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Protein

Mitogen-activated protein kinase

Gene

Mapk9

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.SAAS annotation

GO - Molecular functioni

  • ATP binding Source: RGD
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: RGD
  • JUN kinase activity Source: RGD
  • mitogen-activated protein kinase kinase kinase binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • cellular response to UV Source: RGD
  • central nervous system development Source: RGD
  • JNK cascade Source: RGD
  • JUN phosphorylation Source: RGD
  • neuron projection development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cell morphogenesis involved in differentiation Source: RGD
  • positive regulation of chemokine production Source: RGD
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • positive regulation of nitric oxide biosynthetic process Source: RGD
  • positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  • positive regulation of prostaglandin biosynthetic process Source: RGD
  • positive regulation of prostaglandin secretion Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of transcription, DNA-templated Source: RGD
  • protein phosphorylation Source: RGD
  • protein targeting to mitochondrion Source: RGD
  • regulation of JNK cascade Source: RGD
  • regulation of protein ubiquitination Source: RGD
  • release of cytochrome c from mitochondria Source: RGD
  • response to amine Source: RGD
  • response to drug Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to organic substance Source: RGD
  • response to toxic substance Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseSAAS annotation, Transferase

Keywords - Ligandi

ATP-bindingSAAS annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinaseSAAS annotation (EC:2.7.11.24SAAS annotation)
Gene namesi
Name:Mapk9Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Organism-specific databases

RGDi628847. Mapk9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • mitochondrion Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003987.

Structurei

3D structure databases

ProteinModelPortaliQ6P727.
SMRiQ6P727. Positions 10-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains protein kinase domain.SAAS annotation

Phylogenomic databases

HOGENOMiHOG000233024.
HOVERGENiHBG014652.
KOiK04440.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
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]

Sequencei

Sequence statusi: Complete.

Q6P727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI
60 70 80 90 100
NVAVKKLSRP FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE
110 120 130 140 150
FQDVYLVMEL MDANLCQVIH MELDHERMSY LLYQMLCGIK HLHSAGIIHR
160 170 180 190 200
DLKPSNIVVK SDCTLKILDF GLARTACTNF MMTPYVVTRY YRAPEVILGM
210 220 230 240 250
GYKENVDIWS VGCIMGELVK GCVIFQGTDH IDQWNKVIEQ LGTPSAEFMK
260 270 280 290 300
KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
310 320 330 340 350
MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE
360 370 380
EWKELIYKEV MDWEERSKNG VKDQPSAQMQ Q
Length:381
Mass (Da):43,906
Last modified:July 5, 2004 - v1
Checksum:iFCCB3C77B7B19C9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061870 mRNA. Translation: AAH61870.1.
RefSeqiNP_001257473.1. NM_001270544.1.
NP_001257474.1. NM_001270545.1.
NP_059018.1. NM_017322.2.
UniGeneiRn.177202.
Rn.9910.

Genome annotation databases

GeneIDi50658.
KEGGirno:50658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061870 mRNA. Translation: AAH61870.1.
RefSeqiNP_001257473.1. NM_001270544.1.
NP_001257474.1. NM_001270545.1.
NP_059018.1. NM_017322.2.
UniGeneiRn.177202.
Rn.9910.

3D structure databases

ProteinModelPortaliQ6P727.
SMRiQ6P727. Positions 10-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50658.
KEGGirno:50658.

Organism-specific databases

CTDi5601.
RGDi628847. Mapk9.

Phylogenomic databases

HOGENOMiHOG000233024.
HOVERGENiHBG014652.
KOiK04440.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
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...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: ProstateImported.

Entry informationi

Entry nameiQ6P727_RAT
AccessioniPrimary (citable) accession number: Q6P727
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 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.