| Tag | Content |
|---|
| EKPD ID | EKS-RAN-00474 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| CMGC/MAPK | 436.4 | 5.2E-131 | 27 | 311 | 285 |
|
| Status | Reviewed |
| Ensembl Protein | ENSRNOP00000046455 |
| UniProt Accession | Q63538; |
| Protein Name | Mitogen-activated protein kinase 12 |
| Protein Synonyms/Alias | MAP kinase 12; MAPK 12; Extracellular signal-regulated kinase 6; ERK-6; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 gamma; Stress-activated protein kinase 3; |
| Gene Name | Mapk12 |
| Gene Synonyms/Alias | Mapk12; Sapk3; |
| Ensembl Information | |
| Organism | Rattus norvegicus |
| Functional Description | Serine/threonine kinase which acts as an essentialcomponent of the MAP kinase signal transduction pathway. MAPK12 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 such as ELK1 and ATF2. 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 such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma- radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. |
| Protein Length | 367 |
Protein Sequence
(FASTA) | | MSSPPPARKG FYRQEVTKTA WEVRAVYQDL QPVGSGAYGA VCSAVDSRTG NKVAIKKLYR 60 | | PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM 120 | | KHETLSEDRI QFLVYQMLKG LKYIHAAGVI HRDLKPGNLA VNEDCELKIL DFGLARQADS 180 | | EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKILFKGND HLDQLKEIMK 240 | | VTGTPPPEFV QKLQSAEAKN YMEGLPELEK KDFASVLTNA SPQAVNLLEK MLVLDAEQRV 300 | | TAAEALAHPY FESLRDTEDE PKAQKYDDSF DDVDRTLEEW KRVTYKEVLS FKPPRQLGAR 360 | | VPKETAL 367 |
|
Nucleotide Sequence
(FASTA) | | ATGAGCTCCC CGCCACCCGC CCGCAAGGGC TTTTACCGCC AGGAGGTGAC CAAAACGGCC 60 | | TGGGAGGTGC GCGCCGTGTA CCAGGACCTG CAGCCCGTTG GCTCTGGTGC CTATGGTGCA 120 | | GTGTGCTCTG CAGTAGACAG CCGCACTGGC AACAAGGTGG CCATCAAGAA GTTGTACCGG 180 | | CCCTTCCAGT CGGAGCTGTT TGCCAAGCGC GCCTACAGAG AGTTGCGCCT CCTCAAACAC 240 | | ATGCGCCACG AGAACGTCAT TGGGCTGCTG GATGTGTTCA CTCCCGATGA GACTCTGGAT 300 | | GACTTCACAG ACTTCTACCT GGTGATGCCA TTCATGGGCA CTGACCTGGG CAAGCTCATG 360 | | AAGCACGAGA CTCTGAGTGA AGACAGAATC CAGTTTCTTG TGTATCAGAT GCTGAAGGGG 420 | | CTGAAGTATA TCCACGCTGC CGGCGTCATC CACAGGGACT TGAAACCTGG AAACCTGGCT 480 | | GTGAACGAGG ACTGTGAGCT GAAGATCCTA GATTTTGGCC TTGCCAGGCA GGCGGACAGT 540 | | GAGATGACAG GATATGTGGT AACCCGGTGG TATCGGGCAC CAGAGGTCAT CTTGAATTGG 600 | | ATGCGTTACA CACAGACAGT GGACATTTGG TCTGTTGGCT GCATCATGGC AGAGATGATT 660 | | ACTGGAAAGA TCCTGTTCAA AGGCAATGAC CACCTGGACC AGCTGAAGGA GATCATGAAA 720 | | GTCACAGGGA CACCCCCTCC TGAGTTTGTA CAGAAGCTAC AGAGTGCTGA GGCCAAGAAC 780 | | TACATGGAAG GCCTCCCTGA GTTGGAAAAG AAGGATTTTG CTTCTGTCCT GACCAATGCA 840 | | AGCCCTCAGG CCGTGAATCT CCTGGAAAAG ATGCTGGTGT TGGATGCGGA ACAGCGGGTG 900 | | ACAGCAGCTG AGGCATTAGC CCACCCATAC TTTGAGTCCC TTCGGGACAC TGAGGATGAG 960 | | CCCAAGGCCC AGAAATATGA TGACTCCTTT GATGACGTAG ACCGCACCCT TGAGGAATGG 1020 | | AAGCGTGTTA CGTATAAGGA AGTGCTCAGC TTCAAGCCTC CCAGGCAGCT AGGAGCCAGA 1080 | | GTTCCAAAGG AGACAGCTCT GTGA 1104 |
|
| Domain Profile | S: 1 yeslkplgeGaygvvvsavdkrteervaikklsrpfqketsakrtlRElkllkelkheNi 60 | y++l+p+g+Gayg v+savd+rt+++vaikkl rpfq+e akr++REl+llk+++heN+ | Q: 27 YQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENV 86 | 899********************************************************* |
| S: 61 iklldvftpeeeleelkdvYlvtelmetdLkkviksqklsdehiklllyqilrglkylHs 120 | i lldvftp+e+l++++d+Ylv+ +m+tdL k++k+++ls+++i++l+yq+l+glky+H+ | Q: 87 IGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHA 146 | ************************************************************ |
| S: 121 anviHrDlKPsNllvnedcelkildFGlarsadkekekklteyvatrwYraPeillslke 180 | a+viHrDlKP+Nl+vnedcelkildFGlar+ad+e +t+yv+trwYraPe++l++++ | Q: 147 AGVIHRDLKPGNLAVNEDCELKILDFGLARQADSE----MTGYVVTRWYRAPEVILNWMR 202 | **********************************9....********************* |
| S: 181 ytkavDiWsvGCIlaElltgkplfpgkdeidqlekilevlgtpseeflkkieseearnyi 240 | yt++vDiWsvGCI+aE++tgk+lf+g+d++dql++i++v+gtp ef++k++s ea+ny+ | Q: 203 YTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKVTGTPPPEFVQKLQSAEAKNYM 262 | ************************************************************ |
| S: 241 kslpkkkkkdfeelfpkaseealdLleklLvldpdkRisveeaLehpYl 289 | + lp+ +kkdf++++++as++a++Llek+Lvld+++R++++eaL+hpY+ | Q: 263 EGLPELEKKDFASVLTNASPQAVNLLEKMLVLDAEQRVTAAEALAHPYF 311 | ************************************************6 |
|
Domain Sequence
(FASTA) | | YQDLQPVGSG AYGAVCSAVD SRTGNKVAIK KLYRPFQSEL FAKRAYRELR LLKHMRHENV 60 | | IGLLDVFTPD ETLDDFTDFY LVMPFMGTDL GKLMKHETLS EDRIQFLVYQ MLKGLKYIHA 120 | | AGVIHRDLKP GNLAVNEDCE LKILDFGLAR QADSEMTGYV VTRWYRAPEV ILNWMRYTQT 180 | | VDIWSVGCIM AEMITGKILF KGNDHLDQLK EIMKVTGTPP PEFVQKLQSA EAKNYMEGLP 240 | | ELEKKDFASV LTNASPQAVN LLEKMLVLDA EQRVTAAEAL AHPYF 285 |
|
| Keyword | ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Stress response; Transcription; Transcription regulation; Transferase; Ubl conjugation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
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| Pfam | |
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| Created Date | 20-Feb-2013 |