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Q8IW41 (MAPK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAP kinase-activated protein kinase 5

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
EC=2.7.11.1
Alternative name(s):
p38-regulated/activated protein kinase
Short name=PRAK
Gene names
Name:MAPKAPK5
Synonyms:PRAK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.11 Ref.14 Ref.15

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.1 Ref.6

Subunit structure

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. Ref.6 Ref.8

Subcellular location

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. Ref.6 Ref.7

Tissue specificity

Expressed ubiquitously. Ref.1

Induction

Directly regulated by MYC: expression is activated by MYC, suggesting the existence of a feedback regulatory loop. Ref.1 Ref.6 Ref.15

Post-translational modification

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. Ref.1 Ref.7 Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Caution

The role of p38 MAPK kinases is unclear in phosphorylation and activation of MAPKAPK5. According to some reports, it interacts and is phosphorylated by p38-alpha/MAPK14 and p38-beta/MAPK11 (Ref.1 and Ref.7). According to other reports, it is not activated by p38-alpha/MAPK14 and p38-beta/MAPK11. An explanation for these discrepancies, might be that the interaction with p38 MAPK kinases is weak and occurs only under specific conditions.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Traceable author statement Ref.1. Source: GOC

Ras protein signal transduction

Inferred from direct assay Ref.14. Source: UniProtKB

activation of MAPK activity

Traceable author statement Ref.1. Source: GOC

negative regulation of TOR signaling

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of translation

Inferred from direct assay Ref.15. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

stress-induced premature senescence

Inferred from direct assay Ref.14. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Traceable author statement Ref.1. Source: ProtInc

p53 binding

Inferred from direct assay Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IW41-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q8IW41-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473MAP kinase-activated protein kinase 5
PRO_0000086296

Regions

Domain22 – 304283Protein kinase
Nucleotide binding28 – 369ATP By similarity
Coiled coil409 – 44032 Potential

Sites

Active site1481Proton acceptor By similarity
Binding site511ATP By similarity

Amino acid modifications

Modified residue1151Phosphoserine; by PKA By similarity
Modified residue1821Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA Ref.1 Ref.12
Modified residue2121Phosphoserine Ref.7

Natural variations

Alternative sequence407 – 4082Missing in isoform 2.
VSP_011597
Natural variant671M → I. Ref.13
Corresponds to variant rs34132040 [ dbSNP | Ensembl ].
VAR_040758
Natural variant2821R → K. Ref.13
Corresponds to variant rs34843470 [ dbSNP | Ensembl ].
VAR_040759

Experimental info

Mutagenesis511K → M: Kinase defective mutant, abolishes activity. Ref.7
Mutagenesis1821T → A: No p38-beta/MAPK11-induced activation. Ref.1 Ref.7 Ref.15
Mutagenesis1821T → D: Mimicks phosphorylation state and induces constitutive protein kinase activity. Ref.1 Ref.7 Ref.15
Mutagenesis2121S → D: Mimicks phosphorylation state and displays a slightly higher protein kinase activity. Ref.7
Mutagenesis3371L → G: Induces constitutive protein kinase activity. Ref.15
Sequence conflict2731I → T in CAB53747. Ref.5
Sequence conflict2911E → R in AAC39863. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: F3D9DDC83CC0C49D

FASTA47354,220
        10         20         30         40         50         60 
MSEESDMDKA IKETSILEEY SINWTQKLGA GISGPVRVCV KKSTQERFAL KILLDRPKAR 

        70         80         90        100        110        120 
NEVRLHMMCA THPNIVQIIE VFANSVQFPH ESSPRARLLI VMEMMEGGEL FHRISQHRHF 

       130        140        150        160        170        180 
TEKQASQVTK QIALALRHCH LLNIAHRDLK PENLLFKDNS LDAPVKLCDF GFAKIDQGDL 

       190        200        210        220        230        240 
MTPQFTPYYV APQVLEAQRR HQKEKSGIIP TSPTPYTYNK SCDLWSLGVI IYVMLCGYPP 

       250        260        270        280        290        300 
FYSKHHSRTI PKDMRRKIMT GSFEFPEEEW SQISEMAKDV VRKLLKVKPE ERLTIEGVLD 

       310        320        330        340        350        360 
HPWLNSTEAL DNVLPSAQLM MDKAVVAGIQ QAHAEQLANM RIQDLKVSLK PLHSVNNPIL 

       370        380        390        400        410        420 
RKRKLLGTKP KDSVYIHDHE NGAEDSNVAL EKLRDVIAQC ILPQAGKGEN EDEKLNEVMQ 

       430        440        450        460        470 
EAWKYNRECK LLRDTLQSFS WNGRGFTDKV DRLKLAEIVK QVIEEQTTSH ESQ 

« Hide

Isoform 2 [UniParc].

Checksum: 176FA041A7F28570
Show »

FASTA47154,035

References

« Hide 'large scale' references
[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. 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] (ISOFORM 2).
[3]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].
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-473 (ISOFORM 2).
Tissue: Brain.
[6]"p62 functions as a p38 MAP kinase regulator."
Sudo T., Maruyama M., Osada H.
Biochem. Biophys. Res. Commun. 269:521-525(2000) [PubMed] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-67 AND LYS-282.
[14]"PRAK is essential for ras-induced senescence and tumor suppression."
Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C., Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III, Wright P.E., Han J.
Cell 128:295-308(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44975.1. [Q8IW41-1]
CCDS44976.1. [Q8IW41-2]
PIRT34519.
RefSeqNP_003659.2. NM_003668.3. [Q8IW41-2]
NP_620777.1. NM_139078.2. [Q8IW41-1]
UniGeneHs.333120.
Hs.413901.

3D structure databases

ProteinModelPortalQ8IW41.
SMRQ8IW41. Positions 11-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114120. 16 interactions.
IntActQ8IW41. 14 interactions.
MINTMINT-4711647.
STRING9606.ENSP00000202788.

Chemistry

BindingDBQ8IW41.
ChEMBLCHEMBL3094.
GuidetoPHARMACOLOGY2096.

PTM databases

PhosphoSiteQ8IW41.

Polymorphism databases

DMDM52000829.

Proteomic databases

MaxQBQ8IW41.
PaxDbQ8IW41.
PRIDEQ8IW41.

Protocols and materials databases

DNASU8550.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000550735; ENSP00000449667; ENSG00000089022. [Q8IW41-2]
ENST00000551404; ENSP00000449381; ENSG00000089022. [Q8IW41-1]
GeneID8550.
KEGGhsa:8550.
UCSCuc001tsz.4. human. [Q8IW41-2]
uc001tta.4. human. [Q8IW41-1]

Organism-specific databases

CTD8550.
GeneCardsGC12P112282.
HGNCHGNC:6889. MAPKAPK5.
HPACAB004546.
HPA015515.
MIM606723. gene.
neXtProtNX_Q8IW41.
PharmGKBPA30633.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233031.
HOVERGENHBG106948.
InParanoidQ8IW41.
KOK04442.
OMAQVTKQIA.
PhylomeDBQ8IW41.
TreeFamTF312891.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ8IW41.

Gene expression databases

ArrayExpressQ8IW41.
BgeeQ8IW41.
CleanExHS_MAPKAPK5.
GenevestigatorQ8IW41.

Family and domain databases

Gene3D4.10.1170.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR027442. MAPKAPK_C.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPKAPK5. human.
GeneWikiMAPKAPK5.
GenomeRNAi8550.
NextBio32036.
PROQ8IW41.
SOURCESearch...

Entry information

Entry nameMAPK5_HUMAN
AccessionPrimary (citable) accession number: Q8IW41
Secondary accession number(s): B3KVA5 expand/collapse secondary AC list , O60491, Q86X46, Q9BVX9, Q9UG86
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 121 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM