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Reviewed, UniProtKB/Swiss-Prot P45983 (MK08_HUMAN)

Last modified February 9, 2010. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mitogen-activated protein kinase 8
      Short name=MAP kinase 8
      Short name=MAPK 8
    EC=2.7.11.24
Alternative name(s):
    Stress-activated protein kinase JNK1
    c-Jun N-terminal kinase 1
    JNK-46
    Stress-activated protein kinase 1
Gene names
Name: MAPK8
Synonyms: JNK1, PRKM8, SAPK1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells By similarity. Phosphorylates heat shock factor protein 4 (HSF4). Ref.11 Ref.16

JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. Ref.11 Ref.16

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium. Ref.7

Enzyme regulation

Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. Inhibited by dual specificity phosphatases, such as DUSP1.

Subunit structure

Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway. Interacts with TP53 and WWOX. Interacts with JAMP. Forms a complex with MAPK8IP1 and RGNEF By similarity. Interacts with NFATC4. Interacts with MECOM; regulates JNK signaling. Ref.11 Ref.9 Ref.10 Ref.12

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Post-translational modification

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. Ref.16 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P45983-1)

Also known as: JNK1-alpha-2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P45983-2)

Also known as: JNK1-alpha-1;

The sequence of this isoform differs from the canonical sequence as follows:
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ
Isoform 3 (identifier: P45983-3)

Also known as: JNK1-beta-1;

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH
     380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ
Isoform 4 (identifier: P45983-4)

Also known as: JNK1-beta-2;

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: L → I
     219-230: VCHKILFPGRDY → IKGGVLFPGTDH

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Mitogen-activated protein kinase 8
PRO_0000186262

Regions

Domain26 – 321296Protein kinase
Nucleotide binding32 – 409ATP By similarity
Motif183 – 1853TXY

Sites

Active site1511Proton acceptor By similarity
Binding site551ATP By similarity

Amino acid modifications

Modified residue1551Phosphoserine
Modified residue1831Phosphothreonine Ref.15 Ref.18 Ref.21
Modified residue1851Phosphotyrosine Ref.13 Ref.15 Ref.18 Ref.19 Ref.21
Modified residue2551Phosphothreonine Ref.14
Modified residue2581Phosphothreonine Ref.14
Modified residue2591Phosphotyrosine Ref.14
Modified residue3081N6-acetyllysine Ref.22
Modified residue3571Phosphotyrosine Ref.14
Modified residue3671Phosphothreonine Ref.14
Modified residue3771Phosphoserine Ref.17 Ref.18

Natural variations

Alternative sequence2081L → I in isoform 3 and isoform 4.
VSP_004831
Alternative sequence219 – 23012VCHKI…PGRDY → IKGGVLFPGTDH in isoform 3 and isoform 4.
VSP_004832
Alternative sequence380 – 42748GAAVI…LGCCR → AQVQQ in isoform 1 and isoform 3.
VSP_004833
Natural variant1711G → S in a renal clear cell carcinoma sample; somatic mutation. Ref.23
VAR_042258
Natural variant1771G → R in a glioblastoma multiforme sample; somatic mutation. Ref.23
VAR_042259
Natural variant3651E → K: dbSNP rs45483593.
VAR_050592

Experimental info

Mutagenesis1831T → A: Phosphorylation blocked.
Mutagenesis1851Y → F: Phosphorylation blocked.

Secondary structure

1 ....................................................... 427
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (JNK1-alpha-2) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 94FB6BE0358B9B60

FASTA42748,296
        10         20         30         40         50         60 
MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER NVAIKKLSRP 

        70         80         90        100        110        120 
FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDVYIVMEL MDANLCQVIQ 

       130        140        150        160        170        180 
MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF 

       190        200        210        220        230        240 
MMTPYVVTRY YRAPEVILGM GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ 

       250        260        270        280        290        300 
LGTPCPEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK 

       310        320        330        340        350        360 
MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV 

       370        380        390        400        410        420 
MDLEERTKNG VIRGQPSPLG AAVINGSQHP SSSSSVNDVS SMSTDPTLAS DTDSSLEAAA 


GPLGCCR

« Hide

Isoform 1 (JNK1-alpha-1).

Checksum: A7320EF933E9CF85
Show »

FASTA38444,229
Isoform 3 (JNK1-beta-1).

Checksum: 76E49A950E64C1A1
Show »

FASTA38444,022
Isoform 4 (JNK1-beta-2).

Checksum: 3F5CC3F6A4F3EF2D
Show »

FASTA42748,088

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References

« Hide 'large scale' references
[1]"JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain."
Derijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M., Davis R.J.
Cell 76:1025-1037(1994) [PubMed: 8137421] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"Selective interaction of JNK protein kinase isoforms with transcription factors."
Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K., Derijard B., Davis R.J.
EMBO J. 15:2760-2770(1996) [PubMed: 8654373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Brain.
[3]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[6]"Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms."
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J.
Science 267:682-685(1995) [PubMed: 7839144] [Abstract]
Cited for: MUTAGENESIS.
[7]"Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7."
Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M., Cohen P.
Biochem. J. 352:145-154(2000) [PubMed: 11062067] [Abstract]
Cited for: REGULATION BY MAP2K4 AND MAP2K7, COFACTOR.
[8]"The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents stress-induced cell death."
Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K., Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.
EMBO J. 19:2958-2968(2000) [PubMed: 10856240] [Abstract]
Cited for: INTERACTION WITH MECOM.
[9]"JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1) and inhibits WOX1-mediated apoptosis."
Chang N.-S., Doherty J., Ensign A.
J. Biol. Chem. 278:9195-9202(2003) [PubMed: 12514174] [Abstract]
Cited for: INTERACTION WITH WWOX AND TP53.
[10]"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein."
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.
Biochem. J. 389:73-82(2005) [PubMed: 15693750] [Abstract]
Cited for: INTERACTION WITH SPAG9.
[11]"Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
Hu Y., Mivechi N.F.
Mol. Cell. Biol. 26:3282-3294(2006) [PubMed: 16581800] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSF4.
[12]"Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation."
Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y., Bode A.M., Dong Z.
Cancer Res. 67:8725-8735(2007) [PubMed: 17875713] [Abstract]
Cited for: INTERACTION WITH NFATC4.
[13]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, MASS SPECTROMETRY.
Tissue: Lung.
[14]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255; THR-258; TYR-259; TYR-357 AND THR-367, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
[16]"Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1."
Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.
Anal. Biochem. 376:115-121(2008) [PubMed: 18307971] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF JDP2.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, MASS SPECTROMETRY.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; TYR-185 AND SER-377, MASS SPECTROMETRY.
[19]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[20]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-183; TYR-185 AND SER-377, MASS SPECTROMETRY.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, MASS SPECTROMETRY.
Tissue: T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-308, MASS SPECTROMETRY.
[23]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-171 AND ARG-177.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L26318 mRNA. Translation: AAA36131.1.
U34822 mRNA. Translation: AAC50607.1.
U35004 mRNA. Translation: AAC50610.1.
U35005 mRNA. Translation: AAC50611.1.
AB451231 mRNA. Translation: BAG70045.1.
CH471187 Genomic DNA. Translation: EAW93132.1.
BC144063 mRNA. Translation: AAI44064.1.
IPIIPI00003145.
IPI00024672.
IPI00220305.
IPI00220306.
PIRS71097.
S71099.
RefSeqNP_002741.1.
NP_620634.1.
NP_620635.1.
NP_620637.1.
UniGeneHs.138211

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKHX-ray2.35A1-363[»]
1UKIX-ray2.70A1-363[»]
2G01X-ray3.50A/B1-364[»]
2GMXX-ray3.50A/B1-364[»]
2H96X-ray3.00A/B1-364[»]
2NO3X-ray3.20A/B1-364[»]
3ELJX-ray1.80A1-364[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-249N.
IntActP45983. 18 interactions.
STRINGP45983.

PTM databases

PhosphoSiteP45983.

Proteomic databases

PRIDEP45983.

Genome annotation databases

EnsemblENST00000360332; ENSP00000353483; ENSG00000107643; Homo sapiens. [Genome view]
ENST00000374179; ENSP00000363294; ENSG00000107643; Homo sapiens. [Genome view]
ENST00000374189; ENSP00000363304; ENSG00000107643; Homo sapiens. [Genome view]
GeneID5599.
KEGGhsa:5599.
NMPDRfig|9606.3.peg.3911.
UCSCuc001jgl.1. human.
uc001jgm.1. human.
uc001jgp.1. human.
uc001jgq.1. human.

Organism-specific databases

CTD5599.
GeneCardsGC10P049279.
H-InvDBHIX0008805.
HGNCHGNC:6881. MAPK8.
HPACAB004463.
MIM601158. gene.
PharmGKBPA283.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG755340.
HOVERGENP45983.
InParanoidP45983.
OMALGAAMIN.
PhylomeDBP45983.

Enzyme and pathway databases

BRENDA2.7.11.24. 247.
Pathway_Interaction_DBangiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
bcr_5pathway. BCR signaling pathway.
ceramidepathway. Ceramide signaling pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
ephrinbrevpathway. Ephrin B reverse signaling.
epopathway. EPO signaling pathway.
faspathway. FAS signaling pathway (CD95).
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
foxopathway. FoxO family signaling.
glypican_3pathway. Glypican 3 network.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
il1pathway. IL1-mediated signaling events.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il2_1pathway. IL2-mediated signaling events.
tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
avb3_opn_pathway. Osteopontin-mediated events.
p75ntrpathway. p75(NTR)-mediated signaling.
reelinpathway. Reelin signaling pathway.
ar_tf_pathway. Regulation of Androgen receptor activity.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
s1p_s1p2_pathway. S1P2 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
trail_pathway. TRAIL signaling pathway.
ReactomeREACT_11061. Signalling by NGF.
REACT_578. Apoptosis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP45983.
BgeeP45983.
CleanExHS_MAPK8.
GenevestigatorP45983.
GermOnlineENSG00000107643. Homo sapiens.

Family and domain databases

InterProIPR008351. JNK_MAPK.
IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21738.
SOURCESearch...

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Entry information

Entry nameMK08_HUMAN
AccessionPrimary (citable) accession number: P45983
Secondary accession number(s): B5BTZ5 expand/collapse secondary AC list , B7ZLV4, Q15709, Q15712, Q15713
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents