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Q8IVT5

- KSR1_HUMAN

UniProt

Q8IVT5 - KSR1_HUMAN

Protein

Kinase suppressor of Ras 1

Gene

KSR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (03 Sep 2014)
      Previous versions | rss
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    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 bindingi348 – 3481Zinc 1By similarity
    Metal bindingi360 – 3601Zinc 2By similarity
    Metal bindingi363 – 3631Zinc 2By similarity
    Metal bindingi373 – 3731Zinc 1By similarity
    Metal bindingi376 – 3761Zinc 1By similarity
    Metal bindingi381 – 3811Zinc 2By similarity
    Metal bindingi384 – 3841Zinc 2By similarity
    Metal bindingi391 – 3911Zinc 1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri347 – 39145Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. intracellular signal transduction Source: InterPro
    2. positive regulation of MAPK cascade Source: Ensembl
    3. Ras protein signal transduction Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ8IVT5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinase suppressor of Ras 1
    Gene namesi
    Name:KSR1
    Synonyms:KSR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6465. KSR1.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane By similarity; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane 1 Publication
    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 By similarity.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 923923Kinase suppressor of Ras 1PRO_0000086229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701Phosphothreonine3 Publications
    Modified residuei274 – 2741Phosphothreonine1 Publication
    Modified residuei311 – 3111Phosphoserine2 Publications
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei406 – 4061Phosphoserine2 Publications
    Modified residuei569 – 5691Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on Ser-311 and, to a higher extent, on Ser-406 by MARK3. Dephosphorylated on Ser-406 by PPP2CA. In resting cells, phosphorylated KSR1 is cytoplasmic and in stimulated cells, dephosphorylated KSR1 is membrane-associated By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IVT5.
    PaxDbiQ8IVT5.
    PRIDEiQ8IVT5.

    PTM databases

    PhosphoSiteiQ8IVT5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IVT5.
    BgeeiQ8IVT5.
    CleanExiHS_KSR1.
    GenevestigatoriQ8IVT5.

    Organism-specific databases

    HPAiCAB009623.
    HPA011215.

    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 By similarity. The binding of 14-3-3 proteins to phosphorylated KSR prevents the membrane localization. Interacts with isoform 1 of VRK2.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VRK2Q86Y074EBI-486984,EBI-1207615

    Protein-protein interaction databases

    BioGridi114371. 11 interactions.
    IntActiQ8IVT5. 17 interactions.
    MINTiMINT-87143.
    STRINGi9606.ENSP00000268763.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IVT5.
    SMRiQ8IVT5. Positions 25-170, 343-390, 598-906.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini613 – 883271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 215Poly-Gly
    Compositional biasi289 – 2924Poly-Pro

    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 fingeri347 – 39145Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000113263.
    HOVERGENiHBG052293.
    InParanoidiQ8IVT5.
    KOiK14958.
    OMAiEVSPMRF.
    OrthoDBiEOG7BP81Z.
    PhylomeDBiQ8IVT5.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IVT5-1) [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

    MDRAALRAAA MGEKKEGGGG GDAAAAEGGA GAAASRALQQ CGQLQKLIDI    50
    SIGSLRGLRT KCAVSNDLTQ QEIRTLEAKL VRYICKQRQC KLSVAPGERT 100
    PELNSYPRFS DWLYTFNVRP EVVQEIPRDL TLDALLEMNE AKVKETLRRC 150
    GASGDECGRL QYALTCLRKV TGLGGEHKED SSWSSLDARR ESGSGPSTDT 200
    LSAASLPWPP GSSQLGRAGN SAQGPRSISV SALPASDSPT PSFSEGLSDT 250
    CIPLHASGRL TPRALHSFIT PPTTPQLRRH TKLKPPRTPP PPSRKVFQLL 300
    PSFPTLTRSK SHESQLGNRI DDVSSMRFDL SHGSPQMVRR DIGLSVTHRF 350
    STKSWLSQVC HVCQKSMIFG VKCKHCRLKC HNKCTKEAPA CRISFLPLTR 400
    LRRTESVPSD INNPVDRAAE PHFGTLPKAL TKKEHPPAMN HLDSSSNPSS 450
    TTSSTPSSPA PFPTSSNPSS ATTPPNPSPG QRDSRFNFPA AYFIHHRQQF 500
    IFPVPSAGHC WKCLLIAESL KENAFNISAF AHAAPLPEAA DGTRLDDQPK 550
    ADVLEAHEAE AEEPEAGKSE AEDDEDEVDD LPSSRRPWRG PISRKASQTS 600
    VYLQEWDIPF EQVELGEPIG QGRWGRVHRG RWHGEVAIRL LEMDGHNQDH 650
    LKLFKKEVMN YRQTRHENVV LFMGACMNPP HLAIITSFCK GRTLHSFVRD 700
    PKTSLDINKT RQIAQEIIKG MGYLHAKGIV HKDLKSKNVF YDNGKVVITD 750
    FGLFGISGVV REGRRENQLK LSHDWLCYLA PEIVREMTPG KDEDQLPFSK 800
    AADVYAFGTV WYELQARDWP LKNQAAEASI WQIGSGEGMK RVLTSVSLGK 850
    EVSEILSACW AFDLQERPSF SLLMDMLEKL PKLNRRLSHP GHFWKSADIN 900
    SSKVVPRFER FGLGVLESSN PKM 923
    Length:923
    Mass (Da):102,160
    Last modified:September 3, 2014 - v3
    Checksum:i61BF0F1598349540
    GO
    Isoform 2 (identifier: Q8IVT5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         504-526: VPSAGHCWKCLLIAESLKENAFN → D
         898-923: DINSSKVVPRFERFGLGVLESSNPKM → EL

    Note: No experimental confirmation available.

    Show »
    Length:877
    Mass (Da):97,115
    Checksum:iB316183895D9A4BD
    GO
    Isoform 3 (identifier: Q8IVT5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-137: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:786
    Mass (Da):87,344
    Checksum:i7BDD722CFE4B87BA
    GO
    Isoform 4 (identifier: Q8IVT5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-137: Missing.
         898-923: DINSSKVVPRFERFGLGVLESSNPKM → EL

    Note: No experimental confirmation available.

    Show »
    Length:762
    Mass (Da):84,697
    Checksum:i3034D20D01F33E66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 26523FSEGL…TPRAL → EFRHTSALTQHTAHTQHTSA HTQ in AAH42106. (PubMed:8521512)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti227 – 2271S → P.1 Publication
    VAR_040658
    Natural varianti359 – 3591V → A.1 Publication
    VAR_046048
    Natural varianti663 – 6631Q → H.1 Publication
    VAR_046049

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 137137Missing in isoform 3 and isoform 4. 1 PublicationVSP_055655Add
    BLAST
    Alternative sequencei504 – 52623VPSAG…ENAFN → D in isoform 2. 1 PublicationVSP_055656Add
    BLAST
    Alternative sequencei898 – 92326DINSS…SNPKM → EL in isoform 2 and isoform 4. 1 PublicationVSP_055657Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC069366 Genomic DNA. No translation available.
    AC015688 Genomic DNA. No translation available.
    BC042106 mRNA. Translation: AAH42106.1.
    U43586 mRNA. Translation: AAC50354.1.
    RefSeqiNP_055053.1. NM_014238.1.
    UniGeneiHs.133534.

    Genome annotation databases

    EnsembliENST00000268763; ENSP00000268763; ENSG00000141068. [Q8IVT5-3]
    ENST00000398988; ENSP00000381958; ENSG00000141068. [Q8IVT5-4]
    ENST00000509603; ENSP00000438795; ENSG00000141068. [Q8IVT5-2]
    GeneIDi8844.
    KEGGihsa:8844.

    Polymorphism databases

    DMDMi56749095.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC069366 Genomic DNA. No translation available.
    AC015688 Genomic DNA. No translation available.
    BC042106 mRNA. Translation: AAH42106.1 .
    U43586 mRNA. Translation: AAC50354.1 .
    RefSeqi NP_055053.1. NM_014238.1.
    UniGenei Hs.133534.

    3D structure databases

    ProteinModelPortali Q8IVT5.
    SMRi Q8IVT5. Positions 25-170, 343-390, 598-906.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114371. 11 interactions.
    IntActi Q8IVT5. 17 interactions.
    MINTi MINT-87143.
    STRINGi 9606.ENSP00000268763.

    PTM databases

    PhosphoSitei Q8IVT5.

    Polymorphism databases

    DMDMi 56749095.

    Proteomic databases

    MaxQBi Q8IVT5.
    PaxDbi Q8IVT5.
    PRIDEi Q8IVT5.

    Protocols and materials databases

    DNASUi 8844.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268763 ; ENSP00000268763 ; ENSG00000141068 . [Q8IVT5-3 ]
    ENST00000398988 ; ENSP00000381958 ; ENSG00000141068 . [Q8IVT5-4 ]
    ENST00000509603 ; ENSP00000438795 ; ENSG00000141068 . [Q8IVT5-2 ]
    GeneIDi 8844.
    KEGGi hsa:8844.

    Organism-specific databases

    CTDi 8844.
    GeneCardsi GC17P025783.
    H-InvDB HIX0018394.
    HIX0025516.
    HIX0029273.
    HGNCi HGNC:6465. KSR1.
    HPAi CAB009623.
    HPA011215.
    MIMi 601132. gene.
    neXtProti NX_Q8IVT5.
    PharmGKBi PA30254.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113263.
    HOVERGENi HBG052293.
    InParanoidi Q8IVT5.
    KOi K14958.
    OMAi EVSPMRF.
    OrthoDBi EOG7BP81Z.
    PhylomeDBi Q8IVT5.
    TreeFami TF317006.

    Enzyme and pathway databases

    SignaLinki Q8IVT5.

    Miscellaneous databases

    ChiTaRSi KSR1. human.
    GeneWikii KSR1.
    GenomeRNAii 8844.
    NextBioi 33204.
    PROi Q8IVT5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IVT5.
    Bgeei Q8IVT5.
    CleanExi HS_KSR1.
    Genevestigatori Q8IVT5.

    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. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "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 1-628 (ISOFORM 3).
      Tissue: Brain.
    3. "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] OF 243-899 (ISOFORM 2).
    4. "MAP kinase module: the Ksr connection."
      Roy F., Therrien M.
      Curr. Biol. 12:R325-R327(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270 AND SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; THR-274; SER-334; SER-406 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "VRK2 inhibits mitogen-activated protein kinase signaling and inversely correlates with ErbB2 in human breast cancer."
      Fernandez I.F., Blanco S., Lozano J., Lazo P.A.
      Mol. Cell. Biol. 30:4687-4697(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VRK2.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-227; ALA-359 AND HIS-663.

    Entry informationi

    Entry nameiKSR1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IVT5
    Secondary accession number(s): F8WEA9, H7BYU0, Q13476
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: September 3, 2014
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3