◀ Back to MAPK1
MAPK1 — XRCC5
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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Gene Ontology Complexes protein complex:
protein complex complex (HSF1-TRMT112-HIST1H4A-UBQLN1-CDX2-USP28-HDAC5-CAV3-CANX-LHX1-TUBA3C-TUBA3E-PI4K2A-NR0B2-RYR2-NTRK1-MPP5-N6AMT1-STAP1-ZFP42-FADD-ATP6V0D1-PRKCDBP-AQP2-FNTB-PRPSAP2-WIPI2-CRB3-CRB2-PEX11A-LDB1-RBP4-TMEM102-GATA2-ADCY2-DZIP1-SYK-TUBB4B-PTPN11-KAT5-CEP290-SYP-ASF1B-PLEKHA2-KIF24-MYO5B-RGP1-CFTR-SPTBN5-VPS72-ACTA2-PRKCI-CNST-SNX4-GNAO1-NFKBIA-UBE2D2-EPB41-RAB5A-GLUL-BSND-GSK3B-SKI-XRCC6-PPM1E-TTR-TUBA1A-SUCLG1-TRIAP1-AKT1S1-MYD88-NPPB-GDF11-INCENP-PLCB3-BECN1-PRKAB1-SOD1-TUBB1-NPHS2-NPHS1-EPS8L1-GDI1-TUBB2A-TUBB2B-SUCLG2-PEX3-TUBAL3-ERLIN1-MAGED1-GCH1-TUBB-CPS1-MEF2C-ZNF703-SLC22A6-CPLX1-EIF4EBP1-TUBE1-FLNA-CD19-STX1A-HDAC2-TOMM40L-HDAC6-SMAD6-SMAD7-TLE6-SMAD2-PARD6B-STXBP1-ACR-TRPC1-PARD6A-TRPC4-PANX1-DCTN1-SOX9-PXMP2-BCR-SET-MALT1-BHMT-RILP-TRADD-HIST1H3A-MAPK1-PVALB-NFKB1-NUFIP1-ACVR2B-TAL1-FOXP3-SSX2IP-GNB2-SLC27A5-GOPC-PAX2-CXADR-AIF1L-APBA1-MYL12A-LMO2-ID2-CCDC113-DDOST-SPP2-GATAD2B-PLN-ERCC8-BIRC8-ASF1A-CAB39-BIRC3-BIRC2-CTNNB1-CORO1A-PRELID1-HAND2-CHAF1B-SCAP-GNAT3-CDC20-SMARCA4-IQGAP1-YWHAZ-CEBPA-PRPS2-AXIN1-XRCC5-YWHAQ-UVRAG-SLC51B-RGS4-RGS6-HTT-YWHAB-APCS-CDCA8-RIPK1-MTA2-SIN3A-ANXA1-NOS1-SNTA1-TRAF6-KPNB1-VCL-VCP-PTRF-PRKCZ-SKIL-RAB3A-KRIT1-SSBP3-PRPSAP1-PPP1CC-TAB1-MYO6-ACTL7A-TUBG2-MBD2-COL6A1-COL6A2-BCL3)
Helps et al., Biochem J 2000, Lauderdale et al., Proc Natl Acad Sci U S A 2000, Didichenko et al., FEBS Lett 2000, Koh et al., Curr Biol 2002, Fan et al., Mol Cell Biol 2002, Groisman et al., Cell 2003, Offenhäuser et al., Mol Biol Cell 2004, Tagami et al., Cell 2004, Doyon et al., Mol Cell Biol 2004, Moore et al., Genomics 2004, Sun et al., Mol Cell 2004, Zang et al., J Cell Biochem 2004, Tian et al., Cancer Res 2005, An et al., Biochemistry 2005, Mahajan et al., Proc Natl Acad Sci U S A 2005, Vader et al., EMBO Rep 2006, Yeh et al., J Biol Chem 2006, Li et al., Immunol Rev 2006, Agbas et al., Biochem J 2007, Swiatecka-Urban et al., J Biol Chem 2007, McKeegan et al., Mol Cell Biol 2007, Shono et al., J Am Soc Nephrol 2007, Popov et al., Cell cycle (Georgetown, Tex.) 2007, Sato et al., J Biol Chem 2008, Fitzgerald et al., J Biol Chem 2008, Lyssand et al., J Biol Chem 2008, Figaro et al., FEBS Lett 2008, Ueda et al., Proc Natl Acad Sci U S A 2008, Shimojo et al., J Biol Chem 2008, Costantini et al., Blood 2009, Mitsuishi et al., J Biol Chem 2010, Masuda et al., J Biol Chem 2010, Koch et al., J Cell Sci 2010, Boëda et al., J Biol Chem 2011, Sircoulomb et al., EMBO Mol Med 2011, Hoxhaj et al., J Cell Sci 2012, Uckun et al., Proc Natl Acad Sci U S A 2012, Pusapati et al., J Biol Chem 2012, Ghai et al., Proc Natl Acad Sci U S A 2013, Kelly et al., PLoS Biol 2013, Chiang et al., PloS one 2013, Dauphinee et al., J Immunol 2013, Potting et al., Cell Metab 2013, Ludwig et al., PLoS Biol 2013, Lee et al., Proc Natl Acad Sci U S A 2013, Kobayashi et al., J Cell Biol 2014, Zheng et al., Am J Physiol 1994, Kumar et al., Biochem Biophys Res Commun 1998, Watabe-Uchida et al., J Cell Biol 1998, Haft et al., Mol Cell Biol 1998
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IRef Ophid Interaction:
XRCC5
—
MAPK1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Mochizuki et al., Nature 1999
:
This decrease in GTP bound
Rap1 activates
ERK/MAPK
Palsson et al., J Biol Chem 2000
:
Furthermore, constitutively active
Rap1AV12 inhibited p38
MAPK activation by IL-1, consistent with Rap antagonizing Ras function
Pizon et al., Oncogene 2000
(MAP Kinase Signaling System) :
Although the
role of
Rap1A in
MAPK activation has been analysed in various cell types, the signalling pathways activated by Rap1A have not been explored in myogenic cells
Kievit et al., Mol Endocrinol 2001
(Pituitary Neoplasms) :
These findings provide evidence for a model for cAMP induced PRL transcription involving
Rap1 induced
MAPK activity leading to stimulation of the transcriptional coactivators, CBP and p300
McDermott et al., J Biol Chem 2002
:
In the same manner, the inhibitory effect of Rap on the activation of p38 by IL-1 occurred at a point downstream of MyD88, IRAK, and TRAF6, since the activation of p38
MAPK by these components was
inhibited by overexpressing active
Rap1AV12 , while neither MKK3 nor MKK6 were affected
Huang et al., J Biol Chem 2004
(MAP Kinase Signaling System) :
Rap1 induced p38
mitogen activated protein kinase activation facilitates AMPA receptor trafficking via the GDI.Rab5 complex
Chen et al., Mol Microbiol 2005
(MAP Kinase Signaling System) :
The
Rap-1 inhibitor, GGTI-298,
restored MAPK activation in the presence of cAMP, further suggesting that Rap-1 is responsible for cAMP dependent MAPK inhibition
Li et al., Blood 2005
:
T-cell receptor (TCR)-CD3/CD28 mediated activation of
Rap1 and Akt was retained in Tregs, but activation of Ras,
mitogenactivated protein kinase 1/2 ( MEK1/2 ), and extracellular signal regulated kinase 1/2 ( Erk1/2 ) was
impaired
Stork et al., Blood 2005
:
Rap1 may also regulate cellular differentiation and proliferation via pathways that are distinct from those mediating adhesion, and
involve regulation of the
mitogen activated protein ( MAP ) kinase or ERK ( extracellular signal regulated kinase ) cascade
Karhoff et al., Neuroendocrinology 2007
(Digestive System Neoplasms...) :
In endocrine cells, the small G-protein
Rap1 stimulates
mitogen activated protein kinase ( MAPK ) signaling by activating B-Raf ... Overexpression of
Rap1 and B-Raf
activated MAPK extracellular dependent kinase (ERK)
ERK-2 and ERK dependent transcription factor Elk-1 in neuroendocrine cell lines Bon and INS-1
Minato et al., Adv Immunol 2007
(Neoplasms) :
Rap1 also
regulates MAP kinase ( MAPK ) activity in a manner highly dependent on the context of cell types
Stadtmann et al., Eur J Immunol 2011
(Peritonitis) :
Rap1a activation by CalDAG-GEFI and p38
MAPK is involved in E-selectin dependent slow leukocyte rolling ... Our data demonstrate that
Rap1a activation by p38
MAPK and CalDAG-GEFI is involved in E-selectin dependent slow rolling and leukocyte recruitment