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Q6VAB6

- KSR2_HUMAN

UniProt

Q6VAB6 - KSR2_HUMAN

Protein

Kinase suppressor of Ras 2

Gene

KSR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    Functioni

    Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Kinase activity is inhibited by ASC24.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi413 – 4131Zinc 1By similarity
    Metal bindingi425 – 4251Zinc 2By similarity
    Metal bindingi428 – 4281Zinc 2By similarity
    Metal bindingi438 – 4381Zinc 1By similarity
    Metal bindingi441 – 4411Zinc 1By similarity
    Metal bindingi446 – 4461Zinc 2By similarity
    Metal bindingi449 – 4491Zinc 2By similarity
    Metal bindingi456 – 4561Zinc 1By similarity
    Active sitei786 – 7861Proton donor/acceptor1 Publication
    Binding sitei788 – 7881ATP1 Publication
    Binding sitei803 – 8031ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri412 – 45645Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi672 – 6809ATP1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. calcium-mediated signaling Source: Ensembl
    2. positive regulation of MAPK cascade Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ6VAB6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinase suppressor of Ras 2 (EC:2.7.11.1)
    Short name:
    hKSR2
    Gene namesi
    Name:KSR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18610. KSR2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi718 – 7181R → H: Impairs formation of heterotetramers with MAP2K1, but not the formation of heterodimers. 1 Publication
    Mutagenesisi786 – 7861D → A: Loss of kinase activity. 1 Publication
    Mutagenesisi879 – 8791A → L: Impairs MAP2K1 binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134914125.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 950950Kinase suppressor of Ras 2PRO_0000086231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei474 – 4741Phosphoserine; by MARK3By similarity

    Post-translational modificationi

    Phosphorylated on Ser-474 by MARK3.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ6VAB6.
    PRIDEiQ6VAB6.

    PTM databases

    PhosphoSiteiQ6VAB6.

    Expressioni

    Tissue specificityi

    Mainly expressed in brain and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ6VAB6.
    BgeeiQ6VAB6.
    CleanExiHS_KSR2.
    GenevestigatoriQ6VAB6.

    Organism-specific databases

    HPAiHPA035536.

    Interactioni

    Subunit structurei

    Interacts with MAP2K1, forming a heterodimer that can dimerize to form a heterotetramer. Interacts with MAP3K8, MAPK, RAS and RAF. Interacts with BRAF; this increases the low intrinsic protein kinase activity of KSR2.2 Publications

    Protein-protein interaction databases

    BioGridi129567. 5 interactions.
    DIPiDIP-59195N.
    IntActiQ6VAB6. 10 interactions.
    MINTiMINT-8397064.
    STRINGi9606.ENSP00000339952.

    Structurei

    Secondary structure

    1
    950
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi656 – 6583
    Beta strandi659 – 6613
    Beta strandi675 – 69319
    Turni704 – 7107
    Helixi711 – 7144
    Beta strandi727 – 7304
    Beta strandi735 – 7384
    Beta strandi744 – 7463
    Helixi747 – 7504
    Helixi761 – 77919
    Beta strandi792 – 7943
    Helixi827 – 8304
    Helixi834 – 8374
    Helixi853 – 86917
    Beta strandi873 – 8764
    Helixi879 – 8879
    Helixi903 – 9119
    Turni915 – 9173
    Helixi921 – 9288

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y4IX-ray3.46B634-950[»]
    ProteinModelPortaliQ6VAB6.
    SMRiQ6VAB6. Positions 16-154, 626-931.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini666 – 931266Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi181 – 293113Pro-richAdd
    BLAST
    Compositional biasi510 – 55041Pro-richAdd
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive and seems to have very low intrinsic kinase activity. This low kinase activity can be increased by interaction with BRAF.

    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 fingeri412 – 45645Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000113263.
    HOVERGENiHBG052293.
    InParanoidiQ6VAB6.
    OMAiFCWAYEQ.
    OrthoDBiEOG7BP81Z.
    PhylomeDBiQ6VAB6.
    TreeFamiTF317006.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR025561. KSR_SAM-like_dom.
    IPR002219. Prot_Kinase_C-like_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: Q6VAB6-1) [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

    MDEENMTKSE EQQPLSLQKA LQQCELVQNM IDLSISNLEG LRTKCATSND    50
    LTQKEIRTLE SKLVKYFSRQ LSCKKKVALQ ERNAELDGFP QLRHWFRIVD 100
    VRKEVLEEIS PGQLSLEDLL EMTDEQVCET VEKYGANREE CARLNASLSC 150
    LRNVHMSGGN LSKQDWTIQW PTTETGKENN PVCPPEPTPW IRTHLSQSPR 200
    VPSKCVQHYC HTSPTPGAPV YTHVDRLTVD AYPGLCPPPP LESGHRSLPP 250
    SPRQRHAVRT PPRTPNIVTT VTPPGTPPMR KKNKLKPPGT PPPSSRKLIH 300
    LIPGFTALHR SKSHEFQLGH RVDEAHTPKA KKKSKPLNLK IHSSVGSCEN 350
    IPSQQRSPLL SERSLRSFFV GHAPFLPSTP PVHTEANFSA NTLSVPRWSP 400
    QIPRRDLGNS IKHRFSTKYW MSQTCTVCGK GMLFGLKCKN CKLKCHNKCT 450
    KEAPPCHLLI IHRGDPARLV RTESVPCDIN NPLRKPPRYS DLHISQTLPK 500
    TNKINKDHIP VPYQPDSSSN PSSTTSSTPS SPAPPLPPSA TPPSPLHPSP 550
    QCTRQQKNFN LPASHYYKYK QQFIFPDVVP VPETPTRAPQ VILHPVTSNP 600
    ILEGNPLLQI EVEPTSENEE VHDEAEESED DFEEMNLSLL SARSFPRKAS 650
    QTSIFLQEWD IPFEQLEIGE LIGKGRFGQV YHGRWHGEVA IRLIDIERDN 700
    EDQLKAFKRE VMAYRQTRHE NVVLFMGACM SPPHLAIITS LCKGRTLYSV 750
    VRDAKIVLDV NKTRQIAQEI VKGMGYLHAK GILHKDLKSK NVFYDNGKVV 800
    ITDFGLFSIS GVLQAGRRED KLRIQNGWLC HLAPEIIRQL SPDTEEDKLP 850
    FSKHSDVFAL GTIWYELHAR EWPFKTQPAE AIIWQMGTGM KPNLSQIGMG 900
    KEISDILLFC WAFEQEERPT FTKLMDMLEK LPKRNRRLSH PGHFWKSAEL 950
    Length:950
    Mass (Da):107,632
    Last modified:May 29, 2007 - v2
    Checksum:iDFBC20F4E71077AD
    GO
    Isoform 2 (identifier: Q6VAB6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-303: Missing.
         304-329: GFTALHRSKSHEFQLGHRVDEAHTPK → MYNKKAKMEPNASESAIPARRQRQPR
         740-742: SLC → RPV
         743-950: Missing.

    Show »
    Length:439
    Mass (Da):49,607
    Checksum:iA5D6F1DEAFDA51FC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti676 – 6761R → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040659

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 303303Missing in isoform 2. 1 PublicationVSP_012234Add
    BLAST
    Alternative sequencei304 – 32926GFTAL…AHTPK → MYNKKAKMEPNASESAIPAR RQRQPR in isoform 2. 1 PublicationVSP_012235Add
    BLAST
    Alternative sequencei740 – 7423SLC → RPV in isoform 2. 1 PublicationVSP_012236
    Alternative sequencei743 – 950208Missing in isoform 2. 1 PublicationVSP_012237Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK098831 mRNA. Translation: BAC05426.1.
    AC073864 Genomic DNA. No translation available.
    AC079127 Genomic DNA. No translation available.
    AC084291 Genomic DNA. No translation available.
    AC092936 Genomic DNA. No translation available.
    AY345972 mRNA. Translation: AAQ24226.1.
    BC107106 mRNA. Translation: AAI07107.1.
    BC107107 mRNA. Translation: AAI07108.1.
    BC127603 mRNA. Translation: AAI27604.1.
    RefSeqiNP_775869.3. NM_173598.4.
    UniGeneiHs.375836.

    Genome annotation databases

    EnsembliENST00000339824; ENSP00000339952; ENSG00000171435. [Q6VAB6-1]
    GeneIDi283455.
    KEGGihsa:283455.
    UCSCiuc001two.2. human. [Q6VAB6-1]

    Polymorphism databases

    DMDMi148886599.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK098831 mRNA. Translation: BAC05426.1 .
    AC073864 Genomic DNA. No translation available.
    AC079127 Genomic DNA. No translation available.
    AC084291 Genomic DNA. No translation available.
    AC092936 Genomic DNA. No translation available.
    AY345972 mRNA. Translation: AAQ24226.1 .
    BC107106 mRNA. Translation: AAI07107.1 .
    BC107107 mRNA. Translation: AAI07108.1 .
    BC127603 mRNA. Translation: AAI27604.1 .
    RefSeqi NP_775869.3. NM_173598.4.
    UniGenei Hs.375836.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y4I X-ray 3.46 B 634-950 [» ]
    ProteinModelPortali Q6VAB6.
    SMRi Q6VAB6. Positions 16-154, 626-931.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 129567. 5 interactions.
    DIPi DIP-59195N.
    IntActi Q6VAB6. 10 interactions.
    MINTi MINT-8397064.
    STRINGi 9606.ENSP00000339952.

    PTM databases

    PhosphoSitei Q6VAB6.

    Polymorphism databases

    DMDMi 148886599.

    Proteomic databases

    PaxDbi Q6VAB6.
    PRIDEi Q6VAB6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339824 ; ENSP00000339952 ; ENSG00000171435 . [Q6VAB6-1 ]
    GeneIDi 283455.
    KEGGi hsa:283455.
    UCSCi uc001two.2. human. [Q6VAB6-1 ]

    Organism-specific databases

    CTDi 283455.
    GeneCardsi GC12M117890.
    H-InvDB HIX0018992.
    HGNCi HGNC:18610. KSR2.
    HPAi HPA035536.
    MIMi 610737. gene.
    neXtProti NX_Q6VAB6.
    PharmGKBi PA134914125.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113263.
    HOVERGENi HBG052293.
    InParanoidi Q6VAB6.
    OMAi FCWAYEQ.
    OrthoDBi EOG7BP81Z.
    PhylomeDBi Q6VAB6.
    TreeFami TF317006.

    Enzyme and pathway databases

    SignaLinki Q6VAB6.

    Miscellaneous databases

    ChiTaRSi KSR2. human.
    GenomeRNAii 283455.
    NextBioi 93924.
    PROi Q6VAB6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6VAB6.
    Bgeei Q6VAB6.
    CleanExi HS_KSR2.
    Genevestigatori Q6VAB6.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR025561. KSR_SAM-like_dom.
    IPR002219. Prot_Kinase_C-like_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

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Identification of a novel human kinase supporter of Ras (hKSR-2) that functions as a negative regulator of Cot (Tpl2) signaling."
      Channavajhala P.L., Wu L., Cuozzo J.W., Hall J.P., Liu W., Lin L.-L., Zhang Y.
      J. Biol. Chem. 278:47089-47097(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-950 (ISOFORM 1), FUNCTION, INTERACTION WITH MAP2K; RAS; RAF; MAPK AND MAP3K8, TISSUE SPECIFICITY.
      Tissue: Testis.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-950 (ISOFORM 1).
    5. "hKSR-2 inhibits MEKK3-activated MAP kinase and NF-kappaB pathways in inflammation."
      Channavajhala P.L., Rao V.R., Spaulding V., Lin L.-L., Zhang Y.G.
      Biochem. Biophys. Res. Commun. 334:1214-1218(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK."
      Brennan D.F., Dar A.C., Hertz N.T., Chao W.C., Burlingame A.L., Shokat K.M., Barford D.
      Nature 472:366-369(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 634-950 OF MUTANT ALA-786 IN COMPLEX WITH ATP AND MAP2K1, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH BRAF AND MAP2K1, ACTIVE SITE, MUTAGENESIS OF ARG-718; ASP-786 AND ALA-879.
    7. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
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      Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-676.

    Entry informationi

    Entry nameiKSR2_HUMAN
    AccessioniPrimary (citable) accession number: Q6VAB6
    Secondary accession number(s): A0PJT2, Q3B828, Q8N775
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    KSR2 binds ATP and has very low in vitro protein kinase activity; the physiological relevance of this activity is unknown. KSR2 is proposed to be in an inactive conformation by itself or in complex with MAP2K1. Interaction with BRAF is proposed to induce a conformation change that increases the low intrinsic kinase activity (PubMed:21441910).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3