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O15264 (MK13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
Stress response
Transcription
Transcription regulation
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.1Ref.12. Source: GOC

Ras protein signal transduction

Traceable author statement. Source: Reactome

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to osmotic stress

Inferred from direct assay Ref.12. Source: UniProtKB

response to stress

Inferred from direct assay Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay Ref.1Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19135240PubMed 22447027. Source: IntAct

protein serine/threonine kinase activity

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

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Mitogen-activated protein kinase 13
PRO_0000186286

Regions

Domain25 – 308284Protein kinase
Nucleotide binding31 – 399ATP By similarity
Motif180 – 1823TXY

Sites

Active site1501Proton acceptor By similarity
Binding site541ATP By similarity

Amino acid modifications

Modified residue471Phosphoserine Ref.20
Modified residue1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 Ref.2
Modified residue1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 Ref.2
Modified residue3501Phosphoserine Ref.22

Natural variations

Natural variant411S → L. Ref.28
Corresponds to variant rs55776345 [ dbSNP | Ensembl ].
VAR_042267
Natural variant2821A → V. Ref.28
Corresponds to variant rs55990045 [ dbSNP | Ensembl ].
VAR_042268
Natural variant3001A → T. Ref.28
Corresponds to variant rs41270090 [ dbSNP | Ensembl ].
VAR_042269

Experimental info

Mutagenesis1801T → A: Loss of kinase activity. Ref.2
Mutagenesis1821Y → A: Loss of kinase activity. Ref.2
Sequence conflict13 – 142DV → EL in AAC51374. Ref.4
Sequence conflict391V → W in AAC51374. Ref.4
Sequence conflict561L → P in AAC51758. Ref.3
Sequence conflict1661I → V in AAC51758. Ref.3
Sequence conflict2241K → R in AAC51758. Ref.3
Sequence conflict2241K → R in AAD23377. Ref.5

Secondary structure

............................................................ 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15264 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 52E749EDB2973DDF

FASTA36542,090
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. 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] LEU-41; VAL-282 AND THR-300.
+Additional computationally mapped references.

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.
CCDSCCDS4818.1.
PIRJC5528.
RefSeqNP_002745.1. NM_002754.4.
UniGeneHs.178695.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3COIX-ray2.09A2-352[»]
4EXUX-ray1.70A1-352[»]
4EYJX-ray2.10A1-352[»]
4EYMX-ray2.35A1-352[»]
ProteinModelPortalO15264.
SMRO15264. Positions 2-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111589. 14 interactions.
IntActO15264. 88 interactions.
MINTMINT-1183220.
STRING9606.ENSP00000211287.

Chemistry

BindingDBO15264.
ChEMBLCHEMBL2939.
GuidetoPHARMACOLOGY1502.

PTM databases

PhosphoSiteO15264.

Proteomic databases

MaxQBO15264.
PaxDbO15264.
PRIDEO15264.

Protocols and materials databases

DNASU5603.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000211287; ENSP00000211287; ENSG00000156711.
GeneID5603.
KEGGhsa:5603.
UCSCuc003ols.4. human.

Organism-specific databases

CTD5603.
GeneCardsGC06P036095.
HGNCHGNC:6875. MAPK13.
HPACAB025854.
HPA007667.
MIM602899. gene.
neXtProtNX_O15264.
PharmGKBPA30620.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidO15264.
KOK04441.
OMAEHPYFDN.
OrthoDBEOG7PCJGV.
PhylomeDBO15264.
TreeFamTF105100.

Enzyme and pathway databases

BRENDA2.7.11.24. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.
SignaLinkO15264.

Gene expression databases

ArrayExpressO15264.
BgeeO15264.
CleanExHS_MAPK13.
GenevestigatorO15264.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15264.
GeneWikiMAPK13.
GenomeRNAi5603.
NextBio21772.
PROO15264.
SOURCESearch...

Entry information

Entry nameMK13_HUMAN
AccessionPrimary (citable) accession number: O15264
Secondary accession number(s): O14739 expand/collapse secondary AC list , O15124, Q6FI46, Q9UNU0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 153 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 6

Human chromosome 6: entries, gene names and cross-references to MIM