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Protein

Mitogen-activated protein kinase 10

Gene

MAPK10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the photic regulation of the circadian clock (PubMed:22441692).2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication

Enzyme regulationi

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 HDAC9.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei93ATP1
Active sitei189Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi70 – 78ATP9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • JUN kinase activity Source: UniProtKB
  • MAP kinase kinase activity Source: ProtInc

GO - Biological processi

  • Fc-epsilon receptor signaling pathway Source: Reactome
  • JNK cascade Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  • response to light stimulus Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS03221-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
SignaLinkiP53779.
SIGNORiP53779.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 10 (EC:2.7.11.24)
Short name:
MAP kinase 10
Short name:
MAPK 10
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 namesi
Name:MAPK10
Synonyms:JNK3, JNK3A, PRKM10, SAPK1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6872. MAPK10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi462C → S: Loss of palmitoylation. 1 Publication1
Mutagenesisi463C → S: Loss of palmitoylation. 1 Publication1

Keywords - Diseasei

Epilepsy, Mental retardation

Organism-specific databases

DisGeNETi5602.
MalaCardsiMAPK10.
OpenTargetsiENSG00000109339.
Orphaneti2382. Lennox-Gastaut syndrome.
PharmGKBiPA30617.

Chemistry databases

ChEMBLiCHEMBL2637.
GuidetoPHARMACOLOGYi1498.

Polymorphism and mutation databases

BioMutaiMAPK10.
DMDMi2507196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001862771 – 464Mitogen-activated protein kinase 10Add BLAST464

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221Phosphothreonine; by MAP2K71 Publication1
Modified residuei223Phosphotyrosine; by MAP2K41 Publication1
Lipidationi462S-palmitoyl cysteine1 Publication1
Lipidationi463S-palmitoyl cysteine1 Publication1

Post-translational modificationi

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.1 Publication
Palmitoylation regulates subcellular location and axonal development.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP53779.
MaxQBiP53779.
PaxDbiP53779.
PeptideAtlasiP53779.
PRIDEiP53779.

PTM databases

iPTMnetiP53779.
PhosphoSitePlusiP53779.
SwissPalmiP53779.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000109339.
CleanExiHS_MAPK10.
ExpressionAtlasiP53779. baseline and differential.
GenevisibleiP53779. HS.

Organism-specific databases

HPAiCAB022625.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB1P494072EBI-713543,EBI-743313
JUNP054122EBI-713543,EBI-852823
RELAQ042062EBI-713543,EBI-73886

Protein-protein interaction databases

BioGridi111588. 46 interactors.
DIPiDIP-1015N.
IntActiP53779. 18 interactors.
MINTiMINT-1373516.
STRINGi9606.ENSP00000352157.

Chemistry databases

BindingDBiP53779.

Structurei

Secondary structure

1464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 53Combined sources6
Beta strandi56 – 61Combined sources6
Beta strandi64 – 69Combined sources6
Beta strandi77 – 83Combined sources7
Turni84 – 87Combined sources4
Beta strandi88 – 97Combined sources10
Helixi98 – 100Combined sources3
Helixi102 – 114Combined sources13
Turni115 – 117Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi127 – 130Combined sources4
Turni136 – 138Combined sources3
Beta strandi142 – 147Combined sources6
Beta strandi150 – 152Combined sources3
Helixi153 – 157Combined sources5
Helixi163 – 182Combined sources20
Helixi192 – 194Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi207 – 209Combined sources3
Turni212 – 214Combined sources3
Helixi216 – 219Combined sources4
Beta strandi220 – 222Combined sources3
Helixi227 – 229Combined sources3
Helixi232 – 235Combined sources4
Helixi244 – 258Combined sources15
Helixi268 – 279Combined sources12
Helixi284 – 287Combined sources4
Helixi292 – 299Combined sources8
Helixi309 – 312Combined sources4
Helixi315 – 317Combined sources3
Helixi323 – 339Combined sources17
Turni344 – 346Combined sources3
Helixi350 – 355Combined sources6
Turni357 – 361Combined sources5
Helixi365 – 368Combined sources4
Helixi378 – 382Combined sources5
Helixi387 – 399Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JNKX-ray2.30A1-423[»]
1PMNX-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-ray3.00A45-400[»]
4H39X-ray1.99A45-400[»]
4H3BX-ray2.08A/C45-400[»]
4KKEX-ray2.20A40-402[»]
4KKGX-ray2.40A40-402[»]
4KKHX-ray2.00A40-402[»]
4U79X-ray2.23A39-402[»]
4W4VX-ray2.01A39-402[»]
4W4WX-ray1.90A39-402[»]
4W4XX-ray2.65A39-402[»]
4W4YX-ray2.30A39-402[»]
4WHZX-ray1.79A39-423[»]
4X21X-ray1.95A/B39-402[»]
4Y46X-ray2.04A39-402[»]
4Y5HX-ray2.06A39-402[»]
4Z9LX-ray2.10A40-401[»]
ProteinModelPortaliP53779.
SMRiP53779.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53779.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 359Protein kinasePROSITE-ProRule annotationAdd BLAST296

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi221 – 223TXY3

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP53779.
KOiK04440.
OMAiNVWFDES.
OrthoDBiEOG091G09G2.
PhylomeDBiP53779.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS
60 70 80 90 100
VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ
110 120 130 140 150
NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD
160 170 180 190 200
ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD
210 220 230 240 250
CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG
260 270 280 290 300
CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN
310 320 330 340 350
RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV
360 370 380 390 400
DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN
410 420 430 440 450
SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD
460
SSLEASAGPL GCCR
Length:464
Mass (Da):52,585
Last modified:November 1, 1997 - v2
Checksum:i2E20C05EB89CDA66
GO
Isoform Alpha-1 (identifier: P53779-2) [UniParc]FASTAAdd to basket

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

Show »
Length:422
Mass (Da):48,554
Checksum:iFCC8C11954481C04
GO
Isoform 3 (identifier: P53779-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:426
Mass (Da):48,128
Checksum:i1022B6AC7774A666
GO
Isoform 4 (identifier: P53779-4) [UniParc]FASTAAdd to basket

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

Show »
Length:277
Mass (Da):31,933
Checksum:i5C2FA3CFC85C1FF8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162D → G in BAG51956 (PubMed:14702039).Curated1

Mass spectrometryi

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0419101 – 145Missing in isoform 4. 1 PublicationAdd BLAST145
Alternative sequenceiVSP_0419111 – 38Missing in isoform 3. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_004839418 – 464GAAVN…LGCCR → AQVQQ in isoform Alpha-1 and isoform 4. 3 PublicationsAdd BLAST47

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34026.1. [P53779-1]
CCDS3612.1. [P53779-3]
CCDS43247.1. [P53779-2]
PIRiS71104.
RefSeqiNP_001304996.1. NM_001318067.1.
NP_001304997.1. NM_001318068.1.
NP_001304998.1. NM_001318069.1.
NP_002744.1. NM_002753.4. [P53779-2]
NP_620446.1. NM_138980.3. [P53779-3]
NP_620448.1. NM_138982.3. [P53779-1]
XP_005263186.1. XM_005263129.2. [P53779-1]
XP_005263187.1. XM_005263130.2. [P53779-1]
XP_005263192.1. XM_005263135.3. [P53779-2]
XP_006714331.1. XM_006714268.2. [P53779-3]
XP_011530419.1. XM_011532117.2. [P53779-1]
XP_011530420.1. XM_011532118.2. [P53779-1]
XP_011530422.1. XM_011532120.2. [P53779-3]
XP_011530423.1. XM_011532121.2. [P53779-3]
XP_016863908.1. XM_017008419.1. [P53779-1]
XP_016863909.1. XM_017008420.1. [P53779-1]
XP_016863910.1. XM_017008421.1. [P53779-1]
XP_016863912.1. XM_017008423.1. [P53779-3]
XP_016863913.1. XM_017008424.1. [P53779-3]
XP_016863914.1. XM_017008425.1. [P53779-3]
XP_016863915.1. XM_017008426.1. [P53779-3]
XP_016863918.1. XM_017008429.1. [P53779-2]
XP_016863919.1. XM_017008430.1. [P53779-2]
XP_016863920.1. XM_017008431.1. [P53779-2]
XP_016863921.1. XM_017008432.1. [P53779-2]
XP_016863941.1. XM_017008452.1. [P53779-4]
UniGeneiHs.125503.
Hs.13438.

Genome annotation databases

EnsembliENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
GeneIDi5602.
KEGGihsa:5602.
UCSCiuc003hpp.4. human. [P53779-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34026.1. [P53779-1]
CCDS3612.1. [P53779-3]
CCDS43247.1. [P53779-2]
PIRiS71104.
RefSeqiNP_001304996.1. NM_001318067.1.
NP_001304997.1. NM_001318068.1.
NP_001304998.1. NM_001318069.1.
NP_002744.1. NM_002753.4. [P53779-2]
NP_620446.1. NM_138980.3. [P53779-3]
NP_620448.1. NM_138982.3. [P53779-1]
XP_005263186.1. XM_005263129.2. [P53779-1]
XP_005263187.1. XM_005263130.2. [P53779-1]
XP_005263192.1. XM_005263135.3. [P53779-2]
XP_006714331.1. XM_006714268.2. [P53779-3]
XP_011530419.1. XM_011532117.2. [P53779-1]
XP_011530420.1. XM_011532118.2. [P53779-1]
XP_011530422.1. XM_011532120.2. [P53779-3]
XP_011530423.1. XM_011532121.2. [P53779-3]
XP_016863908.1. XM_017008419.1. [P53779-1]
XP_016863909.1. XM_017008420.1. [P53779-1]
XP_016863910.1. XM_017008421.1. [P53779-1]
XP_016863912.1. XM_017008423.1. [P53779-3]
XP_016863913.1. XM_017008424.1. [P53779-3]
XP_016863914.1. XM_017008425.1. [P53779-3]
XP_016863915.1. XM_017008426.1. [P53779-3]
XP_016863918.1. XM_017008429.1. [P53779-2]
XP_016863919.1. XM_017008430.1. [P53779-2]
XP_016863920.1. XM_017008431.1. [P53779-2]
XP_016863921.1. XM_017008432.1. [P53779-2]
XP_016863941.1. XM_017008452.1. [P53779-4]
UniGeneiHs.125503.
Hs.13438.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JNKX-ray2.30A1-423[»]
1PMNX-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-ray3.00A45-400[»]
4H39X-ray1.99A45-400[»]
4H3BX-ray2.08A/C45-400[»]
4KKEX-ray2.20A40-402[»]
4KKGX-ray2.40A40-402[»]
4KKHX-ray2.00A40-402[»]
4U79X-ray2.23A39-402[»]
4W4VX-ray2.01A39-402[»]
4W4WX-ray1.90A39-402[»]
4W4XX-ray2.65A39-402[»]
4W4YX-ray2.30A39-402[»]
4WHZX-ray1.79A39-423[»]
4X21X-ray1.95A/B39-402[»]
4Y46X-ray2.04A39-402[»]
4Y5HX-ray2.06A39-402[»]
4Z9LX-ray2.10A40-401[»]
ProteinModelPortaliP53779.
SMRiP53779.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111588. 46 interactors.
DIPiDIP-1015N.
IntActiP53779. 18 interactors.
MINTiMINT-1373516.
STRINGi9606.ENSP00000352157.

Chemistry databases

BindingDBiP53779.
ChEMBLiCHEMBL2637.
GuidetoPHARMACOLOGYi1498.

PTM databases

iPTMnetiP53779.
PhosphoSitePlusiP53779.
SwissPalmiP53779.

Polymorphism and mutation databases

BioMutaiMAPK10.
DMDMi2507196.

Proteomic databases

EPDiP53779.
MaxQBiP53779.
PaxDbiP53779.
PeptideAtlasiP53779.
PRIDEiP53779.

Protocols and materials databases

DNASUi5602.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
GeneIDi5602.
KEGGihsa:5602.
UCSCiuc003hpp.4. human. [P53779-1]

Organism-specific databases

CTDi5602.
DisGeNETi5602.
GeneCardsiMAPK10.
H-InvDBHIX0163985.
HGNCiHGNC:6872. MAPK10.
HPAiCAB022625.
MalaCardsiMAPK10.
MIMi602897. gene.
neXtProtiNX_P53779.
OpenTargetsiENSG00000109339.
Orphaneti2382. Lennox-Gastaut syndrome.
PharmGKBiPA30617.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP53779.
KOiK04440.
OMAiNVWFDES.
OrthoDBiEOG091G09G2.
PhylomeDBiP53779.
TreeFamiTF105100.

Enzyme and pathway databases

BioCyciZFISH:HS03221-MONOMER.
BRENDAi2.7.11.24. 2681.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
SignaLinkiP53779.
SIGNORiP53779.

Miscellaneous databases

ChiTaRSiMAPK10. human.
EvolutionaryTraceiP53779.
GeneWikiiMAPK10.
GenomeRNAii5602.
PROiP53779.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109339.
CleanExiHS_MAPK10.
ExpressionAtlasiP53779. baseline and differential.
GenevisibleiP53779. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMK10_HUMAN
AccessioniPrimary (citable) accession number: P53779
Secondary accession number(s): A6NFS3
, A6NG28, B3KQ94, Q15707, Q49AP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 189 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.