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P47812

- MK14_XENLA

UniProt

P47812 - MK14_XENLA

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Protein

Mitogen-activated protein kinase 14

Gene

mapk14

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. mapk14a is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. MPK2 is activated by upstream MAPKK/MAPKKK and stimulates MAPKAP kinase 2 to phosphorylate small heat shock proteins. Does not phosphorylate myelin basic protein or MAPKAP kinase 1.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: UniProtKB
  2. p38MAPK cascade Source: UniProtKB
  3. positive regulation of myoblast differentiation Source: UniProtKB
  4. positive regulation of myoblast fusion Source: UniProtKB
  5. positive regulation of myotube differentiation Source: UniProtKB
  6. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 6726.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14 (EC:2.7.11.24)
Short name:
MAP kinase 14
Short name:
MAPK 14
Alternative name(s):
Mitogen-activated Mitogen-activated protein kinase 2
Short name:
MAP kinase 2
Short name:
MPK2
Gene namesi
Name:mapk14
Synonyms:mpk2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1018624. mapk14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Mitogen-activated protein kinase 14PRO_0000186299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811PhosphothreonineBy similarity
Modified residuei183 – 1831PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-181 and Tyr-183, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP47812.

Interactioni

Protein-protein interaction databases

BioGridi98234. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP47812.
SMRiP47812. Positions 9-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 309285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi181 – 1833TXY

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

HOVERGENiHBG014652.
KOiK04441.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47812 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSNQSYVFY RQELNKTLWE VPDRYQNLTP VGSGAYGSVC SSFDTRTALR
60 70 80 90 100
IAVKKLSRPF QSIIHAKRTY RELRLLKHMK HENVIGLLDV FSPAKSFEEF
110 120 130 140 150
NDVYLVTHLM GADLNNIVKC QKLTDDHVQF LIYQILRGLK YIHSAGIIHR
160 170 180 190 200
DLKPSNLAVN EDCELKILDF GLARHTDEEM TGYVATRWYR APEIMLNWMH
210 220 230 240 250
YNQTVDIWSV GCIMAELLTG RTLFPGTDHI DQLKLILRLV GTPEPELLQK
260 270 280 290 300
ISSEAARNYI QSLPYMPKMN FEDVFLGANP QAVDLLEKML VLDTDKRITA
310 320 330 340 350
AEALAHSYFA QYHDPDDEPI AEPYDQSFES RELDIEEWKR LTYEEVTCFV
360
PPPLDSEEME S
Length:361
Mass (Da):41,719
Last modified:February 1, 1996 - v1
Checksum:iF2B2E6C40800A70D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80751 mRNA. Translation: CAA56727.1.
BC056064 mRNA. Translation: AAH56064.1.
PIRiA54805.
RefSeqiNP_001080300.1. NM_001086831.1.
UniGeneiXl.1245.

Genome annotation databases

GeneIDi379992.
KEGGixla:379992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80751 mRNA. Translation: CAA56727.1 .
BC056064 mRNA. Translation: AAH56064.1 .
PIRi A54805.
RefSeqi NP_001080300.1. NM_001086831.1.
UniGenei Xl.1245.

3D structure databases

ProteinModelPortali P47812.
SMRi P47812. Positions 9-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 98234. 1 interaction.

Proteomic databases

PRIDEi P47812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 379992.
KEGGi xla:379992.

Organism-specific databases

CTDi 1432.
Xenbasei XB-GENE-1018624. mapk14.

Phylogenomic databases

HOVERGENi HBG014652.
KOi K04441.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 6726.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins."
    Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D., Hunt T., Nebreda A.R.
    Cell 78:1027-1037(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.

Entry informationi

Entry nameiMK14_XENLA
AccessioniPrimary (citable) accession number: P47812
Secondary accession number(s): Q5D076
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3