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Protein

Mitogen-activated protein kinase 8A

Gene

mapk8a

Organism
Cyprinus carpio (Common carp)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. May play a role in the regulation of the circadian clock.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei55ATPPROSITE-ProRule annotation1
Active sitei151Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi33 – 38ATPPROSITE-ProRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processBiological rhythms
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 1195.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 8A (EC:2.7.11.24)
Short name:
MAP kinase 8A
Short name:
MAPK 8A
Alternative name(s):
Stress-activated protein kinase JNKa
c-Jun N-terminal kinase A
Gene namesi
Name:mapk8a
OrganismiCyprinus carpio (Common carp)Imported
Taxonomic identifieri7962 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCyprinus

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001862661 – 427Mitogen-activated protein kinase 8AAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei183PhosphothreonineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1

Post-translational modificationi

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ90327.

Expressioni

Tissue specificityi

Expressed in brain and ovary.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ90327.
SMRiQ90327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 321Protein kinasePROSITE-ProRule annotationAdd BLAST296

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi183 – 185TXY3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG014652.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
PRINTSiPR01772. JNKMAPKINASE.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

Q90327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKNKREKEF YSVDVGDSTF TVLKRYQNLR PIGSGAQGIV CSAYDHNLER
60 70 80 90 100
NVAIKKLSRP FQNQTHAKRA YRELVLMKYV NHKNIICLLN VFTSQKTLDE
110 120 130 140 150
FQDVYLVMEL MDANLCQVIQ MELDHERLSY LLYQMLCGIK HLHSAGIIHR
160 170 180 190 200
DLKPSNIVVK SDCTLKILDF GLARTAATGL LMTPYVVTRY YRAPEVILGM
210 220 230 240 250
GYQANVDIWS VGCILAEMVR HKILFPGRDY IDQWNKVIEQ LGTPTQEFMM
260 270 280 290 300
KLNQSVRTYV ENRPRYTGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
310 320 330 340 350
MLVIDASKRI SVEEALQHPY INVWYDPAEV EAPPPVITDK QLDEREHTVE
360 370 380 390 400
EWKELIYKEV LDWEERMKNG AIRGQPSPLG AAVINGSPQP SSSSSINDVS
410 420
SMSTEPTVAS DTDSSLEASA GPLSCCR
Length:427
Mass (Da):48,606
Last modified:November 1, 1996 - v1
Checksum:i518B490DD048120C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83273 mRNA. Translation: BAA11880.1.
PIRiJC5693.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83273 mRNA. Translation: BAA11880.1.
PIRiJC5693.

3D structure databases

ProteinModelPortaliQ90327.
SMRiQ90327.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ90327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG014652.

Enzyme and pathway databases

BRENDAi2.7.11.24. 1195.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
PRINTSiPR01772. JNKMAPKINASE.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMK08A_CYPCA
AccessioniPrimary (citable) accession number: Q90327
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: November 1, 1996
Last modified: March 15, 2017
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.