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Q61097

- KSR1_MOUSE

UniProt

Q61097 - KSR1_MOUSE

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Protein

Kinase suppressor of Ras 1

Gene

Ksr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi334 – 3341Zinc 11 Publication
Metal bindingi346 – 3461Zinc 21 Publication
Metal bindingi349 – 3491Zinc 21 Publication
Metal bindingi359 – 3591Zinc 11 Publication
Metal bindingi362 – 3621Zinc 11 Publication
Metal bindingi367 – 3671Zinc 21 Publication
Metal bindingi370 – 3701Zinc 21 Publication
Metal bindingi377 – 3771Zinc 11 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri333 – 37745Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. MAP-kinase scaffold activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. protein serine/threonine kinase activity Source: InterPro

GO - Biological processi

  1. intracellular signal transduction Source: InterPro
  2. positive regulation of MAPK cascade Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Kinase suppressor of Ras 1
Short name:
mKSR1
Alternative name(s):
Protein Hb
Gene namesi
Name:Ksr1
Synonyms:Ksr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:105051. Ksr1.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein. Endoplasmic reticulum membrane By similarity
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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi297 – 2971S → A: Constitutive targeting to the plasma membrane; when associated with A-392. 1 Publication
Mutagenesisi392 – 3921S → A: Constitutive targeting to the plasma membrane; when associated with A-297. 1 Publication
Mutagenesisi397 – 3971I → A: Decrease in MARK3 binding; when associated with A-401. 1 Publication
Mutagenesisi401 – 4011V → A: Decrease in MARK3 binding; when associated with A-397. 1 Publication
Mutagenesisi572 – 5721G → E: Decrease in MEK binding. 1 Publication
Mutagenesisi589 – 5891R → M: Almost no MEK binding. 1 Publication
Mutagenesisi615 – 6151R → H: Decrease in MEK binding. 1 Publication
Mutagenesisi700 – 7001D → V: Decrease in MEK binding. 1 Publication
Mutagenesisi809 – 8091C → Y: No MEK binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 873873Kinase suppressor of Ras 1PRO_0000086230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561PhosphothreonineBy similarity
Modified residuei260 – 2601PhosphothreonineBy similarity
Modified residuei297 – 2971Phosphoserine; by MARK31 Publication
Modified residuei320 – 3201PhosphoserineBy similarity
Modified residuei392 – 3921Phosphoserine; by MARK31 Publication
Modified residuei518 – 5181PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser-297 and, to a higher extent, on Ser-392 by MARK3. Dephosphorylated on Ser-392 by PPP2CA. Phosphorylated KSR is cytoplasmic and dephosphorylated KSR is membrane-associated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61097.
PaxDbiQ61097.
PRIDEiQ61097.

PTM databases

PhosphoSiteiQ61097.

Expressioni

Tissue specificityi

Expressed in brain, spleen and testis. Isoform 1 is highly expressed spleen and weakly in testis, and isoform 2 is highly expressed in brain and weakly in testis.1 Publication

Gene expression databases

BgeeiQ61097.
CleanExiMM_KSR1.
ExpressionAtlasiQ61097. baseline and differential.
GenevestigatoriQ61097.

Interactioni

Subunit structurei

Interacts with HSPCA/HSP90, YWHAB/14-3-3, CDC37, MAP2K/MEK, MARK3, PPP2R1A and PPP2CA. Also interacts with RAF and MAPK/ERK, in a Ras-dependent manner. The binding of 14-3-3 proteins to phosphorylated KSR prevents the membrane localization. Interacts with VRK2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Arhgef2Q608755EBI-1536336,EBI-772191
BRAFP150563EBI-1536336,EBI-365980From a different organism.
NME1P155317EBI-1536336,EBI-741141From a different organism.
VRK2Q86Y07-18EBI-1536336,EBI-1207633From a different organism.

Protein-protein interaction databases

BioGridi201048. 18 interactions.
IntActiQ61097. 8 interactions.
MINTiMINT-99547.

Structurei

Secondary structure

1
873
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 323
Helixi33 – 364
Helixi37 – 393
Helixi47 – 5812
Helixi65 – 8218
Helixi83 – 853
Helixi88 – 903
Turni94 – 963
Helixi101 – 1033
Turni108 – 1103
Helixi111 – 1144
Helixi118 – 1214
Helixi130 – 1334
Helixi138 – 1469
Turni147 – 1493
Helixi153 – 16210
Helixi163 – 1675
Beta strandi336 – 3394
Beta strandi347 – 3493
Beta strandi356 – 3594
Turni360 – 3634
Beta strandi364 – 3696
Turni371 – 3733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBENMR-A331-378[»]
1KBFNMR-A331-378[»]
2LPENMR-A25-170[»]
ProteinModelPortaliQ61097.
SMRiQ61097. Positions 25-170, 331-378, 501-856.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61097.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini563 – 833271Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 215Poly-Gly
Compositional biasi275 – 2784Poly-Pro
Compositional biasi429 – 49163Ser-richAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri333 – 37745Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000113263.
HOVERGENiHBG052293.
InParanoidiQ61097.
KOiK14958.
OMAiEVSPMRF.
OrthoDBiEOG7BP81Z.
PhylomeDBiQ61097.
TreeFamiTF317006.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR025561. KSR_SAM-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13543. KSR1-SAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q61097-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDRAALRAAA MGEKKEGGGG GAAADGGAGA AVSRALQQCG QLQKLIDISI
60 70 80 90 100
GSLRGLRTKC SVSNDLTQQE IRTLEAKLVK YICKQQQSKL SVTPSDRTAE
110 120 130 140 150
LNSYPRFSDW LYIFNVRPEV VQEIPQELTL DALLEMDEAK AKEMLRRWGA
160 170 180 190 200
STEECSRLQQ ALTCLRKVTG LGGEHKMDSG WSSTDARDSS LGPPMDMLSS
210 220 230 240 250
LGRAGASTQG PRSISVSALP ASDSPVPGLS EGLSDSCIPL HTSGRLTPRA
260 270 280 290 300
LHSFITPPTT PQLRRHAKLK PPRTPPPPSR KVFQLLPSFP TLTRSKSHES
310 320 330 340 350
QLGNRIDDVT PMKFELPHGS PQLVRRDIGL SVTHRFSTKS WLSQVCNVCQ
360 370 380 390 400
KSMIFGVKCK HCRLKCHNKC TKEAPACRIT FLPLARLRRT ESVPSDINNP
410 420 430 440 450
VDRAAEPHFG TLPKALTKKE HPPAMNLDSS SNPSSTTSST PSSPAPFLTS
460 470 480 490 500
SNPSSATTPP NPSPGQRDSR FSFPDISACS QAAPLSSTAD STRLDDQPKT
510 520 530 540 550
DVLGVHEAEA EEPEAGKSEA EDDEEDEVDD LPSSRRPWRG PISRKASQTS
560 570 580 590 600
VYLQEWDIPF EQVELGEPIG QGRWGRVHRG RWHGEVAIRL LEMDGHNQDH
610 620 630 640 650
LKLFKKEVMN YRQTRHENVV LFMGACMNPP HLAIITSFCK GRTLHSFVRD
660 670 680 690 700
PKTSLDINKT RQIAQEIIKG MGYLHAKGIV HKDLKSKNVF YDNGKVVITD
710 720 730 740 750
FGLFGISGVV REERRENQLK LSHDWLCYLA PEIVREMIPG RDEDQLPFSK
760 770 780 790 800
AADVYAFGTV WYELQARDWP FKHQPAEALI WQIGSGEGVR RVLASVSLGK
810 820 830 840 850
EVGEILSACW AFDLQERPSF SLLMDMLERL PKLNRRLSHP GHFWKSADIN
860 870
SSKVMPRFER FGLGTLESGN PKM
Length:873
Mass (Da):96,755
Last modified:November 1, 1996 - v1
Checksum:iEAEEB23FAE715D94
GO
Isoform 2 (identifier: Q61097-2) [UniParc]FASTAAdd to Basket

Also known as: B-KSR1

The sequence of this isoform differs from the canonical sequence as follows:
     474-474: P → PAAYFIHHRQQFIFP
     848-873: DINSSKVMPRFERFGLGTLESGNPKM → EL

Show »
Length:863
Mass (Da):95,861
Checksum:iCAC9B367C41314FA
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei474 – 4741P → PAAYFIHHRQQFIFP in isoform 2. CuratedVSP_012232
Alternative sequencei848 – 87326DINSS…GNPKM → EL in isoform 2. CuratedVSP_012233Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43585 mRNA. Translation: AAC52382.1.
AL592551 Genomic DNA. Translation: CAI24047.1.
X81634 mRNA. Translation: CAA57288.1.
CCDSiCCDS25117.1. [Q61097-1]
PIRiI48379.
RefSeqiNP_038599.1. NM_013571.2. [Q61097-1]
XP_006532398.1. XM_006532335.1. [Q61097-2]
UniGeneiMm.4745.

Genome annotation databases

EnsembliENSMUST00000018478; ENSMUSP00000018478; ENSMUSG00000018334. [Q61097-1]
GeneIDi16706.
KEGGimmu:16706.
UCSCiuc007kkg.1. mouse. [Q61097-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43585 mRNA. Translation: AAC52382.1 .
AL592551 Genomic DNA. Translation: CAI24047.1 .
X81634 mRNA. Translation: CAA57288.1 .
CCDSi CCDS25117.1. [Q61097-1 ]
PIRi I48379.
RefSeqi NP_038599.1. NM_013571.2. [Q61097-1 ]
XP_006532398.1. XM_006532335.1. [Q61097-2 ]
UniGenei Mm.4745.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KBE NMR - A 331-378 [» ]
1KBF NMR - A 331-378 [» ]
2LPE NMR - A 25-170 [» ]
ProteinModelPortali Q61097.
SMRi Q61097. Positions 25-170, 331-378, 501-856.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201048. 18 interactions.
IntActi Q61097. 8 interactions.
MINTi MINT-99547.

PTM databases

PhosphoSitei Q61097.

Proteomic databases

MaxQBi Q61097.
PaxDbi Q61097.
PRIDEi Q61097.

Protocols and materials databases

DNASUi 16706.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018478 ; ENSMUSP00000018478 ; ENSMUSG00000018334 . [Q61097-1 ]
GeneIDi 16706.
KEGGi mmu:16706.
UCSCi uc007kkg.1. mouse. [Q61097-1 ]

Organism-specific databases

CTDi 8844.
MGIi MGI:105051. Ksr1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118807.
HOGENOMi HOG000113263.
HOVERGENi HBG052293.
InParanoidi Q61097.
KOi K14958.
OMAi EVSPMRF.
OrthoDBi EOG7BP81Z.
PhylomeDBi Q61097.
TreeFami TF317006.

Miscellaneous databases

EvolutionaryTracei Q61097.
NextBioi 290486.
PROi Q61097.
SOURCEi Search...

Gene expression databases

Bgeei Q61097.
CleanExi MM_KSR1.
ExpressionAtlasi Q61097. baseline and differential.
Genevestigatori Q61097.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR025561. KSR_SAM-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF13543. KSR1-SAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "KSR, a novel protein kinase required for RAS signal transduction."
    Therrien M., Chang H.C., Solomon N.M., Karim F.D., Wassarman D.A., Rubin G.M.
    Cell 83:879-888(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HSPCA; YWHAB; CDC37 AND MAP2K.
  2. "Identification of B-KSR1, a novel brain-specific isoform of KSR1 that functions in neuronal signaling."
    Mueller J., Cacace A.M., Lyons W.E., McGill C.B., Morrison D.K.
    Mol. Cell. Biol. 20:5529-5539(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), INTERACTION WITH MAPK, MUTAGENESIS OF GLY-572; ARG-589; ARG-615; ASP-700 AND CYS-809, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. Pelan S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "YAC/P1 contigs defining the location of 56 microsatellite markers and several genes across a 3.4cM interval on mouse chromosome 11."
    Nehls M., Luno K., Schorpp M., Pfeifer D., Krause S., Matysiak-Scholze U., Dierbach H., Boehm T.
    Mamm. Genome 6:321-331(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-474 (ISOFORMS 1/2).
    Strain: BALB/c.
  5. "C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1."
    Mueller J., Ory S., Copeland T., Piwnica-Worms H., Morrison D.K.
    Mol. Cell 8:983-993(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MARK3, PHOSPHORYLATION AT SER-297 AND SER-392, MUTAGENESIS OF SER-297; SER-392; ILE-397 AND VAL-401.
  6. "Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites."
    Ory S., Zhou M., Conrads T.P., Veenstra T.D., Morrison D.K.
    Curr. Biol. 13:1356-1364(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP2R1A AND PPP2CA, DEPHOSPHORYLATION BY PPP2CA.
  7. "MAP kinase module: the Ksr connection."
    Roy F., Therrien M.
    Curr. Biol. 12:R325-R327(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR)."
    Zhou M., Horita D.A., Waugh D.S., Byrd R.A., Morrison D.K.
    J. Mol. Biol. 315:435-446(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 331-378 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiKSR1_MOUSE
AccessioniPrimary (citable) accession number: Q61097
Secondary accession number(s): Q61648, Q78DX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3