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Protein

Mitogen-activated protein kinase 15

Gene

Mapk15

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

Functioni

Constitutively active kinase which may function as a negative regulator of cell growth. In vitro, phosphorylates FOS.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation. Inhibited by dual specificity phosphatases, such as DUSP1.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431ATPPROSITE-ProRule annotation
Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • MAPK cascade Source: GOC
  • negative regulation of DNA replication Source: RGD
  • negative regulation of transcription from RNA polymerase II promoter Source: RGD
  • positive regulation of protein catabolic process Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of protein ubiquitination Source: RGD
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: RGD
  • response to estradiol Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 15 (EC:2.7.11.24)
Short name:
MAP kinase 15
Short name:
MAPK 15
Alternative name(s):
Extracellular signal-regulated kinase 7
Short name:
ERK-7
Gene namesi
Name:Mapk15
Synonyms:Erk7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi628675. Mapk15.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431K → R: Loss of autophosphorylation and activity. 1 Publication
Mutagenesisi176 – 1761T → A: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with F-178. 1 Publication
Mutagenesisi178 – 1781Y → F: Loss of autophosphorylation and activity. Loss of autophosphorylation and activity; when associated with A-176. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Mitogen-activated protein kinase 15PRO_0000232639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphothreonine1 Publication
Modified residuei178 – 1781Phosphotyrosine1 Publication

Post-translational modificationi

Dually phosphorylated on Thr-176 and Tyr-178, which activates the enzyme. Autophosphorylated on threonine and tyrosine residues.1 Publication
Ubiquitinated. Ubiquitination may allow its tight kinase activity regulation and rapid turnover. May be ubiquitinated by a SCF E3 ligase.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9Z2A6.
PRIDEiQ9Z2A6.

Expressioni

Tissue specificityi

Ubiquitously expressed at a weak level. Highest expression is found in testis and to a lower extent in lung.2 Publications

Gene expression databases

GenevisibleiQ9Z2A6. RN.

Interactioni

Subunit structurei

Interacts with TGFB1I1.

Protein-protein interaction databases

IntActiQ9Z2A6. 1 interaction.
STRINGi10116.ENSRNOP00000012460.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2A6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 305292Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2020Ubiquitin-conjugatingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi176 – 1783TXY

Domaini

C-terminal domain, rather than the kinase activity, is required for the full function of the enzyme. This region may be a protein interaction domain that regulates kinase localization, activation and transcriptional activity. When C-terminally truncated, the enzyme shows a reduction in the Thr-Glu-Tyr (TEY) phosphorylation level, in the in vitro kinase activity, in its nuclear localization and in its inhibitory effect on cell growth.
The N-terminal region (1-20) is the minimal region necessary for ubiquitination and further proteasomal degradation.
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

eggNOGiCOG0515.
GeneTreeiENSGT00800000124204.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ9Z2A6.
KOiK08293.
OMAiIRGDWNR.
OrthoDBiEOG7VDXPC.
PhylomeDBiQ9Z2A6.
TreeFamiTF105101.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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.

Q9Z2A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAAEVDRHV SQRYLIKRRL GKGAYGIVWK AMDRRTGEVV AIKKIFDAFR
60 70 80 90 100
DQTDAQRTFR EIMLLREFGG HPNIIRLLDV IPAKNDRDIY LVFESMDTDL
110 120 130 140 150
NAVIQKGRLL EDIHKRCIFY QLLRATKFIH SGRVIHRDQK PANVLLDAAC
160 170 180 190 200
RVKLCDFGLA RSLSDFPEGP GGQALTEYVA TRWYRAPEVL LSSRWYTPGV
210 220 230 240 250
DMWSLGCILG EMLRGQPLFP GTSTFHQLEL ILETIPLPSM EELQGLGSDY
260 270 280 290 300
SALILQNLGS RPRQTLDALL PPDTPPEALD LLKRLLAFAP DKRLSAEQAL
310 320 330 340 350
QHPYVQRFHC PDREWTRGSD VRLPVHEGDQ LSAPEYRNRL YQMILERRRN
360 370 380 390 400
SRSPREEDLG VVASRAELRA SQRQSLKPGV LPQVLAETPA RKRGPKPQNG
410 420 430 440 450
HGHDPEHVEV RRQSSDPLYQ LPPPGSGERP PGATGEPPSA PSGVKTHVRA
460 470 480 490 500
VAPSLTSQAA AQAANQPLIR SDPARGGGPR AVGARRVPSR LPREAPEPRP
510 520 530 540
GRRMFGISVS QGAQGAARAA LGGYSQAYGT VCRSALGRLP LLPGPRA
Length:547
Mass (Da):60,724
Last modified:March 1, 2002 - v2
Checksum:iD8B7D9955B06862F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078798 mRNA. Translation: AAD12719.2.
RefSeqiNP_775453.1. NM_173331.2.
XP_006241841.1. XM_006241779.2.
UniGeneiRn.42898.

Genome annotation databases

EnsembliENSRNOT00000012461; ENSRNOP00000012460; ENSRNOG00000009336.
GeneIDi286997.
KEGGirno:286997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078798 mRNA. Translation: AAD12719.2.
RefSeqiNP_775453.1. NM_173331.2.
XP_006241841.1. XM_006241779.2.
UniGeneiRn.42898.

3D structure databases

ProteinModelPortaliQ9Z2A6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z2A6. 1 interaction.
STRINGi10116.ENSRNOP00000012460.

Proteomic databases

PaxDbiQ9Z2A6.
PRIDEiQ9Z2A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012461; ENSRNOP00000012460; ENSRNOG00000009336.
GeneIDi286997.
KEGGirno:286997.

Organism-specific databases

CTDi225689.
RGDi628675. Mapk15.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00800000124204.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ9Z2A6.
KOiK08293.
OMAiIRGDWNR.
OrthoDBiEOG7VDXPC.
PhylomeDBiQ9Z2A6.
TreeFamiTF105101.

Miscellaneous databases

NextBioi625286.
PROiQ9Z2A6.

Gene expression databases

GenevisibleiQ9Z2A6. RN.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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]
ProtoNetiSearch...

Publicationsi

  1. "Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, and cell growth."
    Abe M.K., Kuo W.-L., Hershenson M.B., Rosner M.R.
    Mol. Cell. Biol. 19:1301-1312(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, PHOSPHORYLATION AT THR-176 AND TYR-178, MUTAGENESIS OF LYS-43; THR-176; TYR-178 AND 176-THR--TYR-178.
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 154-161, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. Cited for: DOMAIN, CHARACTERIZATION.
  4. Cited for: FUNCTION.
  5. "ERK7 expression and kinase activity is regulated by the ubiquitin-proteosome pathway."
    Kuo W.-L., Duke C.J., Abe M.K., Kaplan E.L., Gomes S., Rosner M.R.
    J. Biol. Chem. 279:23073-23081(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMK15_RAT
AccessioniPrimary (citable) accession number: Q9Z2A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: July 22, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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.