Q15759 (MK11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 11
Short name=MAP kinase 11
Short name=MAPK 11
EC=2.7.11.24

Alternative name(s):
Mitogen-activated protein kinase p38 beta
Short name=MAP kinase p38 beta
Short name=p38b
Stress-activated protein kinase 2b
Short name=SAPK2b
p38-2

Gene names

Name:	MAPK11
Synonyms:	PRKM11, SAPK2, SAPK2B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 functions are mostly redundant with those of MAPK14. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Additional examples of p38 MAPK substrates are the FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Ref.4 Ref.13 Ref.14 Ref.16 Ref.17
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by phosphorylation on threonine and tyrosine by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 induced by environmental stress. HDAC3 interacts directly and selectively with MAPK11 to repress ATF2 transcriptional activity, and regulate TNF gene expression in LPS-stimulated cells. Inhibited by SB203580 and pyridinyl-imidazole related compounds. Ref.4 Ref.5 Ref.15 Ref.17
Subunit structure	Interacts with HDAC3 and DUSP16. Ref.15 Ref.17
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Highest levels in the brain and heart. Also expressed in the placenta, lung, liver, skeletal muscle, kidney and pancreas.
Domain	The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Post-translational modification	Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6, which activates the enzyme. Ref.17
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent 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 Toll signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome muscle cell differentiation Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: Reactome stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from direct assay Ref.14Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TP53	P04637	2	EBI-298304,EBI-366083

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

Mitogen-activated protein kinase 11

PRO_0000186280

Regions

Domain

24 – 308

285

Protein kinase

Nucleotide binding

30 – 38

9

ATP By similarity

Region

106 – 110

5

Inhibitor-binding

Region

168 – 169

2

Inhibitor-binding

Motif

180 – 182

3

TXY

Sites

Active site

150

1

Proton acceptor By similarity

Binding site

53

1

ATP By similarity

Binding site

71

1

Nilotinib

Amino acid modifications

Modified residue

180

1

Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K6

Modified residue

182

1

Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K6

Modified residue

323

1

Phosphotyrosine; by ZAP70 By similarity

Natural variations

Natural variant

221

1

A → V in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.22

VAR_042264

Natural variant

275

1

R → H. Ref.8 Ref.22
Corresponds to variant rs33932986 [ dbSNP | Ensembl ].

VAR_025176

Experimental info

Mutagenesis

180

1

T → A: Inactivation.

Mutagenesis

182

1

Y → F: Inactivation.

Sequence conflict

122 – 123

2

LS → GAHQGARLAL in AAB05036. Ref.1

Sequence conflict

326

1

S → G in AAB66313. Ref.6

Secondary structure

1

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364

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Beta strand

17 – 21

5

Beta strand

24 – 29

6

Beta strand

31 – 33

3

Turn

34 – 37

4

Beta strand

38 – 43

6

Turn

44 – 47

4

Beta strand

48 – 54

7

Helix

62 – 77

16

Beta strand

86 – 90

5

Helix

96 – 98

3

Beta strand

103 – 107

5

Beta strand

110 – 112

3

Helix

113 – 119

7

Helix

124 – 143

20

Helix

153 – 155

3

Beta strand

156 – 158

3

Beta strand

164 – 166

3

Helix

179 – 182

4

Helix

185 – 188

4

Helix

191 – 194

4

Helix

203 – 218

16

Helix

228 – 239

12

Helix

244 – 249

6

Turn

253 – 255

3

Helix

256 – 260

5

Helix

270 – 273

4

Turn

274 – 276

3

Helix

279 – 285

7

Turn

286 – 288

3

Helix

293 – 295

3

Helix

299 – 302

4

Helix

306 – 308

3

Turn

309 – 311

3

Helix

314 – 316

3

Helix

326 – 329

4

Helix

334 – 347

14

Sequences

	Sequence		Length	Mass (Da)
	Q15759 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 68DA4C7B7C721475	FASTA	364	41,357
	10 20 30 40 50 60 MSGPRAGFYR QELNKTVWEV PQRLQGLRPV GSGAYGSVCS AYDARLRQKV AVKKLSRPFQ 70 80 90 100 110 120 SLIHARRTYR ELRLLKHLKH ENVIGLLDVF TPATSIEDFS EVYLVTTLMG ADLNNIVKCQ 130 140 150 160 170 180 ALSDEHVQFL VYQLLRGLKY IHSAGIIHRD LKPSNVAVNE DCELRILDFG LARQADEEMT 190 200 210 220 230 240 GYVATRWYRA PEIMLNWMHY NQTVDIWSVG CIMAELLQGK ALFPGSDYID QLKRIMEVVG 250 260 270 280 290 300 TPSPEVLAKI SSEHARTYIQ SLPPMPQKDL SSIFRGANPL AIDLLGRMLV LDSDQRVSAA 310 320 330 340 350 360 EALAHAYFSQ YHDPEDEPEA EPYDESVEAK ERTLEEWKEL TYQEVLSFKP PEPPKPPGSL EIEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)." Jiang Y., Chen C., Li Z., Guo W., Gegner J.A., Lin S., Han J. J. Biol. Chem. 271:17920-17926(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	Jiang Y., Han J. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles." Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R. Biochem. Biophys. Res. Commun. 235:533-538(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6." Enslen H., Raingeaud J., Davis R.J. J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, ENZYME REGULATION. Tissue: Brain.
[5]	"Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases." Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P. EMBO J. 16:3563-3571(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION.
[6]	"p38-2, a novel mitogen-activated protein kinase with distinct properties." Stein B., Yang M.X., Young D.B., Janknecht R., Hunter T., Murray B.W., Barbosa M.S. J. Biol. Chem. 272:19509-19517(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	NIEHS SNPs program Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-275.
[9]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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: Brain.
[13]	"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB." Deak M., Clifton A.D., Lucocq J.M., Alessi D.R. EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
[14]	"Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors." Yang S.-H., Galanis A., Sharrocks A.D. Mol. Cell. Biol. 19:4028-4038(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
[15]	"A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs." Tanoue T., Yamamoto T., Maeda R., Nishida E. J. Biol. Chem. 276:26629-26639(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DUSP16, ENZYME REGULATION.
[16]	"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells." Scheper G.C., Morrice N.A., Kleijn M., Proud C.G. Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS MKNK2 KINASE.
[17]	"Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression." Mahlknecht U., Will J., Varin A., Hoelzer D., Herbein G. J. Immunol. 173:3979-3990(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC3, PHOSPHORYLATION, ENZYME REGULATION, FUNCTION IN ATF2 ACTIVATION.
[18]	"In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance." Shi Y., Gaestel M. Biol. Chem. 383:1519-1536(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[19]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"Mechanisms and functions of p38 MAPK signalling." Cuadrado A., Nebreda A.R. Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
[21]	"The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha." Patel S.B., Cameron P.M., O'Keefe S.J., Frantz-Wattley B., Thompson J., O'Neill E.A., Tennis T., Liu L., Becker J.W., Scapin G. Acta Crystallogr. D 65:777-785(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[22]	"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] VAL-221 AND HIS-275.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U53442 mRNA. Translation: AAB05036.1.
AF001008 mRNA. Translation: AAC51250.1.
AF001174 mRNA. Translation: AAC51373.1.
AF031135 mRNA. Translation: AAC12714.1.
Y14440 mRNA. Translation: CAA74792.1.
U92268 mRNA. Translation: AAB66313.1.
CR456514 mRNA. Translation: CAG30400.1.
DQ279722 Genomic DNA. Translation: ABB72677.1.
EU332851 Genomic DNA. Translation: ABY87540.1.
AL022328 Genomic DNA. No translation available.
CH471138 Genomic DNA. Translation: EAW73524.1.
BC027933 mRNA. Translation: AAH27933.1.

IPI

IPI00019473.

PIR

G02524.
JC5529.

RefSeq

NP_002742.3. NM_002751.5.

UniGene

Hs.57732.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GC8	X-ray	2.40	A/B	1-364	[»]
3GC9	X-ray	2.05	A/B	1-364	[»]
3GP0	X-ray	1.90	A	5-350	[»]

ProteinModelPortal

Q15759.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15759. 7 interactions.

MINT

MINT-3032032.

STRING

9606.ENSP00000333685.

PTM databases

PhosphoSite

Q15759.

Polymorphism databases

DMDM

134047835.

Proteomic databases

PaxDb

Q15759.

PRIDE

Q15759.

Protocols and materials databases

DNASU

5600.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330651; ENSP00000333685; ENSG00000185386.
ENST00000395764; ENSP00000379113; ENSG00000185386.

GeneID

5600.

KEGG

hsa:5600.

UCSC

uc003bkr.3. human.

Organism-specific databases

CTD

5600.

GeneCards

GC22M050702.

HGNC

HGNC:6873. MAPK11.

HPA

CAB012961.

MIM

602898. gene.

neXtProt

NX_Q15759.

PharmGKB

PA30618.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

Q15759.

KO

K04441.

OMA

ETIGGCE.

OrthoDB

EOG4PC9SB.

PhylomeDB

Q15759.

Enzyme and pathway databases

BRENDA

2.7.11.24. 2681.

Pathway_Interaction_DB

il2_1pathway. IL2-mediated signaling events.
il6_7pathway. IL6-mediated signaling events.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
txa2pathway. Thromboxane A2 receptor signaling.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_21257. Metabolism of RNA.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15759.

Bgee

Q15759.

CleanEx

HS_MAPK11.

Genevestigator

Q15759.

GermOnline

ENSG00000185386. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01773. P38MAPKINASE.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q15759.

ChEMBL

CHEMBL3961.

EvolutionaryTrace

Q15759.

GenomeRNAi

5600.

NextBio

21748.

SOURCE

Search...

Entry information

Entry name

MK11_HUMAN

Accession

Primary (citable) accession number: Q15759
Secondary accession number(s): B0LPG1 , O00284, O15472, Q2XNF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.