKAP kinase 2;
Short=MAPKAP-K2;
Short=MAPKAPK-2;
Short=MK-2;
Short=MK2;
EC=2.7.11.1;
AltName: Full=P45-54 HSP27 kinase;
Flags: Fragment;
Name=MAPKAPK2;
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese
hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10030;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=7851416; DOI=10.1111/j.1432-1033.1995.tb20404.x;
Huot J., Lambert H., Lavoie J.N., Guimond A., Houle F., Landry J.;
"Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive
kinase which may activate the phosphorylation-dependent protective
function of mammalian 27-kDa heat-shock protein HSP27.";
Eur. J. Biochem. 227:416-427(1995).
-!- FUNCTION: 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, HSP27/HSPB1, KRT18,
KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and
TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with
HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding
and transactivation activities. 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 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 following
ultraviolet irradiation which promotes binding of CEP131 to 14-3-3
proteins and inhibits formation of novel centriolar satellites.
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.
{ECO:0000250|UniProtKB:P49137}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ACTIVITY REGULATION: Activated following phosphorylation by p38-
alpha/MAPK14 following various stresses. Inhibited following
sumoylation. Specifically inhibited by pyrrolopyridine inhibitors
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer with p38-alpha/MAPK14; this heterodimer 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. Interacts with HSF1.
{ECO:0000250|UniProtKB:P49137}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49137}.
Nucleus {ECO:0000250|UniProtKB:P49137}. Note=Phosphorylation and
subsequent activation releases the autoinhibitory helix, resulting
in the export from the nucleus into the cytoplasm.
{ECO:0000250|UniProtKB:P49137}.
-!- PTM: Sumoylation inhibits the protein kinase activity.
{ECO:0000250|UniProtKB:P49137}.
-!- PTM: Phosphorylated and activated by MAP kinase p38-alpha/MAPK14
at Thr-151, Ser-201 and Thr-263. {ECO:0000250|UniProtKB:P49137}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X82220; CAA57700.1; -; mRNA.
PIR; S49490; S49490.
ProteinModelPortal; P49136; -.
SMR; P49136; -.
PRIDE; P49136; -.
HOVERGEN; HBG106948; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
GO; GO:0032675; P:regulation of interleukin-6 production; ISS:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
Gene3D; 4.10.1170.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027442; MAPKAPK_C.
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.
2: Evidence at transcript level;
ATP-binding; Cytoplasm; DNA damage; Isopeptide bond; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN <1 329 MAP kinase-activated protein kinase 2.
/FTId=PRO_0000086287.
DOMAIN <1 254 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND <1 7 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 68 70 Staurosporine binding. {ECO:0000250}.
REGION 257 293 Autoinhibitory helix. {ECO:0000250}.
REGION 295 319 p38 MAPK-binding site. {ECO:0000250}.
MOTIF 285 294 Nuclear export signal (NES).
{ECO:0000250}.
MOTIF 300 303 Bipartite nuclear localization signal 1.
{ECO:0000250}.
MOTIF 314 318 Bipartite nuclear localization signal 2.
{ECO:0000250}.
ACT_SITE 115 115 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 22 22 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 151 151 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:P49137}.
MOD_RES 201 201 Phosphoserine; by MAPK14.
{ECO:0000250|UniProtKB:P49137}.
MOD_RES 257 257 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 263 263 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:P49137}.
CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
NON_TER 1 1
SEQUENCE 329 AA; 38014 MW; A61F67DAA05EB88F CRC64;
LGINGKVLRI FDKRTQQKFA LKMLQDCPKA RREVELHWRA SQCPHIVDIV DVYENLYAGR
KCLLIVMECL DGGELFSRIQ DRGDQAFTER EASEIMKSIG EAIQYLHSIN IAHRDVKPEN
LLYTSKRPNA ILKLTDFGFA KETTSHNSLT TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV
IMYILLCGYP PFYSNHGLAI SPGMKTRIRM GQYEFPNPEW SEVSEEVKML IRNLLKTEPT
QRMTITEFMN HPWIMQSTKV PQTPLHTSRV LKEDKERWED VKEEMTSALA TMRVDYEQIK
IKKIEDASNP LLLKRRKKAR AVEAAALAH


Related products :

Catalog number Product name Quantity
E1632h ELISA kit 3pK,Chromosome 3p kinase,Homo sapiens,Human,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
U1632h CLIA 3pK,Chromosome 3p kinase,Homo sapiens,Human,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
E1632h ELISA 3pK,Chromosome 3p kinase,Homo sapiens,Human,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
E1632r ELISA MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Rat,Rattus norvegicus 96T
E1632m ELISA MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Mouse,Mus musculus 96T
E1632b ELISA Bos taurus,Bovine,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
E1632r ELISA kit MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Rat,Rattus norvegicus 96T
E1632b ELISA kit Bos taurus,Bovine,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
E1632m ELISA kit MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Mouse,Mus musculus 96T
U1632r CLIA MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Rat,Rattus norvegicus 96T
U1632m CLIA MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,Mapkapk3,MAPKAPK-3,Mouse,Mus musculus 96T
U1632b CLIA Bos taurus,Bovine,MAP kinase-activated protein kinase 3,MAPK-activated protein kinase 3,MAPKAP kinase 3,MAPKAPK3,MAPKAPK-3 96T
15-288-22349B MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK Polyclonal 0.1 mg
15-288-22349A MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK Polyclonal 0.05 mg
15-288-22349B MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK Polyclonal 0.05 mg
15-288-22349A MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK Polyclonal 0.1 mg
10-782-55070 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.05 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.001 mg
10-288-22349F MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK 0.1 mg
10-288-22349F MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK 0.05 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.005 mg
10-782-55070 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.02 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.02 mg
10-782-55069 MAP kinase-activated protein kinase 3 - EC 2.7.11.1; MAPK-activated protein kinase 3; MAPKAP kinase 3; MAPKAPK-3; Chromosome 3p kinase; 3pK N_A 0.01 mg
18-003-42985 MAP kinase-activated protein kinase 2 - EC 2.7.11.1; MAPK-activated protein kinase 2; MAPKAP kinase 2; MAPKAPK-2; MK2 Polyclonal 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur