O15264 (MK13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase 13
Short name=MAP kinase 13
Short name=MAPK 13
EC=2.7.11.24

Alternative name(s):
Mitogen-activated protein kinase p38 delta
Short name=MAP kinase p38 delta
Stress-activated protein kinase 4

Gene names

Name:	MAPK13
Synonyms:	PRKM13, SAPK4

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	365 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. MAPK13 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 such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells. Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by phosphorylation on threonine and tyrosine by dual specificity kinases, MAP2K3/MKK3, MAP2K6/MKK6, MAP2K4/MKK4 and MAP2K7/MKK7. Activation by ultraviolet radiation, hyperosmotic shock, anisomycin or by TNF-alpha is mediated by MAP2K3/MKK3. Inhibited by dual specificity phosphatase DUSP1. Ref.1 Ref.2 Ref.15
Subunit structure	Interacts with MAPK8IP2. Ref.14
Tissue specificity	Expressed in testes, pancreas, small intestine, lung and kidney. Abundant in macrophages, also present in neutrophils, CD4+ T-cells, and endothelial cells. Ref.2 Ref.13
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, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1. Ref.2 Ref.21
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	Cell cycle Stress response Transcription Transcription regulation
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	Ras protein signal transduction Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome peptidyl-serine phosphorylation Inferred from direct assay PubMed 15850461. Source: BHF-UCL positive regulation of inflammatory response Inferred by curator PubMed 19279008. Source: BHF-UCL positive regulation of interleukin-6 production Inferred from mutant phenotype PubMed 19279008. Source: BHF-UCL regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to osmotic stress Inferred from direct assay Ref.12. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from direct assay Ref.1Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FPR1	P21462	3	EBI-2116951,EBI-2869495
PRKD1	Q15139	6	EBI-2116951,EBI-1181072

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Mitogen-activated protein kinase 13

PRO_0000186286

Regions

Domain

25 – 308

284

Protein kinase

Nucleotide binding

31 – 39

9

ATP By similarity

Motif

180 – 182

3

TXY

Sites

Active site

150

1

Proton acceptor By similarity

Binding site

54

1

ATP By similarity

Amino acid modifications

Modified residue

47

1

Phosphoserine Ref.20

Modified residue

180

1

Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 Ref.2

Modified residue

182

1

Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 Ref.2

Modified residue

350

1

Phosphoserine Ref.22

Natural variations

Natural variant

41

1

S → L. Ref.28
Corresponds to variant rs55776345 [ dbSNP | Ensembl ].

VAR_042267

Natural variant

282

1

A → V. Ref.28
Corresponds to variant rs55990045 [ dbSNP | Ensembl ].

VAR_042268

Natural variant

300

1

A → T. Ref.28
Corresponds to variant rs41270090 [ dbSNP | Ensembl ].

VAR_042269

Experimental info

Mutagenesis

180

1

T → A: Loss of kinase activity. Ref.2

Mutagenesis

182

1

Y → A: Loss of kinase activity. Ref.2

Sequence conflict

13 – 14

2

DV → EL in AAC51374. Ref.4

Sequence conflict

39

1

V → W in AAC51374. Ref.4

Sequence conflict

56

1

L → P in AAC51758. Ref.3

Sequence conflict

166

1

I → V in AAC51758. Ref.3

Sequence conflict

224

1

K → R in AAC51758. Ref.3

Sequence conflict

224

1

K → R in AAD23377. Ref.5

Secondary structure

1

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365

Helix Strand Turn

Details...

Helix

4 – 8

5

Beta strand

9 – 14

6

Beta strand

17 – 22

6

Beta strand

25 – 33

9

Beta strand

35 – 44

10

Turn

45 – 47

3

Beta strand

50 – 56

7

Helix

63 – 78

16

Beta strand

88 – 91

4

Beta strand

95 – 97

3

Beta strand

104 – 108

5

Beta strand

111 – 113

3

Helix

114 – 117

4

Helix

124 – 143

20

Helix

153 – 155

3

Beta strand

156 – 158

3

Beta strand

164 – 166

3

Helix

191 – 194

4

Helix

204 – 218

15

Beta strand

222 – 226

5

Helix

228 – 239

12

Helix

244 – 247

4

Helix

253 – 261

9

Helix

270 – 273

4

Helix

279 – 288

10

Turn

293 – 295

3

Helix

299 – 303

5

Helix

306 – 308

3

Turn

309 – 311

3

Helix

314 – 316

3

Turn

327 – 330

4

Helix

335 – 348

14

Sequences

	Sequence		Length	Mass (Da)
	O15264 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 52E749EDB2973DDF	FASTA	365	42,090
	10 20 30 40 50 60 MSLIRKKGFY KQDVNKTAWE LPKTYVSPTH VGSGAYGSVC SAIDKRSGEK VAIKKLSRPF 70 80 90 100 110 120 QSEIFAKRAY RELLLLKHMQ HENVIGLLDV FTPASSLRNF YDFYLVMPFM QTDLQKIMGM 130 140 150 160 170 180 EFSEEKIQYL VYQMLKGLKY IHSAGVVHRD LKPGNLAVNE DCELKILDFG LARHADAEMT 190 200 210 220 230 240 GYVVTRWYRA PEVILSWMHY NQTVDIWSVG CIMAEMLTGK TLFKGKDYLD QLTQILKVTG 250 260 270 280 290 300 VPGTEFVQKL NDKAAKSYIQ SLPQTPRKDF TQLFPRASPQ AADLLEKMLE LDVDKRLTAA 310 320 330 340 350 360 QALTHPFFEP FRDPEEETEA QQPFDDSLEH EKLTVDEWKQ HIYKEIVNFS PIARKDSRRR SGMKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. Tissue: Pituitary.
[2]	"Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta." Jiang Y., Gram H., Zhao M., New L., Gu J., Feng L., Di Padova F., Ulevitch R.J., Han J. J. Biol. Chem. 272:30122-30128(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-180 AND TYR-182, MUTAGENESIS OF THR-180 AND TYR-182, ENZYME REGULATION, TISSUE SPECIFICITY. Tissue: Liver.
[3]	"Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase." Wang X.S., Diener K., Manthey C.L., Wang S.-W., Rosenzweig B., Bray J., Delaney J., Cole C., Zukowski M., Yao Z. J. Biol. Chem. 272:23668-23674(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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].
[5]	"Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines." Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R., Tan T.-H. J. Biol. Chem. 274:7095-7102(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Structure and polymorphism of two stress-activated protein kinase genes centromeric of the MHC: SAPK2a and SAPK4." Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N., Christiansen F.T., Price P. DNA Seq. 10:229-243(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	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].
[11]	"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: Lung.
[12]	"Identification of stathmin as a novel substrate for p38 delta." Parker C.G., Hunt J., Diener K., McGinley M., Soriano B., Keesler G.A., Bray J., Yao Z., Wang X.S., Kohno T., Lichenstein H.S. Biochem. Biophys. Res. Commun. 249:791-796(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF STMN1.
[13]	"Differential expression and activation of p38 mitogen-activated protein kinase alpha, beta, gamma, and delta in inflammatory cell lineages." Hale K.K., Trollinger D., Rihanek M., Manthey C.L. J. Immunol. 162:4246-4252(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"Fibroblast growth factor homologous factors are intracellular signaling proteins." Schoorlemmer J., Goldfarb M. Curr. Biol. 11:793-797(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP2.
[15]	"A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta." Knebel A., Morrice N., Cohen P. EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[16]	"Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases in intact cells." Buee-Scherrer V., Goedert M. FEBS Lett. 515:151-154(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[17]	"Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly." Feijoo C., Campbell D.G., Jakes R., Goedert M., Cuenda A. J. Cell Sci. 118:397-408(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[18]	"Activation of PKCdelta and p38delta MAPK during okadaic acid dependent keratinocyte apoptosis." Kraft C.A., Efimova T., Eckert R.L. Arch. Dermatol. Res. 299:71-83(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN KERATINOCYTE APOPTOSIS.
[19]	"p38MAPK delta controls c-Myb degradation in response to stress." Pani E., Ferrari S. Blood Cells Mol. Dis. 40:388-394(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MYB.
[20]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Platelet.
[21]	"MKP-1 inhibits high NaCl-induced activation of p38 but does not inhibit the activation of TonEBP/OREBP: opposite roles of p38alpha and p38delta." Zhou X., Ferraris J.D., Dmitrieva N.I., Liu Y., Burg M.B. Proc. Natl. Acad. Sci. U.S.A. 105:5620-5625(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY DUSP1, FUNCTION.
[22]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, MASS SPECTROMETRY.
[23]	"Human p38 delta MAP kinase mediates UV irradiation induced up-regulation of the gene expression of chemokine BRAK/CXCL14." Ozawa S., Ito S., Kato Y., Kubota E., Hata R. Biochem. Biophys. Res. Commun. 396:1060-1064(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"p38delta mitogen-activated protein kinase regulates skin homeostasis and tumorigenesis." Efimova T. Cell Cycle 9:498-505(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[25]	"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.
[26]	"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].
[27]	"Crystal structure of p38delta kinase." New York structural genomix research consortium (NYSGXRC) Submitted (JUN-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-352.
[28]	"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] LEU-41; VAL-282 AND THR-300.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y10488 mRNA. Translation: CAA71512.1.
U93232 mRNA. Translation: AAB87639.1.
AF015256 mRNA. Translation: AAC51758.1.
AF004709 mRNA. Translation: AAC51374.1.
AF092535 mRNA. Translation: AAD23377.1.
AF100546 mRNA. Translation: AAF36772.1.
BT007221 mRNA. Translation: AAP35885.1.
CR536490 mRNA. Translation: CAG38729.1.
Z95152 Genomic DNA. Translation: CAB08438.1.
CH471081 Genomic DNA. Translation: EAX03875.1.
BC000433 mRNA. Translation: AAH00433.1.
BC001641 mRNA. Translation: AAH01641.1.
BC004428 mRNA. Translation: AAH04428.1.

IPI

IPI00005741.

PIR

JC5528.

RefSeq

NP_002745.1. NM_002754.4.

UniGene

Hs.178695.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3COI	X-ray	2.09	A	2-352	[»]
4EXU	X-ray	1.70	A	1-352	[»]
4EYJ	X-ray	2.10	A	1-352	[»]
4EYM	X-ray	2.35	A	1-352	[»]

ProteinModelPortal

O15264.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15264. 87 interactions.

MINT

MINT-1183220.

STRING

9606.ENSP00000211287.

PTM databases

PhosphoSite

O15264.

Proteomic databases

PaxDb

O15264.

PRIDE

O15264.

Protocols and materials databases

DNASU

5603.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000211287; ENSP00000211287; ENSG00000156711.

GeneID

5603.

KEGG

hsa:5603.

UCSC

uc003ols.3. human.

Organism-specific databases

CTD

5603.

GeneCards

GC06P036095.

HGNC

HGNC:6875. MAPK13.

HPA

CAB025854.
HPA007667.

MIM

602899. gene.

neXtProt

NX_O15264.

PharmGKB

PA30620.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

O15264.

KO

K04441.

OMA

QDVNKTA.

OrthoDB

EOG4R23V4.

PhylomeDB

O15264.

Enzyme and pathway databases

BRENDA

2.7.11.24. 2681.

Pathway_Interaction_DB

p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

SignaLink

O15264.

Gene expression databases

ArrayExpress

O15264.

Bgee

O15264.

CleanEx

HS_MAPK13.

Genevestigator

O15264.

GermOnline

ENSG00000156711. 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

O15264.

ChEMBL

CHEMBL2939.

EvolutionaryTrace

O15264.

GenomeRNAi

5603.

NextBio

21772.

SOURCE

Search...

Entry information

Entry name

MK13_HUMAN

Accession

Primary (citable) accession number: O15264
Secondary accession number(s): O14739 , O15124, Q6FI46, Q9UNU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 141 of the entry and version 1 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.