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P53779 (MK10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 10

Short name=MAP kinase 10
Short name=MAPK 10
EC=2.7.11.24
Alternative name(s):
MAP kinase p49 3F12
Stress-activated protein kinase 1b
Short name=SAPK1b
Stress-activated protein kinase JNK3
c-Jun N-terminal kinase 3
Gene names
Name:MAPK10
Synonyms:JNK3, JNK3A, PRKM10, SAPK1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons. Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium. Ref.7

Enzyme regulation

Activated by threonine and tyrosine phosphorylation by two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K7 phosphorylates MAPK10 on Thr-221 causing a conformational change and a large increase in Vmax. MAP2K4 then phosphorylates Tyr-223 resulting in a further increase in Vmax. Inhibited by dual specificity phosphatases, such as DUSP1. Inhibited by HDAC9. Ref.8 Ref.13

Subunit structure

Interacts with MAPKBP1 By similarity. 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 HDAC9. Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5. Interacts with SARM1 By similarity. Ref.10 Ref.13 Ref.14

Subcellular location

Cytoplasm. Membrane; Lipid-anchor. Nucleus. Mitochondrion. Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 By similarity. Ref.12

Tissue specificity

Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

Domain

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

Post-translational modification

Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, which activates the enzyme. MAP2K7 shows a strong preference for Thr-221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly autophosphorylated on threonine and tyrosine residues in vitro. Ref.7

Palmitoylation regulates subcellular location and axonal development. Ref.15

Involvement in disease

A chromosomal aberration involving MAPK10 has been found in a single patient with pharmacoresistant epileptic encephalopathy. Translocation t(Y;4)(q11.2;q21) which causes MAPK10 truncation. Ref.11

Sequence similarities

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

Contains 1 protein kinase domain.

Mass spectrometry

Molecular mass is 44070 Da from positions 1 - 464. Determined by ESI. Ref.7

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseEpilepsy
Mental retardation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Palmitate
Phosphoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

JNK cascade

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

JUN phosphorylation

Inferred from sequence or structural similarity Ref.2. Source: GOC

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement Ref.1. Source: GOC

innate immune response

Traceable author statement. Source: Reactome

regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.2. Source: ProtInc

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 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

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

JUN kinase activity

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

MAP kinase kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: A similar low level of binding to substrates is observed for isoform alpha-1 and isoform alpha-2. However, there is no correlation between binding and phosphorylation, which is achieved about at the same efficiency by all isoforms.
Isoform Alpha-2 (identifier: P53779-1)

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 Alpha-1 (identifier: P53779-2)

The sequence of this isoform differs from the canonical sequence as follows:
     418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ
Isoform 3 (identifier: P53779-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.
Isoform 4 (identifier: P53779-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-145: Missing.
     418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Mitogen-activated protein kinase 10
PRO_0000186277

Regions

Domain64 – 359296Protein kinase
Nucleotide binding70 – 789ATP
Motif221 – 2233TXY

Sites

Active site1891Proton acceptor
Binding site931ATP

Amino acid modifications

Modified residue1541S-nitrosocysteine By similarity
Modified residue2211Phosphothreonine; by MAP2K7 Ref.7
Modified residue2231Phosphotyrosine; by MAP2K4 Ref.7
Lipidation4621S-palmitoyl cysteine Probable
Lipidation4631S-palmitoyl cysteine Probable

Natural variations

Alternative sequence1 – 145145Missing in isoform 4.
VSP_041910
Alternative sequence1 – 3838Missing in isoform 3.
VSP_041911
Alternative sequence418 – 46447GAAVN…LGCCR → AQVQQ in isoform Alpha-1 and isoform 4.
VSP_004839

Experimental info

Mutagenesis4621C → S: Loss of palmitoylation. Ref.15
Mutagenesis4631C → S: Loss of palmitoylation. Ref.15
Sequence conflict1621D → G in BAG51956. Ref.3

Secondary structure

........................................................................ 464
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 2.
Checksum: 2E20C05EB89CDA66

FASTA46452,585
        10         20         30         40         50         60 
MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV 

        70         80         90        100        110        120 
LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH 

       130        140        150        160        170        180 
KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL 

       190        200        210        220        230        240 
HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY 

       250        260        270        280        290        300 
KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN 

       310        320        330        340        350        360 
RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN 

       370        380        390        400        410        420 
VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA 

       430        440        450        460 
VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR 

« Hide

Isoform Alpha-1 [UniParc].

Checksum: FCC8C11954481C04
Show »

FASTA42248,554
Isoform 3 [UniParc].

Checksum: 1022B6AC7774A666
Show »

FASTA42648,128
Isoform 4 [UniParc].

Checksum: 5C2FA3CFC85C1FF8
Show »

FASTA27731,933

References

« Hide 'large scale' references
[1]"p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system."
Mohit A.A., Martin J.H., Miller C.A.
Neuron 14:67-78(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
Tissue: Hippocampus.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Caudate nucleus.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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] (ISOFORM ALPHA-2).
Tissue: Brain.
[7]"Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3 alpha 1."
Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J., O'Keefe S.J., LoGrasso P.
Biochemistry 39:3141-3148(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7, PHOSPHORYLATION AT THR-221 AND TYR-223, COFACTOR, MASS SPECTROMETRY.
[8]"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] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[9]"c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator SCG10."
Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G., Arkinstall S.
FEBS Lett. 508:259-264(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STMN2.
[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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPAG9.
[11]"Truncation of the CNS-expressed JNK3 in a patient with a severe developmental epileptic encephalopathy."
Shoichet S.A., Duprez L., Hagens O., Waetzig V., Menzel C., Herdegen T., Schweiger S., Dan B., Vamos E., Ropers H.-H., Kalscheuer V.M.
Hum. Genet. 118:559-567(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT, DISEASE.
[12]"Visual and both non-visual arrestins in their 'inactive' conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm."
Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V.
J. Biol. Chem. 281:21491-21499(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Neuroprotection by histone deacetylase-related protein."
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., Olson E.N., D'Mello S.R.
Mol. Cell. Biol. 26:3550-3564(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC9, ENZYME REGULATION.
[14]"Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs."
Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., Kolch W., Houslay M.D., Milligan G.
Biochem. J. 413:51-60(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[15]"Isoform-specific palmitoylation of JNK regulates axonal development."
Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W., Kojic L., Jia W., Cynader M.
Cell Death Differ. 19:553-561(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-462 AND CYS-463, MUTAGENESIS OF CYS-462 AND CYS-463.
[16]"Crystal structure of JNK3: a kinase implicated in neuronal apoptosis."
Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W., Caron P.R., Wilson K.P., Su M.S.-S.
Structure 6:983-991(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07620 mRNA. Translation: AAC50101.1.
U34819 mRNA. Translation: AAC50604.1.
U34820 mRNA. Translation: AAC50605.1.
AK057723 mRNA. Translation: BAG51956.1.
AK124791 mRNA. Translation: BAG54096.1.
AC096953 Genomic DNA. No translation available.
AC104059 Genomic DNA. No translation available.
AC104827 Genomic DNA. No translation available.
AC108054 Genomic DNA. No translation available.
AC110076 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05963.1.
BC035057 mRNA. Translation: AAH35057.1.
PIRS71104.
RefSeqNP_002744.1. NM_002753.3.
NP_620446.1. NM_138980.2.
NP_620447.1. NM_138981.2.
NP_620448.1. NM_138982.2.
XP_005263186.1. XM_005263129.1.
XP_005263187.1. XM_005263130.1.
XP_005263192.1. XM_005263135.2.
UniGeneHs.125503.
Hs.13438.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNKX-ray2.30A1-423[»]
1PMNX-ray2.20A40-401[»]
1PMQX-ray2.20A40-401[»]
1PMUX-ray2.70A40-401[»]
1PMVX-ray2.50A40-401[»]
2B1PX-ray1.90A46-400[»]
2EXCX-ray2.75X45-400[»]
2O0UX-ray2.10A39-402[»]
2O2UX-ray2.45A39-402[»]
2OK1X-ray2.40A40-402[»]
2P33X-ray2.40A40-402[»]
2R9SX-ray2.40A/B46-401[»]
2WAJX-ray2.40A39-402[»]
2ZDTX-ray2.00A39-402[»]
2ZDUX-ray2.50A39-402[»]
3CGFX-ray3.00A40-402[»]
3CGOX-ray3.00A40-402[»]
3DA6X-ray2.00A39-402[»]
3FI2X-ray2.28A39-402[»]
3FI3X-ray2.20A39-402[»]
3FV8X-ray2.28A39-402[»]
3G90X-ray2.40X40-402[»]
3G9LX-ray2.20X40-402[»]
3G9NX-ray2.80A40-402[»]
3KVXX-ray2.40A39-402[»]
3OXIX-ray2.20A40-401[»]
3OY1X-ray1.70A40-401[»]
3PTGX-ray2.43A40-401[»]
3RTPX-ray2.40A40-401[»]
3TTIX-ray2.20A1-464[»]
3TTJX-ray2.10A1-464[»]
3V6RX-ray2.60A/B39-402[»]
3V6SX-ray2.97A/B39-402[»]
4H36X-ray3.00A46-400[»]
4H39X-ray1.99A46-400[»]
4H3BX-ray2.08A/C46-400[»]
ProteinModelPortalP53779.
SMRP53779. Positions 11-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111588. 42 interactions.
DIPDIP-1015N.
IntActP53779. 18 interactions.
MINTMINT-1373516.
STRING9606.ENSP00000352157.

Chemistry

BindingDBP53779.
ChEMBLCHEMBL2637.
GuidetoPHARMACOLOGY1498.

PTM databases

PhosphoSiteP53779.

Polymorphism databases

DMDM2507196.

Proteomic databases

PaxDbP53779.
PRIDEP53779.

Protocols and materials databases

DNASU5602.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
ENST00000395161; ENSP00000378590; ENSG00000109339. [P53779-2]
ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
GeneID5602.
KEGGhsa:5602.
UCSCuc003hpo.3. human. [P53779-1]
uc003hpp.3. human. [P53779-4]
uc003hpt.3. human. [P53779-2]

Organism-specific databases

CTD5602.
GeneCardsGC04M086878.
H-InvDBHIX0163985.
HGNCHGNC:6872. MAPK10.
HPACAB022625.
MIM602897. gene.
neXtProtNX_P53779.
Orphanet2382. Lennox-Gastaut syndrome.
PharmGKBPA30617.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP53779.
KOK04440.
OMAEVMNFEE.
OrthoDBEOG7PCJGV.
PhylomeDBP53779.
TreeFamTF105100.

Enzyme and pathway databases

BRENDA2.7.11.24. 2681.
ReactomeREACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP53779.

Gene expression databases

ArrayExpressP53779.
BgeeP53779.
CleanExHS_MAPK10.
GenevestigatorP53779.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01772. JNKMAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPK10. human.
EvolutionaryTraceP53779.
GeneWikiMAPK10.
GenomeRNAi5602.
NextBio21762.
PROP53779.
SOURCESearch...

Entry information

Entry nameMK10_HUMAN
AccessionPrimary (citable) accession number: P53779
Secondary accession number(s): A6NFS3 expand/collapse secondary AC list , A6NG28, B3KQ94, Q15707, Q49AP1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 162 of the entry and version 2 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 chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM