Ksr1
entrez
16706
canonical
uniprot
Q61097
canonical
ensembl
ENSMUSG00000018334
resolver
ensp
ENSMUSP00000018478
resolver
ensp
ENSMUSP00000154385
resolver
enst
ENSMUST00000226282
resolver
genesymbol
Ksr1
resolver
genesymbol_syn
Ksr
resolver
uniprot
A0A2I3BR95
resolver
uniprot
Q3UV75
resolver
uniprot
Q61648
resolver
uniprot
Q78DX8
resolver
uniprot_entry
A0A2I3BR95_MOUSE
resolver
uniprot_entry
KSR1_MOUSE
resolver
uniprot_entry
Q3UV75_MOUSE
resolver
uniprot_sec
Q61648
resolver
uniprot_sec
Q78DX8
resolver
amino_acid_sequence
MDRAALRAAAMGEKKEGGGGGAAADGGAGAAVSRALQQCGQLQKLIDISIGSLRGLRTKCSVSNDLTQQEIRTLEAKLVKYICKQQQSKLSVTPSDRTAELNSYPRFSDWLYIFNVRPEVVQEIPQELTLDALLEMDEAKAKEMLRRWGASTEECSRLQQALTCLRKVTGLGGEHKMDSGWSSTDARDSSLGPPMDMLSSLGRAGASTQGPRSISVSALPASDSPVPGLSEGLSDSCIPLHTSGRLTPRALHSFITPPTTPQLRRHAKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDDVTPMKFELPHGSPQLVRRDIGLSVTHRFSTKSWLSQVCNVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRITFLPLARLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNLDSSSNPSSTTSSTPSSPAPFLTSSNPSSATTPPNPSPGQRDSRFSFPDISACSQAAPLSSTADSTRLDDQPKTDVLGVHEAEAEEPEAGKSEAEDDEEDEVDDLPSSRRPWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREERRENQLKLSHDWLCYLAPEIVREMIPGRDEDQLPFSKAADVYAFGTVWYELQARDWPFKHQPAEALIWQIGSGEGVRRVLASVSLGKEVGEILSACWAFDLQERPSFSLLMDMLERLPKLNRRLSHPGHFWKSADINSSKVMPRFERFGLGTLESGNPKM
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (PubMed:10409742, PubMed:12932319, PubMed:21102438, PubMed:21441104). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (By similarity). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (PubMed:21102438). Its kinase activity is unsure (PubMed:21441104). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (PubMed:21441104). {ECO:0000250|UniProtKB:Q8IVT5, ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:21441104}.
uniprot
proteins
mass_dalton
96755
uniprot
proteins
mutagenesis
MUTAGEN 56..57; /note="LR->GS: No effect on the interaction with MAP2K1, MAP2K2 and YWHAE. Abolishes interaction with BRAF. Abolishes location at membrane ruffles."; /evidence="ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:23250398"; MUTAGEN 71; /note="I->A: Impairs interaction with BRAF and association with membrane ruffles; when associated with A-78."; /evidence="ECO:0000269|PubMed:23250398"; MUTAGEN 78; /note="L->A: Impairs interaction with BRAF and association with membrane ruffles; when associated with A-78."; /evidence="ECO:0000269|PubMed:23250398"; MUTAGEN 297; /note="S->A: Constitutive targeting to the plasma membrane; when associated with A-392."; /evidence="ECO:0000269|PubMed:11741534"; MUTAGEN 382; /note="L->A: No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 387; /note="L->A: Reduces interaction with MARK3. Reduces phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 389; /note="R->A: Reduces phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 390; /note="T->A: No effect on phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 391; /note="E->A: No effect on phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 392; /note="S->A: Constitutive targeting to the plasma membrane; when associated with A-297. No effect on interaction with MARK3. Abolishes phosphorylation by MARK3."; /evidence="ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12941695"; MUTAGEN 393; /note="V->A: Reduces phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 394; /note="P->A: No effect on phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 395; /note="S->A: No effect on phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 396; /note="D->A: No effect on phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 397; /note="I->A: Decrease in MARK3 binding; when associated with A-401. Abolishes interaction with MARK3. Reduces phosphorylation of S-392 by MARK3."; /evidence="ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12941695"; MUTAGEN 400; /note="P->A: No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 401; /note="V->A: Decrease in MARK3 binding; when associated with A-397. No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12941695"; MUTAGEN 403; /note="R->A: No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 413; /note="P->A: No effect on interaction with MARK3."; /evidence="ECO:0000269|PubMed:12941695"; MUTAGEN 572; /note="G->E: Decrease in MEK binding."; /evidence="ECO:0000269|PubMed:10891492"; MUTAGEN 580; /note="G->E: Partial decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE."; /evidence="ECO:0000269|PubMed:10409742"; MUTAGEN 587; /note="A->F: Loss of ATP binding and reduces MAPK1 and MAPK3 phosphorylation levels. Loss of kinase activity towards MAP2K1 in vitro. Abnormal constitutive interaction with CRAF. No effect on the interaction with BRAF and MAP2K1."; /evidence="ECO:0000269|PubMed:21441104"; MUTAGEN 587; /note="A->V: No effect on ATP binding and MAPK1 and MAPK3 phosphorylation levels. No effect on the interaction with MAP2K1."; /evidence="ECO:0000269|PubMed:21441104"; MUTAGEN 589; /note="R->M: Severe decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE."; /evidence="ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:10891492"; MUTAGEN 615; /note="R->H: Severe decrease in MAP2K1 and MAP2K2 binding. No effect on the interaction with YWHAE."; /evidence="ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:10891492"; MUTAGEN 700; /note="D->V: Decrease in MEK binding."; /evidence="ECO:0000269|PubMed:10891492"; MUTAGEN 809; /note="C->Y: Associates almost exclusively with the membrane. Loss of MAP2K2 and MAP2K2 binding and recruitment to the membrane. Loss of MAP kinase-mediated inhibition of ELK1 phosphorylation. No effect on the interaction with YWHAE."; /evidence="ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:10891492"; MUTAGEN 838; /note="S->A: Abolishes one phosphorylation site. Decreases phosphorylation by PKA."; /evidence="ECO:0000269|PubMed:21102438
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-297 and, to a higher extent, on Ser-392 by MARK3 (PubMed:11741534, PubMed:12941695). Dephosphorylated on Ser-392 by PPP2CA (PubMed:12932319). Phosphorylated KSR1 is cytoplasmic and dephosphorylated KSR1 is membrane-associated (Probable). Phosphorylated by PKA at Ser-838. Phosphorylation at Ser-838 is required for cAMP-dependent activation of MAPK1 and/or MAPK3 (PubMed:21102438). {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:10891492, ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:12941695, ECO:0000269|PubMed:21102438, ECO:0000305}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
TKL Ser/Thr protein kinase family
uniprot
proteins
pubmed
10409742
uniprot
proteins
pubmed
10891492
uniprot
proteins
pubmed
11741534
uniprot
proteins
pubmed
11786023
uniprot
proteins
pubmed
12007434
uniprot
proteins
pubmed
12932319
uniprot
proteins
pubmed
12941695
uniprot
proteins
pubmed
21102438
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21441104
uniprot
proteins
pubmed
23250398
uniprot
proteins
pubmed
7626882
uniprot
proteins
pubmed
8521512
uniprot
proteins
sequence_length
873
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:12941695, ECO:0000269|PubMed:23250398}. Membrane {ECO:0000269|PubMed:10409742}; Peripheral membrane protein {ECO:0000269|PubMed:10409742}. Cell membrane {ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:23250398}; Peripheral membrane protein {ECO:0000269|PubMed:11741534, ECO:0000269|PubMed:12932319, ECO:0000269|PubMed:23250398}. Cell projection, ruffle membrane {ECO:0000269|PubMed:23250398}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IVT5}. Note=In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery. {ECO:0000305|PubMed:12932319}.
uniprot
proteins