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Q8IW41

- MAPK5_HUMAN

UniProt

Q8IW41 - MAPK5_HUMAN

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Protein

MAP kinase-activated protein kinase 5

Gene

MAPKAPK5

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

Functioni

Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated following phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11, ERK2/MAPK1, ERK3/MAPK6, and ERK4/MAPK4. Activated by stress-related extracellular stimuli; such as H2O2, arsenite, anisomycin TNF alpha and also PMA and the calcium ionophore A23187; but to a lesser extent. In vitro, activated by SQSTM1. Inhibited by diterpenoid alkaloid noroxoaconitine.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPPROSITE-ProRule annotation
Active sitei148 – 1481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase activity Source: ProtInc
  3. p53 binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: GOC
  2. MAPK cascade Source: GOC
  3. negative regulation of TOR signaling Source: UniProtKB
  4. protein autophosphorylation Source: UniProtKB
  5. Ras protein signal transduction Source: UniProtKB
  6. regulation of translation Source: UniProtKB
  7. signal transduction Source: ProtInc
  8. stress-induced premature senescence Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
SignaLinkiQ8IW41.

Names & Taxonomyi

Protein namesi
Recommended name:
MAP kinase-activated protein kinase 5 (EC:2.7.11.1)
Short name:
MAPK-activated protein kinase 5
Short name:
MAPKAP kinase 5
Short name:
MAPKAP-K5
Short name:
MAPKAPK-5
Short name:
MK-5
Short name:
MK5
Alternative name(s):
p38-regulated/activated protein kinase
Short name:
PRAK
Gene namesi
Name:MAPKAPK5
Synonyms:PRAK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6889. MAPKAPK5.

Subcellular locationi

Cytoplasm. Nucleus
Note: Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511K → M: Kinase defective mutant, abolishes activity. 1 Publication
Mutagenesisi182 – 1821T → A: No p38-beta/MAPK11-induced activation. 3 Publications
Mutagenesisi182 – 1821T → D: Mimicks phosphorylation state and induces constitutive protein kinase activity. 3 Publications
Mutagenesisi212 – 2121S → D: Mimicks phosphorylation state and displays a slightly higher protein kinase activity. 1 Publication
Mutagenesisi337 – 3371L → G: Induces constitutive protein kinase activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA30633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473MAP kinase-activated protein kinase 5PRO_0000086296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151Phosphoserine; by PKABy similarity
Modified residuei182 – 1821Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA2 Publications
Modified residuei212 – 2121Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the cytoplasm. Autophosphorylated (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IW41.
PaxDbiQ8IW41.
PRIDEiQ8IW41.

PTM databases

PhosphoSiteiQ8IW41.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Inductioni

Directly regulated by MYC: expression is activated by MYC, suggesting the existence of a feedback regulatory loop.1 Publication

Gene expression databases

BgeeiQ8IW41.
CleanExiHS_MAPKAPK5.
ExpressionAtlasiQ8IW41. baseline and differential.
GenevestigatoriQ8IW41.

Organism-specific databases

HPAiCAB004546.
HPA015515.

Interactioni

Subunit structurei

Interacts with ERK3/MAPK6 and ERK4/MAPK4 (via FRIEDE motif); the interaction is direct (By similarity). Interacts with YWHAE; the interaction prevents phosphorylation of HSP27/HSPB1 leading to disrupt F-actin polymerization. Interacts with SQSTM1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-1201460,EBI-352682
MAPK6Q166593EBI-1201460,EBI-1384105
TP53P046372EBI-1201460,EBI-366083

Protein-protein interaction databases

BioGridi114120. 16 interactions.
IntActiQ8IW41. 18 interactions.
MINTiMINT-4711647.
STRINGi9606.ENSP00000202788.

Structurei

3D structure databases

ProteinModelPortaliQ8IW41.
SMRiQ8IW41. Positions 11-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 304283Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili409 – 44032Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119016.
HOGENOMiHOG000233031.
HOVERGENiHBG106948.
InParanoidiQ8IW41.
KOiK04442.
OMAiQVTKQIA.
PhylomeDBiQ8IW41.
TreeFamiTF312891.

Family and domain databases

Gene3Di4.10.1170.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IW41) [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
MSEESDMDKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL
60 70 80 90 100
KILLDRPKAR NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI
110 120 130 140 150
VMEMMEGGEL FHRISQHRHF TEKQASQVTK QIALALRHCH LLNIAHRDLK
160 170 180 190 200
PENLLFKDNS LDAPVKLCDF GFAKIDQGDL MTPQFTPYYV APQVLEAQRR
210 220 230 240 250
HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP FYSKHHSRTI
260 270 280 290 300
PKDMRRKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD
310 320 330 340 350
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK
360 370 380 390 400
PLHSVNNPIL RKRKLLGTKP KDSVYIHDHE NGAEDSNVAL EKLRDVIAQC
410 420 430 440 450
ILPQAGKGEN EDEKLNEVMQ EAWKYNRECK LLRDTLQSFS WNGRGFTDKV
460 470
DRLKLAEIVK QVIEEQTTSH ESQ

Note: No experimental confirmation available.

Length:473
Mass (Da):54,220
Last modified:September 13, 2004 - v2
Checksum:iF3D9DDC83CC0C49D
GO
Isoform 2 (identifier: Q8IW41-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-408: Missing.

Show »
Length:471
Mass (Da):54,035
Checksum:i176FA041A7F28570
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731I → T in CAB53747. (PubMed:17974005)Curated
Sequence conflicti291 – 2911E → R in AAC39863. (PubMed:9628874)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671M → I.1 Publication
Corresponds to variant rs34132040 [ dbSNP | Ensembl ].
VAR_040758
Natural varianti282 – 2821R → K.1 Publication
Corresponds to variant rs34843470 [ dbSNP | Ensembl ].
VAR_040759

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei407 – 4082Missing in isoform 2. 3 PublicationsVSP_011597

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF032437 Genomic DNA. Translation: AAC39863.1.
AK122767 mRNA. Translation: BAG53717.1.
CH471054 Genomic DNA. Translation: EAW97981.1.
BC000833 mRNA. Translation: AAH00833.1.
BC041049 mRNA. Translation: AAH41049.1.
BC047284 mRNA. Translation: AAH47284.2.
AL110301 mRNA. Translation: CAB53747.1.
CCDSiCCDS44975.1. [Q8IW41-1]
CCDS44976.1. [Q8IW41-2]
PIRiT34519.
RefSeqiNP_003659.2. NM_003668.3. [Q8IW41-2]
NP_620777.1. NM_139078.2. [Q8IW41-1]
UniGeneiHs.333120.
Hs.413901.

Genome annotation databases

EnsembliENST00000550735; ENSP00000449667; ENSG00000089022. [Q8IW41-2]
ENST00000551404; ENSP00000449381; ENSG00000089022. [Q8IW41-1]
GeneIDi8550.
KEGGihsa:8550.
UCSCiuc001tsz.4. human. [Q8IW41-2]
uc001tta.4. human. [Q8IW41-1]

Polymorphism databases

DMDMi52000829.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF032437 Genomic DNA. Translation: AAC39863.1 .
AK122767 mRNA. Translation: BAG53717.1 .
CH471054 Genomic DNA. Translation: EAW97981.1 .
BC000833 mRNA. Translation: AAH00833.1 .
BC041049 mRNA. Translation: AAH41049.1 .
BC047284 mRNA. Translation: AAH47284.2 .
AL110301 mRNA. Translation: CAB53747.1 .
CCDSi CCDS44975.1. [Q8IW41-1 ]
CCDS44976.1. [Q8IW41-2 ]
PIRi T34519.
RefSeqi NP_003659.2. NM_003668.3. [Q8IW41-2 ]
NP_620777.1. NM_139078.2. [Q8IW41-1 ]
UniGenei Hs.333120.
Hs.413901.

3D structure databases

ProteinModelPortali Q8IW41.
SMRi Q8IW41. Positions 11-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114120. 16 interactions.
IntActi Q8IW41. 18 interactions.
MINTi MINT-4711647.
STRINGi 9606.ENSP00000202788.

Chemistry

BindingDBi Q8IW41.
ChEMBLi CHEMBL3094.
GuidetoPHARMACOLOGYi 2096.

PTM databases

PhosphoSitei Q8IW41.

Polymorphism databases

DMDMi 52000829.

Proteomic databases

MaxQBi Q8IW41.
PaxDbi Q8IW41.
PRIDEi Q8IW41.

Protocols and materials databases

DNASUi 8550.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000550735 ; ENSP00000449667 ; ENSG00000089022 . [Q8IW41-2 ]
ENST00000551404 ; ENSP00000449381 ; ENSG00000089022 . [Q8IW41-1 ]
GeneIDi 8550.
KEGGi hsa:8550.
UCSCi uc001tsz.4. human. [Q8IW41-2 ]
uc001tta.4. human. [Q8IW41-1 ]

Organism-specific databases

CTDi 8550.
GeneCardsi GC12P112282.
HGNCi HGNC:6889. MAPKAPK5.
HPAi CAB004546.
HPA015515.
MIMi 606723. gene.
neXtProti NX_Q8IW41.
PharmGKBi PA30633.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119016.
HOGENOMi HOG000233031.
HOVERGENi HBG106948.
InParanoidi Q8IW41.
KOi K04442.
OMAi QVTKQIA.
PhylomeDBi Q8IW41.
TreeFami TF312891.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.
SignaLinki Q8IW41.

Miscellaneous databases

ChiTaRSi MAPKAPK5. human.
GeneWikii MAPKAPK5.
GenomeRNAii 8550.
NextBioi 32036.
PROi Q8IW41.
SOURCEi Search...

Gene expression databases

Bgeei Q8IW41.
CleanExi HS_MAPKAPK5.
ExpressionAtlasi Q8IW41. baseline and differential.
Genevestigatori Q8IW41.

Family and domain databases

Gene3Di 4.10.1170.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PRAK, a novel protein kinase regulated by the p38 MAP kinase."
    New L., Jiang Y., Zhao M., Liu K., Zhu W., Flood L.J., Kato Y., Parry G.C.N., Han J.
    EMBO J. 17:3372-3384(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), MUTAGENESIS OF THR-182, FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-182, ENZYME REGULATION.
    Tissue: Placenta.
  2. "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.
    , 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] (ISOFORM 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Cervix, Pancreas and Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-473 (ISOFORM 2).
    Tissue: Brain.
  6. Cited for: INTERACTION WITH SQSTM1, ENZYME REGULATION, SUBCELLULAR LOCATION.
  7. "Regulation of PRAK subcellular location by p38 MAP kinases."
    New L., Jiang Y., Han J.
    Mol. Biol. Cell 14:2603-2616(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-212, MUTAGENESIS OF THR-182, MUTAGENESIS OF LYS-51; THR-182 AND SER-212.
  8. "14-3-3epsilon inhibits MK5-mediated cell migration by disrupting F-actin polymerization."
    Tak H., Jang E., Kim S.B., Park J., Suk J., Yoon Y.S., Ahn J.K., Lee J.H., Joe C.O.
    Cell. Signal. 19:2379-2387(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1, INTERACTION WITH YWHAE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."
    Kostenko S., Johannessen M., Moens U.
    Cell. Signal. 21:712-718(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HSPB1.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-67 AND LYS-282.
  14. Cited for: FUNCTION IN PHOSPHORYLATION OF TP53.
  15. "The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis."
    Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M., Roepman P., Burgering B.M., Bushell M., Rosenwald A., Eilers M.
    Mol. Cell 41:445-457(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FOXO3, AUTOPHOSPHORYLATION, INDUCTION, MUTAGENESIS OF THR-182 AND LEU-337.
  16. "Mitogen-activated protein kinase p38 and MK2, MK3 and MK5: menage a trois or menage a quatre?"
    Shiryaev A., Moens U.
    Cell. Signal. 22:1185-1192(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiMAPK5_HUMAN
AccessioniPrimary (citable) accession number: Q8IW41
Secondary accession number(s): B3KVA5
, O60491, Q86X46, Q9BVX9, Q9UG86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: October 29, 2014
This is version 124 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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